ID   100K_RAT       STANDARD;      PRT;   889 AA.
AC   Q62671;
DT   01-NOV-1997 (Rel. 35, Created)
DT   01-NOV-1997 (Rel. 35, Last sequence update)
DT   15-JUL-1999 (Rel. 38, Last annotation update)
DE   100 KDA PROTEIN (EC 6.3.2.-).
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Rattus.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   STRAIN=WISTAR; TISSUE=TESTIS;
RX   MEDLINE; 92253337.
RA   Mueller D., Rehbein M., Baumeister H., Richter D.;
RT   "Molecular characterization of a novel rat protein structurally
RT   related to poly(A) binding proteins and the 70K protein of the U1
RT   small nuclear ribonucleoprotein particle (snRNP).";
RL   Nucleic Acids Res. 20:1471-1475(1992).
RN   [2]
RP   ERRATUM.
RA   Mueller D., Rehbein M., Baumeister H., Richter D.;
RL   Nucleic Acids Res. 20:2624-2624(1992).
CC   -!- FUNCTION: E3 UBIQUITIN-PROTEIN LIGASE WHICH ACCEPTS UBIQUITIN FROM
CC       AN E2 UBIQUITIN-CONJUGATING ENZYME IN THE FORM OF A THIOESTER AND
CC       THEN DIRECTLY TRANSFERS THE UBIQUITIN TO TARGETED SUBSTRATES (BY
CC       SIMILARITY). THIS PROTEIN MAY BE INVOLVED IN MATURATION AND/OR
CC       POST-TRANSCRIPTIONAL REGULATION OF MRNA.
CC   -!- TISSUE SPECIFICITY: HIGHEST LEVELS FOUND IN TESTIS. ALSO PRESENT
CC       IN LIVER, KIDNEY, LUNG AND BRAIN.
CC   -!- DEVELOPMENTAL STAGE: IN EARLY POST-NATAL LIFE, EXPRESSION IN
CC       THE TESTIS INCREASES TO REACH A MAXIMUM AROUND DAY 28.
CC   -!- MISCELLANEOUS: A CYSTEINE RESIDUE IS REQUIRED FOR
CC       UBIQUITIN-THIOLESTER FORMATION.
CC   -!- SIMILARITY: CONTAINS AN HECT-TYPE E3 UBIQUITIN-PROTEIN LIGASE
CC       DOMAIN.
CC   -!- SIMILARITY: A CENTRAL REGION (AA 485-514) IS SIMILAR TO THE
CC       C-TERMINAL DOMAINS OF MAMMALIAN AND YEAST POLY (A) RNA BINDING
CC       PROTEINS (PABP).
CC   -!- SIMILARITY: THE C-TERMINAL HALF SHOWS HIGH SIMILARITY TO
CC       DROSOPHILA HYPERPLASMIC DISC PROTEIN AND SOME, TO HUMAN E6-AP.
CC   -!- SIMILARITY: CONTAINS MIXED-CHARGE DOMAINS SIMILAR TO RNA-BINDING
CC       PROTEINS.
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DR   EMBL; X64411; CAA45756.1; -.
DR   INTERPRO; IPR000569; -.
DR   INTERPRO; IPR002004; -.
DR   PFAM; PF00632; HECT; 1.
DR   PFAM; PF00658; PABP; 1.
KW   Ubiquitin conjugation; Ligase.
FT   DOMAIN       77     88       ASP/GLU-RICH (ACIDIC).
FT   DOMAIN      127    150       PRO-RICH.
FT   DOMAIN      420    439       ARG/GLU-RICH (MIXED CHARGE).
FT   DOMAIN      448    457       ARG/ASP-RICH (MIXED CHARGE).
FT   DOMAIN      485    514       PABP-LIKE.
FT   DOMAIN      579    590       ASP/GLU-RICH (ACIDIC).
FT   DOMAIN      786    889       HECT DOMAIN.
FT   DOMAIN      827    847       PRO-RICH.
FT   BINDING     858    858       UBIQUITIN (BY SIMILARITY).
SQ   SEQUENCE   889 AA;  100368 MW;  ABD7E3CD53961B78 CRC64;
     MMSARGDFLN YALSLMRSHN DEHSDVLPVL DVCSLKHVAY VFQALIYWIK AMNQQTTLDT
     PQLERKRTRE LLELGIDNED SEHENDDDTS QSATLNDKDD ESLPAETGQN HPFFRRSDSM
     TFLGCIPPNP FEVPLAEAIP LADQPHLLQP NARKEDLFGR PSQGLYSSSA GSGKCLVEVT
     MDRNCLEVLP TKMSYAANLK NVMNMQNRQK KAGEDQSMLA EEADSSKPGP SAHDVAAQLK
     SSLLAEIGLT ESEGPPLTSF RPQCSFMGMV ISHDMLLGRW RLSLELFGRV FMEDVGAEPG
     SILTELGGFE VKESKFRREM EKLRNQQSRD LSLEVDRDRD LLIQQTMRQL NNHFGRRCAT
     TPMAVHRVKV TFKDEPGEGS GVARSFYTAI AQAFLSNEKL PNLDCIQNAN KGTHTSLMQR
     LRNRGERDRE REREREMRRS SGLRAGSRRD RDRDFRRQLS IDTRPFRPAS EGNPSDDPDP
     LPAHRQALGE RLYPRVQAMQ PAFASKITGM LLELSPAQLL LLLASEDSLR ARVEEAMELI
     VAHGRENGAD SILDLGLLDS SEKVQENRKR HGSSRSVVDM DLDDTDDGDD NAPLFYQPGK
     RGFYTPRPGK NTEARLNCFR NIGRILGLCL LQNELCPITL NRHVIKVLLG RKVNWHDFAF
     FDPVMYESLR QLILASQSSD ADAVFSAMDL AFAVDLCKEE GGGQVELIPN GVNIPVTPQN
     VYEYVRKYAE HRMLVVAEQP LHAMRKGLLD VLPKNSLEDL TAEDFRLLVN GCGEVNVQML
     ISFTSFNDES GENAEKLLQF KRWFWSIVER MSMTERQDLV YFWTSSPSLP ASEEGFQPMP
     SITIRPPDDQ HLPTANTCIS RLYVPLYSSK QILKQKLLLA IKTKNFGFV
//
ID   5H1D_FUGRU     STANDARD;      PRT;   379 AA.
AC   P79748;
DT   01-NOV-1997 (REL. 35, CREATED)
DT   01-NOV-1997 (REL. 35, LAST SEQUENCE UPDATE)
DT   01-NOV-1997 (REL. 35, LAST ANNOTATION UPDATE)
DE   5-HYDROXYTRYPTAMINE 1D RECEPTOR (5-HT-1D) (SEROTONIN RECEPTOR).
GN   5HT1D.
OS   FUGU RUBRIPES (JAPANESE PUFFERFISH) (TAKIFUGU RUBRIPES).
OC   EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; PISCES; GNATHOSTOMATA;
OC   OSTEICHTHYES; ACTINOPTERYGII; TETRAODONTIFORMES.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   TISSUE=TESTIS;
RA   YAMAGUCHI F., BRENNER S.;
RL   SUBMITTED (JAN-1997) TO EMBL/GENBANK/DDBJ DATA BANKS.
CC   -!- FUNCTION: THIS IS ONE OF THE SEVERAL DIFFERENT RECEPTORS FOR
CC       5-HYDROXYTRYPTAMINE (SEROTONIN), A BIOGENIC HORMONE THAT FUNCTION
CC       AS A NEUROTRANSMITTER, A HORMONE, AND A MITOGEN. THE ACTIVITY OF
CC       THIS RECEPTOR IS MEDIATED BY G PROTEINS THAT INHIBIT ADENYLATE
CC       CYCLASE ACTIVITY (BY SIMILARITY).
CC   -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN.
CC   -!- SIMILARITY: BELONGS TO FAMILY 1 OF G-PROTEIN COUPLED RECEPTORS.
CC       STRONGEST TO THE OTHER 5HT-1 SUBTYPE RECEPTORS.
DR   EMBL; X83865; E135100; -.
DR   GCRDB; GCR_1112; -.
DR   PROSITE; PS00237; G_PROTEIN_RECEPTOR; 1.
KW   G-PROTEIN COUPLED RECEPTOR; TRANSMEMBRANE; GLYCOPROTEIN;
KW   MULTIGENE FAMILY.
FT   DOMAIN        1     36       EXTRACELLULAR (POTENTIAL).
FT   TRANSMEM     37     60       1 (POTENTIAL).
FT   DOMAIN       61     73       CYTOPLASMIC (POTENTIAL).
FT   TRANSMEM     74     96       2 (POTENTIAL).
FT   DOMAIN       97    106       EXTRACELLULAR (POTENTIAL).
FT   TRANSMEM    107    132       3 (POTENTIAL).
FT   DOMAIN      133    152       CYTOPLASMIC (POTENTIAL).
FT   TRANSMEM    153    174       4 (POTENTIAL).
FT   DOMAIN      175    192       EXTRACELLULAR (POTENTIAL).
FT   TRANSMEM    193    216       5 (POTENTIAL).
FT   DOMAIN      217    307       CYTOPLASMIC (POTENTIAL).
FT   TRANSMEM    308    331       6 (POTENTIAL).
FT   DOMAIN      332    339       EXTRACELLULAR (POTENTIAL).
FT   TRANSMEM    340    364       7 (POTENTIAL).
FT   DOMAIN      365    379       CYTOPLASMIC (POTENTIAL).
FT   DISULFID    109    186       BY SIMILARITY.
FT   CARBOHYD      5      5       POTENTIAL.
FT   CARBOHYD     14     14       POTENTIAL.
FT   CARBOHYD     21     21       POTENTIAL.
SQ   SEQUENCE   379 AA;  42301 MW;  A4090FDD CRC32;
     MELDNNSLDY FSSNFTDIPS NTTVAHWTEA TLLGLQISVS VVLAIVTLAT MLSNAFVIAT
     IFLTRKLHTP ANFLIGSLAV TDMLVSILVM PISIVYTVSK TWSLGQIVCD IWLSSDITFC
     TASILHLCVI ALDRYWAITD ALEYSKRRTM RRAAVMVAVV WVISISISMP PLFWRQAKAH
     EELKECMVNT DQISYTLYST FGAFYVPTVL LIILYGRIYV AARSRIFKTP SYSGKRFTTA
     QLIQTSAGSS LCSLNSASNQ EAHLHSGAGG EGGGSPLFVN SVKVKLADNV LERKRLCAAR
     ERKATKTLGI ILGAFIICWL PFFVVTLVWA ICKECSFDPL LFDVFTWLGY LNSLINPVIY
     TVFNDEFKQA FQKLIKFRR
//
ID   ACT1_FUGRU     STANDARD;      PRT;   375 AA.
AC   P53484;
DT   01-OCT-1996 (REL. 34, CREATED)
DT   01-OCT-1996 (REL. 34, LAST SEQUENCE UPDATE)
DT   01-OCT-1996 (REL. 34, LAST ANNOTATION UPDATE)
DE   ACTIN, CYTOPLASMIC 1 (BETA-ACTIN 1).
OS   FUGU RUBRIPES (JAPANESE PUFFERFISH) (TAKIFUGU RUBRIPES).
OC   EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; PISCES; GNATHOSTOMATA;
OC   OSTEICHTHYES; ACTINOPTERYGII; TETRAODONTIFORMES.
RN   [1]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 96275651.
RA   VENKATESH B., TAY B.H., ELGAR G., BRENNER S.;
RL   J. MOL. BIOL. 259:655-665(1996).
CC   -!- FUNCTION: ACTINS ARE HIGHLY CONSERVED PROTEINS THAT ARE INVOLVED
CC       IN VARIOUS TYPES OF CELL MOTILITY AND ARE UBIQUITOUSLY EXPRESSED
CC       IN ALL EUKARYOTIC CELLS.
CC   -!- SUBUNIT: POLYMERIZATION OF GLOBULAR ACTIN (G-ACTIN) LEADS TO A
CC       STRUCTURAL FILAMENT (F-ACTIN) IN THE FORM OF A TWO-STRANDED
CC       HELIX. EACH ACTIN CAN BIND TO 4 OTHERS.
CC   -!- SUBCELLULAR LOCATION: CYTOPLASMIC.
CC   -!- TISSUE SPECIFICITY: WIDELY DISTRIBUTED. NOT EXPRESSED IN SKELETAL
CC       MUSCLE.
CC   -!- IN VERTEBRATES 3 MAIN GROUPS OF ACTIN ISOFORMS, ALPHA, BETA AND
CC       GAMMA HAVE BEEN IDENTIFIED. THE ALPHA ACTINS ARE FOUND IN MUSCLE
CC       TISSUES AND ARE A MAJOR CONSTITUENT OF THE CONTRACTILE APPARATUS.
CC       THE BETA AND GAMMA ACTINS CO-EXISTS IN MOST CELL TYPES AS
CC       COMPONENTS OF THE CYTOSKELETON AND AS MEDIATORS OF INTERNAL CELL
CC       MOTILITY.
CC   -!- THERE ARE THREE DIFFERENT BETA-CYTOPLASMIC ACTINS IN FUGU
CC       RUBRIPES.
DR   EMBL; U37499; G1335821; -.
DR   PROSITE; PS00406; ACTINS_1; 1.
DR   PROSITE; PS00432; ACTINS_2; 1.
DR   PROSITE; PS01132; ACTINS_ACT_LIKE; 1.
KW   MULTIGENE FAMILY; STRUCTURAL PROTEIN; METHYLATION; ACETYLATION;
KW   CYTOSKELETON.
FT   PROPEP        1      1       REMOVED IN MATURE FORM (BY SIMILARITY).
FT   CHAIN         2    375       ACTIN, CYTOPLASMIC 1.
FT   MOD_RES       1      1       ACETYLATION (BY SIMILARITY).
FT   MOD_RES       2      2       ACETYLATION (BY SIMILARITY).
FT   MOD_RES      73     73       METHYLATION (BY SIMILARITY).
SQ   SEQUENCE   375 AA;  41766 MW;  3A0543DF CRC32;
     MEDEIAALVV DNGSGMCKAG FAGDDAPRAV FPSIVGRPRH QGVMVGMGQK DSYVGDEAQS
     KRGILTLKYP IEHGIVTNWD DMEKIWHHTF YNELRVAPEE HPVLLTEAPL NPKANREKMT
     QIMFETFNTP AMYVAIQAVL SLYASGRTTG IVMDSGDGVT HTVPIYEGYA LPHAILRLDL
     AGRDLTDYLM KILTERGYSF TTTAEREIVR DIKEKLCYVA LDFEQEMGTA ASSSSLEKSY
     ELPDGQVITI GNERFRCPEA LFQPSFLGME SCGIHETTYN SIMKCDVDIR KDLYANTVLS
     GGTTMYPGIA DRMQKEITAL APSTMKIKII APPERKYSVW IGGSILASLS TFQQMWISKQ
     EYDESGPSIV HRKCF
//
ID   ACT2_FUGRU     STANDARD;      PRT;   375 AA.
AC   P53485;
DT   01-OCT-1996 (REL. 34, CREATED)
DT   01-OCT-1996 (REL. 34, LAST SEQUENCE UPDATE)
DT   01-OCT-1996 (REL. 34, LAST ANNOTATION UPDATE)
DE   ACTIN, CYTOPLASMIC 2 (BETA-ACTIN 2).
OS   FUGU RUBRIPES (JAPANESE PUFFERFISH) (TAKIFUGU RUBRIPES).
OC   EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; PISCES; GNATHOSTOMATA;
OC   OSTEICHTHYES; ACTINOPTERYGII; TETRAODONTIFORMES.
RN   [1]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 96275651.
RA   VENKATESH B., TAY B.H., ELGAR G., BRENNER S.;
RL   J. MOL. BIOL. 259:655-665(1996).
CC   -!- FUNCTION: ACTINS ARE HIGHLY CONSERVED PROTEINS THAT ARE INVOLVED
CC       IN VARIOUS TYPES OF CELL MOTILITY AND ARE UBIQUITOUSLY EXPRESSED
CC       IN ALL EUKARYOTIC CELLS.
CC   -!- SUBUNIT: POLYMERIZATION OF GLOBULAR ACTIN (G-ACTIN) LEADS TO A
CC       STRUCTURAL FILAMENT (F-ACTIN) IN THE FORM OF A TWO-STRANDED
CC       HELIX. EACH ACTIN CAN BIND TO 4 OTHERS.
CC   -!- SUBCELLULAR LOCATION: CYTOPLASMIC.
CC   -!- IN VERTEBRATES 3 MAIN GROUPS OF ACTIN ISOFORMS, ALPHA, BETA AND
CC       GAMMA HAVE BEEN IDENTIFIED. THE ALPHA ACTINS ARE FOUND IN MUSCLE
CC       TISSUES AND ARE A MAJOR CONSTITUENT OF THE CONTRACTILE APPARATUS.
CC       THE BETA AND GAMMA ACTINS CO-EXISTS IN MOST CELL TYPES AS
CC       COMPONENTS OF THE CYTOSKELETON AND AS MEDIATORS OF INTERNAL CELL
CC       MOTILITY.
CC   -!- THERE ARE THREE DIFFERENT BETA-CYTOPLASMIC ACTINS IN FUGU
CC       RUBRIPES.
DR   EMBL; U38848; G1335823; -.
DR   PROSITE; PS00406; ACTINS_1; 1.
DR   PROSITE; PS00432; ACTINS_2; 1.
DR   PROSITE; PS01132; ACTINS_ACT_LIKE; 1.
KW   MULTIGENE FAMILY; STRUCTURAL PROTEIN; METHYLATION; ACETYLATION;
KW   CYTOSKELETON.
FT   PROPEP        1      1       REMOVED IN MATURE FORM (BY SIMILARITY).
FT   CHAIN         2    375       ACTIN, CYTOPLASMIC 2.
FT   MOD_RES       1      1       ACETYLATION (BY SIMILARITY).
FT   MOD_RES       2      2       ACETYLATION (BY SIMILARITY).
FT   MOD_RES      73     73       METHYLATION (BY SIMILARITY).
SQ   SEQUENCE   375 AA;  41766 MW;  4A741800 CRC32;
     MDDEIAALVV DNGSGMCKAG FAGDDAPRAV FPSIVGRPRH QGVMVGMGQK DSYVGDEAQS
     KRGILTLKYP IEHGIVTNWD DMEKIWHHTF YNELRVAPEE HPVLLTEAPL NPKANREKMT
     QIMFETFNTP AMYVAIQAVL SLYASGRTTG IVMDSGDGVT HTVPIYEGYA LPHAILRLDL
     AGRDLTDYLM KILTERGYSF TTTAEREIVR DIKEKLCYVA LDFEQEMGTA ASSSSLEKSY
     ELPDGQVITI GNERFRCPEA LFQPSFLGME SCGIHETTFN SIMKCDVDIR KDLYANTVLS
     GGTTMYPGIA DRMQKEITSL APTTMKIKII APPERKYSVW IGGSILASLS TFQQMWISKQ
     EYDESGPSIV HRKCF
//
ID   ACT3_FUGRU     STANDARD;      PRT;   375 AA.
AC   P53486;
DT   01-OCT-1996 (REL. 34, CREATED)
DT   01-OCT-1996 (REL. 34, LAST SEQUENCE UPDATE)
DT   01-OCT-1996 (REL. 34, LAST ANNOTATION UPDATE)
DE   ACTIN, CYTOPLASMIC 3 (BETA-ACTIN 3).
OS   FUGU RUBRIPES (JAPANESE PUFFERFISH) (TAKIFUGU RUBRIPES).
OC   EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; PISCES; GNATHOSTOMATA;
OC   OSTEICHTHYES; ACTINOPTERYGII; TETRAODONTIFORMES.
RN   [1]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 96275651.
RA   VENKATESH B., TAY B.H., ELGAR G., BRENNER S.;
RL   J. MOL. BIOL. 259:655-665(1996).
CC   -!- FUNCTION: ACTINS ARE HIGHLY CONSERVED PROTEINS THAT ARE INVOLVED
CC       IN VARIOUS TYPES OF CELL MOTILITY AND ARE UBIQUITOUSLY EXPRESSED
CC       IN ALL EUKARYOTIC CELLS.
CC   -!- SUBUNIT: POLYMERIZATION OF GLOBULAR ACTIN (G-ACTIN) LEADS TO A
CC       STRUCTURAL FILAMENT (F-ACTIN) IN THE FORM OF A TWO-STRANDED
CC       HELIX. EACH ACTIN CAN BIND TO 4 OTHERS.
CC   -!- SUBCELLULAR LOCATION: CYTOPLASMIC.
CC   -!- TISSUE SPECIFICITY: PREDOMINANTLY EXPRESSED IN GILLS, KIDNEY AND
CC       SKIN.
CC   -!- IN VERTEBRATES 3 MAIN GROUPS OF ACTIN ISOFORMS, ALPHA, BETA AND
CC       GAMMA HAVE BEEN IDENTIFIED. THE ALPHA ACTINS ARE FOUND IN MUSCLE
CC       TISSUES AND ARE A MAJOR CONSTITUENT OF THE CONTRACTILE APPARATUS.
CC       THE BETA AND GAMMA ACTINS CO-EXISTS IN MOST CELL TYPES AS
CC       COMPONENTS OF THE CYTOSKELETON AND AS MEDIATORS OF INTERNAL CELL
CC       MOTILITY.
CC   -!- THERE ARE THREE DIFFERENT BETA-CYTOPLASMIC ACTINS IN FUGU
CC       RUBRIPES.
DR   EMBL; U38849; G1335825; -.
DR   PROSITE; PS00406; ACTINS_1; 1.
DR   PROSITE; PS00432; ACTINS_2; 1.
DR   PROSITE; PS01132; ACTINS_ACT_LIKE; 1.
KW   MULTIGENE FAMILY; STRUCTURAL PROTEIN; METHYLATION; ACETYLATION;
KW   CYTOSKELETON.
FT   PROPEP        1      1       REMOVED IN MATURE FORM (BY SIMILARITY).
FT   CHAIN         2    375       ACTIN, CYTOPLASMIC 3.
FT   MOD_RES       1      1       ACETYLATION (BY SIMILARITY).
FT   MOD_RES       2      2       ACETYLATION (BY SIMILARITY).
FT   MOD_RES      73     73       METHYLATION (BY SIMILARITY).
SQ   SEQUENCE   375 AA;  41782 MW;  E7E73C19 CRC32;
     MEDEVASLVV DNGSGMCKAG FAGDDAPRAV FPSIVGRPRH QGVMVGMGQK DSYVGDEAQS
     KRGILTLKYP IEHGIVTNWD DMEKIWHHTF YNELRVAPEE HPVLLTEAPL NPKANREKMT
     QIMFETFNTP AMYVAIQAVL SLYASGRTTG IVMDSGDGVT HTVPIYEGYA LPHAILRLDL
     AGRDLTDYLM KILTERGYSF TTTAEREIVR DIKEKLCYVA LDFEQEMATA SSSSSLEKSY
     ELPDGQVITI GNERFRCPEA LFQPSFLGME SSGIHETTYN SIMKCDVDIR KDLYANTVLS
     GGTTMYPGIA DRMQKEITAL APSTMKIKII APPERKYSVW IGGSILASLS TFQQMWISKQ
     EYDESGPSIV HRKCF
//
ID   ACTC_FUGRU     STANDARD;      PRT;   377 AA.
AC   P53480;
DT   01-OCT-1996 (REL. 34, CREATED)
DT   01-OCT-1996 (REL. 34, LAST SEQUENCE UPDATE)
DT   01-OCT-1996 (REL. 34, LAST ANNOTATION UPDATE)
DE   ACTIN, ALPHA CARDIAC.
OS   FUGU RUBRIPES (JAPANESE PUFFERFISH) (TAKIFUGU RUBRIPES).
OC   EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; PISCES; GNATHOSTOMATA;
OC   OSTEICHTHYES; ACTINOPTERYGII; TETRAODONTIFORMES.
RN   [1]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 96275651.
RA   VENKATESH B., TAY B.H., ELGAR G., BRENNER S.;
RL   J. MOL. BIOL. 259:655-665(1996).
CC   -!- FUNCTION: ACTINS ARE HIGHLY CONSERVED PROTEINS THAT ARE INVOLVED
CC       IN VARIOUS TYPES OF CELL MOTILITY AND ARE UBIQUITOUSLY EXPRESSED
CC       IN ALL EUKARYOTIC CELLS.
CC   -!- SUBUNIT: POLYMERIZATION OF GLOBULAR ACTIN (G-ACTIN) LEADS TO A
CC       STRUCTURAL FILAMENT (F-ACTIN) IN THE FORM OF A TWO-STRANDED
CC       HELIX. EACH ACTIN CAN BIND TO 4 OTHERS.
CC   -!- SUBCELLULAR LOCATION: CYTOPLASMIC.
CC   -!- TISSUE SPECIFICITY: PREDOMINANTLY EXPRESSED IN HEART. LOWER LEVELS
CC       IN SKELETAL MUSCLE AND SKIN.
CC   -!- IN VERTEBRATES 3 MAIN GROUPS OF ACTIN ISOFORMS, ALPHA, BETA AND
CC       GAMMA HAVE BEEN IDENTIFIED. THE ALPHA ACTINS ARE FOUND IN MUSCLE
CC       TISSUES AND ARE A MAJOR CONSTITUENT OF THE CONTRACTILE APPARATUS.
CC       THE BETA AND GAMMA ACTINS CO-EXISTS IN MOST CELL TYPES AS
CC       COMPONENTS OF THE CYTOSKELETON AND AS MEDIATORS OF INTERNAL CELL
CC       MOTILITY.
CC   -!- THERE ARE THREE GENES CODING FOR CARDIAC ACTIN IN FUGU.
DR   EMBL; U38959; G1335831; -.
DR   EMBL; U38960; G1335833; -.
DR   EMBL; U38961; G1335835; -.
DR   PROSITE; PS00406; ACTINS_1; 1.
DR   PROSITE; PS00432; ACTINS_2; 1.
DR   PROSITE; PS01132; ACTINS_ACT_LIKE; 1.
KW   MULTIGENE FAMILY; STRUCTURAL PROTEIN; METHYLATION; MUSCLE PROTEIN;
KW   ACETYLATION.
FT   PROPEP        1      2       REMOVED IN MATURE FORM (BY SIMILARITY).
FT   CHAIN         3    377       ACTIN, ALPHA CARDIAC.
FT   MOD_RES       3      3       ACETYLATION (BY SIMILARITY).
FT   MOD_RES      75     75       METHYLATION (BY SIMILARITY).
SQ   SEQUENCE   377 AA;  41975 MW;  4BD68409 CRC32;
     MCDDDETTAL VCDNGSGLVK AGFAGDDAPR AVFPSIVGRP RHQGVMVGMG QKDSYVGDEA
     QSKRGILTLK YPIEHGIITN WDDMEKIWHH TFYNELRVAP EEHPTLLTEA PLNPKANREK
     MTQIMFETFN VPAMYVAIQA VLSLYASGRT TGIVLDSGDG VTHNVPIYEG YALPHAIMRL
     DLAGRDLTDY LMKILTERGY SFVTTAEREI VRDIKEKLCY VALDFENEMA TAASSSSLEK
     SYELPDGQVI TIGNERFRCP ETLFQPSFIG MESAGIHETA YNSIMKCDID IRKDLYANNV
     LSGGTTMYPG IADRMQKEIT ALAPSTMKIK IIAPPERKYS VWIGGSILAS LSTFQQMWIS
     KQEYDEAGPS IVHRKCF
//
ID   ACTS_FUGRU     STANDARD;      PRT;   377 AA.
AC   P53481;
DT   01-OCT-1996 (REL. 34, CREATED)
DT   01-OCT-1996 (REL. 34, LAST SEQUENCE UPDATE)
DT   01-OCT-1996 (REL. 34, LAST ANNOTATION UPDATE)
DE   ACTIN, ALPHA SKELETAL MUSCLE 1.
OS   FUGU RUBRIPES (JAPANESE PUFFERFISH) (TAKIFUGU RUBRIPES).
OC   EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; PISCES; GNATHOSTOMATA;
OC   OSTEICHTHYES; ACTINOPTERYGII; TETRAODONTIFORMES.
RN   [1]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 96275651.
RA   VENKATESH B., TAY B.H., ELGAR G., BRENNER S.;
RL   J. MOL. BIOL. 259:655-665(1996).
CC   -!- FUNCTION: ACTINS ARE HIGHLY CONSERVED PROTEINS THAT ARE INVOLVED
CC       IN VARIOUS TYPES OF CELL MOTILITY AND ARE UBIQUITOUSLY EXPRESSED
CC       IN ALL EUKARYOTIC CELLS.
CC   -!- SUBUNIT: POLYMERIZATION OF GLOBULAR ACTIN (G-ACTIN) LEADS TO A
CC       STRUCTURAL FILAMENT (F-ACTIN) IN THE FORM OF A TWO-STRANDED
CC       HELIX. EACH ACTIN CAN BIND TO 4 OTHERS.
CC   -!- SUBCELLULAR LOCATION: CYTOPLASMIC.
CC   -!- TISSUE SPECIFICITY: PREDOMINANTLY EXPRESSED IN SKELETAL MUSCLE.
CC       LOWER LEVELS IN HEART.
CC   -!- IN VERTEBRATES 3 MAIN GROUPS OF ACTIN ISOFORMS, ALPHA, BETA AND
CC       GAMMA HAVE BEEN IDENTIFIED. THE ALPHA ACTINS ARE FOUND IN MUSCLE
CC       TISSUES AND ARE A MAJOR CONSTITUENT OF THE CONTRACTILE APPARATUS.
CC       THE BETA AND GAMMA ACTINS CO-EXISTS IN MOST CELL TYPES AS
CC       COMPONENTS OF THE CYTOSKELETON AND AS MEDIATORS OF INTERNAL CELL
CC       MOTILITY.
CC   -!- THERE ARE TWO DIFFERENT ALPHA-SKELETAL ACTINS IN FUGU RUBRIPES.
DR   EMBL; U38850; G1335827; -.
DR   PROSITE; PS00406; ACTINS_1; 1.
DR   PROSITE; PS00432; ACTINS_2; 1.
DR   PROSITE; PS01132; ACTINS_ACT_LIKE; 1.
KW   MULTIGENE FAMILY; STRUCTURAL PROTEIN; METHYLATION; MUSCLE PROTEIN;
KW   ACETYLATION.
FT   PROPEP        1      2       REMOVED IN MATURE FORM (BY SIMILARITY).
FT   CHAIN         3    377       ACTIN, ALPHA SKELETAL MUSCLE 1.
FT   MOD_RES       3      3       ACETYLATION (BY SIMILARITY).
FT   MOD_RES      75     75       METHYLATION (BY SIMILARITY).
SQ   SEQUENCE   377 AA;  41945 MW;  24356F3F CRC32;
     MCDDDETTAL VCDNGSGLVK AGFAGDDAPR AVFPSIVGRP RHQGVMVGMG QKDSYVGDEA
     QSKRGILTLK YPIEHGIITN WDDMEKIWHH TFYNELRVAP EEHPTLLTEA PLNPKANREK
     MTQIMFETFN VPAMYVAIQA VLSLYASGRT TGIVLDAGDG VTHNVPVYEG YALPHAIMRL
     DLAGRDLTDY LMKILTERGY SFVTTAEREI VRDIKEKLCY VALDFENEMA TAASSSSLEK
     SYELPDGQVI TIGNERFRCP ETLFQPSFIG MESAGIHETA YNSIMKCDID IRKDLYANNV
     LSGGTTMYPG IADRMQKEIT ALAPSTMKIK IIAPPERKYS VWIGGSILAS LSTFQQMWIS
     KQEYDEAGPS IVHRKCF
//
ID   ACTT_FUGRU     STANDARD;      PRT;   377 AA.
AC   P53482;
DT   01-OCT-1996 (REL. 34, CREATED)
DT   01-OCT-1996 (REL. 34, LAST SEQUENCE UPDATE)
DT   01-OCT-1996 (REL. 34, LAST ANNOTATION UPDATE)
DE   ACTIN, ALPHA SKELETAL MUSCLE 2.
OS   FUGU RUBRIPES (JAPANESE PUFFERFISH) (TAKIFUGU RUBRIPES).
OC   EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; PISCES; GNATHOSTOMATA;
OC   OSTEICHTHYES; ACTINOPTERYGII; TETRAODONTIFORMES.
RN   [1]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 96275651.
RA   VENKATESH B., TAY B.H., ELGAR G., BRENNER S.;
RL   J. MOL. BIOL. 259:655-665(1996).
CC   -!- FUNCTION: ACTINS ARE HIGHLY CONSERVED PROTEINS THAT ARE INVOLVED
CC       IN VARIOUS TYPES OF CELL MOTILITY AND ARE UBIQUITOUSLY EXPRESSED
CC       IN ALL EUKARYOTIC CELLS.
CC   -!- SUBUNIT: POLYMERIZATION OF GLOBULAR ACTIN (G-ACTIN) LEADS TO A
CC       STRUCTURAL FILAMENT (F-ACTIN) IN THE FORM OF A TWO-STRANDED
CC       HELIX. EACH ACTIN CAN BIND TO 4 OTHERS.
CC   -!- SUBCELLULAR LOCATION: CYTOPLASMIC.
CC   -!- TISSUE SPECIFICITY: PREDOMINANTLY EXPRESSED IN SKELETAL MUSCLE.
CC       LOWER LEVELS IN HEART, GILLS AND SKIN.
CC   -!- IN VERTEBRATES 3 MAIN GROUPS OF ACTIN ISOFORMS, ALPHA, BETA AND
CC       GAMMA HAVE BEEN IDENTIFIED. THE ALPHA ACTINS ARE FOUND IN MUSCLE
CC       TISSUES AND ARE A MAJOR CONSTITUENT OF THE CONTRACTILE APPARATUS.
CC       THE BETA AND GAMMA ACTINS CO-EXISTS IN MOST CELL TYPES AS
CC       COMPONENTS OF THE CYTOSKELETON AND AS MEDIATORS OF INTERNAL CELL
CC       MOTILITY.
CC   -!- THERE ARE TWO DIFFERENT ALPHA-SKELETAL ACTINS IN FUGU RUBRIPES.
DR   EMBL; U38958; G1335829; -.
DR   PROSITE; PS00406; ACTINS_1; 1.
DR   PROSITE; PS00432; ACTINS_2; 1.
DR   PROSITE; PS01132; ACTINS_ACT_LIKE; 1.
KW   MULTIGENE FAMILY; STRUCTURAL PROTEIN; METHYLATION; MUSCLE PROTEIN;
KW   ACETYLATION.
FT   PROPEP        1      2       REMOVED IN MATURE FORM (BY SIMILARITY).
FT   CHAIN         3    377       ACTIN, ALPHA SKELETAL MUSCLE 2.
FT   MOD_RES       3      3       ACETYLATION (BY SIMILARITY).
FT   MOD_RES      75     75       METHYLATION (BY SIMILARITY).
SQ   SEQUENCE   377 AA;  41977 MW;  BEAD44D3 CRC32;
     MCDDDETTAL VCDNGSGLVK AGFAGDDAPR AVFPSIVGRP RHQGVMVGMG QKDSYVGDEA
     QSKRGILTLK YPIEHGIITN WDDMEKIWHH SFYNELRVAP EEHPTLLTEA PLNPKANREK
     MTQIMFETFN VPAMYVAIQA VLSLYASGRT TGIVLDSGDG VTHNVPIYEG YALPHAIMRL
     DLAGRDLTDY LMKILTERGY SFVTTAEREI VRDIKEKLCY VALDFENEMG TAASSSSLEK
     SYELPDGQVI TIGNERFRCP ETLFQPSFIG MESAGIHETT YNSIMKCDID IRKDLYANNV
     LSGGTTMYPG IADRMQKEIT ALAPSTMKIK IIAPPERKYS VWIGGSILAS LSTFQQMWIS
     KQEYDEAGPS IVHRKCF
//
ID   ACTX_FUGRU     STANDARD;      PRT;   376 AA.
AC   P53483;
DT   01-OCT-1996 (REL. 34, CREATED)
DT   01-OCT-1996 (REL. 34, LAST SEQUENCE UPDATE)
DT   01-OCT-1996 (REL. 34, LAST ANNOTATION UPDATE)
DE   ACTIN, ALPHA ANOMALOUS.
OS   FUGU RUBRIPES (JAPANESE PUFFERFISH) (TAKIFUGU RUBRIPES).
OC   EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; PISCES; GNATHOSTOMATA;
OC   OSTEICHTHYES; ACTINOPTERYGII; TETRAODONTIFORMES.
RN   [1]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 96275651.
RA   VENKATESH B., TAY B.H., ELGAR G., BRENNER S.;
RL   J. MOL. BIOL. 259:655-665(1996).
CC   -!- FUNCTION: ACTINS ARE HIGHLY CONSERVED PROTEINS THAT ARE INVOLVED
CC       IN VARIOUS TYPES OF CELL MOTILITY AND ARE UBIQUITOUSLY EXPRESSED
CC       IN ALL EUKARYOTIC CELLS.
CC   -!- SUBUNIT: POLYMERIZATION OF GLOBULAR ACTIN (G-ACTIN) LEADS TO A
CC       STRUCTURAL FILAMENT (F-ACTIN) IN THE FORM OF A TWO-STRANDED
CC       HELIX. EACH ACTIN CAN BIND TO 4 OTHERS.
CC   -!- SUBCELLULAR LOCATION: CYTOPLASMIC.
CC   -!- TISSUE SPECIFICITY: PREDOMINANTLY EXPRESSED IN TESTIS.
DR   EMBL; U38962; G1335837; -.
DR   PROSITE; PS00432; ACTINS_2; 1.
DR   PROSITE; PS01132; ACTINS_ACT_LIKE; 1.
KW   MULTIGENE FAMILY; STRUCTURAL PROTEIN.
SQ   SEQUENCE   376 AA;  41979 MW;  5B5E44BA CRC32;
     MSDYDETALV CDNGSGLVKA GFAGDDTPRA VFHAIVGRPR HQDDMDDMGK KGYYVGDEAQ
     SKRDILSLKH PIERGIITNW DDMEKIWHHT FYNELCVAPE EHPTLLTEAP LNPKANREKM
     TQIMLETFNM PAMYVSIQAV LSLYASGRTT GIVLDSGEGV THAVPIAEGY ALPPAIMRLN
     LAGRDLTDYL MKILNERGYS FVTTAEREIV RDIKEKLCYV ALDFENEMAT AASSSSLEKR
     YELPDGQVIT IGNERFCCPE TLFQPSFMGM ESAGIHEITH SSIMKCDIEI RKDLYANNVL
     TGGATLFPGI ADRMQKEITA LAPSTMKIQI IAPPERKYSV WIGGSILASL STFQQMWISK
     QEYEEIGPSI IHCKCF
//
ID   ARF3_HUMAN     STANDARD;      PRT;   180 AA.
AC   P16587;
DT   01-AUG-1990 (REL. 15, CREATED)
DT   01-JUN-1994 (REL. 29, LAST SEQUENCE UPDATE)
DT   01-NOV-1997 (REL. 35, LAST ANNOTATION UPDATE)
DE   ADP-RIBOSYLATION FACTOR 3.
GN   ARF3.
OS   HOMO SAPIENS (HUMAN), RATTUS NORVEGICUS (RAT), MUS MUSCULUS (MOUSE),
OS   AND FUGU RUBRIPES (JAPANESE PUFFERFISH) (TAKIFUGU RUBRIPES).
OC   EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; TETRAPODA; MAMMALIA;
OC   EUTHERIA; PRIMATES.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   SPECIES=HUMAN;
RX   MEDLINE; 89345613.
RA   BOBAK D.A., NIGHTINGALE M.S., MURTAGH J.J. JR., PRICE S.R., MOSS J.,
RA   VAUGHAN M.;
RL   PROC. NATL. ACAD. SCI. U.S.A. 86:6101-6105(1989).
RN   [2]
RP   SEQUENCE FROM N.A.
RC   SPECIES=HUMAN;
RX   MEDLINE; 92078170.
RA   TSAI S.C., HAUN R.S., TSUCHIYA M., MOSS J., VAUGHAN M.;
RL   J. BIOL. CHEM. 266:23053-23059(1991).
RN   [3]
RP   SEQUENCE FROM N.A.
RC   SPECIES=RAT; TISSUE=BRAIN;
RA   NIGHTINGALE M.S., PRICE S.R., TSUCHIYA M., MOSS J., VAUGHAN M.;
RL   SUBMITTED (XXX-1994) TO EMBL/GENBANK/DDBJ DATA BANKS.
RN   [4]
RP   SEQUENCE FROM N.A.
RC   SPECIES=MOUSE; STRAIN=ICR; TISSUE=BRAIN;
RX   MEDLINE; 97103475.
RA   HOSAKA M., TODA K., TAKATSU H., TORII S., MURAKAMI K., NAKAYAMA K.;
RL   J. BIOCHEM. 120:813-819(1996).
RN   [5]
RP   SEQUENCE FROM N.A.
RC   SPECIES=F.RUBRIPES;
RA   GELLNER K., BRENNER S.;
RL   SUBMITTED (FEB-1997) TO EMBL/GENBANK/DDBJ DATA BANKS.
CC   -!- FUNCTION: GTP-BINDING PROTEIN THAT FUNCTIONS AS AN ALLOSTERIC
CC       ACTIVATOR OF THE CHOLERA TOXIN CATALYTIC SUBUNIT, AN ADP-
CC       RIBOSYLTRANSFERASE. INVOLVED IN PROTEIN TRAFFICKING; MAY MODULATE
CC       VESICLE BUDDING AND UNCOATING WITHIN THE GOLGI APPARATUS.
CC   -!- SIMILARITY: BELONGS TO THE ARF FAMILY OF GTP-BINDING PROTEINS.
DR   EMBL; M74493; G178160; -.
DR   EMBL; M33384; G178981; -.
DR   EMBL; M74491; G178162; -.
DR   EMBL; L12382; G438866; -.
DR   EMBL; D87900; G1565211; -.
DR   EMBL; U82608; G1814293; -.
DR   PIR; B33283; B33283.
DR   PIR; A41570; A41570.
DR   PIR; B41570; B41570.
DR   MIM; 103190; -.
DR   MGD; MGI:99432; ARF3.
DR   PROSITE; PS01019; ARF; 1.
KW   GTP-BINDING; MULTIGENE FAMILY; MYRISTYLATION; PROTEIN TRANSPORT;
KW   GOLGI STACK.
FT   INIT_MET      0      0       BY SIMILARITY.
FT   LIPID         1      1       MYRISTATE (POTENTIAL).
FT   NP_BIND      23     30       GTP (BY SIMILARITY).
FT   NP_BIND      66     70       GTP (BY SIMILARITY).
FT   NP_BIND     125    128       GTP (BY SIMILARITY).
SQ   SEQUENCE   180 AA;  20469 MW;  307D6BDE CRC32;
     GNIFGNLLKS LIGKKEMRIL MVGLDAAGKT TILYKLKLGE IVTTIPTIGF NVETVEYKNI
     SFTVWDVGGQ DKIRPLWRHY FQNTQGLIFV VDSNDRERVN EAREELMRML AEDELRDAVL
     LVFANKQDLP NAMNAAEITD KLGLHSLRHR NWYIQATCAT SGDGLYEGLD WLANQLKNKK
//
ID   CB1A_FUGRU     STANDARD;      PRT;   468 AA.
AC   Q98894;
DT   01-NOV-1997 (REL. 35, CREATED)
DT   01-NOV-1997 (REL. 35, LAST SEQUENCE UPDATE)
DT   01-NOV-1997 (REL. 35, LAST ANNOTATION UPDATE)
DE   CANNABINOID RECEPTOR TYPE 1A.
GN   CB1A.
OS   FUGU RUBRIPES (JAPANESE PUFFERFISH) (TAKIFUGU RUBRIPES).
OC   EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; PISCES; GNATHOSTOMATA;
OC   OSTEICHTHYES; ACTINOPTERYGII; TETRAODONTIFORMES.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   TISSUE=TESTIS;
RX   MEDLINE; 97001167.
RA   YAMAGUCHI F., MACRAE A., BRENNER S.;
RL   GENOMICS 35:603-605(1996).
CC   -!- FUNCTION: INVOLVED IN CANNABINOID-INDUCED CNS EFFECTS (POTENTIAL).
CC   -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN.
CC   -!- SIMILARITY: BELONGS TO FAMILY 1 OF G-PROTEIN COUPLED RECEPTORS.
DR   EMBL; X94401; E218504; -.
DR   GCRDB; GCR_1110; -.
DR   PROSITE; PS00237; G_PROTEIN_RECEPTOR; 1.
KW   G-PROTEIN COUPLED RECEPTOR; TRANSMEMBRANE; GLYCOPROTEIN.
FT   DOMAIN        1    115       EXTRACELLULAR (POTENTIAL).
FT   TRANSMEM    116    141       1 (POTENTIAL).
FT   DOMAIN      142    153       CYTOPLASMIC (POTENTIAL).
FT   TRANSMEM    154    174       2 (POTENTIAL).
FT   DOMAIN      175    186       EXTRACELLULAR (POTENTIAL).
FT   TRANSMEM    187    211       3 (POTENTIAL).
FT   DOMAIN      212    231       CYTOPLASMIC (POTENTIAL).
FT   TRANSMEM    232    254       4 (POTENTIAL).
FT   DOMAIN      255    272       EXTRACELLULAR (POTENTIAL).
FT   TRANSMEM    273    298       5 (POTENTIAL).
FT   DOMAIN      299    343       CYTOPLASMIC (POTENTIAL).
FT   TRANSMEM    344    364       6 (POTENTIAL).
FT   DOMAIN      365    376       EXTRACELLULAR (POTENTIAL).
FT   TRANSMEM    377    398       7 (POTENTIAL).
FT   DOMAIN      399    468       CYTOPLASMIC (POTENTIAL).
FT   CARBOHYD     78     78       POTENTIAL.
FT   CARBOHYD     87     87       POTENTIAL.
SQ   SEQUENCE   468 AA;  52391 MW;  89244E2C CRC32;
     MKSVLDGVAD TTFRTITSGL QYLGSNDANY DDPLNDAAFK TGFSLQKPLS AFRSNSFPNK
     VPADEELIFK GIPFFPTNST DLFGNRNTTR DENSIQCGEN FMDMECFMIL TPSQQLAVAV
     LSLTLGTFTV LENLVVLCVI FQSRTLRCRP SYHFIGSLAV ADLLGSVIFV YSFLDFHVFH
     KKDSPNVFLF KLGGVTASFT ASVGSLFLTA IDRYISIHRP LAYRRIVTRT KAVIAFCMMW
     TISIIIAVLP LLGWNCKRLN SVCSDIFPLI DENYLMFWIG VTSVLVLFII YAYIYILWKA
     HHHAVRMLSR TSQKSLVVYS AEGTKVQTTR PEQTRMDIRL AKTLVLILAV LVICWGPLLA
     IMVYDLFWKM DDNIKTVFAF CSMLCLLNST VNPIIYALRS RDLRHAFLSS CHACRGSAQQ
     LDNSLESDCQ NRNVNISANR AAESCVKTTV KIAKVTMSVS TETSAEAV
//
ID   CB1B_FUGRU     STANDARD;      PRT;   470 AA.
AC   Q98895;
DT   01-NOV-1997 (REL. 35, CREATED)
DT   01-NOV-1997 (REL. 35, LAST SEQUENCE UPDATE)
DT   01-NOV-1997 (REL. 35, LAST ANNOTATION UPDATE)
DE   CANNABINOID RECEPTOR TYPE 1B.
GN   CB1B.
OS   FUGU RUBRIPES (JAPANESE PUFFERFISH) (TAKIFUGU RUBRIPES).
OC   EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; PISCES; GNATHOSTOMATA;
OC   OSTEICHTHYES; ACTINOPTERYGII; TETRAODONTIFORMES.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   TISSUE=TESTIS;
RX   MEDLINE; 97001167.
RA   YAMAGUCHI F., MACRAE A., BRENNER S.;
RL   GENOMICS 35:603-605(1996).
CC   -!- FUNCTION: INVOLVED IN CANNABINOID-INDUCED CNS EFFECTS (POTENTIAL).
CC   -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN.
CC   -!- SIMILARITY: BELONGS TO FAMILY 1 OF G-PROTEIN COUPLED RECEPTORS.
DR   EMBL; X94402; E218511; -.
DR   GCRDB; GCR_1109; -.
DR   PROSITE; PS00237; G_PROTEIN_RECEPTOR; 1.
KW   G-PROTEIN COUPLED RECEPTOR; TRANSMEMBRANE; GLYCOPROTEIN.
FT   DOMAIN        1    113       EXTRACELLULAR (POTENTIAL).
FT   TRANSMEM    114    139       1 (POTENTIAL).
FT   DOMAIN      140    151       CYTOPLASMIC (POTENTIAL).
FT   TRANSMEM    152    172       2 (POTENTIAL).
FT   DOMAIN      173    184       EXTRACELLULAR (POTENTIAL).
FT   TRANSMEM    185    209       3 (POTENTIAL).
FT   DOMAIN      210    229       CYTOPLASMIC (POTENTIAL).
FT   TRANSMEM    230    252       4 (POTENTIAL).
FT   DOMAIN      253    270       EXTRACELLULAR (POTENTIAL).
FT   TRANSMEM    271    296       5 (POTENTIAL).
FT   DOMAIN      297    341       CYTOPLASMIC (POTENTIAL).
FT   TRANSMEM    342    362       6 (POTENTIAL).
FT   DOMAIN      363    374       EXTRACELLULAR (POTENTIAL).
FT   TRANSMEM    375    396       7 (POTENTIAL).
FT   DOMAIN      397    470       CYTOPLASMIC (POTENTIAL).
FT   CARBOHYD     78     78       POTENTIAL.
FT   CARBOHYD     86     86       POTENTIAL.
SQ   SEQUENCE   470 AA;  52081 MW;  11BCBF0E CRC32;
     MKLALHRIAG ATMAALTTEV QYLGSNDASY EDPQADAALM KSRFNFEKPY SASSSLHRLI
     PGNKELIYGG LSTILPTNAS DFPLSNGSGE ATQCGEDIVD NMECFMILTP AQQLVIVILA
     ITLGTFTVLE NFVVLCVILH SHTLRSRPSY HFIGSLAVAD LIGSIIFVYS FLDFHVLHRK
     DSPSIFLFKL AGVIASFTAS VGSLFLTAID RYVSIHRPMA YKRIITKTKA VIAFSVMWAI
     SIEFSLLPLL GWNCKRLHSV CSDIFPLIDE KYLMFWIGMT TVLLLFIIYA YMFILWKSHH
     HAVRMLSRSS QRSIIVYTSE GTKVQTVRPE QARMDLRLAK TLVLILVALI ICWGPLLAIM
     VYDLFGRVND FIKTVFAFCS MLCLLNSTIN PVIYAMRSKD LRRAFVNICH MCRGTTQSLD
     SSAESDWNSR SVRSTGGRAG KDRSVGGKPQ VKVAQVTVSG VTASSPAEAV
//
ID   CO9_FUGRU      STANDARD;      PRT;   586 AA.
AC   P79755;
DT   01-NOV-1997 (REL. 35, CREATED)
DT   01-NOV-1997 (REL. 35, LAST SEQUENCE UPDATE)
DT   15-JUL-1998 (REL. 36, LAST ANNOTATION UPDATE)
DE   COMPLEMENT COMPONENT C9 PRECURSOR.
GN   C9.
OS   FUGU RUBRIPES (JAPANESE PUFFERFISH) (TAKIFUGU RUBRIPES).
OC   EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; PISCES; GNATHOSTOMATA;
OC   OSTEICHTHYES; ACTINOPTERYGII; TETRAODONTIFORMES.
RN   [1]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 98038993.
RA   YEO G.S.H., ELGAR G., SANDFORD R., BRENNER S.;
RL   GENE 200:203-211(1997).
CC   -!- FUNCTION: C9 IS THE FINAL COMPONENT OF THE COMPLEMENT SYSTEM TO BE
CC       ADDED IN THE ASSEMBLY OF THE MEMBRANE ATTACK COMPLEX. IT IS ABLE
CC       TO ENTER LIPID BILAYERS, FORMING TRANSMEMBRANE CHANNELS (BY
CC       SIMILARITY).
CC   -!- SIMILARITY: TO COMPLEMENT FACTORS C6, C7, C8, AND TO PERFORIN.
CC   -!- SIMILARITY: CONTAINS 2 TYPE-1 TSP REPEATS.
CC   -!- SIMILARITY: CONTAINS 1 EGF-LIKE DOMAIN.
CC   -!- SIMILARITY: CONTAINS 1 LDL-RECEPTOR CLASS A DOMAIN.
DR   EMBL; U87241; G1845349; -.
DR   PROSITE; PS00279; MAC_PERFORIN; 1.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01186; EGF_2; FALSE_NEG.
DR   PROSITE; PS01209; LDLRA_1; 1.
DR   PROSITE; PS50068; LDLRA_2; 1.
KW   COMPLEMENT PATHWAY; COMPLEMENT ALTERNATE PATHWAY; GLYCOPROTEIN;
KW   PLASMA; MEMBRANE ATTACK COMPLEX; CYTOLYSIS; SIGNAL; EGF-LIKE DOMAIN;
KW   REPEAT.
FT   SIGNAL        1     26       POTENTIAL.
FT   CHAIN        27    534       COMPLEMENT COMPONENT C9.
FT   REPEAT       36     93       TYPE-1 TSP 1.
FT   DOMAIN       94    131       LDL-RECEPTOR CLASS A.
FT   DOMAIN      490    524       EGF-LIKE.
FT   REPEAT      540    586       TYPE-1 TSP 2.
FT   DISULFID     96    108       BY SIMILARITY.
FT   DISULFID    103    121       BY SIMILARITY.
FT   DISULFID    115    129       BY SIMILARITY.
FT   DISULFID    363    389       BY SIMILARITY.
FT   DISULFID    494    510       BY SIMILARITY.
FT   DISULFID    497    512       BY SIMILARITY.
FT   DISULFID    514    523       BY SIMILARITY.
FT   CARBOHYD    246    246       POTENTIAL.
FT   CARBOHYD    274    274       POTENTIAL.
FT   CARBOHYD    354    354       POTENTIAL.
FT   CARBOHYD    545    545       POTENTIAL.
SQ   SEQUENCE   586 AA;  65197 MW;  40CEB614 CRC32;
     MRTEAALQLG FCALCVMLAL LGEGMGRELP DPPAVNCVWS RWAPWSSCDP CTNTRRRSRG
     VEVFGQFAGI ACQGSVGDRE YCITNAKCNL PPPRECSDSE FQCESGSCIK LRLKCNGDYD
     CEDGSDEDCE PLRKTCPPTV LDTNEQGRTA GYGINILGAD PRMNPFNNDF FNGRCDKVRN
     PNTLQLDRLP WNIGVLNYQT LVEETASREI YEDSYSLLRE MLKEMSIKVD AGLSFKFKST
     EPSMSNNSLK LDASLEYEKK TMIKDVSELT NIKNKSFMRV KGRLQLSTYR MRSHQLQVAD
     EFVAHVKSLP LEYEKGIYYA FLEDYGTHYT KNGKSGGEYE LVYVLNQDTI KAKNLTERKI
     QECLKIGIEA EFATTSVQDG KAHAKLNKCD DVTTKSQGDV EGKAVVDNVM TSVKGGSLES
     AVTMRAKLNK EGVMDIATYQ NWARTIASAP ALINSEPEPI YMLIPTDIPG ANSRIANLKQ
     ATADYVAEYN VCKCRPCHNG GTLALLDGKC ICMCSNLFEG LGCQNFKGDK ARVPAARPAV
     TQEGNWSCWS SWSNCQGQKR SRTRYCNTEG VLGAECRGEI RSEEYC
//
ID   D1DR_FUGRU     STANDARD;      PRT;   459 AA.
AC   P53452;
DT   01-OCT-1996 (REL. 34, CREATED)
DT   01-OCT-1996 (REL. 34, LAST SEQUENCE UPDATE)
DT   01-OCT-1996 (REL. 34, LAST ANNOTATION UPDATE)
DE   D(1)-LIKE DOPAMINE RECEPTOR.
GN   D14.
OS   FUGU RUBRIPES (JAPANESE PUFFERFISH) (TAKIFUGU RUBRIPES).
OC   EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; PISCES; GNATHOSTOMATA;
OC   OSTEICHTHYES; ACTINOPTERYGII; TETRAODONTIFORMES.
RN   [1]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 95309911.
RA   MACHAE A.D., BRENNER S.;
RL   GENOMICS 25:436-446(1995).
CC   -!- FUNCTION: RECEPTOR FOR DOPAMINE.
CC   -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN.
CC   -!- SIMILARITY: BELONGS TO FAMILY 1 OF G-PROTEIN COUPLED RECEPTORS.
DR   EMBL; X80174; E112837; -.
DR   GCRDB; GCR_1108; -.
DR   PROSITE; PS00237; G_PROTEIN_RECEPTOR; 1.
KW   G-PROTEIN COUPLED RECEPTOR; TRANSMEMBRANE; GLYCOPROTEIN;
KW   MULTIGENE FAMILY.
FT   DOMAIN        1     23       EXTRACELLULAR (POTENTIAL).
FT   TRANSMEM     24     49       1 (POTENTIAL).
FT   DOMAIN       50     60       CYTOPLASMIC (POTENTIAL).
FT   TRANSMEM     61     87       2 (POTENTIAL).
FT   DOMAIN       88     96       EXTRACELLULAR (POTENTIAL).
FT   TRANSMEM     97    119       3 (POTENTIAL).
FT   DOMAIN      120    138       CYTOPLASMIC (POTENTIAL).
FT   TRANSMEM    139    164       4 (POTENTIAL).
FT   DOMAIN      165    191       EXTRACELLULAR (POTENTIAL).
FT   TRANSMEM    192    216       5 (POTENTIAL).
FT   DOMAIN      217    269       CYTOPLASMIC (POTENTIAL).
FT   TRANSMEM    270    297       6 (POTENTIAL).
FT   DOMAIN      298    311       EXTRACELLULAR (POTENTIAL).
FT   TRANSMEM    312    333       7 (POTENTIAL).
FT   DOMAIN      334    459       CYTOPLASMIC (POTENTIAL).
FT   CARBOHYD      4      4       POTENTIAL.
FT   DISULFID     96    187       BY SIMILARITY.
SQ   SEQUENCE   459 AA;  51080 MW;  F2FC7A96 CRC32;
     MAQNFSTVGD GKQMLLERDS SKRVLTGCFL SLLIFTTLLG NTLVCVAVTK FRHLRSKVTN
     FFVISLAISD LLVAILVMPW KAATEIMGFW PFGEFCNIWV AFDIMCSTAS ILNLCVISVD
     RYWAISSPFR YERKMTPKVA CLMISVAWTL SVLISFIPVQ LNWHKAQTAS YVELNGTYAG
     DLPPDNCDSS LNRTYAISSS LISFYIPVAI MIVTYTRIYR IAQKQIRRIS ALERAAESAQ
     NRHSSMGNSL SMESECSFKM SFKRETKVLK TLSVIMGVFV CCWLPFFILN CMVPFCEADD
     TTDFPCISST TFDVFVWFGW ANSSLNPIIY AFNADFRKAF SILLGCHRLC PGNSAIEIVS
     INNTGAPLSN PSCQYQPKSH IPKEGNHSSS YVIPHSILCQ EEELQKKDGF GGEMEVGLVN
     NAMEKVSPAI SGNFDSDAAV TLETINPITQ NGQHKSMSC
//
ID   D2DR_FUGRU     STANDARD;      PRT;   463 AA.
AC   P53453;
DT   01-OCT-1996 (REL. 34, CREATED)
DT   01-OCT-1996 (REL. 34, LAST SEQUENCE UPDATE)
DT   01-OCT-1996 (REL. 34, LAST ANNOTATION UPDATE)
DE   D(2)-LIKE DOPAMINE RECEPTOR.
GN   D215.
OS   FUGU RUBRIPES (JAPANESE PUFFERFISH) (TAKIFUGU RUBRIPES).
OC   EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; PISCES; GNATHOSTOMATA;
OC   OSTEICHTHYES; ACTINOPTERYGII; TETRAODONTIFORMES.
RN   [1]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 95309911.
RA   MACHAE A.D., BRENNER S.;
RL   GENOMICS 25:436-446(1995).
CC   -!- FUNCTION: RECEPTOR FOR DOPAMINE.
CC   -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN.
CC   -!- SIMILARITY: BELONGS TO FAMILY 1 OF G-PROTEIN COUPLED RECEPTORS.
DR   EMBL; X80175; E112838; -.
DR   GCRDB; GCR_1107; -.
DR   PROSITE; PS00237; G_PROTEIN_RECEPTOR; 1.
KW   G-PROTEIN COUPLED RECEPTOR; TRANSMEMBRANE; GLYCOPROTEIN;
KW   MULTIGENE FAMILY.
FT   DOMAIN        1     35       EXTRACELLULAR (POTENTIAL).
FT   TRANSMEM     36     58       1 (POTENTIAL).
FT   DOMAIN       59     69       CYTOPLASMIC (POTENTIAL).
FT   TRANSMEM     70     95       2 (POTENTIAL).
FT   DOMAIN       96    106       EXTRACELLULAR (POTENTIAL).
FT   TRANSMEM    107    128       3 (POTENTIAL).
FT   DOMAIN      129    149       CYTOPLASMIC (POTENTIAL).
FT   TRANSMEM    150    172       4 (POTENTIAL).
FT   DOMAIN      173    187       EXTRACELLULAR (POTENTIAL).
FT   TRANSMEM    188    211       5 (POTENTIAL).
FT   DOMAIN      212    392       CYTOPLASMIC (POTENTIAL).
FT   TRANSMEM    393    416       6 (POTENTIAL).
FT   DOMAIN      417    425       EXTRACELLULAR (POTENTIAL).
FT   TRANSMEM    426    449       7 (POTENTIAL).
FT   DOMAIN      450    463       CYTOPLASMIC (POTENTIAL).
FT   CARBOHYD     10     10       POTENTIAL.
FT   CARBOHYD     16     16       POTENTIAL.
FT   CARBOHYD     22     22       POTENTIAL.
FT   DISULFID    105    183       BY SIMILARITY.
SQ   SEQUENCE   463 AA;  52120 MW;  45C20ABB CRC32;
     MDVFTQYAYN DSIFDNGTWS ANETTKDETH PYNYYAMLLT LLIFVIVFGN VLVCMAVSRE
     KALQTTTNYL IVSLAVADLL VATLVMPWVV YLEVVGEWRF SKIHCDIFVT LDVMMCTASI
     LNLCAISIDR YTAVAMPMLY NTRYSSRRRV TVMISVVWVL SFAISCPLLF GLNNTATRDQ
     SLCFIANPAF VVYSSIVSFY VPFIVTLLVY VQIYVVLRKR RKRVNTKPKQ RLCQAADPDI
     PTSLKDKCTH PEDVRLCTMI VKSNGSFPVN KKKVIFIKDG VNEVEGLELD ELNYCGGSHK
     QPPPQQQPRA LGDTPATSHQ LLMSTKANAS PTSTPPTPPE EGQRTEKNGD PTKEAQGNPA
     PVVALRNGKT QTSLKTLSKR KISQQKEKKA TQMLAIVLGV FIICWLPFFI THILNTHCTR
     CKVPAEMYNA FTWLGYVNSA VNPIIYTTFN VEFRKAFIKI LHC
//
ID   D5DR_FUGRU     STANDARD;      PRT;   463 AA.
AC   P53454;
DT   01-OCT-1996 (REL. 34, CREATED)
DT   01-OCT-1996 (REL. 34, LAST SEQUENCE UPDATE)
DT   01-OCT-1996 (REL. 34, LAST ANNOTATION UPDATE)
DE   D(5)-LIKE DOPAMINE RECEPTOR.
GN   DL.
OS   FUGU RUBRIPES (JAPANESE PUFFERFISH) (TAKIFUGU RUBRIPES).
OC   EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; PISCES; GNATHOSTOMATA;
OC   OSTEICHTHYES; ACTINOPTERYGII; TETRAODONTIFORMES.
RN   [1]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 95309911.
RA   MACHAE A.D., BRENNER S.;
RL   GENOMICS 25:436-446(1995).
CC   -!- FUNCTION: RECEPTOR FOR DOPAMINE.
CC   -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN.
CC   -!- SIMILARITY: BELONGS TO FAMILY 1 OF G-PROTEIN COUPLED RECEPTORS.
DR   EMBL; X80177; E112850; -.
DR   GCRDB; GCR_1105; -.
DR   PROSITE; PS00237; G_PROTEIN_RECEPTOR; 1.
KW   G-PROTEIN COUPLED RECEPTOR; TRANSMEMBRANE; GLYCOPROTEIN;
KW   MULTIGENE FAMILY.
FT   DOMAIN        1     39       EXTRACELLULAR (POTENTIAL).
FT   TRANSMEM     40     65       1 (POTENTIAL).
FT   DOMAIN       66     76       CYTOPLASMIC (POTENTIAL).
FT   TRANSMEM     77    103       2 (POTENTIAL).
FT   DOMAIN      104    112       EXTRACELLULAR (POTENTIAL).
FT   TRANSMEM    113    135       3 (POTENTIAL).
FT   DOMAIN      136    154       CYTOPLASMIC (POTENTIAL).
FT   TRANSMEM    155    180       4 (POTENTIAL).
FT   DOMAIN      181    198       EXTRACELLULAR (POTENTIAL).
FT   TRANSMEM    199    223       5 (POTENTIAL).
FT   DOMAIN      224    273       CYTOPLASMIC (POTENTIAL).
FT   TRANSMEM    274    301       6 (POTENTIAL).
FT   DOMAIN      302    315       EXTRACELLULAR (POTENTIAL).
FT   TRANSMEM    316    337       7 (POTENTIAL).
FT   DOMAIN      338    461       CYTOPLASMIC (POTENTIAL).
FT   CARBOHYD      6      6       POTENTIAL.
FT   DISULFID    112    194       BY SIMILARITY.
SQ   SEQUENCE   463 AA;  51095 MW;  78FE955F CRC32;
     MENFYNETEP TEPRGGVDPL RVVTAAEDVP APVGGVSVRA LTGCVLCALI VSTLLGNTLV
     CAAVIKFRHL RSKVTNAFVV SLAVSDLFVA VLVMPWRAVS EVAGVWLFGR FCDTWVAFDI
     MCSTASILNL CVISMDRYWA ISNPFRYERR MTRRFAFLMI AVAWTLSVLI SFIPVQLNWH
     RADNNSSAHE QGDCNASLNR TYAISSSLIS FYIPVLIMVG TYTRIFRIAQ TQIRRISSLE
     RAAGQRAQNQ SHRASTHDES ALKTSFKRET KVLKTLSVIM GVFVFCWLPF FVLNCVVPFC
     DVDKVGEPPC VSDTTFNIFV WFGWANSSLN PVIYAFNADF RKAFTTILGC SKFCSSSAVQ
     AVDFSNELVS YHHDTTLQKE PVPGPGAHRL VAPLPQNRGD AGPNFDKVSV VSDDSRADRN
     LLLPAILQCD CEAEISLDMV PFGSSGPADS FLIPGQIQDL GDL
//
ID   E2BB_FUGRU     STANDARD;      PRT;   355 AA.
AC   Q90511;
DT   15-JUL-1998 (REL. 36, CREATED)
DT   15-JUL-1998 (REL. 36, LAST SEQUENCE UPDATE)
DT   15-JUL-1998 (REL. 36, LAST ANNOTATION UPDATE)
DE   TRANSLATION INITIATION FACTOR EIF-2B BETA SUBUNIT (EIF-2B GDP-GTP
DE   EXCHANGE FACTOR).
GN   EIF2BB OR S20I15.
OS   FUGU RUBRIPES (JAPANESE PUFFERFISH) (TAKIFUGU RUBRIPES).
OC   EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; PISCES; GNATHOSTOMATA;
OC   OSTEICHTHYES; ACTINOPTERYGII; TETRAODONTIFORMES.
RN   [1]
RP   SEQUENCE FROM N.A.
RA   TROWER M.K., ORTON S.M., PURVIS I.J., SANSEAU P., RILEY J.,
RA   CHRISTODOULOU C., BURT D., SEE C.G., ELGAR G., SHERRINGTON R.,
RA   ROGAEV E.I., ST GEORGE-HYSLOP P., BRENNER S., DYKES C.W.;
RL   SUBMITTED (DEC-1995) TO EMBL/GENBANK/DDBJ DATA BANKS.
CC   -!- FUNCTION: CATALYZES THE EXCHANGE OF EUKARYOTIC INITIATION FACTOR
CC       2-BOUND GDP FOR GTP (BY SIMILARITY).
CC   -!- SUBUNIT: COMPLEX OF FIVE DIFFERENT SUBUNITS; ALPHA, BETA, GAMMA,
CC       DELTA AND EPSILON (BY SIMILARITY).
CC   -!- SIMILARITY: BELONGS TO THE EIF-2B ALPHA/BETA/DELTA SUBUNITS
CC       FAMILY.
DR   EMBL; U40756; G1117954; -.
KW   INITIATION FACTOR; PROTEIN BIOSYNTHESIS.
SQ   SEQUENCE   355 AA;  39129 MW;  A1B2DE8A CRC32;
     MPGADKEVDL TERIEAFLSD LKRGGSGTGP LRGSSETARE TTALLRRITA QARWSSAGDL
     MEIIRKEGRR LIAAQPSETT VGNMIRRVLK IIREEYARSR GSSEEADQQE SLHKLLTSGG
     LSEENFRQHF AALRANVIEA INELLTELEG TTDNIAMQAL EHIHSNEVIM TVGRSRTVEA
     FLKDAARKRK FHVIVAECAP FCQGHKMATS LSTAGIETTV IADAAIFAVM SRVNKVIIGT
     QTVLANGGLR AVNGTHTLAL AAKHHSTPLI VCAPMFKLSP QFPNEEDTFH KFVSPHEVLP
     FTEGEILSKV NVHCPVFDYV PPELITLFIS NIGGHAPSYI YRLMSELYHP EDHEL
//
ID   EM55_FUGRU     STANDARD;      PRT;   467 AA.
AC   P49697;
DT   01-FEB-1996 (REL. 33, CREATED)
DT   01-FEB-1996 (REL. 33, LAST SEQUENCE UPDATE)
DT   01-OCT-1996 (REL. 34, LAST ANNOTATION UPDATE)
DE   55 KD ERYTHROCYTE MEMBRANE PROTEIN (P55).
GN   MPP1.
OS   FUGU RUBRIPES (JAPANESE PUFFERFISH) (TAKIFUGU RUBRIPES).
OC   EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; PISCES; GNATHOSTOMATA;
OC   OSTEICHTHYES; ACTINOPTERYGII; TETRAODONTIFORMES.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   TISSUE=TESTIS;
RX   MEDLINE; 96047329.
RA   ELGAR G.S., RATTRAY F.M., GREYSTRONG J.S., BRENNER S.;
RL   GENOMICS 27:442-446(1995).
CC   -!- SUBCELLULAR LOCATION: MEMBRANE-ASSOCIATED (BY SIMILARITY).
CC   -!- PTM: EXTENSIVELY PALMITOYLATED (BY SIMILARITY).
CC   -!- SIMILARITY: CONTAINS 1 SH3 DOMAIN.
CC   -!- SIMILARITY: CONTAINS A GUANYLATE KINASE-LIKE DOMAIN.
CC   -!- SIMILARITY: MEMBER OF THE MAGUK FAMILY OF CELL JUNCTION PROTEINS.
DR   EMBL; X81359; G608714; -.
DR   PROSITE; PS50002; SH3; 1.
DR   PROSITE; PS00856; GUANYLATE_KINASE_1; 1.
DR   PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
KW   MEMBRANE; ERYTHROCYTE; SH3 DOMAIN; PALMITATE.
FT   DOMAIN      160    230       SH3.
FT   DOMAIN      281    467       GUANYLATE KINASE.
SQ   SEQUENCE   467 AA;  52609 MW;  A62CE2B7 CRC32;
     MTLKSNKNEP ALILDSVTSV RTALSDLYLE QLLQNKPTDK QAAMQTYENK GAEVFSNGSA
     GHINGAELSR MREVAFEKNQ SEPLGVTLKL NDKQRCSVAR ILHGGMIHRQ GSLHEGDEIA
     EINGKSVANQ TVDQLQKILK ETNGVVTMKI IPRPQSRSKP CEMYMRGQFD YDPAMDDLIP
     CKEAGLKFQT GDIIQIINKQ DPNWWQGRVE NNAANFAGLI PSPELQEWRA ASKSKAREGS
     QSCSPFGKKK KCKDKYLAKH SSIFDQLDVI SYEEVVRLPA FKRKTLVLIG APGVGRRHIK
     NVLLTKYPEK FSYPVPHTTR PQRKGDANGE EYFFISNEAM TKCISANELL EYGSFQGYMF
     GTITETIQKI HEQDKIALLD VEPQTMKVLR TADFGPLMVF IAPTDTAAQT ENLQMIQKES
     ETILNTYRQY FDVVLVNNDV NESVKIVEEA LEHATTTPQW VPVSWVY
//
ID   FOS_FUGRU      STANDARD;      PRT;   376 AA.
AC   P53450;
DT   01-OCT-1996 (REL. 34, CREATED)
DT   01-OCT-1996 (REL. 34, LAST SEQUENCE UPDATE)
DT   15-JUL-1998 (REL. 36, LAST ANNOTATION UPDATE)
DE   P55-C-FOS PROTO-ONCOGENE PROTEIN.
GN   FOS.
OS   FUGU RUBRIPES (JAPANESE PUFFERFISH) (TAKIFUGU RUBRIPES).
OC   EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; PISCES; GNATHOSTOMATA;
OC   OSTEICHTHYES; ACTINOPTERYGII; TETRAODONTIFORMES.
RN   [1]
RP   SEQUENCE FROM N.A.
RA   TROWER M.K., ORTON S.M., PURVIS I.J., SANSEAU P., RILEY J.,
RA   CHRISTODOULOU C., BURT D., SEE C.G., ELGAR G., SHERRINGTON R.,
RA   ROGAEV E.I., ST GEORGE-HYSLOP P., BRENNER S., DYKES C.W.;
RL   SUBMITTED (DEC-1995) TO EMBL/GENBANK/DDBJ DATA BANKS.
CC   -!- FUNCTION: C-FOS IS A NUCLEAR PHOSPHOPROTEIN WHICH FORM A TIGHT BUT
CC       NON-COVALENTLY LINKED COMPLEX WITH THE C-JUN/AP-1 TRANSCRIPTION
CC       FACTOR (BY SIMILARITY).
CC   -!- SUBCELLULAR LOCATION: NUCLEAR.
CC   -!- SIMILARITY: TO OTHER BZIP PROTEINS.
DR   EMBL; U40757; G1117956; -.
DR   TRANSFAC; T02205; -.
DR   PROSITE; PS00036; BZIP_BASIC; 1.
KW   PROTO-ONCOGENE; NUCLEAR PROTEIN; PHOSPHORYLATION; DNA-BINDING.
FT   DNA_BIND    123    144       BASIC MOTIF.
FT   DOMAIN      149    177       LEUCINE-ZIPPER.
SQ   SEQUENCE   376 AA;  40826 MW;  FD66FC3F CRC32;
     MMFTSFNAEC DSSSRCSASP VGDNLYYPSP AGSYSSMGSP QSQDFTDLTA SSASFIPTVT
     AISTSPDLQW MVQPLISSVA PSHRAHPYSP SPSYKRTVMR SAASKAHGKR SRVEQTTPEE
     EEKKRIRRER NKQAAAKCRN RRRELTDTLQ AETDQLEDEK SSLQNDIANL LKEKERLEFI
     LAAHQPICKI PSQMDTDFSV VSMSPVHACL STTVSTQLQT SIPEATTVTS SHSTFTSTSN
     SIFSGSSDSL LSTATVSNSV VKMTDLDSSV LEESLDLLAK TEAETARSVP DVNLSNSLFA
     AQDWEPLHAT ISSSDFEPLC TPVVTCTPAC TTLTSSFVFT FPEAETFPTC GVAHRRRSNS
     NDQSSDSLSS PTLLAL
//
ID   G6PD_FUGRU     STANDARD;      PRT;   530 AA.
AC   P54996;
DT   01-OCT-1996 (REL. 34, CREATED)
DT   01-OCT-1996 (REL. 34, LAST SEQUENCE UPDATE)
DT   01-OCT-1996 (REL. 34, LAST ANNOTATION UPDATE)
DE   GLUCOSE-6-PHOSPHATE 1-DEHYDROGENASE (EC 1.1.1.49) (G6PD).
GN   G6PD.
OS   FUGU RUBRIPES (JAPANESE PUFFERFISH) (TAKIFUGU RUBRIPES).
OC   EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; PISCES; GNATHOSTOMATA;
OC   OSTEICHTHYES; ACTINOPTERYGII; TETRAODONTIFORMES.
RN   [1]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 95331796.
RA   MASON P.J., STEVENS D.J., LUZZATTO L., BRENNER S., APARICIO S.;
RL   GENOMICS 26:587-591(1995).
CC   -!- CATALYTIC ACTIVITY: D-GLUCOSE 6-PHOSPHATE + NADP(+) = D-GLUCONO-
CC       DELTA-LACTONE 6-PHOSPHATE + NADPH.
CC   -!- PATHWAY: FIRST STEP IN PENTOSE PHOSPHATE PATHWAY.
DR   EMBL; X83611; -; NOT_ANNOTATED_CDS.
DR   PROSITE; PS00069; G6P_DEHYDROGENASE; 1.
KW   OXIDOREDUCTASE; NADP; GLUCOSE METABOLISM.
FT   ACT_SITE    220    220       BY SIMILARITY.
SQ   SEQUENCE   530 AA;  60469 MW;  C7E663F9 CRC32;
     MMIILFNCFF CASFREDGQH PTVSLGGVWG AAKELHEDKE FHQSDVHVFI IMGASGDLAK
     KKIYPTLWWL FRDGLLPEQT YFVGFARSAL TVDAIRTSCM PYLKVTETES DRLSAFFSRN
     SYISGNYTAG GSFSELNAHI MSLPGASDAN RLFYLALPPT IYHSVTENIK HFCMSAKGWN
     RVIVEKPFGH DLQSSEELST HLSSLFTEDQ IYRIDHYLGK EMVQNLMVLR FGNRIFGPIW
     NRDNVACVVL TFKEPFGTQG RGGYFDDFGI IRDVMQNHML QMLCLVAMEK PASTNSDDVR
     DEKVKVLKCI VPASMSDVVL GQYVGDPEGE GDAKLGYLDD PTVPKGSTQA TFATVVLYVH
     NERWDGVPFI LRCGKALNER KAEVRLQFTD VPGDIFRNQC YRNELVVRVQ PNEAIYAKMM
     SKKPGVYFTP EETELDLTYK SRYKDVKLPD AYERLILDVF CGSQMHFVAS DELREAWRIF
     TPLLHQIEKE KPKPIPYKYG SRGPAEADEL EKRVGFRYEG TYKWVNPHRL
//
ID   HD_FUGRU       STANDARD;      PRT;  3148 AA.
AC   P51112;
DT   01-OCT-1996 (REL. 34, CREATED)
DT   01-OCT-1996 (REL. 34, LAST SEQUENCE UPDATE)
DT   01-OCT-1996 (REL. 34, LAST ANNOTATION UPDATE)
DE   HUNTINGTIN (HUNTINGTON'S DISEASE PROTEIN HOMOLOG) (HD PROTEIN).
GN   HD.
OS   FUGU RUBRIPES (JAPANESE PUFFERFISH) (TAKIFUGU RUBRIPES).
OC   EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; PISCES; GNATHOSTOMATA;
OC   OSTEICHTHYES; ACTINOPTERYGII; TETRAODONTIFORMES.
RN   [1]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 95375788.
RA   BAXENDALE S., ABDULLA S., ELGAR G., BUCK D., BERKS M., MICKLEM G.,
RA   DURBIN R., BATES G., BRENNER S., BECK S., LEHRACH H.;
RL   NAT. GENET. 10:67-76(1995).
CC   -!- FUNCTION: MAY PLAY A ROLE IN MICROTUBULE-MEDIATED TRANSPORT OR
CC       VESICLE FUNCTION.
CC   -!- SUBCELLULAR LOCATION: CYTOPLASMIC (BY SIMILARITY).
CC   -!- POLYMORPHISM: THE POLY-GLN REGION (FOUR RESIDUES) DOES NOT APPEAR
CC       TO BE POLYMORPHIC, EXPLAINING THE ABSENCE OF A HD-LIKE DISORDER.
CC   -!- SIMILARITY: WITH MAMMALIAN HUNGTINTINS.
DR   EMBL; X82939; G804981; -.
KW   REPEAT.
FT   DOMAIN       18     21       POLY-GLN.
FT   DOMAIN      679    682       POLY-ALA.
FT   DOMAIN     1104   1108       POLY-SER.
SQ   SEQUENCE   3148 AA;  348932 MW;  CBB3AA6A CRC32;
     MATMEKLMKA FESLKSFQQQ QGPPTAEEIV QRQKKEQATT KKDRVSHCLT ICENIVAQSL
     RTSPEFQKLL GIAMEMFLLC SDDSESDVRM VADECLNRII KALMDSNLPR LQLELYKEIK
     KNGASRSLRA ALWRFAELAH LIRPQKCRPY LVNLLPCLTR ITKRQEETIQ ETLAAAMPKI
     MAALGHFAND GEIKMLLKSF VANLKSSSPT IRRTAASSAV SVCQHSRRTS YFYTWLLNVL
     LGLLVPVDEE HHSHLILGVL LTLRYLMPLL QQQVNTISLK GSFGVMQKEA DVQPAPEQLL
     QVYELTLHYT QHWDHNVVTA ALELLQQTLR TPPPELLHVL ITAGSIQHAS VFRQDIESRA
     RSGSILELIA GGGSTCSPLL HRKHRGKMLS GEEDALEDDP EKTDVTTGYF TAVGADNSSA
     AQVDIITQQP RSSQHTIQPG DSVDLSASSE QGGRGGGASA SDTPESPNDE EDMLSRSSSC
     GANITPETVE DATPENPAQE GRPVGGSGAY DHSLPPSDSS QTTTEGPDSA VTPSDVAELV
     LDGSESQYSG MQIGTLQDEE DEGTATSSQE DPPDPFLRSA LALSKPHLFE SRGHNRQGSD
     SSVDRFIPKD EPPEPEPDNK MSRIKGAIGH YTDRGAEPVV HCVRLLSASF LLTGQKNGLT
     PDRDVRVSVK ALAVSCVGAA AALHPEAFFN SLYLEPLDGL RAEEQQYISD VLGFIDHGDP
     QIRGATAILC AAIIQAALSK MRYNIHSWLA SVQSKTGNPL SLVDLVPLLQ KALKDESSVT
     CKMACSAVRH CIMSLCGSTL SELGLRLVVD LFALKDSSYW LVRTELLETL AEMDFRLVNF
     LERKSEALHK GEHHYTGRLR LQERVLNDVV IQLLGDDDPR VRHVAASAVS RLVSRLFFDC
     DQGQADPVVA IARDQSSVYL QLLMHETQPP SQLTVSTITR TYRGFNLSNN VADVTVENNL
     SRVVTAVSHA FTSSTSRALT FGCCEALCLL AVHFPICTWT TGWHCGHISS QSSFSSRVGR
     SRGRTLSVSQ SGSTPASSTT SSAVDPERRT LTVGTANMVL SLLSSAWFPL DLSAHQDALL
     LCGNLLAAVA PKCLRNPWAG EDDSSSSSTN TSGGTHKMEE PWAALSDRAF VAMVEQLFSH
     LLKVLNICAH VLDDTPPGPP VKATLPSLTN TPSLSPIRRK GKDKDAVDSS SAPLSPKKGN
     EANTGRPTES TGSTAVHKST TLGSFYHLPP YLKLYDVLKA THANFKVMLD LHSNQEKFGS
     FLRAALDVLS QLLELATLND INKCVEEILG YLKSCFSREP TMATVCVQQL LKTLFGTNLA
     SQYEGFLSGP SRSQGKALRL GSSSLRPGLY HYCFMAPYTH FTQALADASL RNMVQAEHEQ
     DTSGWFDVMQ KTSNQLRSNI ANAARHRGDK NAIHNHIRLF EPLVIKALKQ YTTSTSVALQ
     RQVLDLLAQL VQLRVNYCLL DSDQVFIGFV LKQFEYIEVG QFRDSEAIIP NIFFFLVLLS
     YERYHSKQII SIPKIIQLCD GIMASGRKAV THAIPALQPI VHDLFVLRGS NKADAGKELE
     TQKEVVVSML LRLVQYHQVL EMFILVLQQC HKENEDKWKR LSRQIADVIL PMIAKQQMHL
     DSPEALGVLN TLFETVAPSS LRPVDMLLKS MFTTPVTMAS VATVQLWVSG ILAVLRVLVS
     QSTEDIVLSR IHELSLSPHL LSCHTIKRLQ QPNLSPSDQP AGDGQQNQEP NGEAQKSLPE
     ETFARFLIQL VGVLLDDISS RHVKVDITEQ QHTFYCQQLG TLLMCLIHVF KSGMFRRITV
     AASRLLKGES GSGHSGIEFY PLEGLNSMVH CLITTHPSLV LLWCQVLLII DYTNYSWWTE
     VHQTPKGHSL SCTKLLSPHS SGEGEEKPET RLAMINREIV RRGALILFCD YVCQNLHDSE
     HLTWLIVNHV RDLIDLSHEP PVQDFISAVH RNSAASGLFI QAIQSRCDNL NSPTMLKKTL
     QCLEGIHLSQ SGSLLMLYVD KLLSTPFRVL ARMVDTLACR RVEMLLAETL QNSVAQLPLE
     ELHRIQEYLQ TSGLAQRHQR FYSLLDRFRA TVSDTSSPST PVTSHPLDGD PPPAPELVIA
     DKEWYVALVK SQCCLHGDVS LLETTELLTK LPPADLLSVM SCKEFNLSLL CPCLSLGVQR
     LLRGQGSLLL ETALQVTLEQ LAGATGLLPV PHHSFIPTSH PQSHWKQLAE VYGDPGFYSR
     VLSLCRALSQ YLLTVKQLPS SLRIPSDKEH LITTFTCAAT EVVVWHLLQD QLPLSVDLQW
     ALSCLCLALQ QPCVWNKLST PEYNTHTCSL IYCLHHIILA VAVSPGDQLL HPERKKTKAL
     RHSDDEDQVD SVHDNHTLEW QACEIMAELV EGLQSVLSLG HHRNTAFPAF LTPTLRNIII
     SLSRLPLVNS HTRVPPLVWK LGWSPQPGGE FGTTLPEIPV DFLQEKDVFR EFLYRINTLG
     WSNRTQFEET WATLLGVLVT QPITMDQEEE TQQEEDLERT QLNVLAVQAI TSLVLSAMTL
     PTAGNPAVSC LEQQPRNKSL KALETRFGRK LAVIRGEVER EIQALVSKRD NVHTYHPYHA
     WDPVPSLSAA SPGTLISHEK LLLQINTERE LGNMDYKLGQ VSIHSVWLGN NITPLREEEW
     GEDEDDEADP PAPTSPPLSP INSRKHRAGV DIHSCSQFLL ELYSQWVIPG SPSNRKTPTI
     LISEVVRSLL AVSDLFTERN QFDMMFSTLM ELQKLHPPED EILNQYLVPA ICKAAAVLGM
     DKAIAEPVCR LLETTLRSTH LPSRMGALHG VLYVLECDLL DDTAKQLIPT VSEYLLSNLR
     AIAHCVNLHN QQHVLVMCAV AFYMMENYPL DVGTEFMAGI IQLCGVMVSA SEDSTPSIIY
     HCVLRGLERL LLSEQLSRVD GEALVKLSVD RVNMPSPHRA MAALGLMLTC MYTGKEKASP
     AARSAHSDPQ VPDSESIIVA MERVSVLFDR IRKGLPSEAR VVARILPQFL DDFFPPQDIM
     NKVIGEFLSN QQPYPQFMAT VVYKVFQTLH ATGQSSMVRD WVLLSLSNFT QRTPVAMAMW
     SLSCFFVSAS TSQWISALLP HVISRMGSSD VVDVNLFCLV AMDFYRHQID EELDRRAFQS
     VFETVASPGS PYFQLLACLQ SIHQDKSL
//
ID   HIRA_FUGRU     STANDARD;      PRT;  1025 AA.
AC   O42611;
DT   15-JUL-1998 (REL. 36, CREATED)
DT   15-JUL-1998 (REL. 36, LAST SEQUENCE UPDATE)
DT   15-JUL-1998 (REL. 36, LAST ANNOTATION UPDATE)
DE   HIRA PROTEIN (TUP1 LIKE ENHANCER OF SPLIT PROTEIN 1).
GN   TUPLE1 OR HIRA.
OS   FUGU RUBRIPES (JAPANESE PUFFERFISH) (TAKIFUGU RUBRIPES).
OC   EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; PISCES; GNATHOSTOMATA;
OC   OSTEICHTHYES; ACTINOPTERYGII; TETRAODONTIFORMES.
RN   [1]
RP   SEQUENCE FROM N.A.
RA   PRITCHARD M.A., LLEVADOT R., SCAMBLER P., ESTIVILL X.;
RL   SUBMITTED (MAR-1997) TO EMBL/GENBANK/DDBJ DATA BANKS.
CC   -!- FUNCTION: COULD PLAY A PART IN MECHANISMS OF TRANSCRIPTIONAL
CC       REGULATION SIMILAR TO THAT PLAYED BY YEAST HIR1 AND HIR2 TOGETHER.
CC   -!- SUBCELLULAR LOCATION: NUCLEAR (POTENTIAL).
CC   -!- SIMILARITY: CONTAINS 4 WD REPEATS (TRP-ASP DOMAINS).
CC   -!- SIMILARITY: BELONGS TO THE HIR1 FAMILY OF WD-REPEAT PROTEINS.
DR   EMBL; U94325; G2352036; -.
DR   EMBL; U94324; G2352031; -.
DR   PROSITE; PS00678; WD_REPEATS; 1.
KW   TRANSCRIPTION REGULATION; REPEAT; WD REPEAT; NUCLEAR PROTEIN.
FT   REPEAT       68     98       WD1.
FT   REPEAT      129    159       WD2.
FT   REPEAT      172    202       WD3.
FT   REPEAT      266    313       WD4.
FT   DOMAIN      673    682       POLY-ALA.
FT   DOMAIN      685    688       POLY-ALA.
SQ   SEQUENCE   1025 AA;  111856 MW;  D0BB14BF CRC32;
     MKLLKPSWVS HNGKPIFSVD IHPDGTKFAT GGQGEDSGKV MIWNMAPVLK EEDEKNENVP
     KMLCQMDNHL ACVNCVRWSN NGLYLASGGD DKLVMVWKRA ALIGPSTVFG SSNKLANVEQ
     WRCVTILRNH TGDVMDVSWS PHDVWLASCS VDNTIVIWNA RKFPEMVTCL RGHTGLVKGL
     TWDPVGKYIA SQADDHSLRV WRTVDWQMEA NITKPFSECG GTTHVLRLSW SPDGQYLVSA
     HAMNNSGPTA QIVERDGWRT NMDFVGHRKA VTVVKFNPKI FKKKQKNGGS PKPSCPYCCC
     AVGSKDRSLS VWLTSLKRPL VVIHDLFDKS IMDISWTLTG LGMLVCSMDG TVAYLDFSLD
     ELGDPLSEEE KNSIHQNIYG KSLAITNTEP QLSTTIIENP EMLKYQQERR NSTQANSGPG
     ATGSESATPK LNSVMNGESL EDIRKNLLKK QVETRTPDGR RRITPLCIAQ LDTGDFSPAL
     FNSAPILPSG SSMSNQLTSQ LSSDSSPGQA PPLGLRPSQD PMLISPPPSS AAKVLEDNKD
     GVKSCLLLTS ASKIEPMKAL DSRFTERSKA TPGATAAIAS STGLTPSERP KESTPMQKDV
     KSKEDTSSDS EDKMATINKN LAFNKRKPEL LMDGAEVVEK RKKGRPRKDK MAASIAQPLT
     QTTSPAEREP SRAAAAGAGA AAPTAAAALK LPTPSIKKAF TLQVSMDPSV VLEVENEVSV
     VAGSRLSQLR CSRDGRDWNT LLPSSVLTAA GSSDVVAVAS QDRMLSVFSS CGRRLLPAIQ
     LATPASALHC SAHFVMVLTS GATLSVWDVH KQKALVKNES LLTILSGAAV TVSQSMLTQQ
     GVPVVGLSNG KSYCFSLSLE TWTLIADTAD SLVQCADFRN CLPNQDAPMS SGPLAAMQGR
     NFNAGRLASR LSSTPHHLQQ SMTLAFLENQ LASALTLQSA QEYRYWLLIY ARFLVNEGSE
     YRLRELCKEL LGPVHKSATT SWEPTTLGLR KRDLLREVLP VVGENLRFQR LFTEYQDQLE
     LLRNK
//
ID   RS24_FUGRU     STANDARD;      PRT;   132 AA.
AC   O42387;
DT   15-JUL-1998 (REL. 36, CREATED)
DT   15-JUL-1998 (REL. 36, LAST SEQUENCE UPDATE)
DT   15-JUL-1998 (REL. 36, LAST ANNOTATION UPDATE)
DE   40S RIBOSOMAL PROTEIN S24.
GN   RPS24.
OS   FUGU RUBRIPES (JAPANESE PUFFERFISH) (TAKIFUGU RUBRIPES).
OC   EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; PISCES; GNATHOSTOMATA;
OC   OSTEICHTHYES; ACTINOPTERYGII; TETRAODONTIFORMES.
RN   [1]
RP   SEQUENCE FROM N.A.
RA   CROSIO C., CECCONI F., GIORGI M., AMALDI F., MARIOTTINI P.;
RL   SUBMITTED (SEP-1997) TO EMBL/GENBANK/DDBJ DATA BANKS.
CC   -!- SIMILARITY: BELONGS TO THE S24E FAMILY OF RIBOSOMAL PROTEINS.
DR   EMBL; AJ001398; E339629; -.
DR   PROSITE; PS00529; RIBOSOMAL_S24E; 1.
KW   RIBOSOMAL PROTEIN.
SQ   SEQUENCE   132 AA;  15305 MW;  BCF9EB31 CRC32;
     MNDTVTVRTR KFMTNRLLQR KQMVVDVLHP GKATVPKTEI REKLAKMYKT TPDVVFVFGF
     RTQFGGGKTT GFAMVYDSLD YAKKNEPKHR LARHGLFEKK KTSRKQRKER KNRMKKVRGT
     KKASVGASKK KD
//
ID   RS7_FUGRU      STANDARD;      PRT;   194 AA.
AC   P50894; P53548;
DT   01-OCT-1996 (REL. 34, CREATED)
DT   01-OCT-1996 (REL. 34, LAST SEQUENCE UPDATE)
DT   01-OCT-1996 (REL. 34, LAST ANNOTATION UPDATE)
DE   40S RIBOSOMAL PROTEIN S7.
GN   RPS7.
OS   FUGU RUBRIPES (JAPANESE PUFFERFISH) (TAKIFUGU RUBRIPES).
OC   EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; PISCES; GNATHOSTOMATA;
OC   OSTEICHTHYES; ACTINOPTERYGII; TETRAODONTIFORMES.
RN   [1]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 96371061.
RA   CECCONI F., CROSIO C., MARIOTTINI P., CESARENI G., GIORGI M.,
RA   BRENNER S., AMALDI F.;
RL   NUCLEIC ACIDS RES. 24:3167-3172(1996).
CC   -!- SIMILARITY: BELONGS TO THE S7E FAMILY OF RIBOSOMAL PROTEINS.
DR   EMBL; X94942; E218449; -.
DR   PROSITE; PS00948; RIBOSOMAL_S7E; 1.
KW   RIBOSOMAL PROTEIN.
FT   DOMAIN       98    120       ARG/LYS-RICH (BASIC).
SQ   SEQUENCE   194 AA;  22206 MW;  211C8529 CRC32;
     MFSTSAKIVK PNGEKPDEFE SGISQALLEL EMNSDLKAQL RELNITAAKE IEVGGSRKAI
     IIFVPVPQLK SFQKIQVRLV RELEKKFSGK HVVFIAQRRI LPKPTRKSRS KNKQKRPRSR
     TLTSVHDAIL EDLVFPSEIV GKRIRVKMDS SRLIKVHLDK AQQNNVEHKV ETFSGVYKKL
     TGKDVVFEFP EFQL
//
ID   SSRL_FUGRU     STANDARD;      PRT;   289 AA.
AC   O42179;
DT   15-JUL-1998 (REL. 36, CREATED)
DT   15-JUL-1998 (REL. 36, LAST SEQUENCE UPDATE)
DT   15-JUL-1998 (REL. 36, LAST ANNOTATION UPDATE)
DE   SOMATOSTATIN-LIKE RECEPTOR F_48D10.1.
GN   F_48D10.1.
OS   FUGU RUBRIPES (JAPANESE PUFFERFISH) (TAKIFUGU RUBRIPES).
OC   EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; PISCES; GNATHOSTOMATA;
OC   OSTEICHTHYES; ACTINOPTERYGII; TETRAODONTIFORMES.
RN   [1]
RP   SEQUENCE FROM N.A.
RA   HAWKINS J., GILLAM B.;
RL   SUBMITTED (NOV-1997) TO EMBL/GENBANK/DDBJ DATA BANKS.
CC   -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (BY SIMILARITY).
CC   -!- SIMILARITY: BELONGS TO FAMILY 1 OF G-PROTEIN COUPLED RECEPTORS.
CC   -!- CAUTION: SEEMS TO LACK THE C-TERMINAL PART (TM6 AND TM7).
DR   EMBL; AF013613; G2627438; -.
DR   GCRDB; GCR_2560; -.
DR   PROSITE; PS00237; G_PROTEIN_RECEPTOR; 1.
KW   G-PROTEIN COUPLED RECEPTOR; TRANSMEMBRANE; GLYCOPROTEIN.
FT   DOMAIN        1     57       EXTRACELLULAR (POTENTIAL).
FT   TRANSMEM     58     79       1 (POTENTIAL).
FT   DOMAIN       80     89       CYTOPLASMIC (POTENTIAL).
FT   TRANSMEM     90    110       2 (POTENTIAL).
FT   DOMAIN      111    126       EXTRACELLULAR (POTENTIAL).
FT   TRANSMEM    127    148       3 (POTENTIAL).
FT   DOMAIN      149    170       CYTOPLASMIC (POTENTIAL).
FT   TRANSMEM    171    191       4 (POTENTIAL).
FT   DOMAIN      192    240       EXTRACELLULAR (POTENTIAL).
FT   TRANSMEM    241    261       5 (POTENTIAL).
FT   DOMAIN      262    289       CYTOPLASMIC (POTENTIAL).
FT   CARBOHYD     40     40       POTENTIAL.
FT   DISULFID    125    221       BY SIMILARITY.
SQ   SEQUENCE   289 AA;  32172 MW;  8CB90770 CRC32;
     MEPLDQTPGF PLSPEPNYWY ETTPSLLLVS YPHLLDISSN QSTQSVPFQG SSALLTAVIY
     ITVFVVGLTG NTLAIYVVLR YAGMKTVTNI YILNLAVADE LYIVGLPFLA TQNVLSYWPF
     GSFLCRVVMT ADSMNQFTSI FCLTVMSIDR YLAVVHPIRS TKWRHPRVAK VVSAAVWAVS
     FVVVLPVVIF SDVQVRPSRP LQVGTSSKCL VKRVQETFNS CNMIWPEPKN VWSTAFILYT
     AMVGFFGPLL IICLCYLLIV IKVRHRMSAA QVGAVVSTCP LNICCLSRR
//
ID   SYH_FUGRU      STANDARD;      PRT;   519 AA.
AC   P70076;
DT   01-NOV-1997 (REL. 35, CREATED)
DT   01-NOV-1997 (REL. 35, LAST SEQUENCE UPDATE)
DT   01-NOV-1997 (REL. 35, LAST ANNOTATION UPDATE)
DE   HISTIDYL-TRNA SYNTHETASE (EC 6.1.1.21) (HISTIDINE--TRNA LIGASE)
DE   (HISRS).
GN   HARS OR HISS.
OS   FUGU RUBRIPES (JAPANESE PUFFERFISH) (TAKIFUGU RUBRIPES).
OC   EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; PISCES; GNATHOSTOMATA;
OC   OSTEICHTHYES; ACTINOPTERYGII; TETRAODONTIFORMES.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   TISSUE=TESTIS;
RX   MEDLINE; 96323249.
RA   BRENNER S., CORROCHANO L.M.;
RL   PROC. NATL. ACAD. SCI. U.S.A. 93:8485-8489(1996).
CC   -!- CATALYTIC ACTIVITY: ATP + L-HISTIDINE + TRNA(HIS) = AMP +
CC       PYROPHOSPHATE + L-HISTIDYL-TRNA(HIS).
CC   -!- SUBCELLULAR LOCATION: CYTOPLASMIC.
CC   -!- SIMILARITY: BELONGS TO CLASS-II AMINOACYL-TRNA SYNTHETASE FAMILY.
DR   EMBL; Z54243; E199401; -.
DR   PROSITE; PS00179; AA_TRNA_LIGASE_II_1; 1.
DR   PROSITE; PS00339; AA_TRNA_LIGASE_II_2; 1.
KW   AMINOACYL-TRNA SYNTHETASE; PROTEIN BIOSYNTHESIS; LIGASE; ATP-BINDING.
SQ   SEQUENCE   519 AA;  57913 MW;  E81FDE18 CRC32;
     MLAMHCARVC SVLMGCRTTT RALSIRSFPG VTLAQIDEEV AKLLELKAHL GGDDGKHQFV
     LKTAKGTRDY NPKQMAIREK VFNTIVSCFK RHGAETIDTP VFELKETLTG KYGEDSKLIY
     DLKDQGGELL SLRYDLTVPF ARYLAMNKIT NIKRYHIAKV YRRDNPAMTR GRYREFYQCD
     FDIAGQYDAM IPDAECLKIV HEILSELDLG DFRIKVNDRR ILDGMFAVCG VPDNMFRTIC
     STVDKLDKLP WEAVKNEMVN EKGLSEEAAD QIGVYVGMQG GMDLAERLLQ DQKMCQSTQA
     CAGLTDIKLL FSYLQLFQVT DKVVFDLSLA RGLDYYTGII YEAILTQAGV APVAPETSNE
     APTEECVTVG SVAGGGRYDG LVGMFDPKGR KVPCVGVSIG IERIFSIMEQ KAEASTEKIR
     TTEVQVMVAA AQKNLLEERL RLITELWNAG IKAELMYKKS PKLLSQLQHC EESGIPLVAI
     LGEQELKNGV VKLRNVATRD EVDISRADLI AEIKKRTSA
//
ID   SYV_FUGRU      STANDARD;      PRT;  1217 AA.
AC   P49696;
DT   01-FEB-1996 (REL. 33, CREATED)
DT   01-FEB-1996 (REL. 33, LAST SEQUENCE UPDATE)
DT   01-FEB-1996 (REL. 33, LAST ANNOTATION UPDATE)
DE   VALYL-TRNA SYNTHETASE (EC 6.1.1.9) (VALINE--TRNA LIGASE) (VALRS).
GN   VARS1.
OS   FUGU RUBRIPES (JAPANESE PUFFERFISH) (TAKIFUGU RUBRIPES).
OC   EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; PISCES; GNATHOSTOMATA;
OC   OSTEICHTHYES; ACTINOPTERYGII; TETRAODONTIFORMES.
RN   [1]
RP   SEQUENCE FROM N.A.
RA   LIM E.H., BRENNER S.;
RL   SUBMITTED (SEP-1995) TO EMBL/GENBANK/DDBJ DATA BANKS.
CC   -!- CATALYTIC ACTIVITY: ATP + L-VALINE + TRNA(VAL) = AMP +
CC       PYROPHOSPHATE + L-VALYL-TRNA(VAL).
CC   -!- SIMILARITY: BELONGS TO CLASS-I AMINOACYL-TRNA SYNTHETASE FAMILY.
CC   -!- SIMILARITY: THE N-TERMINAL DOMAIN IS SIMILAR TO ELONGATION
CC       FACTOR 1-GAMMA.
DR   EMBL; X91856; G1041396; -.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
KW   AMINOACYL-TRNA SYNTHETASE; PROTEIN BIOSYNTHESIS; LIGASE; ATP-BINDING.
FT   DOMAIN        1   ?320       EF-1-GAMMA LIKE.
FT   SIMILAR     293    303       "HIGH" REGION.
FT   SIMILAR     809    813       "KMSKS" REGION.
FT   BINDING     812    812       ATP (BY SIMILARITY).
SQ   SEQUENCE   1217 AA;  138218 MW;  EABA1113 CRC32;
     MATLYVSPHL DDFRSLLALV AAEYCGNAKQ QSQVWQWLSF ADNELTPVSC AVVFPLMGMT
     GLDKKIQQNS RVELMRVLKV LDQALEPRTF LVGESITLAD MAVAMAVLLP FKYVLEPSDR
     NVLMNVTRWF TTCINQPEFL KVLGKISLCE KMVPVTAKTS TEEAAAVHPD AAALNGPPKT
     EAQLKKEAKK REKLEKFQQK KEMEAKKKMQ PVAEKKAKPE KRELGVITYD IPTPSGEKKD
     VVSPLPDSYS PQYVEAAWYP WWEKQGFFKP EFGRKSIGEQ NPRGIFMMCI PPPNVTGSLH
     LGHALTNAIQ DTLTRWHRMR GETTLWNPGC DHAGIATQVV VEKKLMREKG TSRHDLGREK
     FIEEVWKWKN EKGDRIYHQL KKLGSSLDWD RACFTMDPKL SYAVQEAFIR MHDEGVIYRS
     KRLVNWSCSL NSAISDIEVD KNELSGRTLL PVPGYKEKVE FGVLVSFAYK VDGSDEEVVV
     ATTRIETMLG DTAVAVHPSD SRYQHLKGKT VLHPFCDRKI PVVFDDFVDM SFGTGAVKIT
     PAHDHNDYEV GVRHNLAFIN ILDENGFVIN VPPPFLGMKR FDARKAVLQA LKDRDQFKEI
     KDNPMVVPVC SRSKDIVEPL MKPQWYVSCS DMGKQAADAV REGRLKIIPD HHSQTWFNWM
     DNIRDWCISR QLWWGHRIPA YFITVSDPSV KPGEDMDGHY RVSGRTPEEA REKAAKRFNV
     SPDKIALRQD EDVLDTWFSS GINPFSILGW PNETEDLNVF YPGTLLETGH DILFFWVARM
     VMMGLKLTGK LPFKEVYHCA VVRDAHGRKM SKSLGNVIDP LDDHIGIALE GLHAQLMDTN
     LDPLEVEKPK KVQKADYPNC IPECGTDALR FALCAYTSQG RDINLDVNRI LGYRHFCNKL
     WNAVKFAMRT LGDQFVPADT SPAEREESVS DRWILSRLST AVAQCDAAFR TYDFPAITTA
     IYNFWLYELC DVYLESVKPV FIKAKEDGSC ERPAAVCRQT LYTCLEVGLR LLAPLMPFVT
     EELYQRLPRR RPQSDPPSIC VTPYPDAAEF CWQCEDVDRD IDFIMGVVRT IRSLRSDYKL
     TKTAADCYLQ CTDAATVSLV QKYSLQIQTL SYSQAIVPLM APQPAPEGCA VAIASDRCTV
     NMMLKGLIDV EKEVPKLMGK KTDLEKQIEK LSEKISKGDY KEKVPVKVQE QDTEKLRQSQ
     TELEKVKEAM DNFQKMM
//
ID   TCPD_FUGRU     STANDARD;      PRT;   536 AA.
AC   P53451;
DT   01-OCT-1996 (REL. 34, CREATED)
DT   01-OCT-1996 (REL. 34, LAST SEQUENCE UPDATE)
DT   01-OCT-1996 (REL. 34, LAST ANNOTATION UPDATE)
DE   T-COMPLEX PROTEIN 1, DELTA SUBUNIT (TCP-1-DELTA) (CCT-DELTA).
GN   CCT4 OR CCTD.
OS   FUGU RUBRIPES (JAPANESE PUFFERFISH) (TAKIFUGU RUBRIPES).
OC   EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; PISCES; GNATHOSTOMATA;
OC   OSTEICHTHYES; ACTINOPTERYGII; TETRAODONTIFORMES.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   TISSUE=TESTIS;
RX   MEDLINE; 96125198.
RA   YODA T., MORITA T., KAWATSU K., SUEKI K., SHIBATA T., HAMANO Y.;
RL   GENE 166:249-253(1995).
CC   -!- FUNCTION: MOLECULAR CHAPERONE; ASSIST THE FOLDING OF PROTEINS UPON
CC       ATP HYDROLYSIS. KNOWN TO PLAY A ROLE, IN VITRO, IN THE FOLDING OF
CC       ACTIN AND TUBULIN.
CC   -!- SUBUNIT: HETERO-OLIGOMERIC COMPLEX OF ABOUT 850 TO 900 KD THAT
CC       FORMS TWO STACKED RINGS, 12 TO 16 NM IN DIAMETER.
CC   -!- SUBCELLULAR LOCATION: CYTOPLASMIC.
CC   -!- SIMILARITY: BELONGS TO THE TCP-1 CHAPERONIN FAMILY.
DR   EMBL; D49483; D1009058; -.
DR   EMBL; D49484; D1019650; -.
DR   PROSITE; PS00750; TCP1_1; 1.
DR   PROSITE; PS00751; TCP1_2; 1.
DR   PROSITE; PS00995; TCP1_3; 1.
KW   CHAPERONE; ATP-BINDING; MULTIGENE FAMILY.
SQ   SEQUENCE   536 AA;  57715 MW;  25313AC3 CRC32;
     MPEGKATSSA SNTGKNKGGA YQDRDKPAQI RYSNISAAKA VADAVRTSLG PKGMDKMIQD
     EKGDVTITND GATILKQMQV LHPSAKMLVE LSKAQDIEAG DGTTSVVVIA GALLDSCNRL
     LQRGIHPTII SESFQKAVDK GVEVLTAMSQ PVQLGDRETL LNSATTSLCS KVVSQYSSLL
     APMSVDAVMR VIDPATATSV DLHDIKIIKK LGGTIDDCEL VEGLVLTQRV ANSSVSRVEK
     AKIGLIQFCL SPPKTDMDNQ IVVSDYTQMD RVLREERAYI LNMVKQIKKA GCNVLFIQKS
     ILRDALSDLA LHFLNKMKIM VVKDIEREDI EFICKTIGTK PIAHIDHFTP EMLGTAELAE
     EVSLDGSGKL VKITGCASPG KTVSIVVRGS NKLVIEEAER SIHDALCVIR CLVKKRALIA
     GGGAPEIELA VRLAEYSRTL GGMEAYCVRA YSDALEVIPS TLAENAGLNP ISTVTELRNR
     HAQGDKMAGI NVRKGGISNI MEELVVQPLL VSISALTLAT ETVRSILKID DVVNAR
//
ID   ACH2_DROME     STANDARD;      PRT;   576 AA.
AC   P17644;
DT   01-AUG-1990 (REL. 15, CREATED)
DT   01-AUG-1990 (REL. 15, LAST SEQUENCE UPDATE)
DT   01-NOV-1997 (REL. 35, LAST ANNOTATION UPDATE)
DE   ACETYLCHOLINE RECEPTOR PROTEIN, ALPHA-LIKE CHAIN 2 PRECURSOR.
GN   ACRE OR SAD OR ACR96AB.
OS   DROSOPHILA MELANOGASTER (FRUIT FLY).
OC   EUKARYOTA; METAZOA; ARTHROPODA; TRACHEATA; HEXAPODA; INSECTA;
OC   PTERYGOTA; DIPTERA; BRACHYCERA; MUSCOMORPHA; EPHYDROIDEA;
OC   DROSOPHILIDAE; DROSOPHILA.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   TISSUE=HEAD;
RX   MEDLINE; 90301489.
RA   BAUMANN A., JONAS P., GUNDELFINGER E.D.;
RT   "Sequence of D alpha 2, a novel alpha-like subunit of Drosophila
RT   nicotinic acetylcholine receptors.";
RL   NUCLEIC ACIDS RES. 18:3640-3640(1990).
RN   [2]
RP   SEQUENCE FROM N.A.
RC   TISSUE=HEAD;
RX   MEDLINE; 90353591.
RA   JONAS P., BAUMANN A., MERZ B., GUNDELFINGER E.D.;
RT   "Structure and developmental expression of the D alpha 2 gene
RT   encoding a novel nicotinic acetylcholine receptor protein of
RT   Drosophila melanogaster.";
RL   FEBS LETT. 269:264-268(1990).
RN   [3]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 90360975.
RA   SAWRUK E., SCHLOSS P., BETZ H., SCHMITT B.;
RT   "Heterogeneity of Drosophila nicotinic acetylcholine receptors: SAD,
RT   a novel developmentally regulated alpha-subunit.";
RL   EMBO J. 9:2671-2677(1990).
CC   -!- FUNCTION: AFTER BINDING ACETYLCHOLINE, THE ACHR RESPONDS BY AN
CC       EXTENSIVE CHANGE IN CONFORMATION THAT AFFECTS ALL SUBUNITS AND
CC       LEADS TO OPENING OF AN ION-CONDUCTING CHANNEL ACROSS THE PLASMA
CC       MEMBRANE.
CC   -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN.
CC   -!- TISSUE SPECIFICITY: CNS IN EMBRYOS.
CC   -!- DEVELOPMENTAL STAGE: LATE EMBRYONIC AND LATE PUPAL STAGES.
CC   -!- SIMILARITY: BELONGS TO THE LIGAND-GATED IONIC CHANNELS FAMILY.
CC   --------------------------------------------------------------------------
CC   This SWISS-PROT entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use  by  non-profit  institutions as long  as its content  is  in  no  way
CC   modified and this statement is not removed.  Usage  by  and for commercial
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CC   or send an email to license@isb-sib.ch).
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DR   EMBL; X52274; G7803; -.
DR   EMBL; X53583; G8533; -.
DR   PIR; S11679; ACFFA2.
DR   FLYBASE; FBgn0000039; nAcR-alpha-96Ab.
DR   PROSITE; PS00236; NEUROTR_ION_CHANNEL; 1.
DR   PFAM; PF00065; neur_chan; 1.
KW   RECEPTOR; POSTSYNAPTIC MEMBRANE; IONIC CHANNEL; GLYCOPROTEIN; SIGNAL;
KW   TRANSMEMBRANE; MULTIGENE FAMILY.
FT   SIGNAL        1     41       PROBABLE.
FT   CHAIN        42    576       ACETYLCHOLINE RECEPTOR PROTEIN, ALPHA-2.
FT   DOMAIN       42    261       EXTRACELLULAR (POTENTIAL).
FT   TRANSMEM    262    285       POTENTIAL.
FT   TRANSMEM    293    311       POTENTIAL.
FT   TRANSMEM    327    346       POTENTIAL.
FT   DOMAIN      347    526       CYTOPLASMIC (POTENTIAL).
FT   TRANSMEM    527    545       POTENTIAL.
FT   DISULFID    169    183       BY SIMILARITY.
FT   DISULFID    243    244       ASSOCIATED WITH RECEPTOR ACTIVATION
FT                                (BY SIMILARITY).
FT   CARBOHYD     65     65       POTENTIAL.
FT   CARBOHYD    254    254       POTENTIAL.
FT   CARBOHYD    570    570       POTENTIAL.
SQ   SEQUENCE   576 AA;  65506 MW;  7B795689 CRC32;
     MAPGCCTTRP RPIALLAHIW RHCKPLCLLL VLLLLCETVQ ANPDAKRLYD DLLSNYNRLI
     RPVSNNTDTV LVKLGLRLSQ LIDLNLKDQI LTTNVWLEHE WQDHKFKWDP SEYGGVTELY
     VPSEHIWLPD IVLYNNADGE YVVTTMTKAI LHYTGKVVWT PPAIFKSSCE IDVRYFPFDQ
     QTCFMKFGSW TYDGDQIDLK HISQKNDKDN KVEIGIDLRE YYPSVEWDIL GVPAERHEKY
     YPCCAEPYPD IFFNITLRRK TLFYTVNLII PCVGISYLSV LVFYLPADSG EKIALCISIL
     LSQTMFFLLI SEIIPSTSLA LPLLGKYLLF TMLLVGLSVV ITIIILNIHY RKPSTHKMRP
     WIRSFFIKRL PKLLLMRVPK DLLRDLAANK INYGLKFSKT KFGQALMDEM QMNSGGSSPD
     SLRRMQGRVG AGGCNGMHVT TATNRFSGLV GALGGGLSTL SGYNGLPSVL SGLDDSLSDV
     AARKKYPFEL EKAIHNVMFI QHHMQRQDEF NAEDQDWGFV AMVMDRLFLW LFMIASLVGT
     FVILGEAPSL YDDTKAIDVQ LSDVAKQIYN LTEKKN
//
ID   HBA_HUMAN      STANDARD;      PRT;   141 AA.
AC   P01922;
DT   21-JUL-1986 (Rel. 01, Created)
DT   21-JUL-1986 (Rel. 01, Last sequence update)
DT   15-JUL-1999 (Rel. 38, Last annotation update)
DE   HEMOGLOBIN ALPHA CHAIN.
GN   HBA1 AND HBA2.
OS   Homo sapiens (Human), Pan troglodytes (Chimpanzee), and
OS   Pan paniscus (Pygmy chimpanzee) (Bonobo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Mammalia;
OC   Eutheria; Primates; Catarrhini; Hominidae; Homo.
RN   [1]
RP   SEQUENCE FROM N.A. (ALPHA-1).
RX   MEDLINE; 81088339.
RA   MICHELSON A.M., ORKIN S.H.;
RT   "The 3' untranslated regions of the duplicated human alpha-globin
RT   genes are unexpectedly divergent.";
RL   Cell 22:371-377(1980).
RN   [2]
RP   SEQUENCE FROM N.A. (ALPHA-2).
RX   MEDLINE; 81175088.
RA   LIEBHABER S.A., GOOSSENS M.J., KAN Y.W.;
RT   "Cloning and complete nucleotide sequence of human 5'-alpha-globin
RT   gene.";
RL   Proc. Natl. Acad. Sci. U.S.A. 77:7054-7058(1980).
RN   [3]
RP   SEQUENCE FROM N.A. (ALPHA-2).
RX   MEDLINE; 80137531.
RA   WILSON J.T., WILSON L.B., REDDY V.B., CAVALLESCO C., GHOSH P.K.,
RA   DERIEL J.K., FORGET B.G., WEISSMAN S.M.;
RT   "Nucleotide sequence of the coding portion of human alpha globin
RT   messenger RNA.";
RL   J. Biol. Chem. 255:2807-2815(1980).
RN   [4]
RP   SEQUENCE FROM N.A. (ALPHA-1 AND ALPHA-2).
RA   FLINT J., HIGGS D.R.;
RL   Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   SEQUENCE.
RA   BRAUNITZER G., GEHRING-MULLER R., HILSCHMANN N., HILSE K., HOBOM G.,
RA   RUDLOFF V., WITTMANN-LIEBOLD B.;
RT   "The constitution of normal adult human haemoglobin.";
RL   Hoppe-Seyler's Z. Physiol. Chem. 325:283-286(1961).
RN   [6]
RP   SEQUENCE.
RA   HILL R.J., KONIGSBERG W.;
RT   "The structure of human hemoglobin: IV. The chymotryptic digestion of
RT   the alpha chain of human hemoglobin.";
RL   J. Biol. Chem. 237:3151-3156(1962).
RN   [7]
RP   SEQUENCE.
RA   SCHROEDER W.A., SHELTON J.R., SHELTON J.B., CORMICK J.;
RT   "The amino acid sequence of the alpha chain of human fetal
RT   hemoglobin.";
RL   Biochemistry 2:1353-1357(1963).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF DEOXYHEMOGLOBIN.
RX   MEDLINE; 76027820.
RA   FERMI G.;
RT   "Three-dimensional fourier synthesis of human deoxyhaemoglobin at
RT   2.5-A resolution: refinement of the atomic model.";
RL   J. Mol. Biol. 97:237-256(1975).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF LIGANDED R2 STATE.
RX   MEDLINE; 92381041.
RA   SILVA M.M., ROGERS P.H., ARNONE A.;
RT   "A third quaternary structure of human hemoglobin A at 1.7-A
RT   resolution.";
RL   J. Biol. Chem. 267:17248-17256(1992).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF HB GOWER 2.
RX   MEDLINE; 98332748.
RA   SUTHERLAND-SMITH A.J., BAKER H.M., HOFMANN O.M., BRITTAIN T.,
RA   BAKER E.N.;
RT   "Crystal structure of a human embryonic haemoglobin: the carbonmonoxy
RT   form of gower II (alpha2 epsilon2) haemoglobin at 2.9-A resolution.";
RL   J. Mol. Biol. 280:475-484(1998).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF HB CATONSVILLE.
RX   MEDLINE; 93192190.
RA   KAVANAUGH J.S., MOO-PENN W.F., ARNONE A.;
RT   "Accommodation of insertions in helices: the mutation in hemoglobin
RT   Catonsville (Pro 37 alpha-Glu-Thr 38 alpha) generates a 3(10)-->alpha
RT   bulge.";
RL   Biochemistry 32:2509-2513(1993).
RN   [12]
RP   SEQUENCE.
RC   SPECIES=P.TROGLODYTES;
RX   MEDLINE; 66071496.
RA   RIFKIN D.B., KONIGSBERG W.;
RT   "The characterization of the tryptic peptides from the hemoglobin of
RT   the chimpanzee (Pan troglodytes).";
RL   Biochim. Biophys. Acta 104:457-461(1965).
RN   [13]
RP   SEQUENCE FROM N.A.
RC   SPECIES=P.TROGLODYTES;
RX   MEDLINE; 84169526.
RA   LIEBHABER S.A., BEGLEY K.A.;
RT   "Structural and evolutionary analysis of the two chimpanzee
RT   alpha-globin mRNAs.";
RL   Nucleic Acids Res. 11:8915-8929(1983).
RN   [14]
RP   SEQUENCE.
RC   SPECIES=P.PANISCUS;
RX   MEDLINE; 83219265.
RA   GOODMAN M., BRAUNITZER G., STANGL A., SCHRANK B.;
RT   "Evidence on human origins from haemoglobins of African apes.";
RL   Nature 303:546-548(1983).
RN   [15]
RP   VARIANT AL-AIN ABU DHABI.
RX   MEDLINE; 93053723.
RA   ABBES S., M'RAD A., FITZGERALD P.A., DORMER P., BLOUQUIT Y.,
RA   KISTER J., GALACTEROS F., WAJCMAN H.;
RT   "HB Al-Ain Abu Dhabi [alpha 18(A16)Gly-->Asp]: a new hemoglobin
RT   variant discovered in an Emiratee family.";
RL   Hemoglobin 16:355-362(1992).
RN   [16]
RP   VARIANT ATAGO.
RX   MEDLINE; 72030550.
RA   FUJIWARA N., MAEKAWA T., MATSUDA G.;
RT   "Hemoglobin Atago (alpha2-85 Tyr beta-2) a new abnormal human
RT   hemoglobin found in Nagasaki. Biochemical studies on hemoglobins and
RT   myoglobins. VI.";
RL   Int. J. Protein Res. 3:35-39(1971).
RN   [17]
RP   VARIANT AUCKLAND.
RX   MEDLINE; 97463291.
RA   BRENNAN S.O., MATTHEWS J.R.;
RT   "Hb Auckland [alpha 87(F8) His-->Asn]: a new mutation of the proximal
RT   histidine identified by electrospray mass spectrometry.";
RL   Hemoglobin 21:393-403(1997).
RN   [18]
RP   VARIANTS J-BUDA AND G-PEST.
RA   BRIMHALL B.J., DUERST M., HOLLAN S.R., STENZEL P., SZELENYI J.,
RA   JONES R.T.;
RT   "Structural characterizations of hemoglobins J-Buda (alpha 61 (E10)
RT   Lys-to-Asn) and G-Pest (alpha 74 (EF3) Asp-to-Asn).";
RL   Biochim. Biophys. Acta 336:344-360(1974).
RN   [19]
RP   VARIANTS CHONGQING AND HARBIN.
RX   MEDLINE; 85130255.
RA   ZENG Y.-T., HUANG S.-Z., QIU X.-K., CHENG G.-C., REN Z.-R., JIN Q.-C.,
RA   CHEN C.-Y., JIAO C.-T., TANG Z.-G., LIU R.-H., BAO X.-H., ZENG L.-Z.,
RA   DUAN Y.-Q., ZHANG G.-Y.;
RT   "Hemoglobin Chongqing [alpha 2(NA2)Leu-->Arg] and hemoglobin Harbin
RT   [alpha 16(A14)Lys-->Met] found in China.";
RL   Hemoglobin 8:569-581(1984).
RN   [20]
RP   VARIANT CLINIC.
RA   AYALA S., COLOMER D., GELPI J.L., CORRON J.L.V.;
RT   "Alpha-thalassaemia due to a single codon deletion in the alpha
RT   1-globin gene. Computational structural analysis of the new
RT   alpha-chain variant.";
RL   Hum. Mutat. 11:412-412(1998).
RN   [21]
RP   VARIANT DAVENPORT.
RX   MEDLINE; 91331854.
RA   WILSON J.B., WEBBER B.B., PLASESKA D., DE ALARCON P.A., MCMILLAN S.K.,
RA   HUISMAN T.H.;
RT   "Hb Davenport or alpha 2(78)(EF7)Asn-->His beta 2.";
RL   Hemoglobin 14:599-605(1990).
RN   [22]
RP   VARIANT EVANS.
RX   MEDLINE; 90109650.
RA   WILSON J.B., WEBBER B.B., KUTLAR A., REESE A.L., MCKIE V.C.,
RA   LUTCHER C.L., FELICE A.E., HUISMAN T.H.J.;
RT   "Hb Evans or alpha 262(E11)Val-->Met beta 2; an unstable hemoglobin
RT   causing a mild hemolytic anemia.";
RL   Hemoglobin 13:557-566(1989).
RN   [23]
RP   VARIANTS FORT DE FRANCE AND SPANISH TOWN.
RX   MEDLINE; 89323437.
RA   CASH F.E., MONPLAISIR N., GOOSSENS M., LIEBHABER S.A.;
RT   "Locus assignment of two alpha-globin structural mutants from the
RT   Caribbean basin: alpha Fort de France (alpha 45 Arg) and alpha
RT   Spanish Town (alpha 27 Val).";
RL   Blood 74:833-835(1989).
RN   [24]
RP   VARIANT GODAVARY.
RX   MEDLINE; 98153063.
RA   WAJCMAN H., KISTER J., RIOU J., GALACTEROS F., GIROT R.,
RA   MAIER-REDELSPERGER M., NAYUDU N.V.S., GIORDANO P.C.;
RT   "Hb Godavari [alpha 95(G2)Pro-->Thr]: a neutral amino acid
RT   substitution in the alpha 1 beta 2 interface that modifies the
RT   electrophoretic mobility of hemoglobin.";
RL   Hemoglobin 22:11-22(1998).
RN   [25]
RP   VARIANT GRADY.
RX   MEDLINE; 75010592.
RA   HUISMAN T.H.J., WILSON J.B., GRAVELY M., HUBBARD M.;
RT   "Hemoglobin Grady: the first example of a variant with elongated
RT   chains due to an insertion of residues.";
RL   Proc. Natl. Acad. Sci. U.S.A. 71:3270-3273(1974).
RN   [26]
RP   VARIANT HANAMAKI.
RX   MEDLINE; 92340291.
RA   ORISAKA M., TAJIMA T., HARANO T., HARANO K., KUSHIDA Y., IMAI K.;
RT   "A new alpha chain variant, Hb Hanamaki or alpha
RT   2(139)(HC1)Lys-->Glu beta 2, found in a Japanese family.";
RL   Hemoglobin 16:67-71(1992).
RN   [27]
RP   VARIANT HANDA.
RX   MEDLINE; 83056269.
RA   HARANO T., HARANO K., SHIBATA S., UEDA S., IMAI K., SEKI M.;
RT   "HB Handa [alpha 90 (FG 2) Lys replaced by Met]: structure and
RT   biosynthesis of a new slightly higher oxygen affinity variant.";
RL   Hemoglobin 6:379-389(1982).
RN   [28]
RP   VARIANT HASHARON.
RX   MEDLINE; 69165810.
RA   CHARACHE S., MONDZAC A.M., GESSNER U.;
RT   "Hemoglobin Hasharon (alpha-2-47 his(CD5)beta-2): a hemoglobin found
RT   in low concentration.";
RL   J. Clin. Invest. 48:834-847(1969).
RN   [29]
RP   VARIANT HOBART.
RX   MEDLINE; 88006902.
RA   FLEMING P.J., SUMNER D.R., WYATT K., HUGHES W.G., MELROSE W.D.,
RA   JUPE D.M.D., BAIKIE M.J.;
RT   "Hemoglobin Hobart or alpha 20(Bl)His-->Arg: a new alpha chain
RT   hemoglobin variant.";
RL   Hemoglobin 11:211-220(1987).
RN   [30]
RP   VARIANT INKSTER.
RX   MEDLINE; 74302151.
RA   REED R.E., WINTER W.P., RUCKNAGEL D.L.;
RT   "Haemoglobin inkster (alpha2 85aspartic acid leads to valine beta2)
RT   coexisting with beta-thalassaemia in a Caucasian family.";
RL   Br. J. Haematol. 26:475-484(1974).
RN   [31]
RP   VARIANT KANAGAWA.
RX   MEDLINE; 92340282.
RA   MIYASHITA H., HASHIMOTO K., MOHRI H., OHOKUBO T., HARANO T.,
RA   HARANO K., IMAI K.;
RT   "Hb Kanagawa [alpha 40(C5)Lys-->Met]: a new alpha chain variant with
RT   an increased oxygen affinity.";
RL   Hemoglobin 16:1-10(1992).
RN   [32]
RP   VARIANT KURDISTAN.
RX   MEDLINE; 94252883.
RA   GIORDANO P.C., HARTEVELD C.L., STRENG H., OOSTERWIJK J.C.,
RA   HEISTER J.G.A.M., AMONS R., BERNINI L.F.;
RT   "Hb Kurdistan [alpha 47(CE5)Asp-->Tyr], a new alpha chain variant in
RT   combination with beta (0)-thalassemia.";
RL   Hemoglobin 18:11-18(1994).
RN   [33]
RP   VARIANT KUROSAKI.
RX   MEDLINE; 96031515.
RA   HARANO T., HARANO K., IMAI K., MURAKAMI T., MATSUBARA H.;
RT   "Hb Kurosaki [alpha 7(A5)Lys-->Glu]: a new alpha chain variant found
RT   in a Japanese woman.";
RL   Hemoglobin 19:197-201(1995).
RN   [34]
RP   VARIANT J-MEERUT OR J-BIRMINGHAM.
RX   MEDLINE; 95229430.
RA   YALCIN A., AVCU F., BEYAN C., GUERGEY A., URAL A.U.;
RT   "A case of HB J-Meerut (or Hb J-Birmingham) [alpha
RT   120(H3)Ala-->Glu].";
RL   Hemoglobin 18:433-435(1994).
RN   [35]
RP   VARIANT MELUSINE.
RX   MEDLINE; 94124250.
RA   WACJMAN H., KLAMES G., GROFF P., PROME D., RIOU J., GALACTEROS F.;
RT   "Hb Melusine [alpha 114(GH2)Pro-->Ser]: a new neutral hemoglobin
RT   variant.";
RL   Hemoglobin 17:397-405(1993).
RN   [36]
RP   VARIANT MONTGOMERY.
RX   MEDLINE; 75109326.
RA   BRIMHALL B., JONES R.T., SCHNEIDER R.G., HOSTY T.S., TOMLIN G.,
RA   ATKINS R.;
RT   "Two new hemoglobins. Hemoglobin Alabama (beta39(C5)Gln leads to Lys)
RT   and hemoglobin Montgomery (alpha 48(CD 6) Leu leads to Arg).";
RL   Biochim. Biophys. Acta 379:28-32(1975).
RN   [37]
RP   VARIANT PETAH TIKVA.
RX   MEDLINE; 81134478.
RA   HONIG G.R., SHAMSUDDIN M., ZAIZOV R., STEINHERZ M., SOLAR I.,
RA   KIRSCHMAN C.;
RT   "Hemoglobin Petah Tikva (alpha 110 Ala replaced by Asp): a new
RT   unstable variant with alpha-thalassemia-like expression.";
RL   Blood 57:705-711(1981).
RN   [38]
RP   VARIANT PHNOM PENH.
RX   MEDLINE; 98112407.
RA   WAJCMAN H., PREHU M.O., PREHU C., BLOUQUIT Y., PROME D.,
RA   GALACTEROS F.;
RT   "Hemoglobin Phnom Penh [alpha117Phe(H1)-Ile-alpha118Thr(H2)];
RT   evidence for a hotspot for insertion of residues in the third exon of
RT   the alpha1-globin gene.";
RL   Hum. Mutat. Suppl. 1:S20-S22(1998).
RN   [39]
RP   VARIANT PORT HURON.
RX   MEDLINE; 92202056.
RA   ZWERDLING T., WILLIAMS S., NASR S.A., RUCKNAGEL D.L.;
RT   "Hb Port Huron [alpha 56 (E5)Lys-->Arg]: a new alpha chain variant.";
RL   Hemoglobin 15:381-391(1991).
RN   [40]
RP   VARIANT SAWARA.
RX   MEDLINE; 74008827.
RA   SUMIDA I., OHTA Y., IMAMURA T., YANASE T.;
RT   "Hemoglobin Sawara: alpha 6(A4) aspartic acid leads to alanine.";
RL   Biochim. Biophys. Acta 322:23-26(1973).
RN   [41]
RP   VARIANT SHENYANG.
RX   MEDLINE; 83135048.
RA   ZENG Y.-T., HUANG S.-Z., ZHOU X., QIU X.-K., DONG Q., LI M., BAI J.;
RT   "Hb Shenyang (alpha 26 (B7) Ala replaced by Glu): a new unstable
RT   variant found in China.";
RL   Hemoglobin 6:625-628(1982).
RN   [42]
RP   VARIANT SUAN-DOK.
RX   MEDLINE; 80006169.
RA   SANGUANSERMSRI T., MATRAGOON S., CHANGLOAH L., FLATZ G.;
RT   "Hemoglobin Suan-Dok (alpha 2 109 (G16) Leu replaced by Arg beta 2):
RT   an unstable variant associated with alpha-thalassemia.";
RL   Hemoglobin 3:161-174(1979).
RN   [43]
RP   VARIANT SUN PRAIRIE.
RX   MEDLINE; 91177710.
RA   HARKNESS M., HARKNESS D.R., KUTLAR F., KUTLAR A., WILSON J.B.,
RA   WEBBER B.B., CODRINGTON J.F., HUISMAN T.H.J.;
RT   "Hb Sun Prairie or alpha(2)130(H13)Ala-->Pro beta 2, a new unstable
RT   variant occurring in low quantities.";
RL   Hemoglobin 14:479-489(1990).
RN   [44]
RP   VARIANT SWAN RIVER.
RX   MEDLINE; 96351655.
RA   HARANO T., HARANO K., IMAI K., TERUNUMA S.;
RT   "HB Swan River [alpha 6(A4)Asp-->Gly] observed in a Japanese man.";
RL   Hemoglobin 20:75-78(1996).
RN   [45]
RP   VARIANT THIONVILLE.
RX   MEDLINE; 92316953.
RA   VASSEUR C., BLOUQUIT Y., KISTER J., PROME D., KAVANAUGH J.S.,
RA   ROGERS P.H., GUILLEMIN C., ARNONE A., GALACTEROS F., POYART C.,
RA   ROSA J., WAJCMAN H.;
RT   "Hemoglobin Thionville. An alpha-chain variant with a substitution of
RT   a glutamate for valine at NA-1 and having an acetylated methionine
RT   NH2 terminus.";
RL   J. Biol. Chem. 267:12682-12691(1992).
RN   [46]
RP   VARIANT TUNIS-BIZERTE.
RX   MEDLINE; 95306384.
RA   DARBELLAY R., MACH-PASCUAL S., ROSE K., GRAF J., BERIS P.;
RT   "Haemoglobin Tunis-Bizerte: a new alpha 1 globin 129 Leu-->Pro
RT   unstable variant with thalassaemic phenotype.";
RL   Br. J. Haematol. 90:71-76(1995).
RN   [47]
RP   VARIANT TURRIFF.
RX   MEDLINE; 92340284.
RA   LANGDOWN J.V., DAVIDSON R.J., WILLIAMSON D.;
RT   "A new alpha chain variant, Hb Turriff [alpha 99(G6)Lys-->Glu]: the
RT   interference of abnormal hemoglobins in Hb A1c determination.";
RL   Hemoglobin 16:11-17(1992).
RN   [48]
RP   VARIANT VAL DE MARNE.
RX   MEDLINE; 94124251.
RA   WACJMAN H., KISTER J., M'RAD A., MARDEN M.C., RIOU J., GALACTEROS F.;
RT   "Hb Val de Marne [alpha 133(H16)Ser-->Arg]: a new hemoglobin variant
RT   with moderate increase in oxygen affinity.";
RL   Hemoglobin 17:407-417(1993).
RN   [49]
RP   VARIANT WESTMEAD.
RX   MEDLINE; 92155975.
RA   JIANG N.H., LIANG S., WEN X.J., LIANG R., SU C., TANG Z.;
RT   "Hb Westmead: an alpha 2-globin gene mutation detected by polymerase
RT   chain reaction and Stu I cleavage.";
RL   Hemoglobin 15:291-295(1991).
RN   [50]
RP   VARIANT WOODVILLE.
RX   MEDLINE; 86167529.
RA   COMO P.F., BARBER S., SAGE R.E., KRONENBERG H.;
RT   "Hemoglobin Woodville: alpha (2)6(A4) aspartic acid-->tyrosine.";
RL   Hemoglobin 10:135-141(1986).
RN   [51]
RP   VARIANT YUDA.
RX   MEDLINE; 93053734.
RA   FUJISAWA K., HATTORI Y., OHBA Y., ANDO S.;
RT   "Hb Yuda or alpha 130(H13)Ala-->Asp; a new alpha chain variant with
RT   low oxygen affinity.";
RL   Hemoglobin 16:435-439(1992).
RN   [52]
RP   VARIANT ZAIRE.
RX   MEDLINE; 92380658.
RA   WAJCMAN H., BLOUQUIT Y., VASSEUR C., LE QUERREC A., LANIECE M.,
RA   MELEVENDI C., RASORE A., GALACTEROS F.;
RT   "Two new human hemoglobin variants caused by unusual mutational
RT   events: Hb Zaire contains a five residue repetition within the
RT   alpha-chain and Hb Duino has two residues substituted in the
RT   beta-chain.";
RL   Hum. Genet. 89:676-680(1992).
CC   -!- SUBUNIT: ALPHA CHAINS BUILD EARLY EMBRYONIC HEMOGLOBIN GOWER-2
CC       (WITH EPSILON CHAINS), FETAL HEMOGLOBIN F (WITH GAMMA CHAINS), AND
CC       ADULT HEMOGLOBIN A (WITH BETA CHAINS).
CC   -!- DISEASE: SOME RARE FORMS OF ALPHA-THALASSEMIA ARE DUE TO POINT
CC       MUTATIONS (NON-DELETIONAL ALPHA-THALASSEMIA). THE THALLASSAEMIC
CC       PHENOTYPE IS DUE TO UNSTABLE GLOBIN ALPHA CHAINS THAT ARE RAPIDLY
CC       CATABOLIZED PRIOR TO FORMATION OF THE ALPHA-BETA DIMERS.
CC   -!- DATABASE: NAME=Hb variant; NOTE=Human hemoglobin variants;
CC       WWW="http://globin.cse.psu.edu/globin/html/huisman/variants/".
CC   --------------------------------------------------------------------------
CC   This SWISS-PROT entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use  by  non-profit  institutions as long  as its content  is  in  no  way
CC   modified and this statement is not removed.  Usage  by  and for commercial
CC   entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC   or send an email to license@isb-sib.ch).
CC   --------------------------------------------------------------------------
DR   EMBL; J00153; AAB59407.1; -.
DR   EMBL; J00153; AAB59408.1; -.
DR   EMBL; V00488; CAA23748.1; -.
DR   EMBL; V00491; CAA23750.1; -.
DR   EMBL; V00493; CAA23752.1; -.
DR   EMBL; V00516; CAA23774.1; -.
DR   EMBL; X00226; CAA25044.1; -.
DR   EMBL; X00227; CAA25045.1; -.
DR   EMBL; Z84721; CAB06554.1; -.
DR   EMBL; Z84721; CAB06555.1; -.
DR   PIR; A02248; HAHU.
DR   PIR; A93303; HACZ.
DR   PIR; C93303; HACZP.
DR   PDB; 1COH; 15-OCT-94.
DR   PDB; 1FDH; 30-SEP-83.
DR   PDB; 1HBS; 29-OCT-85.
DR   PDB; 1HCO; 30-SEP-83.
DR   PDB; 2HCO; 30-SEP-83.
DR   PDB; 1HHO; 31-JAN-84.
DR   PDB; 2HHB; 15-OCT-89.
DR   PDB; 3HHB; 18-JUL-84.
DR   PDB; 4HHB; 15-OCT-89.
DR   PDB; 1THB; 15-JAN-91.
DR   PDB; 1NIH; 15-OCT-92.
DR   PDB; 1BAB; 31-JAN-94.
DR   PDB; 1BBB; 31-JAN-94.
DR   PDB; 1CMY; 31-OCT-93.
DR   PDB; 1DXT; 31-OCT-93.
DR   PDB; 1DXU; 31-OCT-93.
DR   PDB; 1DXV; 31-OCT-93.
DR   PDB; 1HBA; 31-JAN-94.
DR   PDB; 1HBB; 31-JAN-94.
DR   PDB; 2HBC; 07-FEB-95.
DR   PDB; 2HBD; 07-FEB-95.
DR   PDB; 2HBE; 07-FEB-95.
DR   PDB; 2HBF; 07-FEB-95.
DR   PDB; 2HBS; 23-JUL-97.
DR   PDB; 1HGA; 31-JAN-94.
DR   PDB; 1HGB; 31-JAN-94.
DR   PDB; 1HGC; 31-JAN-94.
DR   PDB; 2HHD; 26-JAN-95.
DR   PDB; 2HHE; 26-JAN-95.
DR   PDB; 1CLS; 14-OCT-96.
DR   PDB; 1GBU; 11-JAN-97.
DR   PDB; 1GBV; 11-JAN-97.
DR   PDB; 1GLI; 01-AUG-96.
DR   PDB; 1DSH; 31-MAR-95.
DR   PDB; 1HAB; 12-NOV-97.
DR   PDB; 1HAC; 12-NOV-97.
DR   PDB; 1HDB; 03-APR-96.
DR   PDB; 1SDK; 01-AUG-96.
DR   PDB; 1SDL; 01-AUG-96.
DR   PDB; 1AXF; 28-JAN-98.
DR   PDB; 1ABY; 25-FEB-98.
DR   PDB; 1A00; 18-MAR-98.
DR   PDB; 1A01; 18-MAR-98.
DR   PDB; 1A0U; 18-MAR-98.
DR   PDB; 1A0V; 18-MAR-98.
DR   PDB; 1A0W; 18-MAR-98.
DR   PDB; 1A0X; 18-MAR-98.
DR   PDB; 1A0Y; 18-MAR-98.
DR   PDB; 1A0Z; 18-MAR-98.
DR   PDB; 1RVW; 25-MAR-98.
DR   PDB; 1VWT; 25-MAR-98.
DR   PDB; 1A3N; 29-APR-98.
DR   PDB; 1A3O; 29-APR-98.
DR   PDB; 1AJ9; 20-MAY-98.
DR   PDB; 1A9W; 17-JUN-98.
DR   PDB; 1ABW; 17-JUN-98.
DR   PDB; 1BUW; 16-SEP-98.
DR   PDB; 6HBW; 16-SEP-98.
DR   PDB; 1BZ0; 11-NOV-98.
DR   PDB; 1BZ1; 11-NOV-98.
DR   PDB; 1BZZ; 11-NOV-98.
DR   PDB; 1B86; 19-FEB-99.
DR   PDB; 1BIJ; 30-MAR-99.
DR   SWISS-2DPAGE; P01922; HUMAN.
DR   MIM; 141800; -.
DR   MIM; 141850; -.
DR   MIM; 141860; -.
DR   PFAM; PF00042; globin; 1.
DR   PROSITE; PS01033; GLOBIN; 1.
KW   Heme; Oxygen transport; Respiratory protein; Erythrocyte;
KW   Disease mutation; Polymorphism; Acetylation; 3D-structure.
FT   INIT_MET      0      0
FT   METAL        58     58       IRON (HEME DISTAL LIGAND).
FT   METAL        87     87       IRON (HEME PROXIMAL LIGAND).
FT   MOD_RES       0      0       ACETYLATION (IN VARIANT THIONVILLE; WHERE
FT                                THE INITIATOR MET IS NOT CLEAVED).
FT   VARIANT       1      1       V -> E (IN THIONVILLE; O2 AFFINITY DOWN).
FT                                /FTId=VAR_002719.
FT   VARIANT       2      2       L -> R (IN CHONGQING; O2 AFFINITY UP).
FT                                /FTId=VAR_002720.
FT   VARIANT       5      5       A -> D (IN J-TORONTO).
FT                                /FTId=VAR_002721.
FT   VARIANT       5      5       A -> P (IN KARACHI).
FT                                /FTId=VAR_002722.
FT   VARIANT       6      6       D -> A (IN SAWARA; O2 AFFINITY UP).
FT                                /FTId=VAR_002723.
FT   VARIANT       6      6       D -> G (IN SWAN RIVER).
FT                                /FTId=VAR_002724.
FT   VARIANT       6      6       D -> N (IN DUNN; O2 AFFINITY UP).
FT                                /FTId=VAR_002725.
FT   VARIANT       6      6       D -> V (IN FERNDOWN; O2 AFFINITY UP).
FT                                /FTId=VAR_002726.
FT   VARIANT       6      6       D -> Y (IN WOODVILLE; O2 AFFINITY UP).
FT                                /FTId=VAR_002727.
FT   VARIANT       7      7       K -> E (IN KUROSAKI).
FT                                /FTId=VAR_002728.
FT   VARIANT      11     11       K -> E (IN ANANTHARAJ).
FT                                /FTId=VAR_002729.
FT   VARIANT      12     12       A -> D (IN J-PARIS 1/J-ALJEZUR).
FT                                /FTId=VAR_002730.
FT   VARIANT      14     14       W -> R (IN EVANSTON; O2 AFFINITY UP).
FT                                /FTId=VAR_002731.
FT   VARIANT      15     15       G -> R (IN OTTAWA/SIAM).
FT                                /FTId=VAR_002732.
FT   VARIANT      16     16       K -> M (IN HARBIN; SLIGHTLY UNSTABLE).
FT                                /FTId=VAR_002733.
FT   VARIANT      16     16       K -> N (IN BEIJING).
FT                                /FTId=VAR_002734.
FT   VARIANT      18     18       G -> D (IN AL-AIN-ABU DHABI).
FT                                /FTId=VAR_002735.
FT   VARIANT      18     18       G -> R (IN HANDSWORTH).
FT                                /FTId=VAR_002736.
FT   VARIANT      19     19       A -> D (IN J-KUROSH).
FT                                /FTId=VAR_002737.
FT   VARIANT      19     19       A -> E (IN J-TASHIKUERGAN).
FT                                /FTId=VAR_002738.
FT   VARIANT      20     20       H -> Q (IN LE LAMENTIN).
FT                                /FTId=VAR_002739.
FT   VARIANT      20     20       H -> R (IN HOBART).
FT                                /FTId=VAR_002740.
FT   VARIANT      21     21       A -> D (IN J-NYANZA).
FT                                /FTId=VAR_002741.
FT   VARIANT      21     21       A -> P (IN FONTAINEBLAU).
FT                                /FTId=VAR_002742.
FT   VARIANT      22     22       G -> D (IN J-MEDELLIN).
FT                                /FTId=VAR_002743.
FT   VARIANT      23     23       E -> G (IN REIMS; SLIGHTLY UNSTABLE).
FT                                /FTId=VAR_002744.
FT   VARIANT      23     23       E -> K (IN CHAD).
FT                                /FTId=VAR_002745.
FT   VARIANT      24     24       Y -> H (IN LUXEMBOURG; UNSTABLE).
FT                                /FTId=VAR_002746.
FT   VARIANT      26     26       A -> E (IN SHENYANG; UNSTABLE).
FT                                /FTId=VAR_002747.
FT   VARIANT      27     27       E -> D (IN HEKINAN).
FT                                /FTId=VAR_002748.
FT   VARIANT      27     27       E -> G (IN FORT WORTH).
FT                                /FTId=VAR_002749.
FT   VARIANT      27     27       E -> V (IN SPANISH TOWN).
FT                                /FTId=VAR_002750.
FT   VARIANT      30     30       E -> K (IN O-PADOVA).
FT                                /FTId=VAR_002751.
FT   VARIANT      31     31       R -> S (IN PRATO; UNSTABLE).
FT                                /FTId=VAR_002752.
FT   VARIANT      34     34       L -> R (IN QUEENS/OGI).
FT                                /FTId=VAR_002753.
FT   VARIANT      37     37       P -> R (IN BOURMEDES).
FT                                /FTId=VAR_002754.
FT   VARIANT      37     37       P -> PE (IN CATONSVILLE).
FT                                /FTId=VAR_002755.
FT   VARIANT      40     40       K -> M (IN KANAGAWA; O2 AFFINITY UP).
FT                                /FTId=VAR_002756.
FT   VARIANT      41     41       T -> S (IN MIYANO; O2 AFFINITY UP).
FT                                /FTId=VAR_002757.
FT   VARIANT      43     43       F -> L (IN HIROSAKI; UNSTABLE).
FT                                /FTId=VAR_002758.
FT   VARIANT      44     44       P -> L (IN MILLEDGEVILLE; O2 AFFINITY
FT                                UP).
FT                                /FTId=VAR_002759.
FT   VARIANT      44     44       P -> R (IN KAWACHI; O2 AFFINITY UP).
FT                                /FTId=VAR_002760.
FT   VARIANT      45     45       H -> Q (IN BARI).
FT                                /FTId=VAR_002761.
FT   VARIANT      45     45       H -> R (IN FORT DE FRANCE; O2 AFFINITY
FT                                UP).
FT                                /FTId=VAR_002762.
FT   VARIANT      47     47       D -> A (IN CORDELE; UNSTABLE).
FT                                /FTId=VAR_002763.
FT   VARIANT      47     47       D -> G (IN UMI/MICHIGAN; UNSTABLE).
FT                                /FTId=VAR_002764.
FT   VARIANT      47     47       D -> H (IN HASHARON/SINAI; UNSTABLE).
FT                                /FTId=VAR_002765.
FT   VARIANT      47     47       D -> Y (IN KURDISTAN).
FT                                /FTId=VAR_002766.
FT   VARIANT      48     48       L -> R (IN MONTGOMERY).
FT                                /FTId=VAR_002767.
FT   VARIANT      49     49       S -> R (IN SAVARIA).
FT                                /FTId=VAR_002768.
FT   VARIANT      50     50       H -> R (IN AICHI; SLIGHTLY UNSTABLE).
FT                                /FTId=VAR_002769.
FT   VARIANT      51     51       G -> D (IN J-ABIDJAN).
FT                                /FTId=VAR_002770.
FT   VARIANT      51     51       G -> R (IN RUSS).
FT                                /FTId=VAR_002771.
FT   VARIANT      53     53       A -> D (IN J-ROVIGO; UNSTABLE).
FT                                /FTId=VAR_002772.
FT   VARIANT      54     54       Q -> R (IN HIKOSHIMA/SHIMONOSEKI).
FT                                /FTId=VAR_002773.
FT   VARIANT      56     56       K -> R (IN PORT HURON).
FT                                /FTId=VAR_002774.
FT   VARIANT      56     56       K -> T (IN THAILAND).
FT                                /FTId=VAR_002775.
FT   VARIANT      57     57       G -> R (IN L-PERSIAN GULF).
FT                                /FTId=VAR_002776.
FT   VARIANT      58     58       H -> Y (IN M-BOSTON/M-OSAKA; O2 AFFINITY
FT                                DOWN).
FT                                /FTId=VAR_002777.
FT   VARIANT      59     59       G -> D (IN ADANA; UNSTABLE; CAUSES ALPHA-
FT                                THALASSEMIA).
FT                                /FTId=VAR_002778.
FT   VARIANT      59     59       G -> V (IN TOTTORI; UNSTABLE).
FT                                /FTId=VAR_002779.
FT   VARIANT      60     60       K -> N (IN ZAMBIA).
FT                                /FTId=VAR_002780.
FT   VARIANT      60     60       MISSING (IN CLINIC; UNSTABLE; CAUSES
FT                                ALPHA-THALASSEMIA).
FT                                /FTId=VAR_002781.
FT   VARIANT      61     61       K -> N (IN J-BUDA).
FT                                /FTId=VAR_002782.
FT   VARIANT      61     61       K -> T (IN J-ANATOLIA).
FT                                /FTId=VAR_002783.
FT   VARIANT      62     62       V -> M (IN EVANS; UNSTABLE).
FT                                /FTId=VAR_002784.
FT   VARIANT      63     63       A -> D (IN PONTOISE; UNSTABLE).
FT                                /FTId=VAR_002785.
FT   VARIANT      64     64       D -> Y (IN PERSEPOLIS).
FT                                /FTId=VAR_002786.
FT   VARIANT      68     68       N -> K (IN G-PHILADELPHIA).
FT                                /FTId=VAR_002787.
FT   VARIANT      71     71       A -> E (IN J-HABANA).
FT                                /FTId=VAR_002788.
FT   VARIANT      71     71       A -> V (IN OZIERI).
FT                                /FTId=VAR_002789.
FT   VARIANT      72     72       H -> R (IN DANESKGAH-TEHERAN).
FT                                /FTId=VAR_002790.
FT   VARIANT      74     74       D -> A (IN LILLE).
FT                                /FTId=VAR_002791.
FT   VARIANT      74     74       D -> G (IN CHAPEL HILL).
FT                                /FTId=VAR_002792.
FT   VARIANT      74     74       D -> N (IN G-PEST).
FT                                /FTId=VAR_002793.
FT   VARIANT      75     75       D -> A (IN DUAN).
FT                                /FTId=VAR_002794.
FT   VARIANT      75     75       D -> H (IN Q-IRAN).
FT                                /FTId=VAR_002795.
FT   VARIANT      76     76       M -> K (IN NOKO).
FT                                /FTId=VAR_002796.
FT   VARIANT      76     76       M -> T (IN AZTEC).
FT                                /FTId=VAR_002797.
FT   VARIANT      77     77       P -> R (IN GUIZHOU).
FT                                /FTId=VAR_002798.
FT   VARIANT      78     78       N -> H (IN DAVENPORT).
FT                                /FTId=VAR_002799.
FT   VARIANT      78     78       N -> K (IN STANLEYVILLE-2).
FT                                /FTId=VAR_002800.
FT   VARIANT      80     80       L -> R (IN ANN ARBOR; UNSTABLE).
FT                                /FTId=VAR_002801.
FT   VARIANT      81     81       S -> C (IN NIGERIA).
FT                                /FTId=VAR_002802.
FT   VARIANT      82     82       A -> D (IN GARDEN STATE).
FT                                /FTId=VAR_002803.
FT   VARIANT      84     84       S -> R (IN ETOBICOKE; O2 AFFINITY UP).
FT                                /FTId=VAR_002804.
FT   VARIANT      85     85       D -> V (IN INKSTER; O2 AFFINITY UP).
FT                                /FTId=VAR_002805.
FT   VARIANT      85     85       D -> Y (IN ATAGO; O2 AFFINITY UP).
FT                                /FTId=VAR_002806.
FT   VARIANT      86     86       L -> R (IN MOABIT; UNSTABLE).
FT                                /FTId=VAR_002807.
FT   VARIANT      87     87       H -> N (IN AUCKLAND; UNSTABLE).
FT                                /FTId=VAR_002808.
FT   VARIANT      87     87       H -> R (IN IWATA; UNSTABLE).
FT                                /FTId=VAR_002809.
FT   VARIANT      88     88       A -> S (IN LOIRE; O2 AFFINITY UP).
FT                                /FTId=VAR_002810.
FT   VARIANT      90     90       K -> M (IN HANDA; O2 AFFINITY UP).
FT                                /FTId=VAR_002811.
FT   VARIANT      91     91       L -> P (IN PORT PHILLIP; UNSTABLE).
FT                                /FTId=VAR_002812.
FT   VARIANT      92     92       R -> Q (IN J-CAPE TOWN; O2 AFFINITY UP).
FT                                /FTId=VAR_002813.
FT   VARIANT      94     94       D -> Y (IN SETIF; UNSTABLE).
FT                                /FTId=VAR_002814.
FT   VARIANT      95     95       P -> A (IN DENMARK HILL; O2 AFFINITY UP).
FT                                /FTId=VAR_002815.
FT   VARIANT      95     95       P -> T (IN GODAVARI; O2 AFFINITY UP).
FT                                /FTId=VAR_002816.
FT   VARIANT      97     97       N -> K (IN DALLAS; O2 AFFINITY UP).
FT                                /FTId=VAR_002817.
FT   VARIANT      99     99       K -> E (IN TURRIFF).
FT                                /FTId=VAR_002818.
FT   VARIANT     102    102       S -> R (IN MANITOBA; SLIGHTLY UNSTABLE).
FT                                /FTId=VAR_002819.
FT   VARIANT     103    103       H -> R (IN CONTALDO; UNSTABLE).
FT                                /FTId=VAR_002820.
FT   VARIANT     109    109       L -> R (IN SUAN-DOK; UNSTABLE;
FT                                CAUSES ALPHA-THALASSEMIA).
FT                                /FTId=VAR_002821.
FT   VARIANT     110    110       A -> D (IN PETAH TIKVA; UNSTABLE;
FT                                CAUSES ALPHA-THALASSEMIA).
FT                                /FTId=VAR_002822.
FT   VARIANT     112    112       H -> D (IN HOPKINS-II; UNSTABLE).
FT                                /FTId=VAR_002823.
FT   VARIANT     113    113       L -> H (IN TWIN PEAKS).
FT                                /FTId=VAR_002824.
FT   VARIANT     114    114       P -> L (IN NOUAKCHOTT).
FT                                /FTId=VAR_002825.
FT   VARIANT     114    114       P -> R (IN CHIAPAS).
FT                                /FTId=VAR_002826.
FT   VARIANT     114    114       P -> S (IN MELUSINE).
FT                                /FTId=VAR_002827.
FT   VARIANT     115    115       A -> D (IN J-TONGARIKI).
FT                                /FTId=VAR_002828.
FT   VARIANT     116    116       E -> A (IN UBE-4).
FT                                /FTId=VAR_002829.
FT   VARIANT     116    116       E -> EHLPAE (IN ZAIRE).
FT                                /FTId=VAR_002830.
FT   VARIANT     117    117       F -> FI (IN PHNOM PENH).
FT                                /FTId=VAR_002831.
FT   VARIANT     118    118       T -> TEFT (IN GRADY).
FT                                /FTId=VAR_002832.
FT   VARIANT     120    120       A -> E (IN J-MEERUT/J-BIRMINGHAM).
FT                                /FTId=VAR_002833.
FT   VARIANT     121    121       V -> M (IN OWARI).
FT                                /FTId=VAR_002834.
FT   VARIANT     122    122       H -> Q (IN WESTMEAD).
FT                                /FTId=VAR_002835.
FT   VARIANT     125    125       L -> P (IN QUONG SZE;
FT                                CAUSES ALPHA-THALASSEMIA).
FT                                /FTId=VAR_002836.
FT   VARIANT     126    126       D -> V (IN FUKUTOMI; O2 AFFINITY UP).
FT                                /FTId=VAR_002837.
FT   VARIANT     126    126       D -> Y (IN MONTERIORE; O2 AFFINITY UP).
FT                                /FTId=VAR_002838.
FT   VARIANT     127    127       K -> N (IN JACKSON).
FT                                /FTId=VAR_002839.
FT   VARIANT     129    129       L -> P (IN TUNIS-BIZERTE; UNSTABLE;
FT                                CAUSES ALPHA-THALASSEMIA).
FT                                /FTId=VAR_002840.
FT   VARIANT     130    130       A -> P (IN SUN PRAIRIE; UNSTABLE).
FT                                /FTId=VAR_002841.
FT   VARIANT     130    130       A -> D (IN YUDA; O2 AFFINITY DOWN).
FT                                /FTId=VAR_002842.
FT   VARIANT     131    131       S -> P (IN QUESTEMBERT; HIGHLY UNSTABLE;
FT                                CAUSES ALPHA-THALASSEMIA).
FT                                /FTId=VAR_002843.
FT   VARIANT     133    133       S -> R (IN VAL DE MARNE; O2 AFFINITY UP).
FT                                /FTId=VAR_002844.
FT   VARIANT     135    135       V -> E (IN PAVIE).
FT                                /FTId=VAR_002845.
FT   VARIANT     136    136       L -> M (IN CHICAGO).
FT                                /FTId=VAR_002846.
FT   VARIANT     136    136       L -> P (IN BIBBA; UNSTABLE;
FT                                CAUSES ALPHA-THALASSEMIA).
FT                                /FTId=VAR_002847.
FT   VARIANT     138    138       S -> P (IN ATTLEBORO; O2 AFFINITY UP).
FT                                /FTId=VAR_002848.
FT   VARIANT     139    139       K -> E (IN HANAKAMI; O2 AFFINITY UP).
FT                                /FTId=VAR_002849.
FT   VARIANT     139    139       K -> T (IN TOKONAME; O2 AFFINITY UP).
FT                                /FTId=VAR_002850.
FT   VARIANT     140    140       Y -> H (IN ROUEN; O2 AFFINITY UP).
FT                                /FTId=VAR_002851.
FT   VARIANT     141    141       R -> C (IN NUNOBIKI; O2 AFFINITY UP).
FT                                /FTId=VAR_002852.
FT   VARIANT     141    141       R -> L (IN LEGNANO; O2 AFFINITY UP).
FT                                /FTId=VAR_002853.
FT   VARIANT     141    141       R -> H (IN SURESNES; O2 AFFINITY UP).
FT                                /FTId=VAR_002854.
FT   VARIANT     141    141       R -> P (IN SINGAPORE).
FT                                /FTId=VAR_002855.
FT   HELIX         4     35
FT   HELIX        37     42
FT   TURN         44     45
FT   TURN         50     51
FT   HELIX        53     71
FT   TURN         72     74
FT   HELIX        76     79
FT   TURN         80     80
FT   HELIX        81     89
FT   TURN         90     91
FT   TURN         95     95
FT   HELIX        96    112
FT   TURN        114    116
FT   HELIX       119    136
FT   TURN        137    139
SQ   SEQUENCE   141 AA;  15126 MW;  5EC7DB1E CRC32;
     VLSPADKTNV KAAWGKVGAH AGEYGAEALE RMFLSFPTTK TYFPHFDLSH GSAQVKGHGK
     KVADALTNAV AHVDDMPNAL SALSDLHAHK LRVDPVNFKL LSHCLLVTLA AHLPAEFTPA
     VHASLDKFLA SVSTVLTSKY R
//
ID   HBB_HUMAN      STANDARD;      PRT;   146 AA.
AC   P02023;
DT   21-JUL-1986 (Rel. 01, Created)
DT   21-JUL-1986 (Rel. 01, Last sequence update)
DT   15-JUL-1999 (Rel. 38, Last annotation update)
DE   HEMOGLOBIN BETA CHAIN.
GN   HBB.
OS   Homo sapiens (Human), Pan troglodytes (Chimpanzee), and
OS   Pan paniscus (Pygmy chimpanzee) (Bonobo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Mammalia;
OC   Eutheria; Primates; Catarrhini; Hominidae; Homo.
RN   [1]
RP   SEQUENCE.
RC   SPECIES=HUMAN;
RA   BRAUNITZER G., GEHRING-MULLER R., HILSCHMANN N., HILSE K., HOBOM G.,
RA   RUDLOFF V., WITTMANN-LIEBOLD B.;
RT   "The constitution of normal adult human haemoglobin.";
RL   Hoppe-Seyler's Z. Physiol. Chem. 325:283-286(1961).
RN   [2]
RP   SEQUENCE FROM N.A.
RC   SPECIES=HUMAN;
RX   MEDLINE; 81064667.
RA   LAWN R.M., EFSTRATIADIS A., O'CONNELL C., MANIATIS T.;
RT   "The nucleotide sequence of the human beta-globin gene.";
RL   Cell 21:647-651(1980).
RN   [3]
RP   SEQUENCE OF 121-146 FROM N.A.
RC   SPECIES=HUMAN;
RX   MEDLINE; 85205333.
RA   LANG K.M., SPRITZ R.A.;
RT   "Cloning specific complete polyadenylylated 3'-terminal cDNA
RT   segments.";
RL   Gene 33:191-196(1985).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF DEOXYHEMOGLOBIN.
RC   SPECIES=HUMAN;
RX   MEDLINE; 76027820.
RA   FERMI G.;
RT   "Three-dimensional fourier synthesis of human deoxyhaemoglobin at
RT   2.5-A resolution: refinement of the atomic model.";
RL   J. Mol. Biol. 97:237-256(1975).
RN   [5]
RP   SEQUENCE.
RC   SPECIES=P.TROGLODYTES;
RX   MEDLINE; 66071496.
RA   RIFKIN D.B., KONIGSBERG W.;
RT   "The characterization of the tryptic peptides from the hemoglobin of
RT   the chimpanzee (Pan troglodytes).";
RL   Biochim. Biophys. Acta 104:457-461(1965).
RN   [6]
RP   SEQUENCE.
RC   SPECIES=P.PANISCUS;
RX   MEDLINE; 83219265.
RA   GOODMAN M., BRAUNITZER G., STANGL A., SCHRANK B.;
RT   "Evidence on human origins from haemoglobins of African apes.";
RL   Nature 303:546-548(1983).
RN   [7]
RP   HAPTOGLOBIN BINDING.
RX   MEDLINE; 86242088.
RA   YOSHIOKA N., ATASSI M.Z.;
RT   "Haemoglobin binding with haptoglobin. Localization of the
RT   haptoglobin-binding sites on the beta-chain of human haemoglobin by
RT   synthetic overlapping peptides encompassing the entire chain.";
RL   Biochem. J. 234:453-456(1986).
RN   [8]
RP   GLYCATION IN N-TERMINUS.
RX   MEDLINE; 78138698.
RA   BUNN H.F., GABBAY K.H., GALLOP P.M.;
RT   "The glycosylation of hemoglobin: relevance to diabetes mellitus.";
RL   Science 200:21-27(1978).
RN   [9]
RP   VARIANT ALABAMA.
RX   MEDLINE; 75109326.
RA   BRIMHALL B., JONES R.T., SCHNEIDER R.G., HOSTY T.S., TOMLIN G.,
RA   ATKINS R.;
RT   "Two new hemoglobins. Hemoglobin Alabama (beta39(C5)Gln leads to Lys)
RT   and hemoglobin Montgomery (alpha 48(CD 6) Leu leads to Arg).";
RL   Biochim. Biophys. Acta 379:28-32(1975).
RN   [10]
RP   VARIANT ALESHA.
RX   MEDLINE; 93322192.
RA   MOLCHANOVA T.P., POSTNIKOV Y.V., POBEDIMSKAYA D.D., SMETANINA N.S.,
RA   MOSCHAN A.A., KAZANETZ E.G., TOKAREV Y.N., HUISMAN T.H.J.;
RT   "Hb Alesha or alpha 2 beta (2)67(E11)Val-->Met: a new unstable
RT   hemoglobin variant identified through sequencing of amplified DNA.";
RL   Hemoglobin 17:217-225(1993).
RN   [11]
RP   VARIANT J-ALTGELDS GARDENS.
RX   MEDLINE; 79067354.
RA   ADAMS J.G. III, PRZYWARA K.P., HELLER P., SHAMSUDDIN M.;
RT   "Hemoglobin J Altgeld Gardens. A hemoglobin variant with a
RT   substitution of the proximal histidine of the beta-chain.";
RL   Hemoglobin 2:403-415(1978).
RN   [12]
RP   VARIANT ANKARAS.
RX   MEDLINE; 74297498.
RA   ARCASOY A., CASEY R., LEHMANN H., CAVDAR A.O., BERKI A.;
RT   "A new haemoglobin J from Turkey -- Hb Ankara (beta10 (A7) Ala-Asp).";
RL   FEBS Lett. 42:121-123(1974).
RN   [13]
RP   VARIANTS J-ANTAKYA AND COMPLUTENSE.
RX   MEDLINE; 86216227.
RA   HUISMAN T.H.J., WILSON J.B., KUTLAR A., YANG K.-G., CHEN S.-S.,
RA   WEBBER B.B., ALTAY C., MARTINEZ A.V.;
RT   "Hb J-Antakya or alpha 2 beta (2)65(E9)Lys-->Met in a Turkish family
RT   and Hb complutense or alpha 2 beta (2)127(H5)Gln-->Glu in a Spanish
RT   family; correction of a previously published identification.";
RL   Biochim. Biophys. Acta 871:229-231(1986).
RN   [14]
RP   VARIANT J-AUCKLAND.
RX   MEDLINE; 88006903.
RA   WILLIAMSON D., WELLS R.M.G., ANDERSON R., MATTHEWS J.;
RT   "A new unstable and low oxygen affinity hemoglobin variant: Hb J-
RT   Auckland [beta 25(B7)Gly-->Asp].";
RL   Hemoglobin 11:221-230(1987).
RN   [15]
RP   VARIANT AURORA.
RX   MEDLINE; 96352910.
RA   LAFFERTY J., ALI M., MATTHEW K., ENG B., PATTERSON M., WAYE J.S.;
RT   "Identification of a new high oxygen affinity hemoglobin variant: Hb
RT   Aurora [beta 139(H17) Asn-->Tyr].";
RL   Hemoglobin 19:335-341(1995).
RN   [16]
RP   VARIANT BREST.
RX   MEDLINE; 88256755.
RA   BAUDIN-CHICH V., WAJCMAN H., GOMBAUD-SAINTONGE G., AROUS N., RIOU J.,
RA   BRIERE J., GALACTEROS F.;
RT   "Hemoglobin Brest [beta 127 (H5)Gln-->Lys] a new unstable human
RT   hemoglobin variant located at the alpha 1 beta 1 interface with
RT   specific electrophoretic behavior.";
RL   Hemoglobin 12:179-188(1988).
RN   [17]
RP   VARIANT BRISBANE.
RX   MEDLINE; 81239159.
RA   BRENNAN S.O., WELLS R.M., SMITH H., CARRELL R.W.;
RT   "Hemoglobin Brisbane: beta68 Leu replaced by His. A new high oxygen
RT   affinity variant.";
RL   Hemoglobin 5:325-335(1981).
RN   [18]
RP   VARIANT BUNBURY.
RX   MEDLINE; 84031649.
RA   COMO P.F., KENNETT D., WILKINSON T., KRONENBERG H.;
RT   "A new hemoglobin with high oxygen affinity -- hemoglobin Bunbury:
RT   alpha 2 beta 2 [94 (FG1) Asp replaced by Asn].";
RL   Hemoglobin 7:413-421(1983).
RN   [19]
RP   VARIANT J-CAIRO.
RX   MEDLINE; 76114933.
RA   GAREL M.-C., HASSAN W., COQUELET M.T., GOOSSENS M., ROSA J., AROUS N.;
RT   "Hemoglobin J Cairo: beta 65 (E9) Lys leads to Gln, A new hemoglobin
RT   variant discovered in an Egyptian family.";
RL   Biochim. Biophys. Acta 420:97-104(1976).
RN   [20]
RP   VARIANT CAMPERDOWN.
RX   MEDLINE; 75184109.
RA   WILKINSON T., CHUA C.G., CARRELL R.W., ROBIN H., EXNER T., LEE K.M.,
RA   KRONENBERG H.;
RT   "A new haemoglobin variant, haemoglobin Camperdown (beta 104 (G6)
RT   arginine->serine).";
RL   Biochim. Biophys. Acta 393:195-200(1975).
RN   [21]
RP   VARIANT CARIBBEAN.
RX   MEDLINE; 77048866.
RA   AHERN E., AHERN V., HILTON T., SERJEANT G.R., SERJEANT B.E.,
RA   SEAKINS M., LANG A., MIDDLETON A., LEHMANN H.;
RT   "Haemoglobin caribbean beta91 (F7) Leu replaced by Arg: a mildly
RT   haemoglobin with a low oxygen affinity.";
RL   FEBS Lett. 69:99-102(1976).
RN   [22]
RP   VARIANT CITY OF HOPE.
RX   MEDLINE; 85006311.
RA   RAHBAR S., ASMEROM Y., BLUME K.G.;
RT   "A silent hemoglobin variant detected by HPLC: hemoglobin City of
RT   Hope beta 69 (E13) Gly-->Ser.";
RL   Hemoglobin 8:333-342(1984).
RN   [23]
RP   VARIANT COIMBRA.
RX   MEDLINE; 92267852.
RA   TAMAGNINI G.P., RIBEIRO M.L., VALENTE V., RAMACHANDRAN M.,
RA   WILSON J.B., BAYSAL E., GU L.H., HUISMAN T.H.J.;
RT   "Hb Coimbra or alpha 2 beta (2)99(G1)Asp-->Glu, a newly discovered
RT   high oxygen affinity variant.";
RL   Hemoglobin 15:487-496(1991).
RN   [24]
RP   VARIANT COSTA RICA.
RX   MEDLINE; 96235282.
RA   ROMERO W.E.R., CASTILLO M., CHAVES M.A., SAENZ G.F., GU L.-H.,
RA   WILSON J.B., BAYSAL E., SMETANINA N.S., LEONOVA J.Y., HUISMAN T.H.J.;
RT   "Hb Costa Rica or alpha 2 beta 2 77(EF1)His-->Arg: the first
RT   example of a somatic cell mutation in a globin gene.";
RL   Hum. Genet. 97:829-833(1996).
RN   [25]
RP   VARIANT DEBROUSSE.
RX   MEDLINE; 96180033.
RA   LACAN P., KISTER J., FRANCINA A., SOUILLET G., GALACTEROS F.,
RA   DELAUNAY J., WAJCMAN H.;
RT   "Hemoglobin Debrousse (beta 96[FG3]Leu-->Pro): a new unstable
RT   hemoglobin with twofold increased oxygen affinity.";
RL   Am. J. Hematol. 51:276-281(1996).
RN   [26]
RP   VARIANT DHONBURI.
RX   MEDLINE; 90379198.
RA   BARDAKDJIAN-MICHAU J., FUCHAROEN S., DELANOE-GARIN J., KISTER J.,
RA   LACOMBE C., WINICHAGOON P., BLOUQUIT Y., RIOU J., WASI P.,
RA   GALACTEROS F.;
RT   "Hemoglobin Dhonburi alpha 2 beta 2 126 (H4) Val-->Gly: a new
RT   unstable beta variant producing a beta-thalassemia intermedia
RT   phenotype in association with beta zero-thalassemia.";
RL   Am. J. Hematol. 35:96-99(1990).
RN   [27]
RP   VARIANT DUINO (HB NEWCASTLE AND HB CAMPERDOWN).
RX   MEDLINE; 92380658.
RA   WAJCMAN H., BLOUQUIT Y., VASSEUR C., LE QUERREC A., LANIECE M.,
RA   MELEVENDI C., RASORE A., GALACTEROS F.;
RT   "Two new human hemoglobin variants caused by unusual mutational
RT   events: Hb Zaire contains a five residue repetition within the
RT   alpha-chain and Hb Duino has two residues substituted in the
RT   beta-chain.";
RL   Hum. Genet. 89:676-680(1992).
RN   [28]
RP   VARIANT J-EUROPA.
RX   MEDLINE; 96407264.
RA   KIGER L., KISTER J., GROFF P., KALMES G., PROME D., GALACTEROS F.,
RA   WAJCMAN H.;
RT   "Hb J-Europa [beta 62(E6)Ala-->Asp]: normal oxygen binding properties
RT   in a new variant involving a residue located distal to the heme.";
RL   Hemoglobin 20:135-140(1996).
RN   [29]
RP   VARIANT GEELONG.
RX   MEDLINE; 92010939.
RA   COMO P.F., HOCKING D.R., SWINTON G.W., TRENT R.J., HOLLAND R.A.,
RA   TIBBEN E.A., WILKINSON T., KRONENBERG H.;
RT   "Hb Geelong [beta 139(H17)Asn-->Asp].";
RL   Hemoglobin 15:85-95(1991).
RN   [30]
RP   VARIANT GRANGE-BLANCHE.
RX   MEDLINE; 88030044.
RA   BAKLOUTI F., GIRAUD Y., FRANCINA A., RICHARD G., PERIER C.,
RA   GEYSSANT A., JAUBERT J., BRIZARD C., DELAUNAY J.;
RT   "Hemoglobin Grange-Blanche [beta 27(B9) Ala-->Val], a new variant
RT   with normal expression and increased affinity for oxygen.";
RL   FEBS Lett. 223:59-62(1987).
RN   [31]
RP   VARIANT GRAZ.
RX   MEDLINE; 93138927.
RA   LIU J.S., MOLCHANOVA T.P., GU L.H., WILSON J.B., HOPMEIER P.,
RA   SCHNEDL W., BALAUN E., KREJS G.J., HUISMAN T.H.J.;
RT   "Hb Graz or alpha 2 beta 2(2)(NA2)His-->Leu; a new beta chain variant
RT   observed in four families from southern Austria.";
RL   Hemoglobin 16:493-501(1992).
RN   [32]
RP   VARIANT HELSINKI.
RX   MEDLINE; 77062201.
RA   IKKALA E., KOSKELA J., PIKKARAINEN P., RAHIALA E.-L., EL-HAZMI M.A.F.,
RA   NAGAI K., LANG A., LEHMANN H.;
RT   "Hb Helsinki: a variant with a high oxygen affinity and a
RT   substitution at a 2,3-DPG binding site (beta82[EF6] Lys replaced by
RT   Met).";
RL   Acta Haematol. 56:257-275(1976).
RN   [33]
RP   VARIANT HIMEJI.
RX   MEDLINE; 86167527.
RA   OHBA Y., MIYAJI T., MURAKAMI M., KADOWAKI S., FUJITA T., OIMOMI M.,
RA   HATANAKA H., ISHIKAWA K., BABA S., HITAKA K., IMAI K.;
RT   "Hb Himeji or beta 140 (H18) Ala-->Asp. A slightly unstable
RT   hemoglobin with increased beta N-terminal glycation.";
RL   Hemoglobin 10:109-126(1986).
RN   [34]
RP   VARIANT HINSDALE.
RX   MEDLINE; 90093866.
RA   MOO-PENN W.F., JOHNSON M.H., JUE D.L., LONSER R.;
RT   "Hb Hinsdale [beta 139 (H17)Asn-->Lys]: a variant in the central
RT   cavity showing reduced affinity for oxygen and
RT   2,3-diphosphoglycerate.";
RL   Hemoglobin 13:455-464(1989).
RN   [35]
RP   VARIANT HINWIL.
RX   MEDLINE; 96351651.
RA   FRISCHKNECHT H., VENTRUTO M., HESS D., HUNZIKER P., ROSATELLI M.C.,
RA   CAO A., BREITENSTEIN U., FEHR J., TUCHSCHMID P.;
RT   "HB Hinwil or beta 38(C4)Thr-->Asn: a new beta chain variant detected
RT   in a Swiss family.";
RL   Hemoglobin 20:31-40(1996).
RN   [36]
RP   VARIANT HOWICK.
RX   MEDLINE; 94193408.
RA   OWEN M.C., OCKELFORD P.A., WELLS R.M.G.;
RT   "Hb Howick [beta 37(C3)Trp-->Gly]: a new high oxygen affinity variant
RT   of the alpha 1 beta 2 contact.";
RL   Hemoglobin 17:513-521(1993).
RN   [37]
RP   VARIANT INDIANAPOLIS.
RX   MEDLINE; 79151109.
RA   ADAMS J.G. III, STEINBERG M.H., BOXER L.A., BAEHNER R.L., FORGET B.G.,
RA   TSISTRAKIS G.A.;
RT   "The structure of hemoglobin Indianapolis [beta112(G14) arginine]. An
RT   unstable variant detectable only by isotopic labeling.";
RL   J. Biol. Chem. 254:3479-3482(1979).
RN   [38]
RP   VARIANT ISEHARA.
RX   MEDLINE; 92155974.
RA   HARANO T., HARANO K., KUSHIDA Y., UEDA S., YOSHII A., NISHINARITA M.;
RT   "Hb Isehara (or Hb Redondo) [beta 92 (F8) His-->Asn]: an unstable
RT   variant with a proximal histidine substitution at the heme contact.";
RL   Hemoglobin 15:279-290(1991).
RN   [39]
RP   VARIANT ISTAMBUL.
RX   MEDLINE; 73054825.
RA   AKSOY M., ERDEM S., EFREMOV G.D., WILSON J.B., HUISMAN T.H.J.,
RA   SCHROEDER W.A., SHELTON J.R., SHELTON J.B., ULITIN O.N.,
RA   MUFTUOGLU A.;
RT   "Hemoglobin Istanbul: substitution of glutamine for histidine in a
RT   proximal histidine (F8(92) ).";
RL   J. Clin. Invest. 51:2380-2387(1972).
RN   [40]
RP   VARIANT JACKSONVILLE.
RX   MEDLINE; 91331861.
RA   GAUDRY C.L. JR., PITEL P.A., JUE D.L., HINE T.K., JOHNSON M.H.,
RA   MOO-PENN W.F.;
RT   "Hb Jacksonville [alpha 2 beta 2(54)(D5)Val-->Asp]: a new unstable
RT   variant found in a patient with hemolytic anemia.";
RL   Hemoglobin 14:653-659(1990).
RN   [41]
RP   VARIANT JIANGHUA.
RX   MEDLINE; 84007581.
RA   LU Y.Q., FAN J.L., LIU J.F., HU H.L., PENG X.H., HUANG C.H.,
RA   HUANG P.Y., CHEN S.S., JAI P.C., YANG K.G.;
RT   "Hemoglobin Jianghua [beta 120(GH3) LYS leads to ILE]: a new
RT   fast-moving variant found in China.";
RL   Hemoglobin 7:321-326(1983).
RN   [42]
RP   VARIANT KARLSKOGA.
RX   MEDLINE; 93322190.
RA   LANDIN B.;
RT   "Hb Karlskoga or alpha 2 beta (2)21(B3) Asp-->His: a new slow-moving
RT   variant found in Sweden.";
RL   Hemoglobin 17:201-208(1993).
RN   [43]
RP   VARIANT KNOSSOS.
RX   MEDLINE; 83079719.
RA   AROUS N., GALACTEROS F., FESSAS P., LOUKOPOULOS D., BLOUQUIT Y.,
RA   KOMIS G., SELLAYE M., BOUSSIOU M., ROSA J.;
RT   "Structural study of hemoglobin Knossos, beta 27 (B9) Ala leads to
RT   Ser. A new abnormal hemoglobin present as a silent
RT   beta-thalassemia.";
RL   FEBS Lett. 147:247-250(1982).
RN   [44]
RP   VARIANT KODAIRA.
RX   MEDLINE; 92340295.
RA   HARANO T., HARANO K., KUSHIDA Y., IMAI K., NISHINAKAMURA R.,
RA   MATSUNAGA T.;
RT   "Hb Kodaira [beta 146(HC3)His-->Gln]: a new beta chain variant with
RT   an amino acid substitution at the C-terminus.";
RL   Hemoglobin 16:85-91(1992).
RN   [45]
RP   VARIANT KOFU.
RX   MEDLINE; 86303641.
RA   HARANO T., HARANO K., UEDA S., IMAI N., KITAZUMI T.;
RT   "A new electrophoretically-silent hemoglobin variant: hemoglobin Kofu
RT   or alpha 2 beta 2 84 (EF8) Thr-->Ile.";
RL   Hemoglobin 10:417-420(1986).
RN   [46]
RP   VARIANT KRALOVE.
RX   MEDLINE; 94042221.
RA   DIVOKY V., SVOBODOVA M., INDRAK K., CHROBAK L., MOLCHANOVA T.P.,
RA   HUISMAN T.H.J.;
RT   "Hb Hradec Kralove (Hb HK) or alpha 2 beta 2 115(G17)Ala-->Asp, a
RT   severely unstable hemoglobin variant resulting in a dominant beta-
RT   thalassemia trait in a Czech family.";
RL   Hemoglobin 17:319-328(1993).
RN   [47]
RP   VARIANT LA DESIRADE.
RX   MEDLINE; 87165149.
RA   MERAULT G., KECLARD L., GARIN J., POYART C., BLOUQUIT Y., AROUS N.,
RA   GALACTEROS F., FEINGOLD J., ROSA J.;
RT   "Hemoglobin La Desirade alpha A2 beta 2 129 (H7) Ala-->Val: a new
RT   unstable hemoglobin.";
RL   Hemoglobin 10:593-605(1986).
RN   [48]
RP   VARIANT LAS PALMAS.
RX   MEDLINE; 88256753.
RA   MALCORRA-AZPIAZU J.J., BALDA-AGUIRRE M.I., DIAZ-CHICO J.C., HU H.,
RA   WILSON J.B., WEBBER B.B., KUTLAR F., KUTLAR A., HUISMAN T.H.J.;
RT   "Hb Las Palmas or alpha 2 beta 2(49)(CD8)Ser-->Phe, a mildly
RT   unstable hemoglobin variant.";
RL   Hemoglobin 12:163-170(1988).
RN   [49]
RP   VARIANT LINKOEPING.
RX   MEDLINE; 88083482.
RA   BERLIN G., WRANNE B., JEPPSSON J.-O.;
RT   "Hb Linkoping (beta 36 Pro-->Thr): a new high oxygen affinity
RT   hemoglobin variant found in two families of Finnish origin.";
RL   Eur. J. Haematol. 39:452-456(1987).
RN   [50]
RP   VARIANT MAPUTO.
RX   MEDLINE; 84031650.
RA   MARINUCCI M., BOISSEL J.P., MASSA A., WAJCMAN H., TENTORI L.,
RA   LABIE D.;
RT   "Hemoglobin Maputo: a new beta-chain variant (alpha 2 beta 2 47 (CD6)
RT   Asp replaced by Tyr) in combination with hemoglobin S, identified by
RT   high performance liquid chromatography (HPLC).";
RL   Hemoglobin 7:423-433(1983).
RN   [51]
RP   VARIANT MATERA.
RX   MEDLINE; 90346586.
RA   SCIARRATTA G.V., IVALDI G.;
RT   "Hb Matera [beta 55(D6)Met-->Lys]: a new unstable hemoglobin variant
RT   in an Italian family.";
RL   Hemoglobin 14:79-85(1990).
RN   [52]
RP   VARIANT MIYASHIRO.
RX   MEDLINE; 82166873.
RA   NAKATSUJI T., MIWA S., OHBA Y., HATTORI Y., MIYAJI T., MIYATA H.,
RA   SHINOHARA T., HORI T., TAKAYAMA J.;
RT   "Hemoglobin Miyashiro (beta 23[B5] val substituting for gly) an
RT   electrophoretically silent variant discovered by the isopropanol
RT   test.";
RL   Hemoglobin 5:653-666(1981).
RN   [53]
RP   VARIANT MIZUHO.
RX   MEDLINE; 77248961.
RA   OHBA Y., MIYAJI T., MATSUOKA M., SUGIYAMA K., SUZUKI T., SUGIURA T.;
RT   "Hemoglobin Mizuho or beta 68 (E 12) leucine leads to proline, a new
RT   unstable variant associated with severe hemolytic anemia.";
RL   Hemoglobin 1:467-477(1977).
RN   [54]
RP   VARIANT MUSCAT.
RX   MEDLINE; 92387956.
RA   RAMACHANDRAN M., GU L.H., WILSON J.B., KITUNDU M.N., ADEKILE A.D.,
RA   LIU J.C., MCKIE K.M., HUISMAN T.H.;
RT   "A new variant, HB Muscat [alpha 2 beta (2)32(B14)Leu-->Val]
RT   observed in association with HB S in an Arabian family.";
RL   Hemoglobin 16:259-266(1992).
RN   [55]
RP   VARIANT N-TIMONE.
RX   MEDLINE; 90236754.
RA   LENA-RUSSO D., ORSINI A., VOVAN L., BARDAKDJIAN-MICHAU J., LACOMBE C.,
RA   BLOUQUIT Y., CRAESCU C.T., GALACTEROS F.;
RT   "Hb N-Timone [alpha 2 beta 2(8)(A5)Lys-->Glu]: a new fast-moving
RT   variant with normal stability and oxygen affinity.";
RL   Hemoglobin 13:743-747(1989).
RN   [56]
RP   VARIANT NAGOYA.
RX   MEDLINE; 85206960.
RA   OHBA Y., IMANAKA M., MATSUOKA M., HATTORI Y., MIYAJI T., FUNAKI C.,
RA   SHIBATA K., SHIMOKATA H., KUZUYA F., MIWA S.;
RT   "A new unstable, high oxygen affinity hemoglobin: Hb Nagoya or beta
RT   97 (FG4) His-->Pro.";
RL   Hemoglobin 9:11-24(1985).
RN   [57]
RP   VARIANT D-NEATH.
RX   MEDLINE; 93322197.
RA   WELCH S.G., BATEMAN C.;
RT   "Hb D-Neath or beta 121 (GH4) Glu-->Ala: a new member of the Hb D
RT   family.";
RL   Hemoglobin 17:255-259(1993).
RN   [58]
RP   VARIANT NORTH CHICAGO.
RX   MEDLINE; 86139289.
RA   RAHBAR S., LOUIS J., LEE T., ASMEROM Y.;
RT   "Hemoglobin North Chicago (beta 36 [C2] proline-->serine): a new
RT   high affinity hemoglobin.";
RL   Hemoglobin 9:559-576(1985).
RN   [59]
RP   VARIANT NORTH SHORE.
RX   MEDLINE; 77246803.
RA   ARENDS T., LEHMANN H., PLOWMAN D., STATHOPOULOU R.;
RT   "Haemoglobin North Shore-Caracas beta 134 (H12) valine replaced by
RT   glutamic acid.";
RL   FEBS Lett. 80:261-265(1977).
RN   [60]
RP   VARIANT OLOMOUC.
RX   MEDLINE; 87307470.
RA   INDRAK K., WIEDERMANN B.F., BATEK F., WILSON J.B., WEBBER B.B.,
RA   KUTLAR A., HUISMAN T.H.J.;
RT   "Hb Olomouc or alpha 2 beta 2(86)(F2)Ala-->Asp, a new high oxygen
RT   affinity variant.";
RL   Hemoglobin 11:151-155(1987).
RN   [61]
RP   VARIANT PALMERSTON NORTH.
RX   MEDLINE; 83135041.
RA   BRENNAN S.O., WILLIAMSON D., WHISSON M.E., CARRELL R.W.;
RT   "Hemoglobin Palmerston North beta 23 (B5) Val replaced by Phe. A new
RT   variant identified in a patient with polycythemia.";
RL   Hemoglobin 6:569-575(1982).
RN   [62]
RP   VARIANT PIERRE-BENITE.
RX   MEDLINE; 88256754.
RA   BAKLOUTI F., GIRAUD Y., FRANCINA A., RICHARD G., FAVRE-GILLY J.,
RA   DELAUNAY J.;
RT   "Hemoglobin Pierre-Benite [beta 90(F6)Glu-->Asp], a new high
RT   affinity variant found in a French family.";
RL   Hemoglobin 12:171-177(1988).
RN   [63]
RP   VARIANT PRESBYTERIAN.
RX   MEDLINE; 78215075.
RA   MOO-PENN W.F., WOLFF J.A., SIMON G., VACEK M., JUE D.L., JOHNSON M.H.;
RT   "Hemoglobin Presbyterian: beta108 (G10) asparagine leads to lysine, A
RT   hemoglobin variant with low oxygen affinity.";
RL   FEBS Lett. 92:53-56(1978).
RN   [64]
RP   VARIANT PUTTELANGE.
RX   MEDLINE; 96101899.
RA   WAJCMAN H., GIRODON E., PROME D., NORTH M.L., PLASSA F., DUWIG I.,
RA   KISTER J., BERGERAT J.P., OBERLING F., LAMPERT E., LONSDORFER J.,
RA   GOOSSENS M., GALACTEROS F.;
RT   "Germline mosaicism for an alanine to valine substitution at residue
RT   beta 140 in hemoglobin Puttelange, a new variant with high oxygen
RT   affinity.";
RL   Hum. Genet. 96:711-716(1995).
RN   [65]
RP   VARIANT QUIN-HAI.
RX   MEDLINE; 84031648.
RA   JEN P.C., CHEN L.C., CHEN P.F., WONG Y., CHEN L.F., GUO Y.Y.,
RA   CHANG F.Q., CHOW Y.C., CHIU Y.;
RT   "Hemoglobin Quin-Hai, beta 78 (EF2) Leu replaced by Arg, a new
RT   abnormal hemoglobin found in Guangdong, China.";
RL   Hemoglobin 7:407-412(1983).
RN   [66]
RP   VARIANT RAMBAM.
RX   MEDLINE; 98432396.
RA   BISSE E., ZORN N., EIGEL A., LIZAMA M., HUAMAM-GUILLEN P., MARZ W.,
RA   VAN DORSSELAER A., WIELAND H.;
RT   "Hemoglobin Rambam (beta69[E13]Gly-->Asp), a pitfall in the
RT   assessment of diabetic control: characterization by electrospray mass
RT   spectrometry and HPLC.";
RL   Clin. Chem. 44:2172-2177(1998).
RN   [67]
RP   VARIANT RANDWICK.
RX   MEDLINE; 88256752.
RA   GILBERT A.T., FLEMING P.J., SUMNER D.R., HUGHES W.G., IP F.,
RA   KWAN Y.L., HOLLAND R.A.;
RT   "Hemoglobin Randwick or beta 15 (A12)Trp-->Gly: a new unstable beta-
RT   chain hemoglobin variant.";
RL   Hemoglobin 12:149-161(1988).
RN   [68]
RP   VARIANT RIO GRANDE.
RX   MEDLINE; 83185445.
RA   MOO-PENN W.F., JOHNSON M.H., MCGUFFEY J.E., JUE D.L.,
RA   THERRELL B.L. JR.;
RT   "Hemoglobin Rio Grande [beta 8 (A5) Lys leads to Thr] a new variant
RT   found in a Mexican-American family.";
RL   Hemoglobin 7:91-95(1983).
RN   [69]
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF VARIANT ROTSCHILD.
RX   MEDLINE; 92232710.
RA   KAVANAUGH J.S., ROGERS P.H., CASE D.A., ARNONE A.;
RT   "High-resolution X-ray study of deoxyhemoglobin Rothschild 37 beta
RT   Trp-->Arg: a mutation that creates an intersubunit chloride-binding
RT   site.";
RL   Biochemistry 31:4111-4121(1992).
RN   [70]
RP   VARIANT RUSH.
RX   MEDLINE; 74080282.
RA   ADAMS J.G. III, WINTER W.P., TAUSK K., HELLER P.;
RT   "Hemoglobin Rush (beta 101 (g3) glutamine): a new unstable hemoglobin
RT   causing mild hemolytic anemia.";
RL   Blood 43:261-269(1974).
RN   [71]
RP   VARIANT SAITAMA.
RX   MEDLINE; 83185440.
RA   OHBA Y., HASEGAWA Y., AMINO H., MIWA S., NAKATSUJI T., HATTORI Y.,
RA   MIYAJI T.;
RT   "Hemoglobin Saitama or beta 117 (G19) His leads to Pro, a new variant
RT   causing hemolytic disease.";
RL   Hemoglobin 7:47-56(1983).
RN   [72]
RP   VARIANT M-SASKATOON.
RA   GERALD P.S., EFRON M.L.;
RT   "Chemical studies of several varieties of Hb M.";
RL   Proc. Natl. Acad. Sci. U.S.A. 47:1758-1767(1961).
RN   [73]
RP   VARIANT SHELBY.
RX   MEDLINE; 85130256.
RA   MOO-PENN W.F., JOHNSON M.H., MCGUFFEY J.E., JUE D.L.;
RT   "Hemoglobin Shelby [beta 131(H9) Gln-->Lys] a correction to the
RT   structure of hemoglobin Deaconess and hemoglobin Leslie.";
RL   Hemoglobin 8:583-593(1984).
RN   [74]
RP   VARIANT J-SICILIA.
RX   MEDLINE; 74302182.
RA   RICCO G., PICH P.G., MAZZA U., ROSSI G., AJMAR P., ARESE P., GALLO E.;
RT   "Hb J Sicilia: beta 65 (E9) Lys-Asn, a beta homologue of Hb Zambia.";
RL   FEBS Lett. 39:200-204(1974).
RN   [75]
RP   VARIANT STANMORE.
RX   MEDLINE; 92010936.
RA   COMO P.F., WYLIE B.R., TRENT R.J., BRUCE D., VOLPATO F., WILKINSON T.,
RA   KRONENBERG H., HOLLAND R.A., TIBBEN E.A.;
RT   "A new unstable and low oxygen affinity hemoglobin variant: Hb
RT   Stanmore [beta 111(G13)Val-->Ala].";
RL   Hemoglobin 15:53-65(1991).
RN   [76]
RP   VARIANT ST MANDE.
RX   MEDLINE; 81212764.
RA   AROUS N., BRACONNIER F., THILLET J., BLOUQUIT Y., GALACTEROS F.,
RA   CHEVRIER M., BORDAHANDY C., ROSA J.;
RT   "Hemoglobin Saint Mande beta 102 (G4) asn replaced by tyr: a new low
RT   oxygen affinity variant.";
RL   FEBS Lett. 126:114-116(1981).
RN   [77]
RP   VARIANT WINDSOR.
RX   MEDLINE; 90093865.
RA   GILBERT A.T., FLEMING P.J., SUMNER D.R., HUGHES W.G., HOLLAND R.A.,
RA   TIBBEN E.A.;
RT   "Hemoglobin Windsor or beta 11 (A8)Val-->Asp: a new unstable
RT   beta-chain hemoglobin variant producing a hemolytic anemia.";
RL   Hemoglobin 13:437-453(1989).
RN   [78]
RP   VARIANT YAHATA.
RX   MEDLINE; 92010926.
RA   HARANO T., HARANO K., KUSHIDA Y., UEDA S.;
RT   "A new abnormal variant, Hb Yahata or beta 112(G14)Cys-->Tyr, found
RT   in a Japanese: structural confirmation by DNA sequencing of the beta-
RT   globin gene.";
RL   Hemoglobin 15:109-113(1991).
RN   [79]
RP   VARIANT YOKOHAMA.
RX   MEDLINE; 82166874.
RA   NAKATSUJI T., MIWA S., OHBA Y., HATTORI Y., MIYAJI T., HINO S.,
RA   MATSUMOTO N.;
RT   "A new unstable hemoglobin, Hb Yokohama beta 31 (B13)Leu substituting
RT   for Pro, causing hemolytic anemia.";
RL   Hemoglobin 5:667-678(1981).
CC   -!- PTM: GLUCOSE REACTS NONENZYMATICALLY WITH THE N-TERMINUS OF THE
CC       BETA CHAIN TO FORMS A STABLE KETOAMINE LINKAGE. THIS TAKES PLACE
CC       SLOWLY AND CONTINOUSLY THROUGHOUT THE 120-DAY LIFE-SPAN OF THE RED
CC       CELL. THE RATE OF GLYCATION IS INCREASED IN PATIENTS WITH DIABETES
CC       MELLITUS.
CC   -!- DISEASE: DEFICIENCY IN BETA-GLOBIN IS THE CAUSE OF SICKLE CELL
CC       ANEMIA AND POLYCYTHEMIA.
CC   -!- DATABASE: NAME=Hb variant; NOTE=Human hemoglobin variants;
CC       WWW="http://globin.cse.psu.edu/globin/html/huisman/variants/".
CC   --------------------------------------------------------------------------
CC   This SWISS-PROT entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use  by  non-profit  institutions as long  as its content  is  in  no  way
CC   modified and this statement is not removed.  Usage  by  and for commercial
CC   entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC   or send an email to license@isb-sib.ch).
CC   --------------------------------------------------------------------------
DR   EMBL; U01317; AAA16334.1; -.
DR   EMBL; V00497; CAA23756.1; -.
DR   EMBL; V00499; CAA23758.1; -.
DR   EMBL; V00500; CAA23759.1; ALT_SEQ.
DR   EMBL; L26462; AAA21100.1; -.
DR   EMBL; L26463; AAA21101.1; -.
DR   EMBL; L26464; AAA21102.1; -.
DR   EMBL; L26465; AAA21103.1; -.
DR   EMBL; L26466; AAA21104.1; -.
DR   EMBL; L26467; AAA21105.1; -.
DR   EMBL; L26468; AAA21106.1; -.
DR   EMBL; L26469; AAA21107.1; -.
DR   EMBL; L26470; AAA21108.1; -.
DR   EMBL; L26471; AAA21109.1; -.
DR   EMBL; L26472; AAA21110.1; -.
DR   EMBL; L26473; AAA21111.1; -.
DR   EMBL; L26474; AAA21112.1; -.
DR   EMBL; L26475; AAA21113.1; -.
DR   EMBL; L26476; AAA21114.1; -.
DR   EMBL; L26477; AAA21115.1; -.
DR   EMBL; L26478; AAA21116.1; -.
DR   EMBL; L48213; AAA88063.1; -.
DR   EMBL; L48214; AAA88061.1; -.
DR   EMBL; L48215; AAA88059.1; -.
DR   EMBL; L48216; AAA88065.1; -.
DR   EMBL; L48217; AAA88067.1; -.
DR   EMBL; M36640; AAA52634.1; -.
DR   EMBL; M11428; AAA52633.1; -.
DR   EMBL; A01592; CAA00182.1; -.
DR   PIR; A02352; HBHU.
DR   PIR; B93303; HBCZ.
DR   PIR; D93303; HBCZP.
DR   PDB; 1CBL; 31-JUL-94.
DR   PDB; 1CBM; 31-JUL-94.
DR   PDB; 1COH; 15-OCT-94.
DR   PDB; 1HBS; 29-OCT-85.
DR   PDB; 1HCO; 30-SEP-83.
DR   PDB; 2HCO; 30-SEP-83.
DR   PDB; 1HHO; 31-JAN-84.
DR   PDB; 2HHB; 18-JUL-84.
DR   PDB; 3HHB; 18-JUL-84.
DR   PDB; 4HHB; 17-JUL-84.
DR   PDB; 1THB; 15-JAN-91.
DR   PDB; 1NIH; 15-OCT-92.
DR   PDB; 1BAB; 31-JAN-94.
DR   PDB; 1BBB; 31-JAN-94.
DR   PDB; 1CMY; 31-OCT-93.
DR   PDB; 1DXT; 31-OCT-93.
DR   PDB; 1DXU; 31-OCT-93.
DR   PDB; 1DXV; 31-OCT-93.
DR   PDB; 1HBA; 31-JAN-94.
DR   PDB; 1HBB; 31-JAN-94.
DR   PDB; 2HBC; 07-FEB-95.
DR   PDB; 2HBD; 07-FEB-95.
DR   PDB; 2HBE; 07-FEB-95.
DR   PDB; 2HBF; 07-FEB-95.
DR   PDB; 2HBS; 23-JUL-97.
DR   PDB; 1HGA; 31-JAN-94.
DR   PDB; 1HGB; 31-JAN-94.
DR   PDB; 1HGC; 31-JAN-94.
DR   PDB; 2HHD; 26-JAN-95.
DR   PDB; 2HHE; 26-JAN-95.
DR   PDB; 1CLS; 14-OCT-96.
DR   PDB; 1GBU; 11-JAN-97.
DR   PDB; 1GBV; 11-JAN-97.
DR   PDB; 1GLI; 01-AUG-96.
DR   PDB; 1DSH; 31-MAR-95.
DR   PDB; 1HAB; 12-NOV-97.
DR   PDB; 1HAC; 12-NOV-97.
DR   PDB; 1HDB; 03-APR-96.
DR   PDB; 1SDK; 01-AUG-96.
DR   PDB; 1SDL; 01-AUG-96.
DR   PDB; 1AXF; 28-JAN-98.
DR   PDB; 1ABY; 25-FEB-98.
DR   PDB; 1A00; 18-MAR-98.
DR   PDB; 1A01; 18-MAR-98.
DR   PDB; 1A0U; 18-MAR-98.
DR   PDB; 1A0V; 18-MAR-98.
DR   PDB; 1A0W; 18-MAR-98.
DR   PDB; 1A0X; 18-MAR-98.
DR   PDB; 1A0Y; 18-MAR-98.
DR   PDB; 1A0Z; 18-MAR-98.
DR   PDB; 1RVW; 25-MAR-98.
DR   PDB; 1VWT; 25-MAR-98.
DR   PDB; 1A3N; 29-APR-98.
DR   PDB; 1A3O; 29-APR-98.
DR   PDB; 1AJ9; 20-MAY-98.
DR   PDB; 1ABW; 17-JUN-98.
DR   PDB; 1BUW; 16-SEP-98.
DR   PDB; 6HBW; 16-SEP-98.
DR   PDB; 1BZ0; 11-NOV-98.
DR   PDB; 1BZ1; 11-NOV-98.
DR   PDB; 1BZZ; 11-NOV-98.
DR   PDB; 1B86; 19-FEB-99.
DR   PDB; 1BIJ; 30-MAR-99.
DR   SWISS-2DPAGE; P02023; HUMAN.
DR   HSC-2DPAGE; P02023; HUMAN.
DR   MIM; 141900; -.
DR   MIM; 603903; -.
DR   PFAM; PF00042; globin; 1.
DR   PROSITE; PS01033; GLOBIN; 1.
KW   Heme; Oxygen transport; Respiratory protein; Erythrocyte;
KW   Acetylation; Disease mutation; Polymorphism; 3D-structure.
FT   INIT_MET      0      0
FT   METAL        63     63       IRON (HEME DISTAL LIGAND).
FT   METAL        92     92       IRON (HEME PROXIMAL LIGAND).
FT   MOD_RES       1      1       ACETYLATION (IN VARIANT RALEIGH).
FT   CARBOHYD      1      1       GLUCOSE (GLYCATION) (IN HB A1C).
FT   VARIANT       1      1       V -> A (IN RALEIGH; O2 AFFINITY DOWN).
FT                                /FTId=VAR_002856.
FT   VARIANT       2      2       H -> L (IN GRAZ).
FT                                /FTId=VAR_002857.
FT   VARIANT       2      2       H -> Q (IN OKAYAMA; O2 AFFINITY UP).
FT                                /FTId=VAR_002858.
FT   VARIANT       2      2       H -> R (IN DEER LODGE; O2 AFFINITY UP).
FT                                /FTId=VAR_002859.
FT   VARIANT       2      2       H -> Y (IN FUKUOKA).
FT                                /FTId=VAR_002860.
FT   VARIANT       5      5       P -> R (IN WARWICKSHIRE).
FT                                /FTId=VAR_002861.
FT   VARIANT       6      6       E -> A (IN G-MAKASSAR).
FT                                /FTId=VAR_002862.
FT   VARIANT       6      6       E -> V (IN S; SICKLE CELL ANEMIA).
FT                                /FTId=VAR_002863.
FT   VARIANT       6      6       E -> K (IN C).
FT                                /FTId=VAR_002864.
FT   VARIANT       6      6       E -> Q (IN MACHIDA).
FT                                /FTId=VAR_002865.
FT   VARIANT       7      7       E -> G (IN G-SAN JOSE; MILDLY UNSTABLE).
FT                                /FTId=VAR_002866.
FT   VARIANT       7      7       E -> K (IN G-SIRIRAJ).
FT                                /FTId=VAR_002867.
FT   VARIANT       8      8       K -> E (IN N-TIMONE).
FT                                /FTId=VAR_002868.
FT   VARIANT       8      8       K -> Q (IN J-LUHE).
FT                                /FTId=VAR_002869.
FT   VARIANT       8      8       K -> T (IN RIO GRANDE).
FT                                /FTId=VAR_002870.
FT   VARIANT       9      9       S -> C (IN PORTO ALEGRE; O2 AFFINITY UP).
FT                                /FTId=VAR_002871.
FT   VARIANT      10     10       A -> D (IN ANKARA).
FT                                /FTId=VAR_002872.
FT   VARIANT      11     11       V -> D (IN WINDSOR; O2 AFFINITY UP;
FT                                UNSTABLE).
FT                                /FTId=VAR_002873.
FT   VARIANT      11     11       V -> I (IN HAMILTON).
FT                                /FTId=VAR_002874.
FT   VARIANT      13     13       A -> D (IN J-LENS).
FT                                /FTId=VAR_002875.
FT   VARIANT      14     14       L -> P (IN SAKI; UNSTABLE).
FT                                /FTId=VAR_002876.
FT   VARIANT      14     14       L -> R (IN SOEGN; UNSTABLE).
FT                                /FTId=VAR_002877.
FT   VARIANT      15     15       W -> G (IN RANDWICK; UNSTABLE).
FT                                /FTId=VAR_002878.
FT   VARIANT      15     15       W -> R (IN BELFAST; O2 AFFINITY UP;
FT                                UNSTABLE).
FT                                /FTId=VAR_002879.
FT   VARIANT      16     16       G -> D (IN J-BALTIMORE/J-TRINIDAD/
FT                                J-IRELAND/J-GEORGIA/N-NEW HAVEN).
FT                                /FTId=VAR_002880.
FT   VARIANT      16     16       G -> R (IN D-BUSHMAN).
FT                                /FTId=VAR_002881.
FT   VARIANT      17     17       K -> E (IN NAGASAKI).
FT                                /FTId=VAR_002882.
FT   VARIANT      17     17       K -> N (IN J-AMIENS).
FT                                /FTId=VAR_002883.
FT   VARIANT      17     17       K -> Q (IN NIKOSIA).
FT                                /FTId=VAR_002884.
FT   VARIANT      18     18       V -> M (IN BADEN; SLIGHTLY INSTABLE).
FT                                /FTId=VAR_002885.
FT   VARIANT      19     19       N -> D (IN ALAMO).
FT                                /FTId=VAR_002886.
FT   VARIANT      19     19       N -> K (IN D-OULEH RABAH).
FT                                /FTId=VAR_002887.
FT   VARIANT      19     19       N -> S (IN MALAY).
FT                                /FTId=VAR_002888.
FT   VARIANT      20     20       V -> M (IN OLYMPIA; O2 AFFINITY UP).
FT                                /FTId=VAR_002889.
FT   VARIANT      21     21       D -> G (IN CONNECTICUT; O2 AFFINITY
FT                                DOWN).
FT                                /FTId=VAR_002890.
FT   VARIANT      21     21       D -> N (IN COCODY).
FT                                /FTId=VAR_002891.
FT   VARIANT      21     21       D -> H (IN KARLSKOGA).
FT                                /FTId=VAR_002892.
FT   VARIANT      21     21       D -> Y (IN YUSA).
FT                                /FTId=VAR_002893.
FT   VARIANT      22     22       E -> A (IN G-COUSHATTA/G-SASKATOON/
FT                                G-TAEGU/HSIN CHU).
FT                                /FTId=VAR_002894.
FT   VARIANT      22     22       E -> G (IN G-TAIPEI).
FT                                /FTId=VAR_002895.
FT   VARIANT      22     22       E -> K (IN E-SASKATOON; UNSTABLE).
FT                                /FTId=VAR_002896.
FT   VARIANT      22     22       E -> Q (IN D-IRAN).
FT                                /FTId=VAR_002897.
FT   VARIANT      22     22       E -> V (IN D-GRANADA).
FT                                /FTId=VAR_002898.
FT   VARIANT      23     23       V -> D (IN STRASBOURG; O2 AFFINITY UP).
FT                                /FTId=VAR_002899.
FT   VARIANT      23     23       V -> F (IN PALMERSTON NORTH; O2 AFFINITY
FT                                UP; UNSTABLE).
FT                                /FTId=VAR_002900.
FT   VARIANT      23     23       V -> G (IN MIYASHIRO; O2 AFFINITY UP;
FT                                UNSTABLE).
FT                                /FTId=VAR_002901.
FT   VARIANT      24     24       G -> D (IN MOSCVA; O2 AFFINITY DOWN;
FT                                UNSTABLE).
FT                                /FTId=VAR_002902.
FT   VARIANT      24     24       G -> R (IN RIVERDALE-BRONX; O2 AFFINITY
FT                                UP; UNSTABLE).
FT                                /FTId=VAR_002903.
FT   VARIANT      24     24       G -> V (IN SAVANNAH; UNSTABLE).
FT                                /FTId=VAR_002904.
FT   VARIANT      25     25       G -> D (IN J-AUCKLAND; UNSTABLE; O2
FT                                AFFINITY DOWN).
FT                                /FTId=VAR_002905.
FT   VARIANT      25     25       G -> R (IN G-TAIWAN AMI).
FT                                /FTId=VAR_002906.
FT   VARIANT      26     26       E -> K (IN E).
FT                                /FTId=VAR_002907.
FT   VARIANT      26     26       E -> V (IN HENRI MONDOR; SLIGHTLY
FT                                UNSTABLE).
FT                                /FTId=VAR_002908.
FT   VARIANT      27     27       A -> D (IN VOLGA/DRENTHE; UNSTABLE).
FT                                /FTId=VAR_002909.
FT   VARIANT      27     27       A -> S (IN KNOSSOS).
FT                                /FTId=VAR_002910.
FT   VARIANT      27     27       A -> V (IN GRANGE-BLANCHE; O2 AFFINITY
FT                                UP).
FT                                /FTId=VAR_002911.
FT   VARIANT      28     28       L -> P (IN GENOVA/HYOGO; UNSTABLE).
FT                                /FTId=VAR_002912.
FT   VARIANT      29     29       G -> D (IN LUFKIN; UNSTABLE).
FT                                /FTId=VAR_002913.
FT   VARIANT      30     30       R -> S (IN TACOMA; UNSTABLE).
FT                                /FTId=VAR_002914.
FT   VARIANT      31     31       L -> P (IN YOKOHAMA; UNSTABLE).
FT                                /FTId=VAR_002915.
FT   VARIANT      32     32       L -> R (IN CASTILLA; UNSTABLE).
FT                                /FTId=VAR_002916.
FT   VARIANT      32     32       L -> V (IN MUSCAT; SLIGHTLY UNSTABLE).
FT                                /FTId=VAR_002917.
FT   VARIANT      34     34       V -> F (IN PITIE-SALPETRIERE; O2 AFFINITY
FT                                UP).
FT                                /FTId=VAR_002918.
FT   VARIANT      35     35       Y -> F (IN PHILLY; O2 AFFINITY UP;
FT                                UNSTABLE).
FT                                /FTId=VAR_002919.
FT   VARIANT      36     36       P -> R (IN SUNNYBROOK).
FT                                /FTId=VAR_002920.
FT   VARIANT      36     36       P -> S (IN NORTH CHICAGO; O2 AFFINITY
FT                                UP).
FT                                /FTId=VAR_002921.
FT   VARIANT      36     36       P -> T (IN LINKOEPING/FINLANDIA; O2
FT                                AFFINITY UP).
FT                                /FTId=VAR_002922.
FT   VARIANT      37     37       W -> G (IN HOWICK).
FT                                /FTId=VAR_002923.
FT   VARIANT      37     37       W -> S (IN HIROSE; O2 AFFINITY UP).
FT                                /FTId=VAR_002924.
FT   VARIANT      37     37       W -> R (IN ROTHSCHILD; O2 AFFINITY DOWN).
FT                                /FTId=VAR_002925.
FT   VARIANT      38     38       T -> N (IN HINWIL; O2 AFFINITY UP).
FT                                /FTId=VAR_002926.
FT   VARIANT      39     39       Q -> E (IN VAASA; UNSTABLE).
FT                                /FTId=VAR_002927.
FT   VARIANT      39     39       Q -> K (IN ALABAMA).
FT                                /FTId=VAR_002928.
FT   VARIANT      39     39       Q -> R (IN TIANSHUI).
FT                                /FTId=VAR_002929.
FT   VARIANT      41     41       F -> Y (IN MEQUON).
FT                                /FTId=VAR_002930.
FT   VARIANT      42     42       F -> L (IN LOUISVILLE; UNSTABLE).
FT                                /FTId=VAR_002931.
FT   VARIANT      43     43       E -> Q (IN HOSHIDA/CHAYA).
FT                                /FTId=VAR_002932.
FT   VARIANT      44     44       S -> C (IN MISSISSIPPI).
FT                                /FTId=VAR_002933.
FT   VARIANT      45     45       F -> S (IN CHEVERLY; UNSTABLE).
FT                                /FTId=VAR_002934.
FT   VARIANT      46     46       G -> E (IN K-IBADAN).
FT                                /FTId=VAR_002935.
FT   VARIANT      47     47       D -> A (IN AVICENNA).
FT                                /FTId=VAR_002936.
FT   VARIANT      47     47       D -> G (IN GAVELLO).
FT                                /FTId=VAR_002937.
FT   VARIANT      47     47       D -> Y (IN MAPUTO).
FT                                /FTId=VAR_002938.
FT   VARIANT      48     48       L -> P (IN BAB-SAADOUM; SLIGHLTY
FT                                UNSTABLE).
FT                                /FTId=VAR_002939.
FT   VARIANT      49     49       S -> F (IN LAS PALMAS; SLIGHTLY
FT                                UNSTABLE).
FT                                /FTId=VAR_002940.
FT   VARIANT      50     50       T -> K (IN EDMONTON).
FT                                /FTId=VAR_002941.
FT   VARIANT      51     51       P -> R (IN WILLAMETTE; O2 AFFINITY UP;
FT                                UNSTABLE).
FT                                /FTId=VAR_002942.
FT   VARIANT      52     52       D -> A (IN OCHO RIOS).
FT                                /FTId=VAR_002943.
FT   VARIANT      52     52       D -> H (IN SUMMER HILL).
FT                                /FTId=VAR_002944.
FT   VARIANT      54     54       V -> D (IN JACKSONVILLE; O2 AFFINITY UP;
FT                                UNSTABLE).
FT                                /FTId=VAR_002945.
FT   VARIANT      55     55       M -> K (IN MATERA; UNSTABLE).
FT                                /FTId=VAR_002946.
FT   VARIANT      56     56       G -> R (IN HAMADAN).
FT                                /FTId=VAR_002947.
FT   VARIANT      57     57       N -> K (IN G-FERRARA; UNSTABLE).
FT                                /FTId=VAR_002948.
FT   VARIANT      58     58       P -> R (IN DHOFAR/YUKUHASHI).
FT                                /FTId=VAR_002949.
FT   VARIANT      59     59       K -> E (IN I-HIGH WYCOMBE).
FT                                /FTId=VAR_002950.
FT   VARIANT      60     60       V -> A (IN COLLINGWOOD; UNSTABLE).
FT                                /FTId=VAR_002951.
FT   VARIANT      61     61       K -> E (IN N-SEATLLE).
FT                                /FTId=VAR_002952.
FT   VARIANT      61     61       K -> M (IN BOLOGNA; O2 AFFINITY DOWN).
FT                                /FTId=VAR_002953.
FT   VARIANT      61     61       K -> N (IN HIKARI).
FT                                /FTId=VAR_002954.
FT   VARIANT      62     62       A -> D (IN J-EUROPA).
FT                                /FTId=VAR_002955.
FT   VARIANT      62     62       A -> P (IN DUARTE; UNSTABLE).
FT                                /FTId=VAR_002956.
FT   VARIANT      63     63       H -> Y (IN M-SASKATOON; O2 AFFINITY UP).
FT                                /FTId=VAR_002957.
FT   VARIANT      65     65       K -> M (IN J-ANTAKYA).
FT                                /FTId=VAR_002958.
FT   VARIANT      65     65       K -> N (IN J-SICILIA).
FT                                /FTId=VAR_002959.
FT   VARIANT      65     65       K -> Q (IN J-CAIRO).
FT                                /FTId=VAR_002960.
FT   VARIANT      66     66       K -> T (IN CHICO; O2 AFFINITY DOWN).
FT                                /FTId=VAR_002961.
FT   VARIANT      67     67       V -> A (IN SIDNEY; UNSTABLE).
FT                                /FTId=VAR_002962.
FT   VARIANT      67     67       V -> M (IN ALESHA; UNSTABLE).
FT                                /FTId=VAR_002963.
FT   VARIANT      68     68       L -> H (IN BRISBANE; O2 AFFINITY UP).
FT                                /FTId=VAR_002964.
FT   VARIANT      68     68       L -> P (IN MIZUHO; UNSTABLE).
FT                                /FTId=VAR_002965.
FT   VARIANT      69     69       G -> D (IN RAMBAM).
FT                                /FTId=VAR_002966.
FT   VARIANT      69     69       G -> R (IN KENITRA).
FT                                /FTId=VAR_002967.
FT   VARIANT      69     69       G -> S (IN CITY OF HOPE).
FT                                /FTId=VAR_002968.
FT   VARIANT      70     70       A -> D (IN SEATTLE; O2 AFFINITY DOWN;
FT                                UNSTABLE).
FT                                /FTId=VAR_002969.
FT   VARIANT      71     71       F -> S (IN CHRISTCHURCH; UNSTABLE).
FT                                /FTId=VAR_002970.
FT   VARIANT      73     73       D -> G (IN TILBURG; O2 AFFINITY DOWN).
FT                                /FTId=VAR_002971.
FT   VARIANT      73     73       D -> V (IN MOBILE; O2 AFFINITY DOWN).
FT                                /FTId=VAR_002972.
FT   VARIANT      73     73       D -> Y (IN VANCOUVER; O2 AFFINITY DOWN).
FT                                /FTId=VAR_002973.
FT   VARIANT      74     74       G -> R (IN AALBORG; UNSTABLE).
FT                                /FTId=VAR_002974.
FT   VARIANT      74     74       G -> V (IN BUSHWICK; UNSTABLE).
FT                                /FTId=VAR_002975.
FT   VARIANT      75     75       L -> P (IN ATLANTA; UNSTABLE).
FT                                /FTId=VAR_002976.
FT   VARIANT      75     75       L -> R (IN PASADENA; O2 AFFINITY UP;
FT                                UNSTABLE).
FT                                /FTId=VAR_002977.
FT   VARIANT      76     76       A -> D (IN J-CHICAGO).
FT                                /FTId=VAR_002978.
FT   VARIANT      77     77       H -> D (IN J-IRAN).
FT                                /FTId=VAR_002979.
FT   VARIANT      77     77       H -> R (IN COSTA RICA).
FT                                /FTId=VAR_002980.
FT   VARIANT      77     77       H -> Y (IN FUKUYAMA).
FT                                /FTId=VAR_002981.
FT   VARIANT      78     78       L -> R (IN QUIN-HAI).
FT                                /FTId=VAR_002982.
FT   VARIANT      79     79       D -> Y (IN TAMPA).
FT                                /FTId=VAR_002983.
FT   VARIANT      80     80       N -> K (IN G-SZUHU/GIFU).
FT                                /FTId=VAR_002984.
FT   VARIANT      81     81       L -> R (IN BAYLOR; UNSTABLE).
FT                                /FTId=VAR_002985.
FT   VARIANT      82     82       K -> M (IN HELSINKI; O2 AFFINITY UP).
FT                                /FTId=VAR_002986.
FT   VARIANT      83     83       G -> R (IN MUSKEGON).
FT                                /FTId=VAR_002987.
FT   VARIANT      84     84       T -> I (IN KOFU).
FT                                /FTId=VAR_002988.
FT   VARIANT      86     86       A -> D (IN OLOMOUC; O2 AFFINITY UP).
FT                                /FTId=VAR_002989.
FT   VARIANT      87     87       T -> I (IN QUEBEC-CHORI).
FT                                /FTId=VAR_002990.
FT   VARIANT      87     87       T -> K (IN D-IBADAN).
FT                                /FTId=VAR_002991.
FT   VARIANT      87     87       T -> P (IN VALLETTA).
FT                                /FTId=VAR_002992.
FT   VARIANT      88     88       L -> P (IN SANTA ANA; UNSTABLE).
FT                                /FTId=VAR_002993.
FT   VARIANT      88     88       L -> R (IN BORAS; UNSTABLE).
FT                                /FTId=VAR_002994.
FT   VARIANT      89     89       S -> N (IN CRETEIL; O2 AFFINITY UP).
FT                                /FTId=VAR_002995.
FT   VARIANT      89     89       S -> R (IN VANDERBILT; O2 AFFINITY UP).
FT                                /FTId=VAR_002996.
FT   VARIANT      90     90       E -> D (IN PIERRE-BENITE; O2 AFFINITY
FT                                UP).
FT                                /FTId=VAR_002997.
FT   VARIANT      90     90       E -> K (IN AGENOGI; O2 AFFINITY DOWN).
FT                                /FTId=VAR_002998.
FT   VARIANT      91     91       L -> P (IN SABINE; UNSTABLE).
FT                                /FTId=VAR_002999.
FT   VARIANT      91     91       L -> R (IN CARIBBEAN; O2 AFFINITY DOWN;
FT                                UNSTABLE).
FT                                /FTId=VAR_003000.
FT   VARIANT      92     92       H -> D (IN J-ALTGELDS GARDENS; UNSTABLE).
FT                                /FTId=VAR_003001.
FT   VARIANT      92     92       H -> N (IN ISEHARA; UNSTABLE).
FT                                /FTId=VAR_003002.
FT   VARIANT      92     92       H -> P (IN NEWCASTLE AND DUINO;
FT                                UNSTABLE).
FT                                /FTId=VAR_003003.
FT   VARIANT      92     92       H -> Q (IN ISTAMBUL; O2 AFFINITY UP;
FT                                UNSTABLE).
FT                                /FTId=VAR_003004.
FT   VARIANT      93     93       C -> R (IN OKAZAKI; O2 AFFINITY UP;
FT                                UNSTABLE).
FT                                /FTId=VAR_003005.
FT   VARIANT      94     94       D -> G (IN CHANDIGARH).
FT                                /FTId=VAR_003006.
FT   VARIANT      94     94       D -> H (IN BARCELONA; O2 AFFINITY UP).
FT                                /FTId=VAR_003007.
FT   VARIANT      94     94       D -> N (IN BUNBURY; O2 AFFINITY UP).
FT                                /FTId=VAR_003008.
FT   VARIANT      95     95       K -> M (IN J-CORDOBA).
FT                                /FTId=VAR_003009.
FT   VARIANT      95     95       K -> N (IN DETROIT).
FT                                /FTId=VAR_003010.
FT   VARIANT      96     96       L -> P (IN DEBROUSSE; UNSTABLE; O2
FT                                AFFINITY UP).
FT                                /FTId=VAR_003011.
FT   VARIANT      96     96       L -> V (IN REGINA; O2 AFFINITY UP).
FT                                /FTId=VAR_003012.
FT   VARIANT      97     97       H -> L (IN WOOD; O2 AFFINITY UP).
FT                                /FTId=VAR_003013.
FT   VARIANT      97     97       H -> P (IN NAGOYA; O2 AFFINITY UP;
FT                                UNSTABLE).
FT                                /FTId=VAR_003014.
FT   VARIANT      97     97       H -> Q (IN MALMOE; O2 AFFINITY UP).
FT                                /FTId=VAR_003015.
FT   VARIANT      97     97       H -> Y (IN MORIGUCHI).
FT                                /FTId=VAR_003016.
FT   VARIANT      98     98       V -> G (IN NOTTINGHAM; UNSTABLE).
FT                                /FTId=VAR_003017.
FT   VARIANT      99     99       D -> E (IN COIMBRA; O2 AFFINITY UP).
FT                                /FTId=VAR_003018.
FT   VARIANT     100    100       P -> L (IN BRIGHAM; O2 AFFINITY UP).
FT                                /FTId=VAR_003019.
FT   VARIANT     100    100       P -> R (IN NEW MEXICO).
FT                                /FTId=VAR_003020.
FT   VARIANT     101    101       E -> D (IN POTOMAC; O2 AFFINITY UP).
FT                                /FTId=VAR_003021.
FT   VARIANT     101    101       E -> G (IN ALBERTA; O2 AFFINITY UP).
FT                                /FTId=VAR_003022.
FT   VARIANT     101    101       E -> K (IN BRITISH COLUMBIA; O2 AFFINITY
FT                                UP).
FT                                /FTId=VAR_003023.
FT   VARIANT     101    101       E -> Q (IN RUSH; UNSTABLE).
FT                                /FTId=VAR_003024.
FT   VARIANT     102    102       N -> S (IN BETH ISRAEL; O2 AFFINITY DOWN;
FT                                UNSTABLE).
FT                                /FTId=VAR_003025.
FT   VARIANT     102    102       N -> Y (IN ST MANDE; O2 AFFINITY DOWN).
FT                                /FTId=VAR_003026.
FT   VARIANT     103    103       F -> L (IN HEATHROW; O2 AFFINITY UP).
FT                                /FTId=VAR_003027.
FT   VARIANT     104    104       R -> S (IN CAMPERDOWN AND DUINO).
FT                                /FTId=VAR_003028.
FT   VARIANT     104    104       R -> T (IN SHERWOOD FOREST).
FT                                /FTId=VAR_003029.
FT   VARIANT     107    107       G -> R (IN BURKE; O2 AFFINITY DOWN;
FT                                UNSTABLE).
FT                                /FTId=VAR_003030.
FT   VARIANT     108    108       N -> K (IN PRESBYTERIAN; O2 AFFINITY
FT                                DOWN; UNSTABLE).
FT                                /FTId=VAR_003031.
FT   VARIANT     109    109       V -> M (IN SAN DIEGO; O2 AFFINITY UP).
FT                                /FTId=VAR_003032.
FT   VARIANT     110    110       L -> P (IN SHOWA-YAKUSHIJI).
FT                                /FTId=VAR_003033.
FT   VARIANT     111    111       V -> A (IN STANMORE; O2 AFFINITY DOWN;
FT                                UNSTABLE).
FT                                /FTId=VAR_003034.
FT   VARIANT     112    112       C -> R (IN INDIANAPOLIS).
FT                                /FTId=VAR_003035.
FT   VARIANT     112    112       C -> Y (IN YAHATA).
FT                                /FTId=VAR_003036.
FT   VARIANT     115    115       A -> D (IN HRADEC KRALOVE; UNSTABLE;
FT                                CAUSES SEVERE BETA-THALASSEMIA).
FT                                /FTId=VAR_003037.
FT   VARIANT     115    115       A -> P (IN MADRID; UNSTABLE).
FT                                /FTId=VAR_003038.
FT   VARIANT     116    116       H -> Q (IN HAFNIA).
FT                                /FTId=VAR_003039.
FT   VARIANT     117    117       H -> P (IN SAITAMA; UNSTABLE).
FT                                /FTId=VAR_003040.
FT   VARIANT     117    117       H -> R (IN P-GALVESTON).
FT                                /FTId=VAR_003041.
FT   VARIANT     119    119       G -> A (IN IOWA).
FT                                /FTId=VAR_003042.
FT   VARIANT     120    120       K -> E (IN HIJIYAMA).
FT                                /FTId=VAR_003043.
FT   VARIANT     120    120       K -> I (IN JIANGHUA).
FT                                /FTId=VAR_003044.
FT   VARIANT     120    120       K -> Q (IN TAKAMATSU).
FT                                /FTId=VAR_003045.
FT   VARIANT     121    121       E -> A (IN D-NEATH).
FT                                /FTId=VAR_003046.
FT   VARIANT     121    121       E -> G (IN ST FRANCIS).
FT                                /FTId=VAR_003047.
FT   VARIANT     121    121       E -> Q (IN D-LOS ANGELES/D-PUNJAB/
FT                                D-PORTUGAL/D-CHICAGO/D-OAK RIDGE).
FT                                /FTId=VAR_003048.
FT   VARIANT     121    121       E -> K (IN O-ARAB).
FT                                /FTId=VAR_003049.
FT   VARIANT     121    121       E -> V (IN D-CAMPERDOWN/BEOGRAD).
FT                                /FTId=VAR_003050.
FT   VARIANT     123    123       T -> I (IN VILLEJUIF).
FT                                /FTId=VAR_003051.
FT   VARIANT     124    124       P -> R (IN KHARTOUM; UNSTABLE).
FT                                /FTId=VAR_003052.
FT   VARIANT     124    124       P -> Q (IN TY GARD; O2 AFFINITY UP).
FT                                /FTId=VAR_003053.
FT   VARIANT     124    124       P -> S (IN TUNIS).
FT                                /FTId=VAR_003054.
FT   VARIANT     126    126       V -> A (IN BEIRUT).
FT                                /FTId=VAR_003055.
FT   VARIANT     126    126       V -> G (IN DHONBURI/NEAPOLIS; UNSTABLE;
FT                                BETA-THALASSEMIA).
FT                                /FTId=VAR_003056.
FT   VARIANT     126    126       V -> E (IN HOFU; UNSTABLE).
FT                                /FTId=VAR_003057.
FT   VARIANT     127    127       Q -> E (IN COMPLUTENSE).
FT                                /FTId=VAR_003058.
FT   VARIANT     127    127       Q -> K (IN BREST; UNSTABLE).
FT                                /FTId=VAR_003059.
FT   VARIANT     128    128       A -> D (IN J-GUANTANAMO; UNSTABLE).
FT                                /FTId=VAR_003060.
FT   VARIANT     129    129       A -> P (IN CRETE; O2 AFFINITY UP;
FT                                UNSTABLE).
FT                                /FTId=VAR_003061.
FT   VARIANT     129    129       A -> V (IN LA DESIRADE; O2 AFFINITY
FT                                DOWN; UNSTABLE).
FT                                /FTId=VAR_003062.
FT   VARIANT     130    130       Y -> D (IN WIEN; UNSTABLE).
FT                                /FTId=VAR_003063.
FT   VARIANT     130    130       Y -> S (IN NEVERS).
FT                                /FTId=VAR_003064.
FT   VARIANT     131    131       Q -> E (IN CAMDEN/TOKUCHI/MOTOWN).
FT                                /FTId=VAR_003065.
FT   VARIANT     131    131       Q -> K (IN SHELBY/LESLIE/DEACONESS;
FT                                UNSTABLE).
FT                                /FTId=VAR_003066.
FT   VARIANT     131    131       Q -> P (IN SHANGAI; UNSTABLE).
FT                                /FTId=VAR_003067.
FT   VARIANT     131    131       Q -> R (IN SARREBOURG; UNSTABLE).
FT                                /FTId=VAR_003068.
FT   VARIANT     132    132       K -> N (IN YAMAGATA; O2 AFFINITY DOWN).
FT                                /FTId=VAR_003069.
FT   VARIANT     132    132       K -> Q (IN K-WOOLWICH).
FT                                /FTId=VAR_003070.
FT   VARIANT     133    133       V -> L (IN EXTREDEMURA).
FT                                /FTId=VAR_003071.
FT   VARIANT     134    134       V -> E (IN NORTH SHORE; UNSTABLE).
FT                                /FTId=VAR_003072.
FT   VARIANT     135    135       A -> E (IN BECKMAN; O2 AFFINITY DOWN;
FT                                UNSTABLE).
FT                                /FTId=VAR_003073.
FT   VARIANT     135    135       A -> P (IN ALTDORF; O2 AFFINITY UP;
FT                                UNSTABLE).
FT                                /FTId=VAR_003074.
FT   VARIANT     136    136       G -> D (IN HOPE; O2 AFFINITY DOWN;
FT                                UNSTABLE).
FT                                /FTId=VAR_003075.
FT   VARIANT     138    138       A -> P (IN BROCKTON; UNSTABLE).
FT                                /FTId=VAR_003076.
FT   VARIANT     139    139       N -> D (IN GEELONG; UNSTABLE).
FT                                /FTId=VAR_003077.
FT   VARIANT     139    139       N -> K (IN HINSDALE; O2 AFFINITY DOWN).
FT                                /FTId=VAR_003078.
FT   VARIANT     139    139       N -> Y (IN AURORA; O2 AFFINITY UP).
FT                                /FTId=VAR_003079.
FT   VARIANT     140    140       A -> D (IN HIMEJI; UNSTABLE; O2 AFFINITY
FT                                DOWN).
FT                                /FTId=VAR_003080.
FT   VARIANT     140    140       A -> T (IN ST JACQUES: O2 AFFINITY UP).
FT                                /FTId=VAR_003081.
FT   VARIANT     140    140       A -> V (IN PUTTELANGE; POLYCYTHEMIA;
FT                                O2 AFFINITY UP).
FT                                /FTId=VAR_003082.
FT   VARIANT     141    141       L -> R (IN OLMSTED; UNSTABLE).
FT                                /FTId=VAR_003083.
FT   VARIANT     142    142       A -> D (IN OHIO; O2 AFFINITY UP).
FT                                /FTId=VAR_003084.
FT   VARIANT     143    143       H -> D (IN RANCHO MIRAGE).
FT                                /FTId=VAR_003085.
FT   VARIANT     143    143       H -> Q (IN LITTLE ROCK; O2 AFFINITY UP).
FT                                /FTId=VAR_003086.
FT   VARIANT     143    143       H -> P (IN SYRACUSE; O2 AFFINITY UP).
FT                                /FTId=VAR_003087.
FT   VARIANT     143    143       H -> R (IN ABRUZZO; O2 AFFINITY UP).
FT                                /FTId=VAR_003088.
FT   VARIANT     144    144       K -> E (IN MITO; O2 AFFINITY UP).
FT                                /FTId=VAR_003089.
FT   VARIANT     145    145       Y -> C (IN RAINIER; O2 AFFINITY UP).
FT                                /FTId=VAR_003090.
FT   VARIANT     145    145       Y -> H (IN BETHESDA; O2 AFFINITY UP).
FT                                /FTId=VAR_003091.
FT   VARIANT     146    146       H -> D (IN HIROSHIMA; O2 AFFINITY UP).
FT                                /FTId=VAR_003092.
FT   VARIANT     146    146       H -> L (IN COWTOWN; O2 AFFINITY UP).
FT                                /FTId=VAR_003093.
FT   VARIANT     146    146       H -> P (IN YORK; O2 AFFINITY UP).
FT                                /FTId=VAR_003094.
FT   VARIANT     146    146       H -> Q (IN KODAIRA; O2 AFFINITY UP).
FT                                /FTId=VAR_003095.
FT   HELIX         5     15
FT   TURN         16     17
FT   HELIX        20     34
FT   HELIX        36     41
FT   HELIX        43     45
FT   HELIX        51     55
FT   TURN         56     56
FT   HELIX        58     75
FT   TURN         76     77
FT   HELIX        78     94
FT   TURN         95     96
FT   TURN        100    100
FT   HELIX       101    121
FT   HELIX       124    142
FT   TURN        143    144
SQ   SEQUENCE   146 AA;  15867 MW;  EC9744C9 CRC32;
     VHLTPEEKSA VTALWGKVNV DEVGGEALGR LLVVYPWTQR FFESFGDLST PDAVMGNPKV
     KAHGKKVLGA FSDGLAHLDN LKGTFATLSE LHCDKLHVDP ENFRLLGNVL VCVLAHHFGK
     EFTPPVQAAY QKVVAGVANA LAHKYH
//
ID   LACI_ECOLI     STANDARD;      PRT;   360 AA.
AC   P03023; P71309; Q47338; O09196;
DT   21-JUL-1986 (Rel. 01, Created)
DT   01-NOV-1997 (Rel. 35, Last sequence update)
DT   15-DEC-1998 (Rel. 37, Last annotation update)
DE   LACTOSE OPERON REPRESSOR.
GN   LACI.
OS   Escherichia coli.
OC   Bacteria; Proteobacteria; gamma subdivision; Enterobacteriaceae;
OC   Escherichia.
RN   [1]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 78246991.
RA   FARABAUGH P.J.;
RT   "Sequence of the lacI gene.";
RL   Nature 274:765-769(1978).
RN   [2]
RP   SEQUENCE FROM N.A.
RC   STRAIN=K12 / MG1655;
RX   MEDLINE; 97426617.
RA   BLATTNER F.R., PLUNKETT G. III, BLOCH C.A., PERNA N.T., BURLAND V.,
RA   RILEY M., COLLADO-VIDES J., GLASNER F.D., RODE C.K., MAYHEW G.F.,
RA   GREGOR J., DAVIS N.W., KIRKPATRICK H.A., GOEDEN M.A., ROSE D.J.,
RA   MAU B., SHAO Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1474(1997).
RN   [3]
RP   SEQUENCE FROM N.A.
RC   STRAIN=K12 / MG1655;
RA   DUNCAN M., ALLEN E., ARAUJO R., APARICIO A.M., CHUNG E., DAVIS K.,
RA   FEDERSPIEL N., HYMAN R., KALMAN S., KOMP C., KURDI O., LEW H.,
RA   LIN D., NAMATH A., OEFNER P., ROBERTS D., SCHRAMM S., DAVIS R.W.;
RL   Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   SEQUENCE FROM N.A.
RA   CHEN J., MATTHEWS K.K.S.M.;
RL   Submitted (MAY-1991) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   SEQUENCE FROM N.A.
RA   MARSH S.;
RL   Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   SEQUENCE OF 1-147; 159-230 AND 233-360.
RX   MEDLINE; 76091932.
RA   BEYREUTHER K., ADLER K., FANNING E., MURRAY C., KLEMM A., GEISLER N.;
RT   "Amino-acid sequence of lac repressor from Escherichia coli.
RT   Isolation, sequence analysis and sequence assembly of tryptic
RT   peptides and cyanogen-bromide fragments.";
RL   Eur. J. Biochem. 59:491-509(1975).
RN   [7]
RP   SEQUENCE OF 1-59; 96-101; 206-215 AND 328-347.
RX   MEDLINE; 73143730.
RA   PLATT T., FILES J.G., WEBER K.;
RT   "Lac repressor. Specific proteolytic destruction of the NH 2
RT   -terminal region and loss of the deoxyribonucleic acid-binding
RT   activity.";
RL   J. Biol. Chem. 248:110-121(1973).
RN   [8]
RP   SEQUENCE OF 60-70; 73-78 AND 83-86.
RX   MEDLINE; 74126378.
RA   GANEM D., MILLER J.H., FILES J.G., PLATT T., WEBER K.;
RT   "Reinitiation of a lac repressor fragment at a condon other than
RT   AUG.";
RL   Proc. Natl. Acad. Sci. U.S.A. 70:3165-3169(1973).
RN   [9]
RP   SEQUENCE OF 1-60 FROM N.A.
RX   MEDLINE; 88230449.
RA   GORDON A.J.E., BURNS P.A., FIX D.F., YATAGAI F., ALLEN F.L.,
RA   HORSFALL M.J., HALLIDAY J.A., GRAY J., BERNELOT-MOENS C.,
RA   GLICKMAN B.W.;
RT   "Missense mutation in the lacI gene of Escherichia coli. Inferences
RT   on the structure of the repressor protein.";
RL   J. Mol. Biol. 200:239-251(1988).
RN   [10]
RP   STRUCTURE BY NMR.
RX   MEDLINE; 89113344.
RA   BOELENS R., LAMERICHS R.M.J.N., RULLMANN J.A.C., VAN BOOM J.H.,
RA   KAPTEIN R.;
RT   "The interaction of lac repressor headpiece with its operator: an NMR
RT   view.";
RL   Protein Seq. Data Anal. 1:487-498(1988).
RN   [11]
RP   STRUCTURE BY NMR.
RX   MEDLINE; 89302886.
RA   LAMERICHS R.M.J.N., BOELENS R., VAN DER MAREL G.A., VAN BOOM J.H.,
RA   KAPTEIN R., BUCK F., FERA B., RUTERJANS H.;
RT   "H NMR study of a complex between the lac repressor headpiece and a
RT   22 base pair symmetric lac operator.";
RL   Biochemistry 28:2985-2991(1989).
RN   [12]
RP   STRUCTURE BY NMR OF 1-56.
RX   MEDLINE; 96275660.
RA   SLIJPER M., BONVIN A.M., BOELENS R., KAPTEIN R.;
RT   "Refined structure of lac repressor headpiece (1-56) determined by
RT   relaxation matrix calculations from 2D and 3D NOE data: change of
RT   tertiary structure upon binding to the lac operator.";
RL   J. Mol. Biol. 259:761-773(1996).
RN   [13]
RP   X-RAY CRYSTALLOGRAPHY (4.8 ANGSTROMS).
RX   MEDLINE; 96239623.
RA   LEWIS M., CHANG G., HORTON N.C., KERCHER M.A., PACE H.C.,
RA   SCHUMACHER M.A., BRENNAN R.G., LU P.;
RT   "Crystal structure of the lactose operon repressor and its complexes
RT   with DNA and inducer.";
RL   Science 271:1247-1254(1996).
RN   [14]
RP   MUTAGENESIS.
RX   MEDLINE; 90183956.
RA   LEHMING N., SARTORIUS J., KISTERS-WOIKE B., VON WILCKEN-BERGMANN B.,
RA   MUELLER-HILL B.;
RT   "Mutant lac repressors with new specificities hint at rules for
RT   protein-DNA recognition.";
RL   EMBO J. 9:615-621(1990).
RN   [15]
RP   MUTAGENESIS.
RX   MEDLINE; 94322386.
RA   MARKIEWICZ P., KLEINA L.G., CRUZ C., EHRET S., MILLER J.H.;
RT   "Genetic studies of the lac repressor. XIV. Analysis of 4000 altered
RT   Escherichia coli lac repressors reveals essential and non-essential
RT   residues, as well as 'spacers' which do not require a specific
RT   sequence.";
RL   J. Mol. Biol. 240:421-433(1994).
RN   [16]
RP   3D-STRUCTURE MODELING.
RX   MEDLINE; 91249837.
RA   KISTERS-WOIKE B., LEHMING N., SARTORIUS J., VON WILCKEN-BERGMANN B.,
RA   MUELLER-HILL B.;
RT   "A model of the lac repressor-operator complex based on physical and
RT   genetic data.";
RL   Eur. J. Biochem. 198:411-419(1991).
CC   -!- FUNCTION: REPRESSOR OF THE LACTOSE OPERON. BINDS LACTOSE AS AN
CC       INDUCER.
CC   -!- SUBUNIT: HOMOTETRAMER.
CC   -!- MISCELLANEOUS: REMOVAL OF RESIDUES 1-59 AND 328-347 RESULTS IN THE
CC       MOLECULE LOSING ITS DNA-BINDING ACTIVITY WHILE MAINTAINING ITS
CC       INDUCER-BINDING ACTIVITY AND ITS TETRAMERIC STRUCTURE.
CC   -!- SIMILARITY: BELONGS TO THE LACI FAMILY OF TRANSCRIPTIONAL
CC       REGULATORS.
CC   --------------------------------------------------------------------------
CC   This SWISS-PROT entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use  by  non-profit  institutions as long  as its content  is  in  no  way
CC   modified and this statement is not removed.  Usage  by  and for commercial
CC   entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC   or send an email to license@isb-sib.ch).
CC   --------------------------------------------------------------------------
DR   EMBL; V00294; CAA23569.1; -.
DR   EMBL; J01636; AAA24052.1; -.
DR   EMBL; AE000141; AAC73448.1; -.
DR   EMBL; U73857; AAB18069.1; ALT_INIT.
DR   EMBL; X58469; CAA41383.1; -.
DR   EMBL; U86347; AAB47270.1; ALT_INIT.
DR   EMBL; U72488; AAB36549.1; -.
DR   EMBL; U78872; AAB37348.1; -.
DR   EMBL; U78873; AAB37351.1; -.
DR   EMBL; U78874; AAB37354.1; -.
DR   PIR; A03558; RPECL.
DR   PIR; S02540; S02540.
DR   PDB; 1LCC; 31-JAN-94.
DR   PDB; 1LCD; 31-JAN-94.
DR   PDB; 1LTP; 31-OCT-93.
DR   PDB; 1TLF; 31-JUL-95.
DR   PDB; 1LBG; 11-JUL-96.
DR   PDB; 1LBH; 11-JUL-96.
DR   PDB; 1LBI; 11-JUL-96.
DR   PDB; 1LQC; 12-FEB-97.
DR   ECO2DBASE; H039.0; 6TH EDITION.
DR   ECOGENE; EG10525; LACI.
DR   PFAM; PF00356; lacI; 1.
DR   PFAM; PF00532; Peripla_BP_like; 1.
DR   PROSITE; PS00356; HTH_LACI_FAMILY; 1.
KW   Transcription regulation; DNA-binding; Repressor; 3D-structure.
FT   DNA_BIND      6     25       H-T-H MOTIF.
FT   MUTAGEN      17     17       Y->H: BROADENING OF SPECIFICITY.
FT   MUTAGEN      22     22       R->N: RECOGNIZE AN OPERATOR VARIANT.
FT   VARIANT     282    282       Y -> D (IN T41 MUTANT).
FT   CONFLICT    286    286       S -> L (IN AAA24052, REF. 2, 4 AND 5).
FT   HELIX         6     13
FT   TURN         14     14
FT   HELIX        17     24
FT   HELIX        32     44
FT   TURN         49     50
SQ   SEQUENCE   360 AA;  38564 MW;  4CA5A1D6 CRC32;
     MKPVTLYDVA EYAGVSYQTV SRVVNQASHV SAKTREKVEA AMAELNYIPN RVAQQLAGKQ
     SLLIGVATSS LALHAPSQIV AAIKSRADQL GASVVVSMVE RSGVEACKAA VHNLLAQRVS
     GLIINYPLDD QDAIAVEAAC TNVPALFLDV SDQTPINSII FSHEDGTRLG VEHLVALGHQ
     QIALLAGPLS SVSARLRLAG WHKYLTRNQI QPIAEREGDW SAMSGFQQTM QMLNEGIVPT
     AMLVANDQMA LGAMRAITES GLRVGADISV VGYDDTEDSS CYIPPSTTIK QDFRLLGQTS
     VDRLLQLSQG QAVKGNQLLP VSLVKRKTTL APNTQTASPR ALADSLMQLA RQVSRLESGQ
//
ID   LACY_ECOLI     STANDARD;      PRT;   417 AA.
AC   P02920;
DT   21-JUL-1986 (Rel. 01, Created)
DT   21-JUL-1986 (Rel. 01, Last sequence update)
DT   01-NOV-1997 (Rel. 35, Last annotation update)
DE   LACTOSE PERMEASE (LACTOSE-PROTON SYMPORT).
GN   LACY.
OS   Escherichia coli.
OC   Bacteria; Proteobacteria; gamma subdivision; Enterobacteriaceae;
OC   Escherichia.
RN   [1]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 80120651.
RA   BUCHEL D.E., GRONENBORN B., MULLER-HILL B.;
RT   "Sequence of the lactose permease gene.";
RL   Nature 283:541-545(1980).
RN   [2]
RP   SEQUENCE FROM N.A.
RC   STRAIN=K12;
RA   PASTORE J.C., LARIGAN J.D., CONSLER T.G., KABACK H.R.;
RL   Submitted (SEP-1990) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   SEQUENCE FROM N.A.
RC   STRAIN=K12 / MG1655;
RX   MEDLINE; 97426617.
RA   BLATTNER F.R., PLUNKETT G. III, BLOCH C.A., PERNA N.T., BURLAND V.,
RA   RILEY M., COLLADO-VIDES J., GLASNER F.D., RODE C.K., MAYHEW G.F.,
RA   GREGOR J., DAVIS N.W., KIRKPATRICK H.A., GOEDEN M.A., ROSE D.J.,
RA   MAU B., SHAO Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1474(1997).
RN   [4]
RP   SEQUENCE FROM N.A.
RA   DUNCAN M., ALLEN E., ARAUJO R., APARICIO A.M., CHUNG E., DAVIS K.,
RA   FEDERSPIEL N., HYMAN R., KALMAN S., KOMP C., KURDI O., LEW H.,
RA   LIN D., NAMATH A., OEFNER P., ROBERTS D., SCHRAMM S., DAVIS R.W.;
RL   Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   TOPOLOGY.
RA   VON HEIJNE G.;
RT   "The distribution of positively charged residues in bacterial inner
RT   membrane proteins correlates with the trans-membrane topology.";
RL   EMBO J. 5:3021-3027(1986).
RN   [6]
RP   MUTAGENESIS.
RX   MEDLINE; 91167519.
RA   KING S.C., HANSEN C.L., WILSON T.H.;
RT   "The interaction between aspartic acid 237 and lysine 358 in the
RT   lactose carrier of Escherichia coli.";
RL   Biochim. Biophys. Acta 1062:177-186(1991).
RN   [7]
RP   MUTAGENESIS.
RX   MEDLINE; 92355521.
RA   HUANG A.-M., LEE J.-I., KING S.C., WILSON T.H.;
RT   "Amino acid substitution in the lactose carrier protein with the use
RT   of amber suppressors.";
RL   J. Bacteriol. 174:5436-5441(1992).
RN   [8]
RP   REVIEW.
RX   MEDLINE; 90366577.
RA   KABACK H.R.;
RT   "The lac permease of Escherichia coli: a prototypic
RT   energy-transducing membrane protein.";
RL   Biochim. Biophys. Acta 1018:160-162(1990).
CC   -!- FUNCTION: RESPONSIBLE FOR TRANSPORT OF BETA-GALACTOSIDES INTO THE
CC       CELL, WITH THE CONCOMITANT EXPORT OF A PROTON (SYMPORT SYSTEM).
CC   -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. INNER MEMBRANE.
CC   -!- SIMILARITY: BELONGS TO THE LACY/RAFB FAMILY OF PERMEASES.
CC   --------------------------------------------------------------------------
CC   This SWISS-PROT entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use  by  non-profit  institutions as long  as its content  is  in  no  way
CC   modified and this statement is not removed.  Usage  by  and for commercial
CC   entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC   or send an email to license@isb-sib.ch).
CC   --------------------------------------------------------------------------
DR   EMBL; J01636; AAA24054.1; -.
DR   EMBL; V00295; CAA23571.1; -.
DR   EMBL; X56095; CAA39575.1; -.
DR   EMBL; AE000141; AAC73446.1; -.
DR   EMBL; U73857; AAB18067.1; -.
DR   PIR; A03418; GREC.
DR   PIR; S21314; S21314.
DR   ECOGENE; EG10526; LACY.
DR   PFAM; PF01306; LacY_symp; 1.
DR   PROSITE; PS00896; LACY_1; 1.
DR   PROSITE; PS00897; LACY_2; 1.
KW   Transport; Sugar transport; Symport; Inner membrane; Transmembrane.
FT   DOMAIN        1     10       CYTOPLASMIC.
FT   TRANSMEM     11     33       I.
FT   DOMAIN       34     46       PERIPLASMIC.
FT   TRANSMEM     47     67       II.
FT   DOMAIN       68     74       CYTOPLASMIC.
FT   TRANSMEM     75     99       III.
FT   DOMAIN      100    102       PERIPLASMIC.
FT   TRANSMEM    103    125       IV.
FT   DOMAIN      126    144       CYTOPLASMIC.
FT   TRANSMEM    145    163       V.
FT   DOMAIN      164    167       PERIPLASMIC.
FT   TRANSMEM    168    187       VI.
FT   DOMAIN      188    211       CYTOPLASMIC.
FT   TRANSMEM    212    234       VII.
FT   DOMAIN      235    259       PERIPLASMIC.
FT   TRANSMEM    260    281       VIII.
FT   DOMAIN      282    290       CYTOPLASMIC.
FT   TRANSMEM    291    310       IX.
FT   DOMAIN      311    314       PERIPLASMIC.
FT   TRANSMEM    315    334       X.
FT   DOMAIN      335    346       CYTOPLASMIC.
FT   TRANSMEM    347    366       XI.
FT   DOMAIN      367    379       PERIPLASMIC.
FT   TRANSMEM    380    399       XII.
FT   DOMAIN      400    417       CYTOPLASMIC.
FT   SITE         33     33       MAY BE INVOLVED IN SUGAR RECOGNITION.
FT   MUTAGEN     237    237       D->N,G: DEFECT IN MELIBIOSE TRANSPORT.
FT   MUTAGEN     358    358       K->T: DEFECT IN MELIBIOSE TRANSPORT.
SQ   SEQUENCE   417 AA;  46503 MW;  4EFE9F96 CRC32;
     MYYLKNTNFW MFGLFFFFYF FIMGAYFPFF PIWLHDINHI SKSDTGIIFA AISLFSLLFQ
     PLFGLLSDKL GLRKYLLWII TGMLVMFAPF FIFIFGPLLQ YNILVGSIVG GIYLGFCFNA
     GAPAVEAFIE KVSRRSNFEF GRARMFGCVG WALCASIVGI MFTINNQFVF WLGSGCALIL
     AVLLFFAKTD APSSATVANA VGANHSAFSL KLALELFRQP KLWFLSLYVI GVSCTYDVFD
     QQFANFFTSF FATGEQGTRV FGYVTTMGEL LNASIMFFAP LIINRIGGKN ALLLAGTIMS
     VRIIGSSFAT SALEVVILKT LHMFEVPFLL VGCFKYITSQ FEVRFSATIY LVCFCFFKQL
     AMIFMSVLAG NMYESIGFQG AYLVLGLVAL GFTLISVFTL SGPGPLSLLR RQVNEVA
//
ID   BGAL_ECOLI     STANDARD;      PRT;  1023 AA.
AC   P00722;
DT   21-JUL-1986 (Rel. 01, Created)
DT   21-JUL-1986 (Rel. 01, Last sequence update)
DT   15-JUL-1999 (Rel. 38, Last annotation update)
DE   BETA-GALACTOSIDASE (EC 3.2.1.23) (LACTASE).
GN   LACZ.
OS   Escherichia coli.
OC   Bacteria; Proteobacteria; gamma subdivision; Enterobacteriaceae;
OC   Escherichia.
RN   [1]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 84028567.
RA   KALNINS A., OTTO K., RUTHER U., MULLER-HILL B.;
RT   "Sequence of the lacZ gene of Escherichia coli.";
RL   EMBO J. 2:593-597(1983).
RN   [2]
RP   SEQUENCE FROM N.A.
RC   STRAIN=K12 / MG1655;
RX   MEDLINE; 97426617.
RA   BLATTNER F.R., PLUNKETT G. III, BLOCH C.A., PERNA N.T., BURLAND V.,
RA   RILEY M., COLLADO-VIDES J., GLASNER F.D., RODE C.K., MAYHEW G.F.,
RA   GREGOR J., DAVIS N.W., KIRKPATRICK H.A., GOEDEN M.A., ROSE D.J.,
RA   MAU B., SHAO Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1474(1997).
RN   [3]
RP   SEQUENCE FROM N.A.
RA   DUNCAN M., ALLEN E., ARAUJO R., APARICIO A.M., CHUNG E., DAVIS K.,
RA   FEDERSPIEL N., HYMAN R., KALMAN S., KOMP C., KURDI O., LEW H.,
RA   LIN D., NAMATH A., OEFNER P., ROBERTS D., SCHRAMM S., DAVIS R.W.;
RL   Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   SEQUENCE.
RX   MEDLINE; 78218239.
RA   FOWLER A.V., ZABIN I.;
RT   "Amino acid sequence of beta-galactosidase. XI. Peptide ordering
RT   procedures and the complete sequence.";
RL   J. Biol. Chem. 253:5521-5525(1978).
RN   [5]
RP   SEQUENCE OF 355-475 FROM N.A.
RX   MEDLINE; 80188189.
RA   CALOS M.P., MILLER J.H.;
RT   "Molecular consequences of deletion formation mediated by the
RT   transposon Tn9.";
RL   Nature 285:38-41(1980).
RN   [6]
RP   SEQUENCE OF 1007-1023 FROM N.A.
RX   MEDLINE; 80120651.
RA   BUECHEL D.E., GRONENBORN B., MUELLER-HILL B.;
RT   "Sequence of the lactose permease gene.";
RL   Nature 283:541-545(1980).
RN   [7]
RP   ACTIVE SITE REGIONS.
RX   MEDLINE; 83290932.
RA   FOWLER A.V., SMITH P.J.;
RT   "The active site regions of lacZ and ebg beta-galactosidases are
RT   homologous.";
RL   J. Biol. Chem. 258:10204-10207(1983).
RN   [8]
RP   ACTIVE SITE GLU-461.
RX   MEDLINE; 84108409.
RA   HERRCHEN M., LEGLER G.;
RT   "Identification of an essential carboxylate group at the active site
RT   of lacZ beta-galactosidase from Escherichia coli.";
RL   Eur. J. Biochem. 138:527-531(1984).
RN   [9]
RP   ACTIVE SITE GLU-537.
RX   MEDLINE; 92283812.
RA   GEBLER J.C., AEBERSOLD R., WITHERS S.G.;
RT   "Glu-537, not Glu-461, is the nucleophile in the active site of (lac
RT   Z) beta-galactosidase from Escherichia coli.";
RL   J. Biol. Chem. 267:11126-11130(1992).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS).
RX   MEDLINE; 94277211.
RA   JACOBSON R.H., ZHANG X.-J., DUBOSE R.F., MATTHEWS B.W.;
RT   "Three-dimensional structure of beta-galactosidase from E. coli.";
RL   Nature 369:761-766(1994).
CC   -!- CATALYTIC ACTIVITY: HYDROLYSIS OF TERMINAL, NON-REDUCING BETA-D-
CC       GALACTOSE RESIDUES IN BETA-D-GALACTOSIDES.
CC   -!- SUBUNIT: HOMOTETRAMER.
CC   -!- SIMILARITY: BELONGS TO FAMILY 2 OF GLYCOSYL HYDROLASES.
CC   -!- DATABASE: NAME=Worthington enzyme manual;
CC       WWW="http://www.worthington-biochem.com/manual/G/BG.html".
CC   -!- DATABASE: NAME=ProZyme technical fact sheet;
CC       WWW="http://www.prozyme.com/technical/bgaldata.html".
CC   --------------------------------------------------------------------------
CC   This SWISS-PROT entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use  by  non-profit  institutions as long  as its content  is  in  no  way
CC   modified and this statement is not removed.  Usage  by  and for commercial
CC   entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC   or send an email to license@isb-sib.ch).
CC   --------------------------------------------------------------------------
DR   EMBL; J01636; AAA24053.1; -.
DR   EMBL; AE000141; AAC73447.1; -.
DR   EMBL; U73857; AAB18068.1; -.
DR   EMBL; V00296; CAA23573.1; -.
DR   EMBL; V00295; CAA23570.1; -.
DR   PIR; A00898; GBEC.
DR   PDB; 1BGL; 07-DEC-95.
DR   PDB; 1BGM; 07-DEC-95.
DR   ECO2DBASE; E123.0; 6TH EDITION.
DR   ECOGENE; EG10527; LACZ.
DR   PFAM; PF00703; Glyco_hydro_2; 1.
DR   PROSITE; PS00719; GLYCOSYL_HYDROL_F2_1; 1.
DR   PROSITE; PS00608; GLYCOSYL_HYDROL_F2_2; 1.
KW   Hydrolase; Glycosidase; 3D-structure.
FT   INIT_MET      0      0
FT   ACT_SITE    461    461       PROTON DONOR.
FT   ACT_SITE    537    537       NUCLEOPHILE.
SQ   SEQUENCE   1023 AA;  116351 MW;  BFFE7869 CRC32;
     TMITDSLAVV LQRRDWENPG VTQLNRLAAH PPFASWRNSE EARTDRPSQQ LRSLNGEWRF
     AWFPAPEAVP ESWLECDLPE ADTVVVPSNW QMHGYDAPIY TNVTYPITVN PPFVPTENPT
     GCYSLTFNVD ESWLQEGQTR IIFDGVNSAF HLWCNGRWVG YGQDSRLPSE FDLSAFLRAG
     ENRLAVMVLR WSDGSYLEDQ DMWRMSGIFR DVSLLHKPTT QISDFHVATR FNDDFSRAVL
     EAEVQMCGEL RDYLRVTVSL WQGETQVASG TAPFGGEIID ERGGYADRVT LRLNVENPKL
     WSAEIPNLYR AVVELHTADG TLIEAEACDV GFREVRIENG LLLLNGKPLL IRGVNRHEHH
     PLHGQVMDEQ TMVQDILLMK QNNFNAVRCS HYPNHPLWYT LCDRYGLYVV DEANIETHGM
     VPMNRLTDDP RWLPAMSERV TRMVQRDRNH PSVIIWSLGN ESGHGANHDA LYRWIKSVDP
     SRPVQYEGGG ADTTATDIIC PMYARVDEDQ PFPAVPKWSI KKWLSLPGET RPLILCEYAH
     AMGNSLGGFA KYWQAFRQYP RLQGGFVWDW VDQSLIKYDE NGNPWSAYGG DFGDTPNDRQ
     FCMNGLVFAD RTPHPALTEA KHQQQFFQFR LSGQTIEVTS EYLFRHSDNE LLHWMVALDG
     KPLASGEVPL DVAPQGKQLI ELPELPQPES AGQLWLTVRV VQPNATAWSE AGHISAWQQW
     RLAENLSVTL PAASHAIPHL TTSEMDFCIE LGNKRWQFNR QSGFLSQMWI GDKKQLLTPL
     RDQFTRAPLD NDIGVSEATR IDPNAWVERW KAAGHYQAEA ALLQCTADTL ADAVLITTAH
     AWQHQGKTLF ISRKTYRIDG SGQMAITVDV EVASDTPHPA RIGLNCQLAQ VAERVNWLGL
     GPQENYPDRL TAACFDRWDL PLSDMYTPYV FPSENGLRCG TRELNYGPHQ WRGDFQFNIS
     RYSQQQLMET SHRHLLHAEE GTWLNIDGFH MGIGGDDSWS PSVSAEFQLS AGRYHYQLVW
     CQK
//
ID   THGA_ECOLI     STANDARD;      PRT;   203 AA.
AC   P07464;
DT   01-APR-1988 (Rel. 07, Created)
DT   01-APR-1988 (Rel. 07, Last sequence update)
DT   15-JUL-1998 (Rel. 36, Last annotation update)
DE   GALACTOSIDE O-ACETYLTRANSFERASE (EC 2.3.1.18) (THIOGALACTOSIDE
DE   ACETYLTRANSFERASE).
GN   LACA.
OS   Escherichia coli.
OC   Bacteria; Proteobacteria; gamma subdivision; Enterobacteriaceae;
OC   Escherichia.
RN   [1]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 86016712.
RA   HEDIGER M.A., JOHNSON D.F., NIERLICH D.P., ZABIN I.;
RT   "DNA sequence of the lactose operon: the lacA gene and the
RT   transcriptional termination region.";
RL   Proc. Natl. Acad. Sci. U.S.A. 82:6414-6418(1985).
RN   [2]
RP   SEQUENCE FROM N.A.
RC   STRAIN=K12 / MG1655;
RX   MEDLINE; 97426617.
RA   BLATTNER F.R., PLUNKETT G. III, BLOCH C.A., PERNA N.T., BURLAND V.,
RA   RILEY M., COLLADO-VIDES J., GLASNER F.D., RODE C.K., MAYHEW G.F.,
RA   GREGOR J., DAVIS N.W., KIRKPATRICK H.A., GOEDEN M.A., ROSE D.J.,
RA   MAU B., SHAO Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1474(1997).
RN   [3]
RP   SEQUENCE.
RX   MEDLINE; 85200082.
RA   FOWLER A.V., HEDIGER M.A., MUSSO R.E., ZABIN I.;
RT   "The amino acid sequence of thiogalactoside transacetylase of
RT   Escherichia coli.";
RL   Biochimie 67:101-108(1985).
RN   [4]
RP   SEQUENCE OF 1-26 FROM N.A.
RX   MEDLINE; 80120651.
RA   BUECHEL D.E., GRONENBORN B., MUELLER-HILL B.;
RT   "Sequence of the lactose permease gene.";
RL   Nature 283:541-545(1980).
CC   -!- CATALYTIC ACTIVITY: ACETYL-COA + A BETA-D-GALACTOSIDE = COA +
CC       A 6-ACETYL-BETA-D-GALACTOSIDE.
CC   -!- PATHWAY: BIOSYNTHESIS OF LACTOSE.
CC   -!- SUBUNIT: HOMODIMER.
CC   -!- SUBCELLULAR LOCATION: CYTOPLASMIC.
CC   -!- PTM: THE AMINO TERMINUS OF THIS PROTEIN IS HETEROGENOUS BECAUSE
CC       THE INITIATOR METHIONINE IS ONLY PARTIALLY CLEAVED.
CC   -!- SIMILARITY: BELONGS TO THE CYSE/LACA/LPXA/NODL FAMILY OF
CC       ACETYLTRANSFERASES. COMPOSED OF MULTIPLE REPEATS OF [LIV]-G-X(4).
CC   --------------------------------------------------------------------------
CC   This SWISS-PROT entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use  by  non-profit  institutions as long  as its content  is  in  no  way
CC   modified and this statement is not removed.  Usage  by  and for commercial
CC   entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC   or send an email to license@isb-sib.ch).
CC   --------------------------------------------------------------------------
DR   EMBL; J01636; AAA24055.1; -.
DR   EMBL; X51872; CAA36162.1; -.
DR   EMBL; AE000141; AAC73445.1; -.
DR   EMBL; V00295; CAA23572.1; -.
DR   PIR; A23558; XXECTG.
DR   ECOGENE; EG10524; LACA.
DR   PFAM; PF00132; hexapep; 2.
DR   PROSITE; PS00101; HEXAPEP_TRANSFERASES; 1.
KW   Lactose biosynthesis; Transferase; Acyltransferase; Repeat.
SQ   SEQUENCE   203 AA;  22799 MW;  0EF7D5BC CRC32;
     MNMPMTERIR AGKLFTDMCE GLPEKRLRGK TLMYEFNHSH PSEVEKRESL IKEMFATVGE
     NAWVEPPVYF SYGSNIHIGR NFYANFNLTI VDDYTVTIGD NVLIAPNVTL SVTGHPVHHE
     LRKNGEMYSF PITIGNNVWI GSHVVINPGV TIGDNSVIGA GSIVTKDIPP NVVAAGVPCR
     VIREINDRDK HYYFKDYKVE SSV
//
ID   12S1_ARATH     STANDARD;      PRT;   472 AA.
AC   P15455;
DT   01-APR-1990 (Rel. 14, Created)
DT   01-APR-1990 (Rel. 14, Last sequence update)
DT   15-DEC-1998 (Rel. 37, Last annotation update)
DE   12S SEED STORAGE PROTEIN PRECURSOR.
GN   CRA1.
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   euphyllophytes; Spermatophyta; Magnoliophyta; eudicotyledons;
OC   core eudicots; Rosidae; eurosids II; Brassicales; Brassicaceae;
OC   Arabidopsis.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   STRAIN=CV. LANDSBERG ERECTA;
RA   PANG P.P., PRUITT R.E., MEYEROWITZ E.M.;
RT   "Molecular cloning, genome organization , expression and evolution of
RT   12S seed storage protein genes of Arabidopsis thaliana.";
RL   Plant Mol. Biol. 11:805-820(1988).
RN   [2]
RP   SEQUENCE OF 420-472 FROM N.A.
RC   STRAIN=CV. COLUMBIA;
RA   RAYNAL M., GRELLET F., LAUDIE M., MEYER Y., COOKE R., DELSENY M.;
RL   Submitted (OCT-1992) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: THIS IS A SEED STORAGE PROTEIN.
CC   -!- SUBUNIT: HEXAMER; EACH SUBUNIT IS COMPOSED OF AN ACIDIC AND A
CC       BASIC CHAIN DERIVED FROM A SINGLE PRECURSOR AND LINKED BY A
CC       DISULFIDE BOND.
CC   -!- SIMILARITY: BELONGS TO THE 11S SEED STORAGE PROTEINS (GLOBULINS)
CC       FAMILY.
CC   --------------------------------------------------------------------------
CC   This SWISS-PROT entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use  by  non-profit  institutions as long  as its content  is  in  no  way
CC   modified and this statement is not removed.  Usage  by  and for commercial
CC   entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC   or send an email to license@isb-sib.ch).
CC   --------------------------------------------------------------------------
DR   EMBL; M37247; AAA32777.1; -.
DR   EMBL; X14312; CAA32493.1; -.
DR   EMBL; Z17590; CAA79005.1; -.
DR   PIR; S08509; S08509.
DR   PFAM; PF00190; Seedstore_11s; 1.
DR   PROSITE; PS00305; 11S_SEED_STORAGE; 1.
KW   Seed storage protein; Multigene family; Signal.
FT   SIGNAL        1     24       POTENTIAL.
FT   CHAIN        25    282       ACIDIC CHAIN (BY SIMILARITY).
FT   CHAIN       283    472       BASIC CHAIN (BY SIMILARITY).
FT   DISULFID    112    289       INTERCHAIN (ALPHA-BETA) (POTENTIAL).
SQ   SEQUENCE   472 AA;  52624 MW;  E78F359C CRC32;
     MARVSSLLSF CLTLLILFHG YAAQQGQQGQ QFPNECQLDQ LNALEPSHVL KSEAGRIEVW
     DHHAPQLRCS GVSFARYIIE SKGLYLPSFF NTAKLSFVAK GRGLMGKVIP GCAETFQDSS
     EFQPRFEGQG QSQRFRDMHQ KVEHIRSGDT IATTPGVAQW FYNDGQQPLV IVSVFDLASH
     QNQLDRNPRP FYLAGNNPQG QVWLQGREQQ PQKNIFNGFG PEVIAQALKI DLQTAQQLQN
     QDDNRGNIVR VQGPFGVIRP PLRGQRPQEE EEEEGRHGRH GNGLEETICS ARCTDNLDDP
     SRADVYKPQL GYISTLNSYD LPILRFIRLS ALRGSIRQNA MVLPQWNANA NAILYETDGE
     AQIQIVNDNG NRVFDGQVSQ GQLIAVPQGF SVVKRATSNR FQWVEFKTNA NAQINTLAGR
     TSVLRGLPLE VITNGFQISP EEARRVKFNT LETTLTHSSG PASYGRPRVA AA
//
ID   OPSD_HUMAN     STANDARD;      PRT;   348 AA.
AC   P08100; Q16414;
DT   01-AUG-1988 (Rel. 08, Created)
DT   01-AUG-1988 (Rel. 08, Last sequence update)
DT   15-JUL-1999 (Rel. 38, Last annotation update)
DE   RHODOPSIN.
GN   RHO.
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Mammalia;
OC   Eutheria; Primates; Catarrhini; Hominidae; Homo.
RN   [1]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 84272729.
RA   NATHANS J., HOGNESS D.S.;
RT   "Isolation and nucleotide sequence of the gene encoding human
RT   rhodopsin.";
RL   Proc. Natl. Acad. Sci. U.S.A. 81:4851-4855(1984).
RN   [2]
RP   SEQUENCE OF 1-120 FROM N.A.
RA   BENNETT J., BELLER B., SUN D., KARIKO K.;
RL   Submitted (NOV-1994) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   REVIEW ON ADRP VARIANTS.
RX   MEDLINE; 94004905.
RA   AL-MAGHTHEH M., GREGORY C., INGLEHEARN C., HARDCASTLE A.,
RA   BHATTACHARYA S.;
RT   "Rhodopsin mutations in autosomal dominant retinitis pigmentosa.";
RL   Hum. Mutat. 2:249-255(1993).
RN   [4]
RP   VARIANT ADRP HIS-23.
RX   MEDLINE; 90136922.
RA   DRYJA T.P., MCGEE T.L., REICHEI E., HAHN L.B., COWLEY G.S.,
RA   YANDELL D.W., SANDBERG M.A., BERSON E.L.;
RT   "A point mutation of the rhodopsin gene in one form of retinitis
RT   pigmentosa.";
RL   Nature 343:364-366(1990).
RN   [5]
RP   VARIANTS ADRP.
RX   MEDLINE; 91051574.
RA   FARRAR G.J., KENNA P., REDMOND R., MCWILLIAM P., BRADLEY D.G.,
RA   HUMPHRIES M.M., SHARP E.M., INGLEHEARN C.F., BASHIR R., JAY M.,
RA   WATTY A., LUDWIG M., SCHINZEL A., SAMANNS C., GAL A.,
RA   BHATTACHARYA S.S., HUMPHRIES P.;
RT   "Autosomal dominant retinitis pigmentosa: absence of the rhodopsin
RT   proline-->histidine substitution (codon 23) in pedigrees from
RT   Europe.";
RL   Am. J. Hum. Genet. 47:941-945(1990).
RN   [6]
RP   VARIANTS ADRP HIS-23; ARG-58; LEU-347 AND SER-347.
RX   MEDLINE; 91015273.
RA   DRYJA T.P., MCGEE T.L., HAHN L.B., COWLEY G.S., OLSSON J.E.,
RA   REICHEL E., SANDBERG M.A., BERSON E.L.;
RT   "Mutations within the rhodopsin gene in patients with autosomal
RT   dominant retinitis pigmentosa.";
RL   New Engl. J. Med. 323:1302-1307(1990).
RN   [7]
RP   VARIANT ADRP ILE-255 DEL.
RX   MEDLINE; 91090106.
RA   INGLEHEARN C.F., BASHIR R., LESTER D.H., JAY M., BIRD A.C.,
RA   BHATTACHARYA S.S.;
RT   "A 3-bp deletion in the rhodopsin gene in a family with autosomal
RT   dominant retinitis pigmentosa.";
RL   Am. J. Hum. Genet. 48:26-30(1991).
RN   [8]
RP   VARIANT ADRP PRO-347.
RX   MEDLINE; 92120672.
RA   GAL A., ARTLICH A., LUDWIG M., NIEMEYER G., OLEK K.,
RA   SCHWINGER E., SCHINZEL A.;
RT   "Pro-347-Arg mutation of the rhodopsin gene in autosomal dominant
RT   retinitis pigmentosa.";
RL   Genomics 11:468-470(1991).
RN   [9]
RP   VARIANTS ADRP.
RX   MEDLINE; 91319709.
RA   SUNG C.H., DAVENPORT C.M., HENNESSEY J.C., MAUMENEE I.H.,
RA   JACOBSON S.G., HECKENLIVELY J.R., NOWAKOWSKI R., FISHMAN G.,
RA   GOURAS P., NATHANS J.;
RT   "Rhodopsin mutations in autosomal dominant retinitis pigmentosa.";
RL   Proc. Natl. Acad. Sci. U.S.A. 88:6481-6485(1991).
RN   [10]
RP   VARIANTS ADRP.
RX   MEDLINE; 92021049.
RA   DRYJA T.P., HAHN L.B., COWLEY G.S., MCGEE T.L., BERSON E.L.;
RT   "Mutation spectrum of the rhodopsin gene among patients with
RT   autosomal dominant retinitis pigmentosa.";
RL   Proc. Natl. Acad. Sci. U.S.A. 88:9370-9374(1991).
RN   [11]
RP   VARIANTS ADRP MET-17; HIS-23; ARG-58; SER-182 AND LEU-267.
RX   MEDLINE; 91377732.
RA   SHEFFIELD V.C., FISHMAN G.A., BECK J.S., KIMURA A.E., STONE E.M.;
RT   "Identification of novel rhodopsin mutations associated with
RT   retinitis pigmentosa by GC-clamped denaturing gradient gel
RT   electrophoresis.";
RL   Am. J. Hum. Genet. 49:699-706(1991).
RN   [12]
RP   VARIANT ADRP ARG-207.
RX   MEDLINE; 93258325.
RA   FARRAR G.J., FINDLAY J.B.C., KUMAR-SINGH R., KENNA P., HUMPHRIES M.M.,
RA   SHARPE E., HUMPHRIES P.;
RT   "Autosomal dominant retinitis pigmentosa: a novel mutation in the
RT   rhodopsin gene in the original 3q linked family.";
RL   Hum. Mol. Genet. 1:769-771(1992).
RN   [13]
RP   VARIANTS ADRP MET-17; AND LEU-347.
RX   MEDLINE; 93004784.
RA   FUJIKI K., HOTTA Y., HAYAKAWA M., SAKUMA H., SHIONO T., NORO M.,
RA   SAKUMA T., TAMAI M., HIKIJI K., KAWAGUCHI R., HOSHI A., NAKAJIMA A.,
RA   KANAI A.;
RT   "Point mutations of rhodopsin gene found in Japanese families with
RT   autosomal dominant retinitis pigmentosa (ADRP).";
RL   Jpn. J. Hum. Genet. 37:125-132(1992).
RN   [14]
RP   VARIANTS ADRP A-51; I-104; R-106; G-135; S-140; E-188; M-209 & R-211.
RX   MEDLINE; 93304432.
RA   MACKE J.P., DAVENPORT C.M., JACOBSON S.G., HENNESSEY J.C.,
RA   GONZALEZ-FERNANDEZ F., CONWAY B.P., HECKENLIVELY J., PALMER R.,
RA   MAUMENEE I.H., SIEVING P., GOURAS P., GOOD W., NATHANS J.;
RT   "Identification of novel rhodopsin mutations responsible for
RT   retinitis pigmentosa: implications for the structure and function of
RT   rhodopsin.";
RL   Am. J. Hum. Genet. 53:80-89(1993).
RN   [15]
RP   VARIANT ADRP SER-15.
RX   MEDLINE; 93357759.
RA   KRANICH H., BARTKOWSKI S., DENTON M.J., KREY S., DICKINSON P.,
RA   DUVIGNEAU C., GAL A.;
RT   "Autosomal dominant 'sector' retinitis pigmentosa due to a point
RT   mutation predicting an Asn-15-Ser substitution of rhodopsin.";
RL   Hum. Mol. Genet. 2:813-814(1993).
RN   [16]
RP   VARIANT CSNB4 GLU-292.
RX   MEDLINE; 93364423.
RA   DRYJA T.P., BERSON E.L., RAO V.R., OPRIAN D.D.;
RT   "Heterozygous missense mutation in the rhodopsin gene as a cause of
RT   congenital stationary night blindness.";
RL   Nat. Genet. 4:280-283(1993).
RN   [17]
RP   VARIANTS ADRP.
RX   MEDLINE; 94375083.
RA   VAITHINATHAN R., BERSON E.L., DRYJA T.P.;
RT   "Further screening of the rhodopsin gene in patients with autosomal
RT   dominant retinitis pigmentosa.";
RL   Genomics 21:461-463(1994).
RN   [18]
RP   VARIANT ADRP THR-44.
RX   MEDLINE; 94357587.
RA   REIG C., ANTICH J., GEAN E., GARCIA-SANDOVAL B., RAMOS C., AYUSO C.,
RA   CARBALLO M.;
RT   "Identification of a novel rhodopsin mutation (Met-44-Thr) in a
RT   simplex case of retinitis pigmentosa.";
RL   Hum. Genet. 94:283-286(1994).
RN   [19]
RP   VARIANTS ADRP PHE-110; PRO-131 AND VAL-164.
RX   MEDLINE; 95072600.
RA   FUCHS S., KRANICH H., DENTON M.J., ZRENNER E., BHATTACHARYA S.S.,
RA   HUMPHRIES P., GAL A.;
RT   "Three novel rhodopsin mutations (C110F, L131P, A164V) in patients
RT   with autosomal dominant retinitis pigmentosa.";
RL   Hum. Mol. Genet. 3:1203-1203(1994).
RN   [20]
RP   VARIANT ADRP GLN-171.
RX   MEDLINE; 95078852.
RA   ANTINOLO G., SANCHEZ B., BORREGO S., RUEDA T., CHAPARRO P.,
RA   CABEZA J.C.;
RT   "Identification of a new mutation at codon 171 of rhodopsin gene
RT   causing autosomal dominant retinitis pigmentosa.";
RL   Hum. Mol. Genet. 3:1421-1421(1994).
RN   [21]
RP   VARIANTS ADRP PHE-127; PRO-131; ASN-178; ARG-267 AND ARG-297.
RX   MEDLINE; 95078858.
RA   SOUIED E., GERBER S., ROZET J.M., BONNEAU D., DUFIER J.L., GHAZI I.,
RA   PHILIP N., SOUBRANE G., COSCAS G., MUNNICH A.;
RT   "Five novel missense mutations of the rhodopsin gene in autosomal
RT   dominant retinitis pigmentosa.";
RL   Hum. Mol. Genet. 3:1433-1434(1994).
RN   [22]
RP   VARIANTS ADRP ARG-40 AND LYS-216.
RX   MEDLINE; 94362717.
RA   AL-MAGHTHEH M., INGLEHEARN C., LUNT P., JAY M., BIRD A.,
RA   BHATTACHARYA S.;
RT   "Two new rhodopsin transversion mutations (L40R; M216K) in families
RT   with autosomal dominant retinitis pigmentosa.";
RL   Hum. Mutat. 3:409-410(1994).
RN   [23]
RP   VARIANT ADRP LEU-345.
RX   MEDLINE; 94321123.
RA   ROSAS D.J., ROMAN A.J., WEISSBROD P., MACKE J.P., NATHANS J.;
RT   "Autosomal dominant retinitis pigmentosa in a large family: a
RT   clinical and molecular genetic study.";
RL   Invest. Ophthalmol. Vis. Sci. 35:3134-3144(1994).
RN   [24]
RP   VARIANT ARRP LYS-150.
RX   MEDLINE; 95078913.
RA   KUMARAMANICKAVEL G., MAW M., DENTON M.J., JOHN S., SRIKUMARI C.R.,
RA   ORTH U., OEHLMANN R., GAL A.;
RT   "Missense rhodopsin mutation in a family with recessive RP.";
RL   Nat. Genet. 8:10-11(1994).
RN   [25]
RP   VARIANT ADRP ALA-347.
RX   MEDLINE; 95359993.
RA   MACKE J.P., HENNESSEY J.C., NATHANS J.;
RT   "Rhodopsin mutation proline347-to-alanine in a family with autosomal
RT   dominant retinitis pigmentosa indicates an important role for proline
RT   at position 347.";
RL   Hum. Mol. Genet. 4:775-776(1995).
RN   [26]
RP   VARIANT CSNB4 ASP-90.
RX   MEDLINE; 95148641.
RA   SIEVING P.A., RICHARDS J.E., NAARENDORP F., BINGHAM E.L., SCOTT K.,
RA   ALPERN M.;
RT   "Dark-light: model for nightblindness from the human rhodopsin
RT   Gly-90-->Asp mutation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 92:880-884(1995).
RN   [27]
RP   VARIANT ADRP TRP-135.
RX   MEDLINE; 96142043.
RA   SOUIED E., SOUBRANE G., BENLIAN P., COSCAS G.J., GERBER S.,
RA   MUNNICH A., KAPLAN J.;
RT   "Retinitis punctata albescens associated with the Arg135Trp mutation
RT   in the rhodopsin gene.";
RL   Am. J. Ophthalmol. 121:19-25(1996).
RN   [28]
RP   VARIANT ADRP ARG-109.
RX   MEDLINE; 98112414.
RA   GOLIATH R., BARDIEN S., SEPTEMBER A., MARTIN R., RAMESAR R.,
RA   GREENBERG J.;
RT   "Rhodopsin mutation G109R in a family with autosomal dominant
RT   retinitis pigmentosa.";
RL   Hum. Mutat. Suppl. 1:S40-S41(1998).
RN   [29]
RP   VARIANT CSNB4 ILE-94.
RX   MEDLINE; 99103467.
RA   AL-JANDAL N., FARRAR G.J., KIANG A.-S., HUMPHRIES M.M., BANNON N.,
RA   FINDLAY J.B.C., HUMPHRIES P., KENNA P.F.;
RT   "A novel mutation within the rhodopsin gene (Thr-94-Ile) causing
RT   autosomal dominant congenital stationary night blindness.";
RL   Hum. Mutat. 13:75-81(1999).
CC   -!- FUNCTION: VISUAL PIGMENTS ARE THE LIGHT-ABSORBING MOLECULES THAT
CC       MEDIATE VISION. THEY CONSIST OF AN APOPROTEIN, OPSIN, COVALENTLY
CC       LINKED TO CIS-RETINAL.
CC   -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN.
CC   -!- TISSUE SPECIFICITY: ROD SHAPED PHOTORECEPTOR CELLS WHICH MEDIATES
CC       VISION IN DIM LIGHT.
CC   -!- PTM: SOME OR ALL OF THE CARBOXYL-TERMINAL SER OR THR RESIDUES MAY
CC       BE PHOSPHORYLATED.
CC   -!- DISEASE: DEFECTS IN RHO ARE ONE OF THE CAUSES OF AUTOSOMAL
CC       DOMINANT RETINITIS PIGMENTOSA (ADRP). PATIENTS TYPICALLY HAVE
CC       NIGHT VISION BLINDNESS AND LOSS OF MIDPERIPHERAL VISUAL FIELD; AS
CC       THEIR CONDITION PROGRESSES, THEY LOSE THEIR FAR PERIPHERAL VISUAL
CC       FIELD AND EVENTUALLY CENTRAL VISION AS WELL.
CC   -!- DISEASE: DEFECTS IN RHO ARE ONE OF THE CAUSES OF AUTOSOMAL
CC       RECESSIVE RETINITIS PIGMENTOSA (ARRP).
CC   -!- DISEASE: DEFECTS IN RHO ARE ALSO ONE OF THE CAUSES OF CONGENITAL
CC       STATIONARY NIGHT BLINDNESS (CSNB4).
CC   -!- MISCELLANEOUS: THIS RHODOPSIN HAS AN ABSORPTION MAXIMA AT 495 NM.
CC   -!- SIMILARITY: BELONGS TO FAMILY 1 OF G-PROTEIN COUPLED RECEPTORS.
CC       OPSIN SUBFAMILY.
CC   -!- DATABASE: NAME=RHO; NOTE=Rhodopsin mutations page;
CC       WWW="http://mol.ophth.uiowa.edu/MOL_WWW/Rhotab.html".
CC   --------------------------------------------------------------------------
CC   This SWISS-PROT entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use  by  non-profit  institutions as long  as its content  is  in  no  way
CC   modified and this statement is not removed.  Usage  by  and for commercial
CC   entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC   or send an email to license@isb-sib.ch).
CC   --------------------------------------------------------------------------
DR   EMBL; U49742; AAC31763.1; -.
DR   EMBL; U16824; AAA97436.1; -.
DR   EMBL; S81166; AAB35906.1; -.
DR   PIR; A41200; OOHU.
DR   GCRDB; GCR_0085; -.
DR   MIM; 180380; -.
DR   MIM; 268000; -.
DR   MIM; 163500; -.
DR   PFAM; PF00001; 7tm_1; 1.
DR   PROSITE; PS00237; G_PROTEIN_RECEPTOR; 1.
DR   PROSITE; PS00238; OPSIN; 1.
KW   Photoreceptor; Retinal protein; Transmembrane; Glycoprotein; Vision;
KW   Phosphorylation; Lipoprotein; Palmitate; G-protein coupled receptor;
KW   Acetylation; Retinitis pigmentosa; Disease mutation.
FT   DOMAIN        1     36       EXTRACELLULAR.
FT   TRANSMEM     37     61       1 (POTENTIAL).
FT   DOMAIN       62     73       CYTOPLASMIC.
FT   TRANSMEM     74     98       2 (POTENTIAL).
FT   DOMAIN       99    113       EXTRACELLULAR.
FT   TRANSMEM    114    133       3 (POTENTIAL).
FT   DOMAIN      134    152       CYTOPLASMIC.
FT   TRANSMEM    153    176       4 (POTENTIAL).
FT   DOMAIN      177    202       EXTRACELLULAR.
FT   TRANSMEM    203    230       5 (POTENTIAL).
FT   DOMAIN      231    252       CYTOPLASMIC.
FT   TRANSMEM    253    276       6 (POTENTIAL).
FT   DOMAIN      277    284       EXTRACELLULAR.
FT   TRANSMEM    285    309       7 (POTENTIAL).
FT   DOMAIN      310    348       CYTOPLASMIC.
FT   MOD_RES       1      1       ACETYLATION (BY SIMILARITY).
FT   CARBOHYD      2      2       BY SIMILARITY.
FT   CARBOHYD     15     15       BY SIMILARITY.
FT   DISULFID    110    187       BY SIMILARITY.
FT   BINDING     296    296       RETINAL CHROMOPHORE.
FT   LIPID       322    322       PALMITATE (BY SIMILARITY).
FT   LIPID       323    323       PALMITATE (BY SIMILARITY).
FT   MOD_RES     343    343       PHOSPHORYLATION (BY RK) (BY SIMILARITY).
FT   VARIANT       4      4       T -> K (IN ADRP).
FT                                /FTId=VAR_004765.
FT   VARIANT      15     15       N -> S (IN ADRP).
FT                                /FTId=VAR_004766.
FT   VARIANT      17     17       T -> M (IN ADRP).
FT                                /FTId=VAR_004767.
FT   VARIANT      23     23       P -> H (IN ADRP; MOST COMMON VARIANT).
FT                                /FTId=VAR_004768.
FT   VARIANT      23     23       P -> L (IN ADRP).
FT                                /FTId=VAR_004769.
FT   VARIANT      28     28       Q -> H (IN ADRP).
FT                                /FTId=VAR_004770.
FT   VARIANT      40     40       L -> R (IN ADRP).
FT                                /FTId=VAR_004771.
FT   VARIANT      44     44       M -> T (IN ADRP).
FT                                /FTId=VAR_004772.
FT   VARIANT      45     45       F -> L (IN ADRP).
FT                                /FTId=VAR_004773.
FT   VARIANT      46     46       L -> R (IN ADRP).
FT                                /FTId=VAR_004774.
FT   VARIANT      51     51       G -> A (EFFECT NOT KNOWN).
FT                                /FTId=VAR_004775.
FT   VARIANT      51     51       G -> R (IN ADRP).
FT                                /FTId=VAR_004776.
FT   VARIANT      51     51       G -> V (IN ADRP).
FT                                /FTId=VAR_004777.
FT   VARIANT      53     53       P -> R (IN ADRP).
FT                                /FTId=VAR_004778.
FT   VARIANT      58     58       T -> R (IN ADRP).
FT                                /FTId=VAR_004779.
FT   VARIANT      68     71       MISSING (IN ADRP).
FT                                /FTId=VAR_004780.
FT   VARIANT      87     87       V -> D (IN ADRP).
FT                                /FTId=VAR_004781.
FT   VARIANT      89     89       G -> D (IN ADRP).
FT                                /FTId=VAR_004782.
FT   VARIANT      90     90       G -> D (IN ADRP).
FT                                /FTId=VAR_004783.
FT   VARIANT      94     94       T -> I (IN CSNB4).
FT                                /FTId=VAR_004784.
FT   VARIANT     104    104       V -> I.
FT                                /FTId=VAR_004785.
FT   VARIANT     106    106       G -> R (IN ADRP).
FT                                /FTId=VAR_004786.
FT   VARIANT     106    106       G -> W (IN ADRP).
FT                                /FTId=VAR_004787.
FT   VARIANT     109    109       G -> R (IN ADRP).
FT                                /FTId=VAR_004788.
FT   VARIANT     110    110       C -> F (IN ADRP).
FT                                /FTId=VAR_004789.
FT   VARIANT     110    110       C -> Y (IN ADRP).
FT                                /FTId=VAR_004790.
FT   VARIANT     114    114       G -> D (IN ADRP).
FT                                /FTId=VAR_004791.
FT   VARIANT     125    125       L -> R (IN ADRP).
FT                                /FTId=VAR_004792.
FT   VARIANT     127    127       S -> F (IN ADRP).
FT                                /FTId=VAR_004793.
FT   VARIANT     131    131       L -> P (IN ADRP).
FT                                /FTId=VAR_004794.
FT   VARIANT     135    135       R -> G (IN ADRP).
FT                                /FTId=VAR_004795.
FT   VARIANT     135    135       R -> L (IN ADRP).
FT                                /FTId=VAR_004796.
FT   VARIANT     135    135       R -> W (IN ADRP).
FT                                /FTId=VAR_004797.
FT   VARIANT     140    140       C -> S (IN ADRP).
FT                                /FTId=VAR_004798.
FT   VARIANT     150    150       E -> K (IN ARRP).
FT                                /FTId=VAR_004799.
FT   VARIANT     164    164       A -> E (IN ADRP).
FT                                /FTId=VAR_004800.
FT   VARIANT     164    164       A -> V (IN ADRP).
FT                                /FTId=VAR_004801.
FT   VARIANT     167    167       C -> R (IN ADRP).
FT                                /FTId=VAR_004802.
FT   VARIANT     171    171       P -> L (IN ADRP).
FT                                /FTId=VAR_004803.
FT   VARIANT     171    171       P -> Q (IN ADRP).
FT                                /FTId=VAR_004804.
FT   VARIANT     171    171       P -> S (IN ADRP).
FT                                /FTId=VAR_004805.
FT   VARIANT     178    178       Y -> C (IN ADRP).
FT                                /FTId=VAR_004806.
FT   VARIANT     178    178       Y -> N (IN ADRP).
FT                                /FTId=VAR_004807.
FT   VARIANT     181    181       E -> K (IN ADRP).
FT                                /FTId=VAR_004808.
FT   VARIANT     182    182       G -> S (IN ADRP).
FT                                /FTId=VAR_004809.
FT   VARIANT     186    186       S -> P (IN ADRP).
FT                                /FTId=VAR_004810.
FT   VARIANT     188    188       G -> E (IN ADRP).
FT                                /FTId=VAR_004811.
FT   VARIANT     188    188       G -> R (IN ADRP).
FT                                /FTId=VAR_004812.
FT   VARIANT     190    190       D -> N (IN ADRP).
FT                                /FTId=VAR_004813.
FT   VARIANT     190    190       D -> G (IN ADRP).
FT                                /FTId=VAR_004814.
FT   VARIANT     190    190       D -> Y (IN ADRP).
FT                                /FTId=VAR_004815.
FT   VARIANT     207    207       M -> R (IN ADRP).
FT                                /FTId=VAR_004816.
FT   VARIANT     209    209       V -> M (EFFECT NOT KNOWN).
FT                                /FTId=VAR_004817.
FT   VARIANT     211    211       H -> P (IN ADRP).
FT                                /FTId=VAR_004818.
FT   VARIANT     211    211       H -> R (IN ADRP).
FT                                /FTId=VAR_004819.
FT   VARIANT     216    216       M -> K (IN ADRP).
FT                                /FTId=VAR_004820.
FT   VARIANT     220    220       F -> C (IN ADRP).
FT                                /FTId=VAR_004821.
FT   VARIANT     222    222       C -> R (IN ADRP).
FT                                /FTId=VAR_004822.
FT   VARIANT     255    255       MISSING (IN ADRP).
FT                                /FTId=VAR_004823.
FT   VARIANT     264    264       MISSING (IN ADRP).
FT                                /FTId=VAR_004824.
FT   VARIANT     267    267       P -> L (IN ADRP).
FT                                /FTId=VAR_004825.
FT   VARIANT     267    267       P -> R (IN ADRP).
FT                                /FTId=VAR_004826.
FT   VARIANT     292    292       A -> E (IN CSNB4).
FT                                /FTId=VAR_004827.
FT   VARIANT     296    296       K -> E (IN ADRP).
FT                                /FTId=VAR_004828.
FT   VARIANT     297    297       S -> R (IN ADRP).
FT                                /FTId=VAR_004829.
FT   VARIANT     342    342       T -> M (IN ADRP).
FT                                /FTId=VAR_004830.
FT   VARIANT     345    345       V -> L (IN ADRP).
FT                                /FTId=VAR_004831.
FT   VARIANT     345    345       V -> M (IN ADRP).
FT                                /FTId=VAR_004832.
FT   VARIANT     347    347       P -> A (IN ADRP).
FT                                /FTId=VAR_004833.
FT   VARIANT     347    347       P -> L (IN ADRP; COMMON VARIANT).
FT                                /FTId=VAR_004834.
FT   VARIANT     347    347       P -> Q (IN ADRP).
FT                                /FTId=VAR_004835.
FT   VARIANT     347    347       P -> R (IN ADRP).
FT                                /FTId=VAR_004836.
FT   VARIANT     347    347       P -> S (IN ADRP).
FT                                /FTId=VAR_004837.
SQ   SEQUENCE   348 AA;  38892 MW;  07443BEA CRC32;
     MNGTEGPNFY VPFSNATGVV RSPFEYPQYY LAEPWQFSML AAYMFLLIVL GFPINFLTLY
     VTVQHKKLRT PLNYILLNLA VADLFMVLGG FTSTLYTSLH GYFVFGPTGC NLEGFFATLG
     GEIALWSLVV LAIERYVVVC KPMSNFRFGE NHAIMGVAFT WVMALACAAP PLAGWSRYIP
     EGLQCSCGID YYTLKPEVNN ESFVIYMFVV HFTIPMIIIF FCYGQLVFTV KEAAAQQQES
     ATTQKAEKEV TRMVIIMVIA FLICWVPYAS VAFYIFTHQG SNFGPIFMTI PAFFAKSAAI
     YNPVIYIMMN KQFRNCMLTT ICCGKNPLGD DEASATVSKT ETSQVAPA
//
ID   AMIC_PSEAE     STANDARD;      PRT;   384 AA.
AC   P27017;
DT   01-AUG-1992 (Rel. 23, Created)
DT   01-DEC-1992 (Rel. 24, Last sequence update)
DT   15-DEC-1998 (Rel. 37, Last annotation update)
DE   ALIPHATIC AMIDASE EXPRESSION-REGULATING PROTEIN.
GN   AMIC.
OS   Pseudomonas aeruginosa.
OC   Bacteria; Proteobacteria; gamma subdivision; Pseudomonas group;
OC   Pseudomonas.
RN   [1]
RP   SEQUENCE FROM N.A., AND SEQUENCE OF 1-18.
RC   STRAIN=PAC;
RX   MEDLINE; 91317707.
RA   WILSON S.A., DREW R.E.;
RT   "Cloning and DNA sequence of amiC, a new gene regulating expression
RT   of the Pseudomonas aeruginosa aliphatic amidase, and purification of
RT   the amiC product.";
RL   J. Bacteriol. 173:4914-4921(1991).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY.
RX   MEDLINE; 92106343.
RA   WILSON S.A., CHAYEN N.E., HEMMINGS A.M., DREW R.E., PEARL L.H.;
RT   "Crystallization of and preliminary X-ray data for the negative
RT   regulator (AmiC) of the amidase operon of Pseudomonas aeruginosa.";
RL   J. Mol. Biol. 222:869-871(1991).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
RX   MEDLINE; 95112789.
RA   PEARL L.H., O'HARA B., DREW R.E., WILSON S.A.;
RT   "Crystal structure of AmiC: the controller of transcription
RT   antitermination in the amidase operon of Pseudomonas aeruginosa.";
RL   EMBO J. 13:5810-5817(1994).
CC   -!- FUNCTION: NEGATIVELY REGULATES THE EXPRESSION OF THE ALIPHATIC
CC       AMIDASE OPERON. AMIC FUNCTIONS BY INHIBITING THE ACTION OF AMIR
CC       AT THE PROTEIN LEVEL. IT BINDS TO AMIR. IT EXHIBITS PROTEIN KINASE
CC       ACTIVITY.
CC   -!- SUBUNIT: HOMODIMER.
CC   -!- DOMAIN: CONSISTS OF TWO BETA-ALPHA-BETA DOMAINS WITH A CENTRAL
CC       CLEFT IN WHICH THE AMIDE BINDS.
CC   --------------------------------------------------------------------------
CC   This SWISS-PROT entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use  by  non-profit  institutions as long  as its content  is  in  no  way
CC   modified and this statement is not removed.  Usage  by  and for commercial
CC   entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC   or send an email to license@isb-sib.ch).
CC   --------------------------------------------------------------------------
DR   EMBL; X13776; CAA32024.1; -.
DR   PIR; A40359; A40359.
DR   PDB; 1PEA; 03-APR-96.
KW   Transferase; Kinase; Repressor; 3D-structure.
FT   INIT_MET      0      0
SQ   SEQUENCE   384 AA;  42704 MW;  68FF861F CRC32;
     GSHQERPLIG LLFSETGVTA DIERSHAYGA LLAVEQLNRE GGVGGRPIET LSQDPGGDPD
     RYRLCAEDFI RNRGVRFLVG CYMSHTRKAV MPVVERADAL LCYPTPYEGF EYSPNIVYGG
     PAPNQNSAPL AAYLIRHYGE RVVFIGSDYI YPRESNHVMR HLYRQHGGTV LEEIYIPLYP
     SDDDLQRAVE RIYQARADVV FSTVVGTGTA ELYRAIARRY GDGRRPPIAS LTTSEAEVAK
     MESDVAEGQV VVAPYFSSID TPASRAFVQA CHGFFPENAT ITAWAEAAYW QTLLLGRAAQ
     AAGNWRVEDV QRHLYDIDID APQGPVRVER QNNHSRLSSR IAEIDARGVF QVRWQSPEPI
     RPDPYVVVHN LDDWSASMGG GPLP
//
ID   AMIR_PSEAE     STANDARD;      PRT;   196 AA.
AC   P10932;
DT   01-JUL-1989 (Rel. 11, Created)
DT   01-JUL-1989 (Rel. 11, Last sequence update)
DT   15-DEC-1998 (Rel. 37, Last annotation update)
DE   ALIPHATIC AMIDASE REGULATOR.
GN   AMIR.
OS   Pseudomonas aeruginosa.
OC   Bacteria; Proteobacteria; gamma subdivision; Pseudomonas group;
OC   Pseudomonas.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   STRAIN=PAC;
RX   MEDLINE; 89211409.
RA   LOWE N., RICE P.M., DREW R.E.;
RT   "Nucleotide sequence of the aliphatic amidase regulator gene (amiR)
RT   of Pseudomonas aeruginosa.";
RL   FEBS Lett. 246:39-43(1989).
RN   [2]
RP   CHARACTERIZATION.
RX   MEDLINE; 95286483.
RA   WILSON S.A., DREW R.E.;
RT   "Transcriptional analysis of the amidase operon from Pseudomonas
RT   aeruginosa.";
RL   J. Bacteriol. 177:3052-3057(1995).
CC   -!- FUNCTION: POSITIVE CONTROLLING ELEMENT OF AMIE, THE GENE FOR
CC       ALIPHATIC AMIDASE. ACTS AS A TRANSCRIPTIONAL ANTITERMINATION
CC       FACTOR. IT IS THOUGHT TO ALLOW RNA POLYMERASE READ THROUGH A RHO-
CC       INDEPENDENT TRANSCRIPTION TERMINATOR BETWEEN THE AMIE PROMOTER AND
CC       GENE.
CC   --------------------------------------------------------------------------
CC   This SWISS-PROT entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use  by  non-profit  institutions as long  as its content  is  in  no  way
CC   modified and this statement is not removed.  Usage  by  and for commercial
CC   entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC   or send an email to license@isb-sib.ch).
CC   --------------------------------------------------------------------------
DR   EMBL; X13776; CAA32023.1; -.
DR   PIR; S03884; S03884.
KW   Transcription regulation; Activator.
SQ   SEQUENCE   196 AA;  21776 MW;  560A8AE3 CRC32;
     MSANSLLGSL RELQVLVLNP PGEVSDALVL QLIRIGCSVR QCWPPPEAFD VPVDVVFTSI
     FQNGHHDEIA ALLAAGTPRT TLVALVEYES PAVLSQIIEL ECHGVITQPL DAHRVLPVLV
     SARRISEEMA KLKQKTEQLQ DRIAGQARIN QAKVLLMQRH GWDEREAHQH LSREAMKRRE
     PILKIAQELL GNEPSA
//
ID   GCN4_YEAST     STANDARD;      PRT;   281 AA.
AC   P03069; P03068;
DT   21-JUL-1986 (Rel. 01, Created)
DT   21-JUL-1986 (Rel. 01, Last sequence update)
DT   15-JUL-1999 (Rel. 38, Last annotation update)
DE   GENERAL CONTROL PROTEIN GCN4 (AMINO ACID BIOSYNTHESIS REGULATORY
DE   PROTEIN).
GN   GCN4 OR ARG9 OR AAS3 OR YEL009C.
OS   Saccharomyces cerevisiae (Baker's yeast).
OC   Eukaryota; Fungi; Ascomycota; Hemiascomycetes; Saccharomycetales;
OC   Saccharomycetaceae; Saccharomyces.
RN   [1]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 85038531.
RA   HINNEBUSCH A.G.;
RT   "Evidence for translational regulation of the activator of general
RT   amino acid control in yeast.";
RL   Proc. Natl. Acad. Sci. U.S.A. 81:6442-6446(1984).
RN   [2]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 84298088.
RA   THIREOS G., PENN M.D., GREER H.;
RT   "5' untranslated sequences are required for the translational control
RT   of a yeast regulatory gene.";
RL   Proc. Natl. Acad. Sci. U.S.A. 81:5096-5100(1984).
RN   [3]
RP   SEQUENCE FROM N.A.
RC   STRAIN=S288C / AB972;
RA   DIETRICH F.S., MULLIGAN J.T., HENNESSEY K.M., ALLEN E., ARAUJO R.,
RA   AVILES E., BERNO A., BRENNAN T., CARPENTER J., CHEN E., CHERRY J.M.,
RA   CHUNG E., DUNCAN M., GUZMAN E., HARTZELL G., HUNICKE-SMITH S.,
RA   HYMAN R., KAYSER A., KOMP C., LASHKARI D., LEW H., LIN D.,
RA   MOSEDALE D., NAKAHARA K., NAMATH A., NORGREN R., OEFNER P., OH C.,
RA   PETEL F.X., ROBERTS D., SEHL P., SCHRAMM S., SHOGREN T., SMITH V.,
RA   TAYLOR P., WEI Y., YELTON M., BOTSTEIN D., DAVIS R.W.;
RL   Submitted (DEC-1994) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   DOMAINS.
RX   MEDLINE; 87002456.
RA   HOPE I.A., STRUHL K.;
RT   "Functional dissection of a eukaryotic transcriptional activator
RT   protein, GCN4 of yeast.";
RL   Cell 46:885-894(1986).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 250-281.
RX   MEDLINE; 92054531.
RA   O'SHEA E.K., KLEMM J.D., KIM P.S., ALBER T.;
RT   "X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel
RT   coiled coil.";
RL   Science 254:539-544(1991).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 226-281.
RX   MEDLINE; 93113690.
RA   ELLENBERGER T.E., BRANDL C.J., STRUHL K., HARRISON S.C.;
RT   "The GCN4 basic region leucine zipper binds DNA as a dimer of
RT   uninterrupted alpha helices: crystal structure of the protein-DNA
RT   complex.";
RL   Cell 71:1223-1237(1992).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 249-281.
RX   MEDLINE; 99057965.
RA   ECKERT D.M., MALASHKEVICH V.N., KIM P.S.;
RT   "Crystal structure of GCN4-pIQI, a trimeric coiled coil with buried
RT   polar residues.";
RL   J. Mol. Biol. 284:859-865(1998).
RN   [8]
RP   STRUCTURE BY NMR OF 237-281.
RX   MEDLINE; 91367802.
RA   SAUDEK V., PASTORE A., MORELLI M.A., FRANK R., GAUSEPOHL H.,
RA   GIBSON T.;
RT   "The solution structure of a leucine-zipper motif peptide.";
RL   Protein Eng. 4:519-529(1991).
CC   -!- FUNCTION: IS A TRANSCRIPTION FACTOR THAT IS RESPONSIBLE FOR THE
CC       ACTIVATION OF MORE THAN 30 GENES REQUIRED FOR AMINO ACID OR FOR
CC       PURINE BIOSYNTHESIS IN RESPONSE TO AMINO ACID OR PURINE
CC       STARVATION. BINDS AND RECOGNIZE THE DNA SEQUENCE:
CC       5'-TGA[CG]TCA-3'.
CC   -!- SUBUNIT: BINDS DNA AS A DIMER.
CC   -!- SUBCELLULAR LOCATION: NUCLEAR.
CC   -!- SIMILARITY: TO OTHER BZIP PROTEINS.
CC   --------------------------------------------------------------------------
CC   This SWISS-PROT entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use  by  non-profit  institutions as long  as its content  is  in  no  way
CC   modified and this statement is not removed.  Usage  by  and for commercial
CC   entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC   or send an email to license@isb-sib.ch).
CC   --------------------------------------------------------------------------
DR   EMBL; K02205; AAA34640.1; -.
DR   EMBL; K02649; AAA65521.1; -.
DR   EMBL; U18530; AAB64486.1; -.
DR   PIR; A03604; RGBYA1.
DR   PIR; A03605; RGBYA2.
DR   PDB; 1ZTA; 15-APR-93.
DR   PDB; 2ZTA; 15-OCT-92.
DR   PDB; 1YSA; 31-OCT-93.
DR   PDB; 1DGC; 22-JUN-94.
DR   PDB; 2DGC; 08-MAR-96.
DR   PDB; 1GCL; 03-JUN-95.
DR   PDB; 1GCM; 29-JAN-96.
DR   PDB; 1SWI; 08-NOV-96.
DR   PDB; 1ZII; 07-JUL-97.
DR   PDB; 1ZIJ; 07-JUL-97.
DR   PDB; 1ZIK; 07-JUL-97.
DR   PDB; 1ZIL; 07-JUL-97.
DR   PDB; 1ZIM; 07-JUL-97.
DR   PDB; 1PIQ; 30-SEP-98.
DR   PDB; 1CE9; 25-MAR-99.
DR   TRANSFAC; T00321; -.
DR   SGD; L0000683; GCN4.
DR   PFAM; PF00170; bZIP; 1.
DR   PROSITE; PS00036; BZIP_BASIC; 1.
KW   Amino-acid biosynthesis; Transcription regulation; Activator;
KW   DNA-binding; Nuclear protein; 3D-structure.
FT   DOMAIN      106    125       REQUIRED FOR TRANSCRIPTIONAL ACTIVATION.
FT   DNA_BIND    231    249       BASIC MOTIF.
FT   DOMAIN      253    274       LEUCINE-ZIPPER.
FT   CONFLICT    239    281       ARRSRARKLQRMKQLEDKVEELLSKNYHLENEVARLKKLVG
FT                                ER -> PGVLVRESCKE (IN REF. 2).
FT   HELIX       227    276
FT   TURN        277    277
SQ   SEQUENCE   281 AA;  31310 MW;  A2155238 CRC32;
     MSEYQPSLFA LNPMGFSPLD GSKSTNENVS ASTSTAKPMV GQLIFDKFIK TEEDPIIKQD
     TPSNLDFDFA LPQTATAPDA KTVLPIPELD DAVVESFFSS STDSTPMFEY ENLEDNSKEW
     TSLFDNDIPV TTDDVSLADK AIESTEEVSL VPSNLEVSTT SFLPTPVLED AKLTQTRKVK
     KPNSVVKKSH HVGKDDESRL DHLGVVAYNR KQRSIPLSPI VPESSDPAAL KRARNTEAAR
     RSRARKLQRM KQLEDKVEEL LSKNYHLENE VARLKKLVGE R
//
ID   FLAV_ANASP     STANDARD;      PRT;   169 AA.
AC   P11241;
DT   01-JUL-1989 (Rel. 11, Created)
DT   01-NOV-1990 (Rel. 16, Last sequence update)
DT   15-DEC-1998 (Rel. 37, Last annotation update)
DE   FLAVODOXIN.
GN   ISIB.
OS   Anabaena sp. (strain PCC 7120), and Anabaena sp. (strain PCC 7119).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Anabaena.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   STRAIN=PCC 7120;
RX   MEDLINE; 89296496.
RA   Leonhardt K.G., Straus N.A.;
RT   "Sequence of the flavodoxin gene from Anabaena variabilis 7120.";
RL   Nucleic Acids Res. 17:4384-4384(1989).
RN   [2]
RP   SEQUENCE FROM N.A.
RC   STRAIN=PCC 7119;
RX   MEDLINE; 92074973.
RA   Fillat M.F., Borrias W.E., Weisbeek P.J.;
RT   "Isolation and overexpression in Escherichia coli of the flavodoxin
RT   gene from Anabaena PCC 7119.";
RL   Biochem. J. 280:187-191(1991).
RN   [3]
RP   SEQUENCE OF 1-36.
RC   STRAIN=PCC 7119;
RX   MEDLINE; 90381288.
RA   Fillat M.F., Edmondson D.E., Gomez-Moreno C.;
RT   "Structural and chemical properties of a flavodoxin from Anabaena PCC
RT   7119.";
RL   Biochim. Biophys. Acta 1040:301-307(1990).
RN   [4]
RP   STRUCTURE BY NMR.
RC   STRAIN=PCC 7120;
RX   MEDLINE; 91104858.
RA   Stockman B.J., Krezel A.M., Markley J.L., Leonhardt K.G.,
RA   Straus N.A.;
RT   "Hydrogen-1, carbon-13, and nitrogen-15 NMR spectroscopy of Anabaena
RT   7120 flavodoxin: assignment of beta-sheet and flavin binding site
RT   resonances and analysis of protein-flavin interactions.";
RL   Biochemistry 29:9600-9609(1990).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RC   STRAIN=PCC 7120;
RX   MEDLINE; 93271891.
RA   Rao S.T., Shaffie F., Yu C., Satyshur K.A., Stockman B.J.,
RA   Markley J.L., Sundaralingam M.;
RT   "Structure of the oxidized long-chain flavodoxin from Anabaena 7120
RT   at 2-A resolution.";
RL   Protein Sci. 1:1413-1427(1992).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS).
RC   STRAIN=PCC 7120;
RA   Burkhart B.M., Ramakrishnan B., Yan H., Reedstrom R.J., Markley J.L.,
RA   Straus N.A., Sundaralingam M.;
RT   "Structure of the trigonal form of recombinant oxidized flavodoxin
RT   from Anabaena 7120 at 1.40-A resolution.";
RL   Acta Crystallogr. D 51:318-330(1995).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RC   STRAIN=PCC 7119;
RX   MEDLINE; 99318886.
RA   Fernandez-Recio J., Romero A., Sancho J.;
RT   "Energetics of a hydrogen bond (charged and neutral) and of a
RT   cation-pi interaction in apoflavodoxin.";
RL   J. Mol. Biol. 290:319-330(1999).
CC   -!- FUNCTION: LOW-POTENTIAL ELECTRON DONOR TO A NUMBER OF REDOX
CC       ENZYMES.
CC   -!- COFACTOR: FMN.
CC   -!- SIMILARITY: BELONGS TO THE FLAVODOXIN FAMILY.
CC   --------------------------------------------------------------------------
CC   This SWISS-PROT entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use  by  non-profit  institutions as long  as its content  is  in  no  way
CC   modified and this statement is not removed.  Usage  by  and for commercial
CC   entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC   or send an email to license@isb-sib.ch).
CC   --------------------------------------------------------------------------
DR   EMBL; S68006; AAB20462.1; -.
DR   EMBL; X14577; CAA32720.1; -.
DR   PIR; S04600; S04600.
DR   PIR; S18374; S18374.
DR   PIR; S20298; S20298.
DR   PDB; 1FLV; 31-OCT-93.
DR   PDB; 1FTG; 23-DEC-96.
DR   PDB; 1RCF; 26-JAN-95.
DR   PDB; 1QHE; 20-MAY-99.
DR   INTERPRO; IPR001226; -.
DR   PFAM; PF00258; flavodoxin; 1.
DR   PROSITE; PS00201; FLAVODOXIN; 1.
KW   Electron transport; Flavoprotein; FMN; 3D-structure.
FT   INIT_MET      0      0
FT   STRAND        4      8
FT   HELIX        14     26
FT   STRAND       31     35
FT   TURN         36     37
FT   HELIX        41     46
FT   STRAND       49     53
FT   STRAND       56     57
FT   TURN         58     60
FT   STRAND       61     62
FT   HELIX        64     70
FT   TURN         71     72
FT   HELIX        73     75
FT   TURN         79     80
FT   STRAND       82     88
FT   TURN         91     96
FT   TURN         98     99
FT   HELIX       100    111
FT   TURN        112    113
FT   STRAND      115    116
FT   STRAND      120    120
FT   TURN        123    124
FT   TURN        131    132
FT   STRAND      133    134
FT   TURN        135    136
FT   STRAND      137    138
FT   STRAND      141    143
FT   TURN        145    147
FT   HELIX       149    165
FT   TURN        166    168
SQ   SEQUENCE   169 AA;  18832 MW;  BB0BBD0B6DEF9A58 CRC64;
     SKKIGLFYGT QTGKTESVAE IIRDEFGNDV VTLHDVSQAE VTDLNDYQYL IIGCPTWNIG
     ELQSDWEGLY SELDDVDFNG KLVAYFGTGD QIGYADNFQD AIGILEEKIS QRGGKTVGYW
     STDGYDFNDS KALRNGKFVG LALDEDNQSD LTDDRIKSWV AQLKSEFGL
//
ID   FLAV_AQUAE     STANDARD;      PRT;   185 AA.
AC   O67866;
DT   30-MAY-2000 (Rel. 39, Created)
DT   30-MAY-2000 (Rel. 39, Last sequence update)
DT   30-MAY-2000 (Rel. 39, Last annotation update)
DE   FLAVODOXIN.
GN   FLDA OR FLOX OR AQ_2096.
OS   Aquifex aeolicus.
OC   Bacteria; Aquificales; Aquificaceae; Aquifex.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   STRAIN=VF5;
RX   MEDLINE; 98196666.
RA   Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA   Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA   Feldman R.A., Short J.M., Olson G.J., Swanson R.V.;
RT   "The complete genome of the hyperthermophilic bacterium Aquifex
RT   aeolicus.";
RL   Nature 392:353-358(1998).
CC   -!- FUNCTION: LOW-POTENTIAL ELECTRON DONOR TO A NUMBER OF REDOX
CC       ENZYMES (BY SIMILARITY).
CC   -!- COFACTOR: FMN (BY SIMILARITY).
CC   -!- SIMILARITY: BELONGS TO THE FLAVODOXIN FAMILY.
CC   --------------------------------------------------------------------------
CC   This SWISS-PROT entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use  by  non-profit  institutions as long  as its content  is  in  no  way
CC   modified and this statement is not removed.  Usage  by  and for commercial
CC   entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC   or send an email to license@isb-sib.ch).
CC   --------------------------------------------------------------------------
DR   EMBL; AE000772; AAC07825.1; -.
DR   INTERPRO; IPR001226; -.
DR   PFAM; PF00258; flavodoxin; 1.
DR   PROSITE; PS00201; FLAVODOXIN; 1.
KW   Electron transport; Flavoprotein; FMN.
SQ   SEQUENCE   185 AA;  20443 MW;  7C138666D5B89281 CRC64;
     MGKVLVIYDT RTGNTKKMAE LVAEGARSLE GTEVRLKHVD EATKEDVLWA DGLAVGSPTN
     MGLVSWKMKR FFDDVLGDLW GEIDGKIACA FSSSGGWGGG NEVACMSILT MLMNFGFLVF
     GVTDYVGKKF TLHYGAVVAG EPRSEEEKEA CRRLGRRLAE WVAIFVDGRK ELLEKIRKDP
     ARFVD
//
ID   FLAV_ARATH     STANDARD;      PRT;   336 AA.
AC   Q96330; O04830; O04730; O04831; O04731; O04832; O04732;
DT   15-JUL-1999 (Rel. 38, Created)
DT   15-JUL-1999 (Rel. 38, Last sequence update)
DT   15-JUL-1999 (Rel. 38, Last annotation update)
DE   FLAVONOL SYNTHASE (EC 1.3.-.-) (FLS).
GN   FLS1.
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Embryophyta; Tracheophyta; Spermatophyta;
OC   Magnoliophyta; eudicotyledons; Rosidae; eurosids II; Brassicales;
OC   Brassicaceae; Arabidopsis.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   STRAIN=CV. LANDSBERG ERECTA;
RX   MEDLINE; 97267154.
RA   Pelletier M.K., Murrell J.R., Shirley B.W.;
RT   "Characterization of flavonol synthase and leucoanthocyanidin
RT   dioxygenase genes in Arabidopsis. Further evidence for differential
RT   regulation of 'early' and 'late' genes.";
RL   Plant Physiol. 113:1437-1445(1997).
RN   [2]
RP   SEQUENCE FROM N.A.
RC   STRAIN=CV. COLUMBIA, AND CV. LANDSBERG ERECTA;
RA   Hartmann U., Weisshaar B.;
RT   "Isolation of an Arabidopsis clone encoding flavonol synthase.";
RL   Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: CATALYZES THE FORMATION OF FLAVONOLS FROM
CC       DIHYDROFLAVONOLS. IT CAN ACT ON DIHYDROKAEMPFEROL TO PRODUCE
CC       KAEMPFEROL, ON DIHYDROQUERCETIN TO PRODUCE QUERCITIN AND ON
CC       DIHYDROMYRICETIN TO PRODUCE MYRICETIN.
CC   -!- COFACTOR: IRON AND ASCORBATE.
CC   -!- PATHWAY: PART OF THE BIOSYNTHETIC PATHWAY FOR FLAVONOLS WHICH ARE
CC       FLAVONOIDS. FLAVONOLS ARE IMPORTANT CO-PIGMENTS IN FLOWER OR FRUIT
CC       COLOR AND ARE ALSO ESSENTIAL FOR POLLEN TUBE GROWTH.
CC   -!- SUBCELLULAR LOCATION: CYTOPLASMIC.
CC   -!- SIMILARITY: BELONGS TO THE IRON/ASCORBATE-DEPENDENT FAMILY OF
CC       OXIDOREDUCTASES.
CC   --------------------------------------------------------------------------
CC   This SWISS-PROT entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use  by  non-profit  institutions as long  as its content  is  in  no  way
CC   modified and this statement is not removed.  Usage  by  and for commercial
CC   entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC   or send an email to license@isb-sib.ch).
CC   --------------------------------------------------------------------------
DR   EMBL; U72631; AAB17393.1; -.
DR   EMBL; U84258; AAC69362.1; -.
DR   EMBL; U84259; AAC69363.1; -.
DR   EMBL; U84260; AAB41504.1; -.
DR   MENDEL; 6623; ARAth;1185;2.
DR   INTERPRO; IPR002419; -.
DR   PFAM; PF00671; Fe_Asc_oxidored; 1.
KW   Flavonoid biosynthesis; Oxidoreductase; Dioxygenase; Iron; Vitamin C.
SQ   SEQUENCE   336 AA;  38281 MW;  3283E3AFE603D2A9 CRC64;
     MEVERVQDIS SSSLLTEAIP LEFIRSEKEQ PAITTFRGPT PAIPVVDLSD PDEESVRRAV
     VKASEEWGLF QVVNHGIPTE LIRRLQDVGR KFFELPSSEK ESVAKPEDSK DIEGYGTKLQ
     KDPEGKKAWV DHLFHRIWPP SCVNYRFWPK NPPEYREVNE EYAVHVKKLS ETLLGILSDG
     LGLKRDALKE GLGGEMAEYM MKINYYPPCP RPDLALGVPA HTDLSGITLL VPNEVPGLQV
     FKDDHWFDAE YIPSAVIVHI GDQILRLSNG RYKNVLHRTT VDKEKTRMSW PVFLEPPREK
     IVGPLPELTG DDNPPKFKPF AFKDYSYRKL NKLPLD
//
ID   FLAV_AZOCH     STANDARD;      PRT;   179 AA.
AC   P23001; P35708;
DT   01-AUG-1991 (Rel. 19, Created)
DT   01-JUN-1994 (Rel. 29, Last sequence update)
DT   15-DEC-1998 (Rel. 37, Last annotation update)
DE   FLAVODOXIN B (FLDB).
GN   NIFF.
OS   Azotobacter chroococcum mcd 1.
OC   Bacteria; Proteobacteria; gamma subdivision; Azotobacteraceae;
OC   Azotobacter.
RN   [1]
RP   SEQUENCE FROM N.A.
RA   Robson R.L.;
RL   Submitted (XXX-1993) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   SEQUENCE OF 1-20.
RC   STRAIN=MCD 1155;
RX   MEDLINE; 91315397.
RA   Bagby S., Barker P.D., Hill H.A.O., Sanghera G.S., Dunbar B.,
RA   Ashby G.A., Eady R.R., Thorneley R.N.F.;
RT   "Direct electrochemistry of two genetically distinct flavodoxins
RT   isolated from Azotobacter chroococcum grown under nitrogen-fixing
RT   conditions.";
RL   Biochem. J. 277:313-319(1991).
CC   -!- FUNCTION: LOW-POTENTIAL ELECTRON DONOR TO A NUMBER OF REDOX
CC       ENZYMES. NIFF IS THE ELECTRON DONOR TO NITROGENASE.
CC   -!- COFACTOR: FMN.
CC   -!- SIMILARITY: BELONGS TO THE FLAVODOXIN FAMILY.
CC   --------------------------------------------------------------------------
CC   This SWISS-PROT entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use  by  non-profit  institutions as long  as its content  is  in  no  way
CC   modified and this statement is not removed.  Usage  by  and for commercial
CC   entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC   or send an email to license@isb-sib.ch).
CC   --------------------------------------------------------------------------
DR   EMBL; M73019; AAB36613.1; -.
DR   PIR; S17461; S17461.
DR   HSSP; P11241; 1FTG.
DR   INTERPRO; IPR001226; -.
DR   PFAM; PF00258; flavodoxin; 1.
DR   PROSITE; PS00201; FLAVODOXIN; 1.
KW   Nitrogen fixation; Electron transport; Flavoprotein; FMN.
FT   INIT_MET      0      0
SQ   SEQUENCE   179 AA;  19392 MW;  4C9BAA14E4BDE7D6 CRC64;
     AKIGLFFGSN TGKTRKVAKS IKKRFDDETM SDAVNVNRVS AEDFAQYQFL ILGTPTLGEG
     ELPGLSSDCE NESWEEFLPK IEGLDFSGKT VALFGLGDQV GYPENFLDAM GELHSFFTER
     GAKVVGAWST DGYEFEGSTA VVDGKFVGLA LDLDNQSGKT DERVAAWLAQ IAPEFGLSL
//
ID   FLAV_AZOVI     STANDARD;      PRT;   179 AA.
AC   P00324;
DT   21-JUL-1986 (Rel. 01, Created)
DT   21-JUL-1986 (Rel. 01, Last sequence update)
DT   15-DEC-1998 (Rel. 37, Last annotation update)
DE   FLAVODOXIN 2.
GN   NIFF.
OS   Azotobacter vinelandii.
OC   Bacteria; Proteobacteria; gamma subdivision; Azotobacteraceae;
OC   Azotobacter.
RN   [1]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 89123097.
RA   Jacobson M.R., Brigle K.E., Bennett L.T., Setterquist R.A.,
RA   Wilson M.S., Cash V.L., Beynon J., Newton W.E., Dean D.R.;
RT   "Physical and genetic map of the major nif gene cluster from
RT   Azotobacter vinelandii.";
RL   J. Bacteriol. 171:1017-1027(1989).
RN   [2]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 88087273.
RA   Bennett L., Jacobson M., Dean D.R.;
RT   "Isolation, sequencing, and mutagenesis of the nifF gene encoding
RT   flavodoxin from Azotobacter vinelandii.";
RL   J. Biol. Chem. 263:1364-1369(1988).
RN   [3]
RP   SEQUENCE.
RC   STRAIN=OP;
RX   MEDLINE; 77242321.
RA   Tanaka M., Haniu M., Yasunobu K.T., Yoch D.C.;
RT   "Complete amino acid sequence of azotoflavin, a flavodoxin from
RT   Azotobacter vinelandii.";
RL   Biochemistry 16:3525-3537(1977).
RN   [4]
RP   SEQUENCE OF 1-20.
RC   STRAIN=UW 136;
RX   MEDLINE; 96276406.
RA   Gangeswaran R., Eady R.R.;
RT   "Flavodoxin 1 of Azotobacter vinelandii: characterization and role in
RT   electron donation to purified assimilatory nitrate reductase.";
RL   Biochem. J. 317:103-108(1996).
RN   [5]
RP   STRUCTURE BY NMR.
RC   STRAIN=ATCC 478;
RX   MEDLINE; 98180401.
RA   Steensma E., Nijman M.J.M., Bollen Y.J.M., de Jager P.A.,
RA   van den Berg W.A.M., van Dongen W.M.A.M., van Mierlo C.P.M.;
RT   "Apparent local stability of the secondary structure of Azotobacter
RT   vinelandii holoflavodoxin II as probed by hydrogen exchange:
RT   implications for redox potential regulation and flavodoxin folding.";
RL   Protein Sci. 7:306-317(1998).
CC   -!- FUNCTION: LOW-POTENTIAL ELECTRON DONOR TO A NUMBER OF REDOX
CC       ENZYMES. NIFF IS THE ELECTRON DONOR TO NITROGENASE.
CC   -!- COFACTOR: FMN.
CC   -!- SUBUNIT: MONOMER.
CC   -!- MASS SPECTROMETRY: MW=19533; MW_ERR=5; METHOD=ELECTROSPRAY.
CC   -!- SIMILARITY: BELONGS TO THE FLAVODOXIN FAMILY.
CC   --------------------------------------------------------------------------
CC   This SWISS-PROT entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use  by  non-profit  institutions as long  as its content  is  in  no  way
CC   modified and this statement is not removed.  Usage  by  and for commercial
CC   entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC   or send an email to license@isb-sib.ch).
CC   --------------------------------------------------------------------------
DR   EMBL; M20568; AAA64735.1; -.
DR   EMBL; J03519; AAA22154.1; -.
DR   PIR; A00334; FXAVEP.
DR   PIR; A29935; A29935.
DR   HSSP; P11241; 1FTG.
DR   INTERPRO; IPR001094; -.
DR   INTERPRO; IPR001226; -.
DR   PFAM; PF00258; flavodoxin; 1.
DR   PRINTS; PR00369; FLAVODOXIN.
DR   PROSITE; PS00201; FLAVODOXIN; 1.
KW   Nitrogen fixation; Electron transport; Flavoprotein; FMN.
FT   INIT_MET      0      0
SQ   SEQUENCE   179 AA;  19532 MW;  661B0EC667375A7F CRC64;
     AKIGLFFGSN TGKTRKVAKS IKKRFDDETM SDALNVNRVS AEDFAQYQFL ILGTPTLGEG
     ELPGLSSDCE NESWEEFLPK IEGLDFSGKT VALFGLGDQV GYPENYLDAL GELYSFFKDR
     GAKIVGSWST DGYEFESSEA VVDGKFVGLA LDLDNQSGKT DERVAAWLAQ IAPEFGLSL
//
ID   FLAV_BACSU     STANDARD;      PRT;   158 AA.
AC   O34737;
DT   15-DEC-1998 (Rel. 37, Created)
DT   15-DEC-1998 (Rel. 37, Last sequence update)
DT   15-DEC-1998 (Rel. 37, Last annotation update)
DE   PROBABLE FLAVODOXIN 1.
GN   YKUN.
OS   Bacillus subtilis.
OC   Bacteria; Firmicutes; Bacillus/Clostridium group;
OC   Bacillus/Staphylococcus group; Bacillus.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   STRAIN=168;
RA   Scanlan E., Devine K.M.;
RL   Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: LOW-POTENTIAL ELECTRON DONOR TO A NUMBER OF REDOX
CC       ENZYMES (POTENTIAL).
CC   -!- COFACTOR: FMN (BY SIMILARITY).
CC   -!- SIMILARITY: BELONGS TO THE FLAVODOXIN FAMILY.
CC   --------------------------------------------------------------------------
CC   This SWISS-PROT entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use  by  non-profit  institutions as long  as its content  is  in  no  way
CC   modified and this statement is not removed.  Usage  by  and for commercial
CC   entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC   or send an email to license@isb-sib.ch).
CC   --------------------------------------------------------------------------
DR   EMBL; AJ222587; CAA10877.1; -.
DR   EMBL; Z99111; CAB13288.1; -.
DR   SUBTILIST; BG13298; YKUN.
DR   INTERPRO; IPR001226; -.
DR   PFAM; PF00258; flavodoxin; 1.
DR   PROSITE; PS00201; FLAVODOXIN; FALSE_NEG.
KW   Electron transport; Flavoprotein; FMN.
SQ   SEQUENCE   158 AA;  17793 MW;  FECE71BF6E552D3F CRC64;
     MAKALITYAS MSGNTEDIAF IIKDTLQEYE LDIDCVEIND MDASCLTSYD YVLIGTYTWG
     DGDLPYEAED FFEEVKQIQL NGLKTACFGS GDYSYPKFCE AVNLFNVMLQ EAGAAVYQET
     LKIELAPETD EDVESCRAFA RGFLAWADYM NKEKIHVS
//
ID   FLAV_CHOCR     STANDARD;      PRT;   173 AA.
AC   P14070;
DT   01-JAN-1990 (Rel. 13, Created)
DT   01-JAN-1990 (Rel. 13, Last sequence update)
DT   15-DEC-1998 (Rel. 37, Last annotation update)
DE   FLAVODOXIN.
OS   Chondrus crispus (Carragheen).
OC   Eukaryota; Rhodophyta; Florideophyceae; Gigartinales; Gigartinaceae;
OC   Chondrus.
RN   [1]
RP   SEQUENCE.
RX   MEDLINE; 90088453.
RA   Wakabayashi S., Kimura K., Matsubara H., Rogers L.J.;
RT   "The amino acid sequence of a flavodoxin from the eukaryotic red alga
RT   Chondrus crispus.";
RL   Biochem. J. 263:981-984(1989).
RN   [2]
RP   SEQUENCE OF 1-34.
RA   Takruri I.A.H., Boulter D., Fitzgerald M.P., Hutber G.N., Rogers L.J.;
RT   "N-terminal amino acid sequences of flavodoxins from Chondrus crispus
RT   and Nostoc strain MAC.";
RL   Phytochemistry 25:2113-2115(1986).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS).
RX   MEDLINE; 90368796.
RA   Fukuyama K., Wakabayashi S., Matsubara H., Rogers L.J.;
RT   "Tertiary structure of oxidized flavodoxin from an eukaryotic red
RT   alga Chondrus crispus at 2.35-A resolution. Localization of charged
RT   residues and implication for interaction with electron transfer
RT   partners.";
RL   J. Biol. Chem. 265:15804-15812(1990).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX   MEDLINE; 92292160.
RA   Fukuyama K., Matsubara H., Rogers L.J.;
RT   "Crystal structure of oxidized flavodoxin from a red alga Chondrus
RT   crispus refined at 1.8-A resolution. Description of the flavin
RT   mononucleotide binding site.";
RL   J. Mol. Biol. 225:775-789(1992).
CC   -!- FUNCTION: LOW-POTENTIAL ELECTRON DONOR TO A NUMBER OF REDOX
CC       ENZYMES.
CC   -!- COFACTOR: FMN.
CC   -!- SIMILARITY: BELONGS TO THE FLAVODOXIN FAMILY.
DR   PIR; S06648; S06648.
DR   PIR; PA0003; PA0003.
DR   PDB; 2FCR; 15-JAN-92.
DR   INTERPRO; IPR001226; -.
DR   PFAM; PF00258; flavodoxin; 1.
DR   PROSITE; PS00201; FLAVODOXIN; 1.
KW   Electron transport; Flavoprotein; FMN; 3D-structure.
FT   CONFLICT     29     29       D -> S (IN REF. 2).
FT   CONFLICT     33     33       D -> S (IN REF. 2).
FT   STRAND        2      6
FT   HELIX        12     27
FT   STRAND       28     28
FT   STRAND       32     33
FT   HELIX        34     36
FT   HELIX        40     45
FT   STRAND       48     54
FT   TURN         58     59
FT   TURN         68     68
FT   HELIX        69     75
FT   TURN         76     76
FT   HELIX        77     79
FT   TURN         83     84
FT   STRAND       86     93
FT   TURN         95     97
FT   TURN         99    100
FT   TURN        102    104
FT   HELIX       105    115
FT   TURN        116    117
FT   STRAND      119    121
FT   STRAND      124    124
FT   HELIX       126    128
FT   TURN        135    136
FT   STRAND      137    138
FT   TURN        139    140
FT   STRAND      141    142
FT   STRAND      145    148
FT   TURN        149    151
FT   HELIX       156    171
FT   TURN        172    172
SQ   SEQUENCE   173 AA;  18871 MW;  EF1F3A3554CA4166 CRC64;
     KIGIFFSTST GNTTEVADFI GKTLGAKADA PIDVDDVTDP QALKDYDLLF LGAPTWNTGA
     DTERSGTSWD EFLYDKLPEV DMKDLPVAIF GLGDAEGYPD NFCDAIEEIH DCFAKQGAKP
     VGFSNPDDYD YEESKSVRDG KFLGLPLDMV NDQIPMEKRV AGWVEAVVSE TGV
//
ID   FLAV_CLOAB     STANDARD;      PRT;   160 AA.
AC   P18855;
DT   01-NOV-1990 (Rel. 16, Created)
DT   01-NOV-1990 (Rel. 16, Last sequence update)
DT   15-DEC-1998 (Rel. 37, Last annotation update)
DE   FLAVODOXIN.
GN   FLOX.
OS   Clostridium acetobutylicum.
OC   Bacteria; Firmicutes; Bacillus/Clostridium group; Clostridiaceae;
OC   Clostridium.
RN   [1]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 91123180.
RA   Santangelo J.D., Jones D.T., Woods D.R.;
RT   "Metronidazole activation and isolation of Clostridium acetobutylicum
RT   electron transport genes.";
RL   J. Bacteriol. 173:1088-1095(1991).
CC   -!- FUNCTION: LOW-POTENTIAL ELECTRON DONOR TO A NUMBER OF REDOX
CC       ENZYMES.
CC   -!- COFACTOR: FMN.
CC   -!- SIMILARITY: BELONGS TO THE FLAVODOXIN FAMILY.
CC   --------------------------------------------------------------------------
CC   This SWISS-PROT entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use  by  non-profit  institutions as long  as its content  is  in  no  way
CC   modified and this statement is not removed.  Usage  by  and for commercial
CC   entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC   or send an email to license@isb-sib.ch).
CC   --------------------------------------------------------------------------
DR   EMBL; M36770; AAA23238.1; -.
DR   PIR; A38177; A38177.
DR   HSSP; P00322; 2FVX.
DR   INTERPRO; IPR001226; -.
DR   PFAM; PF00258; flavodoxin; 1.
DR   PROSITE; PS00201; FLAVODOXIN; 1.
KW   Electron transport; Flavoprotein; FMN.
SQ   SEQUENCE   160 AA;  17763 MW;  6153F8A1F0BCDC8D CRC64;
     MKISILYSSK TGKTERVAKL IEEGVKRSGN IEVKTMNLDA VDKKFLQESE GIIFGTPTYY
     ANISWEMKKW IDESSEFNLE GKLGAAFSTA NSIAGGSDIA LLTILNHLMV KGMLVYSGGV
     AFGKPKTHLG YVHINEIQEN EDENARIFGE RIANKVKQIF
//
ID   FLAV_CLOBE     STANDARD;      PRT;   138 AA.
AC   P00322;
DT   21-JUL-1986 (Rel. 01, Created)
DT   21-JUL-1986 (Rel. 01, Last sequence update)
DT   15-DEC-1998 (Rel. 37, Last annotation update)
DE   FLAVODOXIN.
OS   Clostridium beijerinckii (Clostridium MP).
OC   Bacteria; Firmicutes; Bacillus/Clostridium group; Clostridiaceae;
OC   Clostridium.
RN   [1]
RP   SEQUENCE.
RX   MEDLINE; 74277392.
RA   Tanaka M., Haniu M., Yasunobu K.T., Mayhew S.G.;
RT   "The amino acid sequence of the Clostridium MP flavodoxin.";
RL   J. Biol. Chem. 249:4393-4396(1974).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF OXIDIZED FORM.
RX   MEDLINE; 74277391.
RA   Burnett R.M., Darling G.D., Kendall D.S., Lequesne M.E., Mayhew S.G.,
RA   Smith W.W., Ludwig M.L.;
RT   "The structure of the oxidized form of clostridial flavodoxin at
RT   1.9-A resolution.";
RL   J. Biol. Chem. 249:4383-4392(1974).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX   MEDLINE; 97178811.
RA   Ludwig M.L., Pattridge K.A., Metzger A.L., Dixon M.M., Eren M.,
RA   Feng Y., Swenson R.P.;
RT   "Control of oxidation-reduction potentials in flavodoxin from
RT   Clostridium beijerinckii: the role of conformation changes.";
RL   Biochemistry 36:1259-1280(1997).
CC   -!- FUNCTION: LOW-POTENTIAL ELECTRON DONOR TO A NUMBER OF REDOX
CC       ENZYMES.
CC   -!- COFACTOR: FMN.
CC   -!- SIMILARITY: BELONGS TO THE FLAVODOXIN FAMILY.
DR   PIR; A00332; FXCLEX.
DR   PDB; 3NLL; 12-MAR-97.
DR   PDB; 4NLL; 12-MAR-97.
DR   PDB; 5NLL; 12-MAR-97.
DR   PDB; 4NUL; 12-MAR-97.
DR   PDB; 5NUL; 12-MAR-97.
DR   PDB; 6NUL; 12-MAR-97.
DR   PDB; 5ULL; 12-MAR-97.
DR   PDB; 2FAX; 12-MAR-97.
DR   PDB; 2FDX; 01-APR-97.
DR   PDB; 1FLA; 12-MAR-97.
DR   PDB; 1FLD; 12-MAR-97.
DR   PDB; 1FLN; 12-MAR-97.
DR   PDB; 2FLV; 12-MAR-97.
DR   PDB; 2FOX; 12-MAR-97.
DR   PDB; 1FVX; 12-MAR-97.
DR   PDB; 2FVX; 12-MAR-97.
DR   INTERPRO; IPR001226; -.
DR   PFAM; PF00258; flavodoxin; 1.
DR   PROSITE; PS00201; FLAVODOXIN; 1.
KW   Electron transport; Flavoprotein; FMN; 3D-structure.
FT   STRAND        2      6
FT   HELIX        11     25
FT   TURN         26     27
FT   STRAND       31     34
FT   TURN         35     37
FT   TURN         41     45
FT   STRAND       48     53
FT   STRAND       56     56
FT   TURN         57     59
FT   STRAND       60     60
FT   TURN         63     65
FT   HELIX        66     73
FT   TURN         75     76
FT   TURN         78     79
FT   STRAND       81     88
FT   HELIX        94    105
FT   TURN        106    107
FT   STRAND      109    110
FT   STRAND      115    118
FT   HELIX       122    136
FT   TURN        137    137
SQ   SEQUENCE   138 AA;  15332 MW;  98BE3746EC000FF1 CRC64;
     MKIVYWSGTG NTEKMAELIA KGIIESGKDV NTINVSDVNI DELLNEDILI LGCSAMGDEV
     LEESEFEPFI EEISTKISGK KVALFGSYGW GDGKWMRDFE ERMNGYGCVV VETPLIVQNE
     PDEAEQDCIE FGKKIANI
//
ID   FLAV_DESDE     STANDARD;      PRT;   148 AA.
AC   P26492;
DT   01-AUG-1992 (Rel. 23, Created)
DT   01-AUG-1992 (Rel. 23, Last sequence update)
DT   15-DEC-1998 (Rel. 37, Last annotation update)
DE   FLAVODOXIN.
OS   Desulfovibrio desulfuricans.
OC   Bacteria; Proteobacteria; delta subdivision; Desulfovibrio.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   STRAIN=ATCC 29577 / NCIB 8307;
RX   MEDLINE; 91316149.
RA   Helms L.R., Swenson R.P.;
RT   "Cloning and characterization of the flavodoxin gene from
RT   Desulfovibrio desulfuricans.";
RL   Biochim. Biophys. Acta 1089:417-419(1991).
CC   -!- FUNCTION: LOW-POTENTIAL ELECTRON DONOR TO A NUMBER OF REDOX
CC       ENZYMES.
CC   -!- COFACTOR: FMN.
CC   -!- SIMILARITY: BELONGS TO THE FLAVODOXIN FAMILY.
CC   --------------------------------------------------------------------------
CC   This SWISS-PROT entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use  by  non-profit  institutions as long  as its content  is  in  no  way
CC   modified and this statement is not removed.  Usage  by  and for commercial
CC   entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC   or send an email to license@isb-sib.ch).
CC   --------------------------------------------------------------------------
DR   EMBL; X59438; CAA42064.1; -.
DR   PIR; S17000; FXDVD.
DR   HSSP; P00323; 1FX1.
DR   INTERPRO; IPR001226; -.
DR   PFAM; PF00258; flavodoxin; 1.
DR   PROSITE; PS00201; FLAVODOXIN; 1.
KW   Electron transport; Flavoprotein; FMN.
SQ   SEQUENCE   148 AA;  15694 MW;  1CE35B4B79817459 CRC64;
     MSKVLIVFGS STGNTESIAQ KLEELIAAGG HEVTLLNAAD ASAENLADGY DAVLFGCSAW
     GMEDLEMQDD FLSLFEEFNR IGLAGRKVAA FASGDQEYEH FCGAVPAIEE RAKELGATII
     AEGLKMEGDA SNDPEAVASF AEDVLKQL
//
ID   FLAV_DESGI     STANDARD;      PRT;   146 AA.
AC   Q01095;
DT   01-APR-1993 (Rel. 25, Created)
DT   01-APR-1993 (Rel. 25, Last sequence update)
DT   15-DEC-1998 (Rel. 37, Last annotation update)
DE   FLAVODOXIN.
OS   Desulfovibrio gigas.
OC   Bacteria; Proteobacteria; delta subdivision; Desulfovibrio.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   STRAIN=ATCC 19364 / NCIB 9332;
RX   MEDLINE; 92329549.
RA   Helms L.R., Swenson R.P.;
RT   "The primary structures of the flavodoxins from two strains of
RT   Desulfovibrio gigas. Cloning and nucleotide sequence of the
RT   structural genes.";
RL   Biochim. Biophys. Acta 1131:325-328(1992).
CC   -!- FUNCTION: ELECTRON-TRANSFER PROTEINS THAT FUNCTION IN VARIOUS
CC       ELECTRON TRANSPORT SYSTEMS IN MICRO-ORGANISMS. FUNCTIONALLY
CC       INTERCHANGEABLE WITH FERREDOXIN.
CC   -!- COFACTOR: FMN.
CC   -!- SIMILARITY: BELONGS TO THE FLAVODOXIN FAMILY.
CC   --------------------------------------------------------------------------
CC   This SWISS-PROT entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use  by  non-profit  institutions as long  as its content  is  in  no  way
CC   modified and this statement is not removed.  Usage  by  and for commercial
CC   entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC   or send an email to license@isb-sib.ch).
CC   --------------------------------------------------------------------------
DR   EMBL; X64766; CAA46013.1; -.
DR   PIR; S24311; S24311.
DR   HSSP; P00323; 1FX1.
DR   INTERPRO; IPR001094; -.
DR   INTERPRO; IPR001226; -.
DR   PFAM; PF00258; flavodoxin; 1.
DR   PRINTS; PR00369; FLAVODOXIN.
DR   PROSITE; PS00201; FLAVODOXIN; 1.
KW   Electron transport; Flavoprotein; FMN.
SQ   SEQUENCE   146 AA;  15470 MW;  95D9E73B1FCF1403 CRC64;
     MPKALIVYGS TTGNTEGVAE AIAKTLNSEG METTVVNVAD VTAPGLAEGY DVVLLGCSTW
     GDDEIELQED FVPLYEDLDR AGLKDKKVGV FGCGDSSYTY FCGAVDVIEK KAEELGATLV
     ASSLKIDGEP DSAEVLDWAR EVLARV
//
ID   FLAV_DESSA     STANDARD;      PRT;   146 AA.
AC   P18086;
DT   01-NOV-1990 (Rel. 16, Created)
DT   01-NOV-1990 (Rel. 16, Last sequence update)
DT   15-DEC-1998 (Rel. 37, Last annotation update)
DE   FLAVODOXIN.
OS   Desulfovibrio salexigens.
OC   Bacteria; Proteobacteria; delta subdivision; Desulfovibrio.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   STRAIN=ATCC 14822;
RX   MEDLINE; 90241257.
RA   Helms L.R., Krey G.D., Swenson R.P.;
RT   "Identification, sequence determination, and expression of the
RT   flavodoxin gene from Desulfovibrio salexigens.";
RL   Biochem. Biophys. Res. Commun. 168:809-817(1990).
CC   -!- FUNCTION: LOW-POTENTIAL ELECTRON DONOR TO A NUMBER OF REDOX
CC       ENZYMES.
CC   -!- COFACTOR: FMN.
CC   -!- SIMILARITY: BELONGS TO THE FLAVODOXIN FAMILY.
CC   --------------------------------------------------------------------------
CC   This SWISS-PROT entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use  by  non-profit  institutions as long  as its content  is  in  no  way
CC   modified and this statement is not removed.  Usage  by  and for commercial
CC   entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC   or send an email to license@isb-sib.ch).
CC   --------------------------------------------------------------------------
DR   EMBL; M35475; AAA23368.1; -.
DR   PIR; A34640; A34640.
DR   HSSP; P00323; 1FX1.
DR   INTERPRO; IPR001094; -.
DR   INTERPRO; IPR001226; -.
DR   PFAM; PF00258; flavodoxin; 1.
DR   PRINTS; PR00369; FLAVODOXIN.
DR   PROSITE; PS00201; FLAVODOXIN; 1.
KW   Electron transport; Flavoprotein; FMN.
SQ   SEQUENCE   146 AA;  15812 MW;  BDE3651310E1F780 CRC64;
     MSKSLIVYGS TTGNTETAAE YVAEAFENKE IDVELKNVTD VSVADLGNGY DIVLFGCSTW
     GEEEIELQDD FIPLYDSLEN ADLKGKKVSV FGCGDSDYTY FCGAVDAIEE KLEKMGAVVI
     GDSLKIDGDP ERDEIVSWGS GIADKI
//
ID   FLAV_DESVH     STANDARD;      PRT;   148 AA.
AC   P00323;
DT   21-JUL-1986 (Rel. 01, Created)
DT   01-NOV-1990 (Rel. 16, Last sequence update)
DT   15-JUL-1999 (Rel. 38, Last annotation update)
DE   FLAVODOXIN.
OS   Desulfovibrio vulgaris (strain Hildenborough).
OC   Bacteria; Proteobacteria; delta subdivision; Desulfovibrio.
RN   [1]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 89008444.
RA   Krey G.D., Vanin E.F., Swenson R.P.;
RT   "Cloning, nucleotide sequence, and expression of the flavodoxin gene
RT   from Desulfovibrio vulgaris (Hildenborough).";
RL   J. Biol. Chem. 263:15436-15443(1988).
RN   [2]
RP   SEQUENCE FROM N.A.
RA   Curley G.P., Voordouw G.;
RT   "Cloning and sequencing of the gene encoding flavodoxin from
RT   Desulfovibrio vulgaris Hildenborough.";
RL   FEMS Microbiol. Lett. 49:295-299(1988).
RN   [3]
RP   SEQUENCE.
RX   MEDLINE; 77118626.
RA   Dubourdieu M., Fox J.L.;
RT   "Amino acid sequence of Desulfovibrio vulgaris flavodoxin.";
RL   J. Biol. Chem. 252:1453-1463(1977).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX   MEDLINE; 91162643.
RA   Warr W., Tulinsky A., Swenson R.P., Watenpaugh K.D.;
RT   "Comparison of the crystal structures of a flavodoxin in its three
RT   oxidation states at cryogenic temperatures.";
RL   J. Mol. Biol. 218:195-208(1991).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX   MEDLINE; 74087652.
RA   Watenpaugh K.D., Sieker L.C., Jensen L.H.;
RT   "The binding of riboflavin-5'-phosphate in a flavoprotein: flavodoxin
RT   at 2.0-A resolution.";
RL   Proc. Natl. Acad. Sci. U.S.A. 70:3857-3860(1973).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX   MEDLINE; 73044810.
RA   Watenpaugh K.D., Sieker L.C., Jensen L.H., Legall J., Dubourdieu M.;
RT   "Structure of the oxidized form of a flavodoxin at 2.5-A resolution:
RT   resolution of the phase ambiguity by anomalous scattering.";
RL   Proc. Natl. Acad. Sci. U.S.A. 69:3185-3188(1972).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX   MEDLINE; 99089597.
RA   Walsh M.A., McCarthy A., O'Farrell P.A., McArdle P., Cunningham P.D.,
RA   Mayhew S.G., Higgins T.M.;
RT   "X-ray crystal structure of the Desulfovibrio vulgaris (Hildenborough)
RT   apoflavodoxin-riboflavin complex.";
RL   Eur. J. Biochem. 258:362-371(1998).
RN   [8]
RP   STRUCTURE BY NMR.
RX   MEDLINE; 93238683.
RA   Knauf M.A., Loehr F., Curley G.P., O'Farrell P., Mayhew S.G.,
RA   Mueller F., Rueterjans H.;
RT   "Homonuclear and heteronuclear NMR studies of oxidized Desulfovibrio
RT   vulgaris flavodoxin. Sequential assignments and identification of
RT   secondary structure elements.";
RL   Eur. J. Biochem. 213:167-184(1993).
RN   [9]
RP   STRUCTURE BY NMR.
RX   MEDLINE; 96283837.
RA   Knauf M.A., Loehr F., Bluemel M., Mayhew S.G., Rueterjans H.;
RT   "NMR investigation of the solution conformation of oxidized
RT   flavodoxin from Desulfovibrio vulgaris. Determination of the tertiary
RT   structure and detection of protein-bound water molecules.";
RL   Eur. J. Biochem. 238:423-434(1996).
RN   [10]
RP   STRUCTURE BY NMR.
RX   MEDLINE; 93237739.
RA   Stockman B.J., Euvrard A., Kloosterman D.A., Scahill T.A.,
RA   Swenson R.P.;
RT   "1H and 15N resonance assignments and solution secondary structure of
RT   oxidized Desulfovibrio vulgaris flavodoxin determined by
RT   heteronuclear three-dimensional NMR spectroscopy.";
RL   J. Biomol. NMR 3:133-149(1993).
CC   -!- FUNCTION: LOW-POTENTIAL ELECTRON DONOR TO A NUMBER OF REDOX
CC       ENZYMES.
CC   -!- COFACTOR: FMN.
CC   -!- SIMILARITY: BELONGS TO THE FLAVODOXIN FAMILY.
CC   --------------------------------------------------------------------------
CC   This SWISS-PROT entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use  by  non-profit  institutions as long  as its content  is  in  no  way
CC   modified and this statement is not removed.  Usage  by  and for commercial
CC   entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC   or send an email to license@isb-sib.ch).
CC   --------------------------------------------------------------------------
DR   EMBL; J04033; AAA23367.1; -.
DR   PIR; A31991; FXDV.
DR   PDB; 1FX1; 02-JAN-85.
DR   PDB; 2FX2; 31-OCT-93.
DR   PDB; 3FX2; 31-OCT-93.
DR   PDB; 4FX2; 31-OCT-93.
DR   PDB; 5FX2; 31-OCT-93.
DR   PDB; 1AZL; 20-MAY-98.
DR   PDB; 1AKQ; 02-DEC-98.
DR   PDB; 1AKR; 27-MAY-98.
DR   PDB; 1AKT; 27-MAY-98.
DR   PDB; 1AKU; 02-DEC-98.
DR   PDB; 1AKV; 02-DEC-98.
DR   PDB; 1AKW; 27-MAY-98.
DR   PDB; 1BU5; 09-FEB-99.
DR   INTERPRO; IPR001094; -.
DR   INTERPRO; IPR001226; -.
DR   PFAM; PF00258; flavodoxin; 1.
DR   PRINTS; PR00369; FLAVODOXIN.
DR   PROSITE; PS00201; FLAVODOXIN; 1.
KW   Electron transport; Flavoprotein; FMN; 3D-structure.
FT   CONFLICT     28     28       D -> N (IN REF. 2).
FT   STRAND        3      9
FT   HELIX        14     27
FT   TURN         28     30
FT   STRAND       32     37
FT   TURN         38     40
FT   TURN         44     49
FT   STRAND       52     57
FT   STRAND       59     60
FT   STRAND       66     67
FT   TURN         69     70
FT   HELIX        72     76
FT   TURN         77     79
FT   TURN         84     85
FT   STRAND       87     94
FT   TURN         96     97
FT   TURN        101    102
FT   HELIX       103    113
FT   TURN        114    116
FT   STRAND      118    119
FT   STRAND      124    127
FT   HELIX       130    132
FT   HELIX       134    145
FT   TURN        146    147
SQ   SEQUENCE   148 AA;  15823 MW;  E07630E7047ABD3F CRC64;
     MPKALIVYGS TTGNTEYTAE TIARELADAG YEVDSRDAAS VEAGGLFEGF DLVLLGCSTW
     GDDSIELQDD FIPLFDSLEE TGAQGRKVAC FGCGDSSYEY FCGAVDAIEE KLKNLGAEIV
     QDGLRIDGDP RAARDDIVGW AHDVRGAI
//
ID   FLAV_DESVM     STANDARD;      PRT;   148 AA.
AC   P71165;
DT   15-DEC-1998 (Rel. 37, Created)
DT   15-DEC-1998 (Rel. 37, Last sequence update)
DT   15-DEC-1998 (Rel. 37, Last annotation update)
DE   FLAVODOXIN.
OS   Desulfovibrio vulgaris (strain Miyazaki).
OC   Bacteria; Proteobacteria; delta subdivision; Desulfovibrio.
RN   [1]
RP   SEQUENCE FROM N.A., AND CHARACTERIZATION.
RC   STRAIN=MIYAZAKI F;
RX   MEDLINE; 98230696.
RA   Kitamura M., Sagara T., Taniguchi M., Ashida M., Ezoe K., Kohno K.,
RA   Kojima S., Ozawa K., Akutsu H., Kumagai I., Nakaya T.;
RT   "Cloning and expression of the gene encoding flavodoxin from
RT   Desulfovibrio vulgaris (Miyazaki F).";
RL   J. Biochem. 123:891-898(1998).
CC   -!- FUNCTION: LOW-POTENTIAL ELECTRON DONOR TO A NUMBER OF REDOX
CC       ENZYMES.
CC   -!- COFACTOR: FMN.
CC   -!- SIMILARITY: BELONGS TO THE FLAVODOXIN FAMILY.
CC   --------------------------------------------------------------------------
CC   This SWISS-PROT entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use  by  non-profit  institutions as long  as its content  is  in  no  way
CC   modified and this statement is not removed.  Usage  by  and for commercial
CC   entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC   or send an email to license@isb-sib.ch).
CC   --------------------------------------------------------------------------
DR   EMBL; D88493; BAA13628.1; -.
DR   INTERPRO; IPR001094; -.
DR   INTERPRO; IPR001226; -.
DR   PFAM; PF00258; flavodoxin; 1.
DR   PRINTS; PR00369; FLAVODOXIN.
DR   PROSITE; PS00201; FLAVODOXIN; 1.
KW   Electron transport; Flavoprotein; FMN.
SQ   SEQUENCE   148 AA;  15656 MW;  9D321268D04D89B4 CRC64;
     MANVLIVYGS TTGNTAWVAE TVGRDIAEAG HSVEIRDAGQ VEAEGLCEGR DLVLFGCSTW
     GDDEIELQDD FIHLYESLEA TGAGKGRAAC FGCGDSSYTY FCGPVDAIEE RLSGLGADIV
     ADSLKIDGDP RTMRDDVSAW AGRVVTAL
//
ID   FLAV_ECOLI     STANDARD;      PRT;   175 AA.
AC   P23243;
DT   01-NOV-1991 (Rel. 20, Created)
DT   01-NOV-1991 (Rel. 20, Last sequence update)
DT   15-DEC-1998 (Rel. 37, Last annotation update)
DE   FLAVODOXIN 1.
GN   FLDA.
OS   Escherichia coli.
OC   Bacteria; Proteobacteria; gamma subdivision; Enterobacteriaceae;
OC   Escherichia.
RN   [1]
RP   SEQUENCE FROM N.A., AND SEQUENCE OF 1-14.
RX   MEDLINE; 91154129.
RA   Osborne C., Chen L.-M., Matthews R.G.;
RT   "Isolation, cloning, mapping, and nucleotide sequencing of the gene
RT   encoding flavodoxin in Escherichia coli.";
RL   J. Bacteriol. 173:1729-1737(1991).
RN   [2]
RP   SEQUENCE FROM N.A.
RC   STRAIN=K12 / MG1655;
RX   MEDLINE; 97426617.
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
RA   Mau B., Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1474(1997).
RN   [3]
RP   SEQUENCE FROM N.A.
RC   STRAIN=K12;
RX   MEDLINE; 97061202.
RA   Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A.,
RA   Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K.,
RA   Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K.,
RA   Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N.,
RA   Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y.,
RA   Yano M., Horiuchi T.;
RT   "A 718-kb DNA sequence of the Escherichia coli K-12 genome
RT   corresponding to the 12.7-28.0 min region on the linkage map.";
RL   DNA Res. 3:137-155(1996).
RN   [4]
RP   SEQUENCE OF 1-10.
RX   MEDLINE; 95050480.
RA   Jenkins C.M., Waterman M.R.;
RT   "Flavodoxin and NADPH-flavodoxin reductase from Escherichia coli
RT   support bovine cytochrome P450c17 hydroxylase activities.";
RL   J. Biol. Chem. 269:27401-27408(1994).
RN   [5]
RP   STRUCTURE BY NMR.
RX   MEDLINE; 97234567.
RA   Ponstingl H., Otting G.;
RT   "NMR assignments, secondary structure and hydration of oxidized
RT   Escherichia coli flavodoxin.";
RL   Eur. J. Biochem. 244:384-399(1997).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX   MEDLINE; 98078562.
RA   Hoover D.M., Ludwig M.L.;
RT   "A flavodoxin that is required for enzyme activation: the structure
RT   of oxidized flavodoxin from Escherichia coli at 1.8-A resolution.";
RL   Protein Sci. 6:2525-2537(1997).
CC   -!- FUNCTION: LOW-POTENTIAL ELECTRON DONOR TO A NUMBER OF REDOX
CC       ENZYMES (POTENTIAL).
CC   -!- COFACTOR: FMN.
CC   -!- SIMILARITY: BELONGS TO THE FLAVODOXIN FAMILY.
CC   --------------------------------------------------------------------------
CC   This SWISS-PROT entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use  by  non-profit  institutions as long  as its content  is  in  no  way
CC   modified and this statement is not removed.  Usage  by  and for commercial
CC   entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC   or send an email to license@isb-sib.ch).
CC   --------------------------------------------------------------------------
DR   EMBL; M59426; AAA23789.1; -.
DR   EMBL; AE000172; AAC73778.1; -.
DR   EMBL; D90707; BAA35333.1; -.
DR   EMBL; D90708; BAA35341.1; -.
DR   PIR; A37319; A37319.
DR   PDB; 1AHN; 10-DEC-97.
DR   PDB; 1AG9; 24-DEC-97.
DR   ECO2DBASE; A019.0; 6TH EDITION.
DR   ECOGENE; EG10318; FLDA.
DR   INTERPRO; IPR001226; -.
DR   PFAM; PF00258; flavodoxin; 1.
DR   PROSITE; PS00201; FLAVODOXIN; 1.
KW   Electron transport; Flavoprotein; FMN; 3D-structure.
FT   INIT_MET      0      0
SQ   SEQUENCE   175 AA;  19606 MW;  A5FA68D12CE30828 CRC64;
     AITGIFFGSD TGNTENIAKM IQKQLGKDVA DVHDIAKSSK EDLEAYDILL LGIPTWYYGE
     AQCDWDDFFP TLEEIDFNGK LVALFGCGDQ EDYAEYFCDA LGTIRDIIEP RGATIVGHWP
     TAGYHFEASK GLADDDHFVG LAIDEDRQPE LTAERVEKWV KQISEELHLD EILNA
//
ID   FLAV_ENTAG     STANDARD;      PRT;   177 AA.
AC   P28579;
DT   01-DEC-1992 (Rel. 24, Created)
DT   01-DEC-1992 (Rel. 24, Last sequence update)
DT   15-DEC-1998 (Rel. 37, Last annotation update)
DE   FLAVODOXIN.
GN   NIFF.
OS   Enterobacter agglomerans.
OG   Plasmid pEA3.
OC   Bacteria; Proteobacteria; gamma subdivision; Enterobacteriaceae;
OC   Pantoea.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   STRAIN=333;
RX   MEDLINE; 91217003.
RA   Kreutzer R., Dayananda S., Klingmueller W.;
RT   "Cotranscription of the electron transport protein genes nifJ and
RT   nifF in Enterobacter agglomerans 333.";
RL   J. Bacteriol. 173:3252-3256(1991).
RN   [2]
RP   SEQUENCE OF 1-21 FROM N.A.
RC   STRAIN=333;
RA   Schwickerath O.;
RL   Submitted (MAR-1994) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: LOW-POTENTIAL ELECTRON DONOR TO A NUMBER OF REDOX
CC       ENZYMES. NIFF IS THE ELECTRON DONOR TO NITROGENASE.
CC   -!- COFACTOR: FMN.
CC   -!- SIMILARITY: BELONGS TO THE FLAVODOXIN FAMILY.
CC   --------------------------------------------------------------------------
CC   This SWISS-PROT entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use  by  non-profit  institutions as long  as its content  is  in  no  way
CC   modified and this statement is not removed.  Usage  by  and for commercial
CC   entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC   or send an email to license@isb-sib.ch).
CC   --------------------------------------------------------------------------
DR   EMBL; M38221; AAA23385.1; -.
DR   EMBL; X99694; CAA68010.1; -.
DR   EMBL; X78558; CAA55301.1; -.
DR   PIR; A39414; A39414.
DR   HSSP; P10340; 1OFV.
DR   INTERPRO; IPR001226; -.
DR   PFAM; PF00258; flavodoxin; 1.
DR   PROSITE; PS00201; FLAVODOXIN; 1.
KW   Nitrogen fixation; Electron transport; Flavoprotein; FMN; Plasmid.
SQ   SEQUENCE   177 AA;  19581 MW;  3D54F95F7EC60B41 CRC64;
     MATIGIFFGS DTGQTRKVAK LIHQKLDGIA DAPLDVRRAT REQFLSYPVL LLGTPTLGDG
     ELPGVEAGSQ YDSWQEFTNT LSEADLTGKT VALFGLGDQL NYSKNFVSAM RILYDLVIAR
     GACVVGNWPR EGYKFSFSAA LLENNEFVGL PLDQENQYDL TEERIDSWLE KLKPAVL
//
ID   FLAV_HAEIN     STANDARD;      PRT;   173 AA.
AC   P44562;
DT   01-NOV-1995 (Rel. 32, Created)
DT   01-NOV-1995 (Rel. 32, Last sequence update)
DT   15-DEC-1998 (Rel. 37, Last annotation update)
DE   FLAVODOXIN.
GN   FLDA OR HI0191.
OS   Haemophilus influenzae.
OC   Bacteria; Proteobacteria; gamma subdivision; Pasteurellaceae;
OC   Haemophilus.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   STRAIN=RD / KW20;
RX   MEDLINE; 95350630.
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G., Fitzhugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M.,
RA   Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D.,
RA   Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C.,
RA   Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M.,
RA   Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O.,
RA   Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus
RT   influenzae Rd.";
RL   Science 269:496-512(1995).
CC   -!- FUNCTION: LOW-POTENTIAL ELECTRON DONOR TO A NUMBER OF REDOX
CC       ENZYMES (BY SIMILARITY).
CC   -!- COFACTOR: FMN (BY SIMILARITY).
CC   -!- SIMILARITY: BELONGS TO THE FLAVODOXIN FAMILY.
CC   --------------------------------------------------------------------------
CC   This SWISS-PROT entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use  by  non-profit  institutions as long  as its content  is  in  no  way
CC   modified and this statement is not removed.  Usage  by  and for commercial
CC   entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC   or send an email to license@isb-sib.ch).
CC   --------------------------------------------------------------------------
DR   EMBL; U32704; AAC21860.1; -.
DR   HSSP; P23243; 1AHN.
DR   TIGR; HI0191; -.
DR   INTERPRO; IPR001226; -.
DR   PFAM; PF00258; flavodoxin; 1.
DR   PROSITE; PS00201; FLAVODOXIN; 1.
KW   Electron transport; Flavoprotein; FMN.
FT   INIT_MET      0      0       BY SIMILARITY.
SQ   SEQUENCE   173 AA;  19495 MW;  EC5E4ADCADDEC318 CRC64;
     AIVGLFYGSD TGNTENIAKQ IQKQLGSDLI DIRDIAKSSK EDIEAYDFLL FGIPTWYYGE
     AQADWDDFFP TLEEIDFTDK LVGIFGCGDQ EDYADYFCDA IGTVRDIIEP HGAIVVGNWP
     TEGYNFEASK ALLEDGTFIG LCIDEDRQPE LTAERVEKWC KQIYDEMCLA ELA
//
ID   FLAV_HELPY     STANDARD;      PRT;   164 AA.
AC   O25776;
DT   15-DEC-1998 (Rel. 37, Created)
DT   15-DEC-1998 (Rel. 37, Last sequence update)
DT   15-DEC-1998 (Rel. 37, Last annotation update)
DE   FLAVODOXIN.
GN   FLDA OR HP1161.
OS   Helicobacter pylori (Campylobacter pylori).
OC   Bacteria; Proteobacteria; epsilon subdivision; Helicobacter group;
OC   Helicobacter.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   STRAIN=26695 / ATCC 700392;
RX   MEDLINE; 97394467.
RA   Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA   Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S., Dougherty B.A.,
RA   Nelson K., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.,
RA   Loftus B., Richardson D., Dodson R., Khalak H.G., Glodek A.,
RA   McKenney K., Fitzgerald L.M., Lee N., Adams M.D., Hickey E.K.,
RA   Berg D.E., Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M.,
RA   Cotton M.D., Weidman J.M., Fujii C., Bowman C., Watthey L., Wallin E.,
RA   Hayes W.S., Borodovsky M., Karp P.D., Smith H.O., Fraser C.M.,
RA   Venter J.C.;
RT   "The complete genome sequence of the gastric pathogen Helicobacter
RT   pylori.";
RL   Nature 388:539-547(1997).
CC   -!- FUNCTION: LOW-POTENTIAL ELECTRON DONOR TO A NUMBER OF REDOX
CC       ENZYMES (BY SIMILARITY).
CC   -!- COFACTOR: FMN (BY SIMILARITY).
CC   -!- SIMILARITY: BELONGS TO THE FLAVODOXIN FAMILY.
CC   --------------------------------------------------------------------------
CC   This SWISS-PROT entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use  by  non-profit  institutions as long  as its content  is  in  no  way
CC   modified and this statement is not removed.  Usage  by  and for commercial
CC   entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC   or send an email to license@isb-sib.ch).
CC   --------------------------------------------------------------------------
DR   EMBL; AE000622; AAD08207.1; -.
DR   TIGR; HP1161; -.
DR   INTERPRO; IPR001226; -.
DR   PFAM; PF00258; flavodoxin; 1.
DR   PROSITE; PS00201; FLAVODOXIN; FALSE_NEG.
KW   Electron transport; Flavoprotein; FMN.
SQ   SEQUENCE   164 AA;  17492 MW;  EBAD44D97964608C CRC64;
     MGKIGIFFGT DSGNAEAIAE KISKAIGNAE VVDVAKASKE QFNSFTKVIL VAPTAGAGDL
     QTDWEDFLGT LEASDFATKT IGLVGLGDQD TYSETFAEGI FHIYEKAKAG KVVGQTPTDG
     YHFEASKAVE GGKFVGLVID EDNQDDLTDE RISKWVEQVK GSFA
//
ID   FLAV_KLEPN     STANDARD;      PRT;   176 AA.
AC   O07026;
DT   01-NOV-1997 (Rel. 35, Created)
DT   15-JUL-1999 (Rel. 38, Last sequence update)
DT   15-JUL-1999 (Rel. 38, Last annotation update)
DE   FLAVODOXIN.
GN   FLDA.
OS   Klebsiella pneumoniae.
OC   Bacteria; Proteobacteria; gamma subdivision; Enterobacteriaceae;
OC   Klebsiella.
RN   [1]
RP   SEQUENCE FROM N.A., AND INDUCTION.
RC   STRAIN=ATCC 13883;
RX   MEDLINE; 97417492.
RA   Achenbach L.A., Genova E.G.;
RT   "Transcriptional regulation of a second flavodoxin gene from
RT   Klebsiella pneumoniae.";
RL   Gene 194:235-240(1997).
RN   [2]
RP   SEQUENCE OF 135-176 FROM N.A.
RC   STRAIN=ATCC 13883;
RX   MEDLINE; 97208874.
RA   Achenbach L.A., Yang W.;
RT   "The fur gene from Klebsiella pneumoniae: characterization, genomic
RT   organization and phylogenetic analysis.";
RL   Gene 185:201-207(1997).
CC   -!- FUNCTION: LOW-POTENTIAL ELECTRON DONOR TO A NUMBER OF REDOX
CC       ENZYMES (BY SIMILARITY).
CC   -!- COFACTOR: FMN (BY SIMILARITY).
CC   -!- INDUCTION: BY LOW IRON CONDITIONS AND BY HEAT SHOCK. IRON
CC       REGULATION IS MEDIATED THROUGH THE FUR PROTEIN.
CC   -!- SIMILARITY: BELONGS TO THE FLAVODOXIN FAMILY.
CC   --------------------------------------------------------------------------
CC   This SWISS-PROT entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use  by  non-profit  institutions as long  as its content  is  in  no  way
CC   modified and this statement is not removed.  Usage  by  and for commercial
CC   entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC   or send an email to license@isb-sib.ch).
CC   --------------------------------------------------------------------------
DR   EMBL; U67169; AAB65080.1; -.
DR   EMBL; L23871; AAB51076.1; -.
DR   HSSP; P23243; 1AHN.
DR   INTERPRO; IPR001226; -.
DR   PFAM; PF00258; flavodoxin; 1.
DR   PROSITE; PS00201; FLAVODOXIN; 1.
KW   Electron transport; Flavoprotein; FMN.
SQ   SEQUENCE   176 AA;  19765 MW;  C40E5F80287D3636 CRC64;
     MAIIGIFFGS DTGNTENIAK MIQKQLGKDV ADVHDIAKSS KEDLEAHDIL LLGIPTWYYG
     EAQCDWDDFF PTLEEIDFNG KLVALFGCGD QEDYAEYFCD ALGTIRDIIE PRGATIVGHW
     PTAGYHFEAS KGLADDDHFV GLAIDEDRQP ELTNERVEKW VKQVAEELHL EEIKNA
//
ID   FLAV_MATIN     STANDARD;      PRT;   291 AA.
AC   O04395;
DT   15-JUL-1999 (Rel. 38, Created)
DT   15-JUL-1999 (Rel. 38, Last sequence update)
DT   15-JUL-1999 (Rel. 38, Last annotation update)
DE   FLAVONOL SYNTHASE (EC 1.3.-.-) (FLS) (FRAGMENT).
OS   Matthiola incana (Common stock).
OC   Eukaryota; Viridiplantae; Embryophyta; Tracheophyta; Spermatophyta;
OC   Magnoliophyta; eudicotyledons; Rosidae; eurosids II; Brassicales;
OC   Brassicaceae; Matthiola.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   TISSUE=FLOWER BUDS, AND PETAL;
RA   Henkel J., Forkmann G.;
RT   "Cloning and expression of a flavonol synthase gene from common
RT   stock (Matthiola incana).";
RL   Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: CATALYZES THE FORMATION OF FLAVONOLS FROM
CC       DIHYDROFLAVONOLS. IT CAN ACT ON DIHYDROKAEMPFEROL TO PRODUCE
CC       KAEMPFEROL, ON DIHYDROQUERCETIN TO PRODUCE QUERCITIN AND ON
CC       DIHYDROMYRICETIN TO PRODUCE MYRICETIN.
CC   -!- COFACTOR: IRON AND ASCORBATE.
CC   -!- PATHWAY: PART OF THE BIOSYNTHETIC PATHWAY FOR FLAVONOLS WHICH ARE
CC       FLAVONOIDS. FLAVONOLS ARE IMPORTANT CO-PIGMENTS IN FLOWER OR FRUIT
CC       COLOR AND ARE ALSO ESSENTIAL FOR POLLEN TUBE GROWTH.
CC   -!- SUBCELLULAR LOCATION: CYTOPLASMIC.
CC   -!- SIMILARITY: BELONGS TO THE IRON/ASCORBATE-DEPENDENT FAMILY OF
CC       OXIDOREDUCTASES.
CC   --------------------------------------------------------------------------
CC   This SWISS-PROT entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use  by  non-profit  institutions as long  as its content  is  in  no  way
CC   modified and this statement is not removed.  Usage  by  and for commercial
CC   entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC   or send an email to license@isb-sib.ch).
CC   --------------------------------------------------------------------------
DR   EMBL; AF001391; AAB58800.1; -.
DR   MENDEL; 15155; MATin;1185;mn15155.
DR   INTERPRO; IPR002419; -.
DR   PFAM; PF00671; Fe_Asc_oxidored; 1.
KW   Flavonoid biosynthesis; Oxidoreductase; Dioxygenase; Iron; Vitamin C.
FT   NON_TER       1      1
SQ   SEQUENCE   291 AA;  33430 MW;  6B8E4E3D2834720A CRC64;
     QVPVVDLSCP DEELVARTVV KASEDWGVFQ VVNHGIPTEL IQRLQKVGRE FFELPEAEKR
     SCAREAGSVE GYGRRIELDI KKRKGIVDQI YLSTWPPSSV NYRYWPKSPP DYREVNEEYA
     RHVKTLSEKI MEWLSEGLGL GREAIKEVNG CWYVMNINHY PPYPHSDSFN GLEPHTDING
     LTLIITNEIP GLQVFKDDHW IEVEYIPSAI IVNIGDQIMM LSNGKYKNVL HKTTVDKEKT
     RMSWPVLVSP TYDMVVGPLP ELTSEDDPPK FKPIAYKDYV HNKITFLKNK S
//
ID   FLAV_MEGEL     STANDARD;      PRT;   137 AA.
AC   P00321;
DT   21-JUL-1986 (Rel. 01, Created)
DT   21-JUL-1986 (Rel. 01, Last sequence update)
DT   15-DEC-1998 (Rel. 37, Last annotation update)
DE   FLAVODOXIN.
OS   Megasphaera elsdenii.
OC   Bacteria; Firmicutes; Bacillus/Clostridium group; Sporomusa subbranch;
OC   Megasphaera.
RN   [1]
RP   SEQUENCE.
RC   STRAIN=LC1;
RX   MEDLINE; 73197809.
RA   Tanaka M., Haniu M., Yasunobu K.T., Mayhew S.G., Massey V.;
RT   "The primary structure of Peptostreptococcus elsdenii flavodoxin.";
RL   J. Biol. Chem. 248:4354-4366(1973).
RN   [2]
RP   REVISIONS TO 78-82.
RX   MEDLINE; 74277393.
RA   Tanaka M., Haniu M., Yasunobu K.T., Mayhew S.G., Massey V.;
RT   "Correction of the amino acid sequence of Peptostreptococcus elsdenii
RT   flavodoxin.";
RL   J. Biol. Chem. 249:4397-4397(1974).
RN   [3]
RP   STRUCTURE BY NMR.
RX   MEDLINE; 90276429.
RA   van Mierlo C.P.M., Mueller F., Vervoort J.;
RT   "Secondary and tertiary structure characteristics of Megasphaera
RT   elsdenii flavodoxin in the reduced state as determined by two-
RT   dimensional 1H NMR.";
RL   Eur. J. Biochem. 189:589-600(1990).
RN   [4]
RP   STRUCTURE BY NMR.
RX   MEDLINE; 91071190.
RA   van Mierlo C.P.M., Lijnzaad P., Vervoort J., Mueller F.,
RA   Berendsen H.J.C., de Vlieg J.;
RT   "Tertiary structure of two-electron reduced Megasphaera elsdenii
RT   flavodoxin and some implications, as determined by two-dimensional
RT   1H-NMR and restrained molecular dynamics.";
RL   Eur. J. Biochem. 194:185-198(1990).
CC   -!- FUNCTION: LOW-POTENTIAL ELECTRON DONOR TO A NUMBER OF REDOX
CC       ENZYMES.
CC   -!- COFACTOR: FMN.
CC   -!- SIMILARITY: BELONGS TO THE FLAVODOXIN FAMILY.
DR   PIR; A00331; FXME.
DR   HSSP; P00322; 2FVX.
DR   INTERPRO; IPR001226; -.
DR   PFAM; PF00258; flavodoxin; 1.
DR   PROSITE; PS00201; FLAVODOXIN; 1.
KW   Electron transport; Flavoprotein; FMN.
SQ   SEQUENCE   137 AA;  14550 MW;  86BD744412D6F869 CRC64;
     MVEIVYWSGT GNTEAMANEI EAAVKAAGAD VESVRFEDTN VDDVASKDVI LLGCPAMGSE
     ELEDSVVEPF FTDLAPKLKG KKVGLFGSYG WGSGEWMDAW KQRTEDTGAT VIGTAIVNEM
     PDNAPECKEL GEAAAKA
//
ID   FLAV_NOSSM     STANDARD;      PRT;    35 AA.
AC   P35707;
DT   01-JUN-1994 (Rel. 29, Created)
DT   01-JUN-1994 (Rel. 29, Last sequence update)
DT   15-DEC-1998 (Rel. 37, Last annotation update)
DE   FLAVODOXIN (FRAGMENT).
OS   Nostoc sp. (strain MAC).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
RN   [1]
RP   SEQUENCE.
RA   Takruri I.A.H., Boulter D., Fitzgerald M.P., Hutber G.N., Rogers L.J.;
RT   "N-terminal amino acid sequences of flavodoxins from Chondrus crispus
RT   and Nostoc strain MAC.";
RL   Phytochemistry 25:2113-2115(1986).
CC   -!- FUNCTION: LOW-POTENTIAL ELECTRON DONOR TO A NUMBER OF REDOX
CC       ENZYMES.
CC   -!- COFACTOR: FMN.
CC   -!- SIMILARITY: BELONGS TO THE FLAVODOXIN FAMILY.
DR   PIR; PA0004; PA0004.
DR   HSSP; P11241; 1RCF.
DR   INTERPRO; IPR001226; -.
DR   PFAM; PF00258; flavodoxin; 1.
DR   PROSITE; PS00201; FLAVODOXIN; 1.
KW   Electron transport; Flavoprotein; FMN.
FT   NON_TER      35     35
SQ   SEQUENCE   35 AA;  3820 MW;  B6EEB5CA7A45DDA6 CRC64;
     SKKIGLFYGT ZTGKTESVAE IIDEFGDEVV TLDID
//
ID   FLAV_PETHY     STANDARD;      PRT;   348 AA.
AC   Q07512;
DT   01-OCT-1996 (Rel. 34, Created)
DT   01-OCT-1996 (Rel. 34, Last sequence update)
DT   15-JUL-1999 (Rel. 38, Last annotation update)
DE   FLAVONOL SYNTHASE (EC 1.3.-.-) (FLS).
GN   FL.
OS   Petunia hybrida (Petunia).
OC   Eukaryota; Viridiplantae; Embryophyta; Tracheophyta; Spermatophyta;
OC   Magnoliophyta; eudicotyledons; Asteridae; euasterids I; Solanales;
OC   Solanaceae; Petunia.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   STRAIN=CV. OLD GLORY BLUE; TISSUE=PETAL;
RX   MEDLINE; 94108485.
RA   Holton T.A., Brugliera F., Tanaka Y.;
RT   "Cloning and expression of flavonol synthase from Petunia hybrida.";
RL   Plant J. 4:1003-1010(1993).
CC   -!- FUNCTION: CATALYZES THE FORMATION OF FLAVONOLS FROM
CC       DIHYDROFLAVONOLS. IT CAN ACT ON DIHYDROKAEMPFEROL TO PRODUCE
CC       KAEMPFEROL, ON DIHYDROQUERCETIN TO PRODUCE QUERCITIN AND ON
CC       DIHYDROMYRICETIN TO PRODUCE MYRICETIN.
CC   -!- COFACTOR: IRON AND ASCORBATE.
CC   -!- PATHWAY: PART OF THE BIOSYNTHETIC PATHWAY FOR FLAVONOLS WHICH ARE
CC       FLAVONOIDS. FLAVONOLS ARE IMPORTANT CO-PIGMENTS IN FLOWER OR FRUIT
CC       COLOR AND ARE ALSO ESSENTIAL FOR POLLEN TUBE GROWTH.
CC   -!- SUBCELLULAR LOCATION: CYTOPLASMIC.
CC   -!- DEVELOPMENTAL STAGE: EXPRESSED AT HIGHEST LEVEL DURING THE FIRST
CC       STAGE OF FLOWER DEVELOPMENT.
CC   -!- SIMILARITY: BELONGS TO THE IRON/ASCORBATE-DEPENDENT FAMILY OF
CC       OXIDOREDUCTASES.
CC   --------------------------------------------------------------------------
CC   This SWISS-PROT entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use  by  non-profit  institutions as long  as its content  is  in  no  way
CC   modified and this statement is not removed.  Usage  by  and for commercial
CC   entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC   or send an email to license@isb-sib.ch).
CC   --------------------------------------------------------------------------
DR   EMBL; Z22543; CAA80264.1; -.
DR   INTERPRO; IPR002419; -.
DR   PFAM; PF00671; Fe_Asc_oxidored; 1.
KW   Flavonoid biosynthesis; Oxidoreductase; Dioxygenase; Iron; Vitamin C.
SQ   SEQUENCE   348 AA;  39427 MW;  B39E1E4381DE6379 CRC64;
     MKTAQGVSAT LTMEVARVQA IASLSKCMDT IPSEYIRSEN EQPAATTLHG VVLQVPVIDL
     RDPDENKMVK LIADASKEWG IFQLINHGIP DEAIADLQKV GKEFFEHVPQ EEKELIAKTP
     GSNDIEGYGT SLQKEVEGKK GWVDHLFHKI WPPSAVNYRY WPKNPPSYRE ANEEYGKRMR
     EVVDRIFKSL SLGLGLEGHE MIEAAGGDEI VYLLKINYYP PCPRPDLALG VVAHTDMSYI
     TILVPNEVQG LQVFKDGHWY DVKYIPNALI VHIGDQVEIL SNGKYKSVYH RTTVNKDKTR
     MSWPVFLEPP SEHEVGPIPK LLSEANPPKF KTKKYKDYVY CKLNKLPQ
//
ID   FLAV_RHOCA     STANDARD;      PRT;   181 AA.
AC   P52967;
DT   01-OCT-1996 (Rel. 34, Created)
DT   01-OCT-1996 (Rel. 34, Last sequence update)
DT   15-DEC-1998 (Rel. 37, Last annotation update)
DE   FLAVODOXIN 2.
GN   NIFF.
OS   Rhodobacter capsulatus (Rhodopseudomonas capsulata).
OC   Bacteria; Proteobacteria; alpha subdivision; Rhodobacter group;
OC   Rhodobacter.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   STRAIN=SB1003;
RA   Gennaro G., Huebner P., Sandmeier U., Yakunin A.F.,
RA   Hallenbeck P.C.;
RL   Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: LOW-POTENTIAL ELECTRON DONOR TO A NUMBER OF REDOX
CC       ENZYMES. NIFF IS THE ELECTRON DONOR TO NITROGENASE.
CC   -!- COFACTOR: FMN.
CC   -!- SIMILARITY: BELONGS TO THE FLAVODOXIN FAMILY.
CC   --------------------------------------------------------------------------
CC   This SWISS-PROT entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use  by  non-profit  institutions as long  as its content  is  in  no  way
CC   modified and this statement is not removed.  Usage  by  and for commercial
CC   entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC   or send an email to license@isb-sib.ch).
CC   --------------------------------------------------------------------------
DR   EMBL; L42290; AAC05792.1; -.
DR   HSSP; P10340; 1OFV.
DR   INTERPRO; IPR001226; -.
DR   PFAM; PF00258; flavodoxin; 1.
DR   PROSITE; PS00201; FLAVODOXIN; 1.
KW   Nitrogen fixation; Electron transport; Flavoprotein; FMN.
FT   INIT_MET      0      0       BY SIMILARITY.
SQ   SEQUENCE   181 AA;  19688 MW;  639E906EE80C79BC CRC64;
     AKIGLFFGSD TGTTRKIAKQ IKDMFDDEVM AKPLNVNRAD VADFMAYDFL ILGTPTLGDG
     QLPGLSANAA SESWEEFLPR IADQDFSGKT IALFGLGDQV TYPLEFVNAL FFLHEFFSDR
     GANVVGRWPA KGYGFEDSLA VVEGEFLGLA LDQDNQAALT PERLKGWLSL IAADFGLVLP
     A
//
ID   FLAV_SOLTU     STANDARD;      PRT;   349 AA.
AC   Q41452;
DT   01-NOV-1997 (Rel. 35, Created)
DT   01-NOV-1997 (Rel. 35, Last sequence update)
DT   15-JUL-1999 (Rel. 38, Last annotation update)
DE   FLAVONOL SYNTHASE (EC 1.3.-.-) (FLS).
OS   Solanum tuberosum (Potato).
OC   Eukaryota; Viridiplantae; Embryophyta; Tracheophyta; Spermatophyta;
OC   Magnoliophyta; eudicotyledons; Asteridae; euasterids I; Solanales;
OC   Solanaceae; Solanum.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   TISSUE=PISTIL;
RX   MEDLINE; 97177800.
RA   van Eldik G.J., Ruiter R.K., Reijnen W.H., van Herpen M.M.A.,
RA   Schrauwen J.A.M., Wullems G.J.;
RT   "Regulation of flavonol biosynthesis during anther and pistil
RT   development, and during pollen tube growth in Solanum tuberosum.";
RL   Plant J. 11:105-113(1997).
CC   -!- FUNCTION: CATALYZES THE FORMATION OF FLAVONOLS FROM
CC       DIHYDROFLAVONOLS. IT CAN ACT ON DIHYDROKAEMPFEROL TO PRODUCE
CC       KAEMPFEROL, ON DIHYDROQUERCETIN TO PRODUCE QUERCITIN AND ON
CC       DIHYDROMYRICETIN TO PRODUCE MYRICETIN.
CC   -!- COFACTOR: IRON AND ASCORBATE (BY SIMILARITY).
CC   -!- PATHWAY: PART OF THE BIOSYNTHETIC PATHWAY FOR FLAVONOLS WHICH ARE
CC       FLAVONOIDS. FLAVONOLS ARE IMPORTANT CO-PIGMENTS IN FLOWER OR FRUIT
CC       COLOR AND ARE ALSO ESSENTIAL FOR POLLEN TUBE GROWTH.
CC   -!- SUBCELLULAR LOCATION: CYTOPLASMIC.
CC   -!- DEVELOPMENTAL STAGE: TEMPORALLY EXPRESSED DURING FLOWER
CC       DEVELOPMENT.
CC   -!- SIMILARITY: BELONGS TO THE IRON/ASCORBATE-DEPENDENT FAMILY OF
CC       OXIDOREDUCTASES.
CC   --------------------------------------------------------------------------
CC   This SWISS-PROT entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use  by  non-profit  institutions as long  as its content  is  in  no  way
CC   modified and this statement is not removed.  Usage  by  and for commercial
CC   entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC   or send an email to license@isb-sib.ch).
CC   --------------------------------------------------------------------------
DR   EMBL; X92178; CAA63092.1; -.
DR   INTERPRO; IPR002419; -.
DR   PFAM; PF00671; Fe_Asc_oxidored; 1.
KW   Flavonoid biosynthesis; Oxidoreductase; Dioxygenase; Iron; Vitamin C.
SQ   SEQUENCE   349 AA;  39728 MW;  ADBBC3F6B10A0E05 CRC64;
     MKTIQGQSAT TALTMEVARV QAISSITKCM DTIPSEYIRS ENEQPAATTL QGVVLEVPVI
     DISNVDDDEE KLVKEIVEAS KEWGIFQVIN HGIPDEVIEN LQKVGKEFFE EVPQEEKELI
     AKKPGAQSLE GYGTSLQKEI EGKKGWVDHL FHKIWPPSAI NYRYWPKNPP SYREANEEYA
     KWLRKVADGI FRSLSLGLGL EGHEMMEAAG SEDIVYMLKI NYYPPCPRPD LALGVVAHTD
     MSYITLLVPN EVQVFKDGHW YDVNYIPNAI IVHIGDQVEI LSNGKYKSVY HRTTVNKYKT
     RMSWPVFLEP SSEHEVGPIP NLINEANPPK FKTKKYKDYV YCKLNKLPQ
//
ID   FLAV_SYNP2     STANDARD;      PRT;   169 AA.
AC   P31158;
DT   01-JUL-1993 (Rel. 26, Created)
DT   01-JUL-1993 (Rel. 26, Last sequence update)
DT   15-DEC-1998 (Rel. 37, Last annotation update)
DE   FLAVODOXIN.
GN   ISIB.
OS   Synechococcus sp. (strain PCC 7002) (Agmenellum quadruplicatum).
OC   Bacteria; Cyanobacteria; Chroococcales; Synechococcus.
RN   [1]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 92407507.
RA   Leonhardt K.G., Straus N.A.;
RT   "An iron stress operon involved in photosynthetic electron transport
RT   in the marine cyanobacterium Synechococcus sp. PCC 7002.";
RL   J. Gen. Microbiol. 138:1613-1621(1992).
CC   -!- FUNCTION: LOW-POTENTIAL ELECTRON DONOR TO A NUMBER OF REDOX
CC       ENZYMES.
CC   -!- COFACTOR: FMN.
CC   -!- INDUCTION: BY IRON-STRESS.
CC   -!- SIMILARITY: BELONGS TO THE FLAVODOXIN FAMILY.
CC   --------------------------------------------------------------------------
CC   This SWISS-PROT entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use  by  non-profit  institutions as long  as its content  is  in  no  way
CC   modified and this statement is not removed.  Usage  by  and for commercial
CC   entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC   or send an email to license@isb-sib.ch).
CC   --------------------------------------------------------------------------
DR   EMBL; M88253; AAA27318.1; -.
DR   PIR; B47673; B47673.
DR   HSSP; P10340; 1OFV.
DR   INTERPRO; IPR001226; -.
DR   PFAM; PF00258; flavodoxin; 1.
DR   PROSITE; PS00201; FLAVODOXIN; 1.
KW   Electron transport; Flavoprotein; FMN.
FT   INIT_MET      0      0       BY SIMILARITY.
SQ   SEQUENCE   169 AA;  18348 MW;  422E50BFADEBA8E0 CRC64;
     SKIGLFFGTQ TGNTEELAQA IQAAFGGSDI VELFDVAEVD IEALRDFDQL IIGCPTWNVG
     ELQSDWEALY DDLDDVDFSG KTIAYFGAGD QVGYADNFQD AMGVLEEKIT SLGGKTVGQW
     PTAGYDHSES KAERDGKFVG LAIDEDNQPE LTAERIQAWV AQLKPAFGL
//
ID   FLAV_SYNP7     STANDARD;      PRT;   169 AA.
AC   P10340;
DT   01-MAR-1989 (Rel. 10, Created)
DT   01-JAN-1990 (Rel. 13, Last sequence update)
DT   30-MAY-2000 (Rel. 39, Last annotation update)
DE   FLAVODOXIN.
GN   ISIB.
OS   Synechococcus sp. (strain PCC 7942) (Anacystis nidulans R2).
OC   Bacteria; Cyanobacteria; Chroococcales; Synechococcus.
RN   [1]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 88086879.
RA   Laudenbach D.E., Reith M.E., Straus N.A.;
RT   "Isolation, sequence analysis, and transcriptional studies of the
RT   flavodoxin gene from Anacystis nidulans R2.";
RL   J. Bacteriol. 170:258-265(1988).
RN   [2]
RP   SEQUENCE OF 1-55, AND X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX   MEDLINE; 83216115.
RA   Smith W.W., Pattridge K.A., Ludwig M.L., Petsko G.A., Tsernoglou D.,
RA   Tanaka M., Yasunobu K.T.;
RT   "Structure of oxidized flavodoxin from Anacystis nidulans.";
RL   J. Mol. Biol. 165:737-755(1983).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
RX   MEDLINE; 20079529.
RA   Drennan C.L., Pattridge K.A., Weber C.H., Metzger A.L., Hoover D.M.,
RA   Ludwig M.L.;
RT   "Refined structures of oxidized flavodoxin from Anacystis nidulans.";
RL   J. Mol. Biol. 294:711-724(1999).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS).
RX   MEDLINE; 20079530.
RA   Hoover D.M., Drennan C.L., Metzger A.L., Osborne C., Weber C.H.,
RA   Pattridge K.A., Ludwig M.L.;
RT   "Comparisons of wild-type and mutant flavodoxins from Anacystis
RT   nidulans. Structural determinants of the redox potentials.";
RL   J. Mol. Biol. 294:725-743(1999).
RN   [5]
RP   STRUCTURE BY NMR.
RX   MEDLINE; 91329335.
RA   Clubb R.T., Thanabal V., Osborne C., Wagner G.;
RT   "1H and 15N resonance assignments of oxidized flavodoxin from
RT   Anacystis nidulans with 3D NMR.";
RL   Biochemistry 30:7718-7730(1991).
CC   -!- FUNCTION: LOW-POTENTIAL ELECTRON DONOR TO A NUMBER OF REDOX
CC       ENZYMES.
CC   -!- COFACTOR: FMN.
CC   -!- INDUCTION: BY IRON-STRESS.
CC   -!- SIMILARITY: BELONGS TO THE FLAVODOXIN FAMILY.
CC   --------------------------------------------------------------------------
CC   This SWISS-PROT entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use  by  non-profit  institutions as long  as its content  is  in  no  way
CC   modified and this statement is not removed.  Usage  by  and for commercial
CC   entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC   or send an email to license@isb-sib.ch).
CC   --------------------------------------------------------------------------
DR   EMBL; M19116; AAA22050.1; -.
DR   PIR; A05103; A05103.
DR   PIR; A28670; A28670.
DR   PDB; 1OFV; 31-JAN-94.
DR   PDB; 1CZH; 29-DEC-99.
DR   PDB; 1CZK; 29-DEC-99.
DR   PDB; 1CZL; 29-DEC-99.
DR   PDB; 1CZN; 29-DEC-99.
DR   PDB; 1CZO; 29-DEC-99.
DR   PDB; 1CZR; 29-DEC-99.
DR   PDB; 1CZU; 29-DEC-99.
DR   PDB; 1D03; 29-DEC-99.
DR   PDB; 1D04; 29-DEC-99.
DR   INTERPRO; IPR001226; -.
DR   PFAM; PF00258; flavodoxin; 1.
DR   PROSITE; PS00201; FLAVODOXIN; 1.
KW   Electron transport; Flavoprotein; FMN; 3D-structure.
FT   INIT_MET      0      0
FT   CONFLICT     54     54       C -> S (IN REF. 2).
FT   CONFLICT    167    168       FG -> GF (IN REF. 2).
FT   STRAND        3      7
FT   HELIX        13     25
FT   TURN         26     26
FT   TURN         28     30
FT   STRAND       31     35
FT   HELIX        36     38
FT   HELIX        41     46
FT   STRAND       49     53
FT   STRAND       56     57
FT   TURN         58     60
FT   STRAND       61     62
FT   HELIX        64     75
FT   TURN         79     80
FT   STRAND       82     88
FT   TURN         91     96
FT   TURN         98     99
FT   HELIX       100    111
FT   TURN        112    113
FT   STRAND      115    116
FT   STRAND      120    121
FT   TURN        123    124
FT   TURN        131    132
FT   STRAND      133    134
FT   TURN        135    136
FT   STRAND      137    138
FT   STRAND      141    143
FT   TURN        145    147
FT   HELIX       149    166
FT   TURN        167    168
SQ   SEQUENCE   169 AA;  18646 MW;  CF049E12F9C6AA1F CRC64;
     AKIGLFYGTQ TGVTQTIAES IQQEFGGESI VDLNDIANAD ASDLNAYDYL IIGCPTWNVG
     ELQSDWEGIY DDLDSVNFQG KKVAYFGAGD QVGYSDNFQD AMGILEEKIS SLGSQTVGYW
     PIEGYDFNES KAVRNNQFVG LAIDEDNQPD LTKNRIKTWV SQLKSEFGL
//
ID   FLAV_SYNY3     STANDARD;      PRT;   170 AA.
AC   P27319;
DT   01-AUG-1992 (Rel. 23, Created)
DT   01-JUN-1994 (Rel. 29, Last sequence update)
DT   15-DEC-1998 (Rel. 37, Last annotation update)
DE   FLAVODOXIN.
GN   ISIB OR SLL0248.
OS   Synechocystis sp. (strain PCC 6803).
OC   Bacteria; Cyanobacteria; Chroococcales; Synechocystis.
RN   [1]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 94320780.
RA   Poncelet M.G.M., Cassier-Chauvat C.J.S., Chauvat F.R.L.;
RT   "Sequence of the flavodoxin-encoding gene from the cyanobacterium
RT   Synechocystis PCC6803.";
RL   Gene 145:153-154(1994).
RN   [2]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 97061201.
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T.,
RA   Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K.,
RA   Okumura S., Shimpo S., Takeuchi C., Wada T., Watanabe A.,
RA   Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the
RT   entire genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
RN   [3]
RP   SEQUENCE OF 1-42.
RX   MEDLINE; 92338182.
RA   Bottin H., Lagoutte B.;
RT   "Ferredoxin and flavodoxin from the cyanobacterium Synechocystis sp
RT   PCC 6803.";
RL   Biochim. Biophys. Acta 1101:48-56(1992).
CC   -!- FUNCTION: LOW-POTENTIAL ELECTRON DONOR TO A NUMBER OF REDOX
CC       ENZYMES. THE MIDPOINT REDOX POTENTIALS ARE -433 MV AND -238 MV.
CC   -!- COFACTOR: FMN.
CC   -!- SIMILARITY: BELONGS TO THE FLAVODOXIN FAMILY.
CC   --------------------------------------------------------------------------
CC   This SWISS-PROT entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use  by  non-profit  institutions as long  as its content  is  in  no  way
CC   modified and this statement is not removed.  Usage  by  and for commercial
CC   entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC   or send an email to license@isb-sib.ch).
CC   --------------------------------------------------------------------------
DR   EMBL; Z27091; CAA81614.1; -.
DR   EMBL; L25881; AAA27288.1; -.
DR   EMBL; D90910; BAA17947.1; -.
DR   PIR; S38632; S38632.
DR   HSSP; P10340; 1OFV.
DR   INTERPRO; IPR001094; -.
DR   INTERPRO; IPR001226; -.
DR   PFAM; PF00258; flavodoxin; 1.
DR   PRINTS; PR00369; FLAVODOXIN.
DR   PROSITE; PS00201; FLAVODOXIN; 1.
KW   Electron transport; Flavoprotein; FMN.
FT   CONFLICT      2      2       MISSING (IN REF. 3).
FT   CONFLICT     40     40       A -> AA (IN REF. 3).
SQ   SEQUENCE   170 AA;  18822 MW;  B2937F347796BBD9 CRC64;
     MTKIGLFYGT QTGNTETIAE LIQKEMGGDS VVDMMDISQA DVDDFRQYSC LIIGCPTWNV
     GELQSDWEGF YDQLDEIDFN GKKVAYFGAG DQVGYADNFQ DAMGILEEKI SGLGGKTVGF
     WPTAGYDFDE SKAVKNGKFV GLALDEDNQP ELTELRVKTW VSEIKPILQS
//
ID   FLAV_TREPA     STANDARD;      PRT;   146 AA.
AC   O83895;
DT   15-DEC-1998 (Rel. 37, Created)
DT   15-DEC-1998 (Rel. 37, Last sequence update)
DT   30-MAY-2000 (Rel. 39, Last annotation update)
DE   FLAVODOXIN.
GN   FLDA OR TP0925.
OS   Treponema pallidum.
OC   Bacteria; Spirochaetales; Spirochaetaceae; Treponema.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   STRAIN=NICHOLS;
RX   MEDLINE; 98332770.
RA   Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G.,
RA   Dodson R., Gwinn M., Hickey E.K., Clayton R., Ketchum K.A.,
RA   Sodergren E., Hardham J.M., McLeod M.P., Salzberg S., Peterson J.,
RA   Khalak H., Richardson D., Howell J.K., Chidambaram M., Utterback T.,
RA   McDonald L., Artiach P., Bowman C., Cotton M.D., Fujii C., Garland S.,
RA   Hatch B., Horst K., Roberts K., Sandusky M., Weidman J., Smith H.O.,
RA   Venter J.C.;
RT   "Complete genome sequence of Treponema pallidum, the syphilis
RT   spirochete.";
RL   Science 281:375-388(1998).
CC   -!- FUNCTION: LOW-POTENTIAL ELECTRON DONOR TO A NUMBER OF REDOX
CC       ENZYMES (BY SIMILARITY).
CC   -!- COFACTOR: FMN (BY SIMILARITY).
CC   -!- SIMILARITY: BELONGS TO THE FLAVODOXIN FAMILY.
CC   --------------------------------------------------------------------------
CC   This SWISS-PROT entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use  by  non-profit  institutions as long  as its content  is  in  no  way
CC   modified and this statement is not removed.  Usage  by  and for commercial
CC   entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC   or send an email to license@isb-sib.ch).
CC   --------------------------------------------------------------------------
DR   EMBL; AE001261; AAC65882.1; -.
DR   TIGR; TP0925; -.
DR   INTERPRO; IPR001226; -.
DR   PFAM; PF00258; flavodoxin; 1.
DR   PROSITE; PS00201; FLAVODOXIN; 1.
KW   Electron transport; Flavoprotein; FMN.
SQ   SEQUENCE   146 AA;  15793 MW;  398A7D7C8530F2CE CRC64;
     MAKVAVIFWS GTGHTETMAR CIVEGLNVGG AKADLFSVMD FDVGTFDSYD RFAFGCSAAG
     SEELESSEFE PFFTSIEGRL SGKKVALFGS YEWAGEGEGG EWMVNWVERC KAAGADVFEG
     KGEIAYDDPS EEAQASCKAF GERFAR
//
ID   FLAV_TRIER     STANDARD;      PRT;   144 AA.
AC   O52659;
DT   15-DEC-1998 (Rel. 37, Created)
DT   15-DEC-1998 (Rel. 37, Last sequence update)
DT   15-DEC-1998 (Rel. 37, Last annotation update)
DE   FLAVODOXIN (FRAGMENT).
GN   FLD.
OS   Trichodesmium erythraeum.
OC   Bacteria; Cyanobacteria; Oscillatoriales; Trichodesmium.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   STRAIN=IMS101;
RA   Lin S., Carpenter E.J.;
RL   Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: LOW-POTENTIAL ELECTRON DONOR TO A NUMBER OF REDOX
CC       ENZYMES (BY SIMILARITY).
CC   -!- COFACTOR: FMN (BY SIMILARITY).
CC   -!- SIMILARITY: BELONGS TO THE FLAVODOXIN FAMILY.
CC   --------------------------------------------------------------------------
CC   This SWISS-PROT entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use  by  non-profit  institutions as long  as its content  is  in  no  way
CC   modified and this statement is not removed.  Usage  by  and for commercial
CC   entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC   or send an email to license@isb-sib.ch).
CC   --------------------------------------------------------------------------
DR   EMBL; AF044318; AAC02683.1; -.
DR   INTERPRO; IPR001226; -.
DR   PFAM; PF00258; flavodoxin; 1.
DR   PROSITE; PS00201; FLAVODOXIN; 1.
KW   Electron transport; Flavoprotein; FMN.
FT   NON_TER       1      1
FT   NON_TER     144    144
SQ   SEQUENCE   144 AA;  15599 MW;  D73BED7C4C4F19AB CRC64;
     KMGLFFGTTT GKTEEAAEKI KEEFGGDDVV TIHDISEASP EDFDGYQNVI IGCPTWDVGE
     LQSDWSGFYS EELDNVKFTG KKVAYFGTGD QIGYADNFQD AMGILEEKIT GLGGTTIGSW
     STEGYDHVDS KAVKNGKFVG LALD
//
ID   PAX1_HUMAN     STANDARD;      PRT;   361 AA.
AC   P15863; Q9Y558;
DT   01-APR-1990 (Rel. 14, Created)
DT   30-MAY-2000 (Rel. 39, Last sequence update)
DT   30-MAY-2000 (Rel. 39, Last annotation update)
DE   PAIRED BOX PROTEIN PAX-1 (HUP48).
GN   PAX1 OR HUP48.
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
RN   [1]
RP   SEQUENCE FROM N.A.
RA   Smith M.;
RL   Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   SEQUENCE OF 1-142 FROM N.A.
RX   MEDLINE; 89305521.
RA   Burri M., Tromvoukis Y., Bopp D., Frigerio G., Noll M.;
RT   "Conservation of the paired domain in metazoans and its structure in
RT   three isolated human genes.";
RL   EMBO J. 8:1183-1190(1989).
RN   [3]
RP   VARIANT HIS-45.
RX   MEDLINE; 97016531.
RA   Hol F.A., Geurds M.P.A., Chatkupt S., Shugart Y.Y., Balling R.,
RA   Schrander-Stumpel C.T.R.M., Johnson W.G., Hamel B.C.J.,
RA   Mariman E.C.M.;
RT   "PAX genes and human neural tube defects: an amino acid substitution
RT   in PAX1 in a patient with spina bifida.";
RL   J. Med. Genet. 33:655-660(1996).
CC   -!- FUNCTION: THIS PROTEIN IS A TRANSCRIPTIONAL ACTIVATOR. IT MAY PLAY
CC       A ROLE IN THE FORMATION OF SEGMENTED STRUCTURES OF THE EMBRYO. MAY
CC       PLAY AN IMPORTANT ROLE IN THE NORMAL DEVELOPMENT OF THE VERTEBRAL
CC       COLUMN (BY SIMILARITY).
CC   -!- SUBCELLULAR LOCATION: NUCLEAR.
CC   -!- SIMILARITY: CONTAINS A PAIRED BOX DOMAIN.
CC   --------------------------------------------------------------------------
CC   This SWISS-PROT entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use  by  non-profit  institutions as long  as its content  is  in  no  way
CC   modified and this statement is not removed.  Usage  by  and for commercial
CC   entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC   or send an email to license@isb-sib.ch).
CC   --------------------------------------------------------------------------
DR   EMBL; AL035562; CAB46996.1; ALT_SEQ.
DR   EMBL; X15044; CAA33146.1; ALT_INIT.
DR   PIR; S06961; S06961.
DR   HSSP; P06601; 1PDN.
DR   TRANSFAC; T00398; -.
DR   MIM; 167411; -.
DR   INTERPRO; IPR001523; -.
DR   PFAM; PF00292; PAX; 1.
DR   PRINTS; PR00027; PAIREDBOX.
DR   PROSITE; PS00034; PAIRED_BOX; 1.
KW   Paired box; Developmental protein; Nuclear protein; DNA-binding;
KW   Transcription regulation; Activator; Polymorphism.
FT   DOMAIN        4    128       PAIRED BOX.
FT   VARIANT      45     45       Q -> H (FOUND IN A PATIENT WITH NEURAL
FT                                TUBE DEFECTS, BUT NOT CLEARLY LINKED TO
FT                                THE DISEASE).
FT                                /FTId=VAR_003787.
FT   CONFLICT      1      1       M -> A (IN REF. 2).
SQ   SEQUENCE   361 AA;  37825 MW;  03B85D83A00D86E1 CRC64;
     MEQTYGEVNQ LGGVFVNGRP LPNAIRLRIV ELAQLGIRPC DISRQLRVSH GCVSKILARY
     NETGSILPGA IGGSKPRVTT PNVVKHIRDY KQGDPGIFAW EIRDRLLADG VCDKYNVPSV
     SSISRILRNK IGSLAQPGPY EASKQPPSQP TLPYNHIYQY PYPSPVSPTG AKMGSHPGVP
     GTAGHVSIPR SWPSAHSVSN ILGIRTFMEQ TGALAGSEGT AYSPKMEDWA GVNRTAFPAT
     PAVNGLEKPA LEADIKYTQS ASTLSAVGGF LPACAYPASN QHGVYSAPGG GYLAPGPPWP
     PAQGPPLAPP GAGVAVHGGE LAAAMTFKHR EGTDRKPPSS GSKAPDALSS LHGLPIPAST
     S
//
ID   PAX2_HUMAN     STANDARD;      PRT;   416 AA.
AC   Q02962; Q15837; Q15105; Q15110;
DT   01-JUL-1993 (Rel. 26, Created)
DT   01-NOV-1997 (Rel. 35, Last sequence update)
DT   30-MAY-2000 (Rel. 39, Last annotation update)
DE   PAIRED BOX PROTEIN PAX-2.
GN   PAX2.
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
RN   [1]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 96299768.
RA   Sanyanusin P., Norrish J.H., Ward T.A., Nebel A., McNoe L.A.,
RA   Eccles M.R.;
RT   "Genomic structure of the human PAX2 gene.";
RL   Genomics 35:258-261(1996).
RN   [2]
RP   SEQUENCE FROM N.A.
RC   TISSUE=KIDNEY;
RX   MEDLINE; 92338102.
RA   Eccles M.R., Wallis L.J., Fidler A.E., Spurr N.K.,
RA   Goodfellow P.J., Reeve A.E.;
RT   "Expression of the PAX2 gene in human fetal kidney and Wilms' tumor.";
RL   Cell Growth Differ. 3:279-289(1992).
RN   [3]
RP   SEQUENCE OF 1-136 FROM N.A.
RX   MEDLINE; 95072651.
RA   Stapleton P., Weith A., Urbanek P., Kozmik Z., Busslinger M.;
RT   "Chromosomal localization of seven PAX genes and cloning of a novel
RT   family member, PAX-9.";
RL   Nat. Genet. 3:292-298(1993).
RN   [4]
RP   SEQUENCE FROM N.A. (ALTERNATIVE SPLICING).
RC   TISSUE=KIDNEY CORTEX;
RA   Ward T.A., Nebel A., Eccles M.R.;
RL   Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   VARIANTS RCS 75-GLU-THR INS AND SER-76.
RX   MEDLINE; 98430997.
RA   Devriendt K., Matthijs G., van Damme B., van Caesbroeck D., Eccles M.,
RA   Vanrenterghem Y., Fryns J.P., Leys A.;
RT   "Missense mutation and hexanucleotide duplication in the PAX2 gene in
RT   two unrelated families with renal-coloboma syndrome (MIM 120330).";
RL   Hum. Genet. 103:149-153(1998).
CC   -!- FUNCTION: PROBABLE TRANSCRIPTION FACTOR THAT MAY HAVE A ROLE IN
CC       KIDNEY CELL DIFFERENTIATION. HAS A CRITICAL ROLE IN THE
CC       DEVELOPMENT OF THE UROGENITAL TRACT, THE EYES, AND THE CNS.
CC   -!- SUBCELLULAR LOCATION: NUCLEAR.
CC   -!- ALTERNATIVE PRODUCTS: ALTERNATIVE PRODUCTS ARE PRODUCED BY
CC       ALTERNATIVE SPLICING.
CC   -!- TISSUE SPECIFICITY: EXPRESSED IN PRIMITIVE CELLS OF THE KIDNEY,
CC       URETER, EYE, EAR AND CENTRAL NERVOUS SYSTEM.
CC   -!- DEVELOPMENTAL STAGE: MAINLY IN FETAL KIDNEY AND JUVENILE
CC       NEPHROGENIC RESTS.
CC   -!- DISEASE: DEFECTS IN PAX2 IS THE CAUSE OF AUTOSOMAL DOMINANT RENAL-
CC       COLOBOMA SYNDROME (RCS). RCS IS THE ASSOCIATION OF A UROLOGICAL
CC       MALFORMATION WITH DYSPLASIA OF THE RETINA AND OPTIC DISK.
CC   -!- SIMILARITY: CONTAINS A PAIRED BOX DOMAIN.
CC   --------------------------------------------------------------------------
CC   This SWISS-PROT entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use  by  non-profit  institutions as long  as its content  is  in  no  way
CC   modified and this statement is not removed.  Usage  by  and for commercial
CC   entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC   or send an email to license@isb-sib.ch).
CC   --------------------------------------------------------------------------
DR   EMBL; U45255; AAC63385.1; -.
DR   EMBL; U45245; AAC63385.1; JOINED.
DR   EMBL; U45246; AAC63385.1; JOINED.
DR   EMBL; U45247; AAC63385.1; JOINED.
DR   EMBL; U45248; AAC63385.1; JOINED.
DR   EMBL; U45249; AAC63385.1; JOINED.
DR   EMBL; U45250; AAC63385.1; JOINED.
DR   EMBL; U45251; AAC63385.1; JOINED.
DR   EMBL; U45253; AAC63385.1; JOINED.
DR   EMBL; U45254; AAC63385.1; JOINED.
DR   EMBL; M89470; AAA60024.1; -.
DR   EMBL; L09747; AAC41711.1; -.
DR   EMBL; L09748; AAC41711.1; JOINED.
DR   EMBL; L09746; AAC41711.1; JOINED.
DR   EMBL; L25597; AAA36417.1; -.
DR   PIR; A49008; A49008.
DR   HSSP; P06601; 1PDN.
DR   TRANSFAC; T01823; -.
DR   MIM; 167409; -.
DR   MIM; 120330; -.
DR   INTERPRO; IPR001523; -.
DR   PFAM; PF00292; PAX; 1.
DR   PRINTS; PR00027; PAIREDBOX.
DR   PROSITE; PS00034; PAIRED_BOX; 1.
KW   Paired box; Developmental protein; Nuclear protein; DNA-binding;
KW   Transcription regulation; Differentiation; Alternative splicing;
KW   Disease mutation.
FT   DOMAIN       16    140       PAIRED BOX.
FT   VARSPLIC    206    228       MISSING (IN ISOFORM 3).
FT   VARSPLIC    364    416       GSEFSGNPYSHPQYTAYNEAWRFSNPALLSSPYYYSAAPRS
FT                                APAARAAAYDRH -> EAAVGPSSSLMSKPGRKLAEVPPCV
FT                                QPTGASSPATRTATPSTRPTTRLGDSATPPY (IN FETAL
FT                                KIDNEY ISOFORM).
FT   VARIANT      75     75       T -> TET (IN RCS).
FT                                /FTId=VAR_003788.
FT   VARIANT      76     76       G -> S (IN RCS).
FT                                /FTId=VAR_003789.
FT   CONFLICT     15     16       PG -> R (IN REF. 3).
SQ   SEQUENCE   416 AA;  44734 MW;  88A42F5D8307F80E CRC64;
     MDMHCKADPF SAMHPGHGGV NQLGGVFVNG RPLPDVVRQR IVELAHQGVR PCDISRQLRV
     SHGCVSKILG RYYETGSIKP GVIGGSKPKV ATPKVVDKIA EYKRQNPTMF AWEIRDRLLA
     EGICDNDTVP SVSSINRIIR TKVQQPFHPT PDGAGTGVTA PGHTIVPSTA SPPVSSASND
     PVGSYSINGI LGIPRSNGEK RKRDEVEVYT DPAHIRGGGG LHLVWTLRDV SEGSVPNGDS
     QSGVDSLRKH LRADTFTQQQ LEALDRVFER PSYPDVFQAS EHIKSEQGNE YSLPALTPGL
     DEVKSSLSAS TNPELGSNVS GTQTYPVVTG RDMASTTLPG YPPHVPPTGQ GSYPTSTLAG
     MVPGSEFSGN PYSHPQYTAY NEAWRFSNPA LLSSPYYYSA APRSAPAARA AAYDRH
//
ID   PAX3_HUMAN     STANDARD;      PRT;   479 AA.
AC   P23760; Q16448;
DT   01-NOV-1991 (Rel. 20, Created)
DT   01-NOV-1995 (Rel. 32, Last sequence update)
DT   30-MAY-2000 (Rel. 39, Last annotation update)
DE   PAIRED BOX PROTEIN PAX-3 (HUP2).
GN   PAX3 OR HUP2.
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
RN   [1]
RP   SEQUENCE OF 1-29 AND 197-479 FROM N.A.
RA   Riethman H.C., Macina R.A.;
RL   Submitted (JUL-1994) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   SEQUENCE OF 30-195 FROM N.A.
RX   MEDLINE; 89305521.
RA   Burri M., Tromvoukis Y., Bopp D., Frigerio G., Noll M.;
RT   "Conservation of the paired domain in metazoans and its structure in
RT   three isolated human genes.";
RL   EMBO J. 8:1183-1190(1989).
RN   [3]
RP   SEQUENCE OF 196-392 FROM N.A., AND VARIANTS WS1 LEU-45 AND ASP-99.
RX   MEDLINE; 95072569.
RA   Tassabehji M., Newton V.E., Leverton K., Turnbull K., Seemanova E.,
RA   Kunze J., Sperling K., Strachan T., Read A.P.;
RT   "PAX3 gene structure and mutations: close analogies between
RT   Waardenburg syndrome and the Splotch mouse.";
RL   Hum. Mol. Genet. 3:1069-1074(1994).
RN   [4]
RP   SEQUENCE FROM N.A. (PAX3A AND PAX3B).
RX   MEDLINE; 94171226.
RA   Tsukamoto K., Nakamura Y., Niikawa N.;
RT   "Isolation of two isoforms of the PAX3 gene transcripts and their
RT   tissue-specific alternative expression in human adult tissues.";
RL   Hum. Genet. 93:270-274(1994).
RN   [5]
RP   SEQUENCE OF 56-74 FROM N.A., AND VARIANT WS1 ALA-63--ILE-67 DEL.
RX   MEDLINE; 92168113.
RA   Tassabehji M., Read A.P., Newton V.E., Harris R., Balling R.,
RA   Gruss P., Strachan T.;
RT   "Waardenburg's syndrome patients have mutations in the human
RT   homologue of the Pax-3 paired box gene.";
RL   Nature 355:635-636(1992).
RN   [6]
RP   SEQUENCE OF 265-319 FROM N.A.
RA   Lalwani A.K., Ploplis B., Fex J., Grundfast K.M., San Agustin T.,
RA   Wilcox E.R.;
RL   Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   VARIANT WS1 LEU-50.
RX   MEDLINE; 92168114.
RA   Baldwin C.T., Hoth C.F., Amos J.A., Da-Silva E.O., Milunsky A.;
RT   "An exonic mutation in the HuP2 paired domain gene causes
RT   Waardenburg's syndrome.";
RL   Nature 355:637-638(1992).
RN   [8]
RP   VARIANT WS2 ALA-81.
RX   MEDLINE; 93258399.
RA   Tassabehji M., Read A.P., Newton V.E., Patton M., Gruss P., Harris R.,
RA   Strachan T.;
RT   "Mutations in the PAX3 gene causing Waardenburg syndrome type 1 and
RT   type 2.";
RL   Nat. Genet. 3:26-30(1993).
RN   [9]
RP   VARIANTS WS3 HIS-47 AND WS1 LEU-56.
RX   MEDLINE; 93190976.
RA   Hoth C.F., Milunsky A., Lipsky N., Sheffer R., Clarren S.K.,
RA   Baldwin C.T.;
RT   "Mutations in the paired domain of the human PAX3 gene cause Klein-
RT   Waardenburg syndrome (WS-III) as well as Waardenburg syndrome type I
RT   (WS-I).";
RL   Am. J. Hum. Genet. 52:455-462(1993).
RN   [10]
RP   VARIANT WS1 VAL-62.
RX   MEDLINE; 95135456.
RA   Pierpont J.W., Doolan L.D., Amann K., Snead G.R., Erickson R.P.;
RT   "A single base pair substitution within the paired box of PAX3 in an
RT   individual with Waardenburg syndrome type 1 (WS1).";
RL   Hum. Mutat. 4:227-228(1994).
RN   [11]
RP   VARIANTS WS1 PHE-265 AND GLY-271.
RX   MEDLINE; 95126143.
RA   Lalwani A.K., Brister J.R., Fex J., Grundfast K.M., Ploplis B.,
RA   San Agustin T.B., Wilcox E.R.;
RT   "Further elucidation of the genomic structure of PAX3, and
RT   identification of two different point mutations within the PAX3
RT   homeobox that cause Waardenburg syndrome type 1 in two families.";
RL   Am. J. Hum. Genet. 56:75-83(1995).
RN   [12]
RP   VARIANT WS3 PHE-84.
RX   MEDLINE; 95243235.
RA   Zlotogora J., Lerer I., Bar-David S., Ergaz Z., Abeliovich D.;
RT   "Homozygosity for Waardenburg syndrome.";
RL   Am. J. Hum. Genet. 56:1173-1178(1995).
RN   [13]
RP   VARIANTS WS1 MET-60; GLU-85 AND SER-238.
RX   MEDLINE; 96042708.
RA   Baldwin C.T., Hoth C.F., Macina R.A., Milunsky A.;
RT   "Mutations in PAX3 that cause Waardenburg syndrome type I: ten new
RT   mutations and review of the literature.";
RL   Am. J. Med. Genet. 58:115-122(1995).
RN   [14]
RP   VARIANT CDHS LYS-47.
RX   MEDLINE; 96263735.
RA   Asher J.H. Jr., Sommer A., Morell R., Friedman T.B.;
RT   "Missense mutation in the paired domain of PAX3 causes craniofacial-
RT   deafness-hand syndrome.";
RL   Hum. Mutat. 7:30-35(1996).
RN   [15]
RP   VARIANT LYS-315.
RX   MEDLINE; 97016531.
RA   Hol F.A., Geurds M.P.A., Chatkupt S., Shugart Y.Y., Balling R.,
RA   Schrander-Stumpel C.T.R.M., Johnson W.G., Hamel B.C.J.,
RA   Mariman E.C.M.;
RT   "PAX genes and human neural tube defects: an amino acid substitution
RT   in PAX1 in a patient with spina bifida.";
RL   J. Med. Genet. 33:655-660(1996).
RN   [16]
RP   VARIANT WS1 PHE-59.
RX   MEDLINE; 97220597.
RA   Soejima H., Fujimoto M., Tsukamoto K., Matsumoto N., Yoshiura K.-I.,
RA   Fukushima Y., Jinno Y., Niikawa N.;
RT   "Three novel PAX3 mutations observed in patients with Waardenburg
RT   syndrome type 1.";
RL   Hum. Mutat. 9:177-180(1997).
RN   [17]
RP   VARIANT WS1 VAL-62.
RX   MEDLINE; 98112449.
RA   Hol F.A., Geurds M.P.A., Cremers C.W.R.J., Hamel B.C.J.,
RA   Mariman E.C.M.;
RT   "Identification of two PAX3 mutations causing Waardenburg syndrome,
RT   one within the paired domain (M62V) and the other downstream of the
RT   homeodomain (Q282X).";
RL   Hum. Mutat. Suppl. 1:S145-S147(1998).
RN   [18]
RP   VARIANT WS1 ASN-59.
RA   Markova T.G., Shevtsov S.P., Moskolenko L.N., Lantsov A.A.,
RA   Schwartz E.I.;
RT   "A novel missense mutation Ile59Asn in the PAX3 gene in a family with
RT   Waardenburg syndrome type I.";
RL   Hum. Mutat. 13:85-85(1999).
CC   -!- FUNCTION: PROBABLE TRANSCRIPTION FACTOR ASSOCIATED WITH
CC       DEVELOPMENT OF ALVEOLAR RHABDOMYOSARCOMA.
CC   -!- SUBUNIT: CAN BIND AS A HETERODIMER WITH PAX7.
CC   -!- SUBCELLULAR LOCATION: NUCLEAR.
CC   -!- ALTERNATIVE PRODUCTS: IN ADDITION TO THE NORMAL PAX3 PROTEIN, THE
CC       GENE CAN PRODUCES, BY ALTERNATIVE SPLICING, TWO TRUNCATED FORMS
CC       WHICH ARE CALLED PAX3A AND PAX3B.
CC   -!- DISEASE: DEFECT IN PAX3 ARE THE CAUSE OF WAARDENBURG'S SYNDROME
CC       (WS), AN AUTOSOMAL DOMINANT DISORDER, CHARACTERIZED WITH NON
CC       PROGRESSIVE SENSORY-NEURAL DEAFNESS, AS WELL AS PIGMENTARY CHANGES
CC       OF THE IRISES AND OF THE HAIR AND SKIN; EACH OF THESE FEATURES
CC       MAY BE UNI- OR BILATERAL. ON THE BASIS OF THE PRESENCE OR ABSENCE
CC       OF DYSTOPIA CANTHORUM (LATERAL DISPLACEMENT OF THE INNER CORNER OF
CC       THE EYE), TYPE I (WS1) AND TYPE II (WS2: DOES NOT MAP TO PAX3) ARE
CC       DISTINGUISHED. TYPE III (WS3 OR KLEIN-WAARDENBURG SYNDROME) IS
CC       CHARACTERIZED WITH WS1 AND UPPER-LIMB INVOLVEMENT INCLUDING MUSCLE
CC       HYPOPLASIA WITH JOINT CONTRACTURES.
CC   -!- DISEASE: CRANIOFACIAL-DEAFNESS-HAND SYNDROME (CDHS), IS THOUGHT
CC       TO BE AN AUTOSOMAL DOMINANT DISEASE WHICH COMPRISES ABSENCE OR
CC       HYPOPLASIA OF THE NASAL BONES, HYPOPLASTIC MAXILLA, SMALL AND
CC       SHORT NOSE WITH THIN NARES, LIMITED MOVEMENT OF THE WRIST, SHORT
CC       PALPEBRAL FISSURES, ULNAR DEVIATION OF THE FINGERS, HYPERTELORISM
CC       AND PROFOUND SENSORY-NEURAL DEAFNESS.
CC   -!- DISEASE: RHABDOMYOSARCOMA-2 (RMS2) IS CHARACTERIZED BY A
CC       CHROMOSOMAL TRANSLOCATION T(2;13)(Q35;Q14) WHICH INVOLVES PAX3 AND
CC       FOXO1A. THE RESULTING PROTEIN IS A TRANSCRIPTIONAL ACTIVATOR.
CC   -!- SIMILARITY: BELONGS TO THE PAIRED FAMILY OF HOMEOBOX PROTEINS.
CC   -!- SIMILARITY: CONTAINS A PAIRED BOX DOMAIN.
CC   --------------------------------------------------------------------------
CC   This SWISS-PROT entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use  by  non-profit  institutions as long  as its content  is  in  no  way
CC   modified and this statement is not removed.  Usage  by  and for commercial
CC   entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC   or send an email to license@isb-sib.ch).
CC   --------------------------------------------------------------------------
DR   EMBL; U12263; AAA80573.1; -.
DR   EMBL; U12259; AAA80574.1; -.
DR   EMBL; U12258; AAA80574.1; JOINED.
DR   EMBL; U12260; AAA80574.1; JOINED.
DR   EMBL; U12262; AAA80574.1; JOINED.
DR   EMBL; X15043; CAA33145.1; -.
DR   EMBL; X15252; CAA33145.1; JOINED.
DR   EMBL; X15253; CAA33145.1; JOINED.
DR   EMBL; Z29972; -; NOT_ANNOTATED_CDS.
DR   EMBL; Z29973; -; NOT_ANNOTATED_CDS.
DR   EMBL; Z29974; -; NOT_ANNOTATED_CDS.
DR   EMBL; S69369; AAB30167.1; -.
DR   EMBL; S69370; AAB30168.1; -.
DR   EMBL; S83614; AAB21476.1; -.
DR   EMBL; L10614; AAA91849.1; -.
DR   PIR; S06960; S06960.
DR   HSSP; P06601; 1FJL.
DR   TRANSFAC; T00679; -.
DR   MIM; 193500; -.
DR   MIM; 148820; -.
DR   MIM; 268220; -.
DR   MIM; 122880; -.
DR   INTERPRO; IPR001356; -.
DR   INTERPRO; IPR001523; -.
DR   PFAM; PF00292; PAX; 1.
DR   PFAM; PF00046; homeobox; 1.
DR   PRINTS; PR00027; PAIREDBOX.
DR   PROSITE; PS00027; HOMEOBOX_1; 1.
DR   PROSITE; PS50071; HOMEOBOX_2; 1.
DR   PROSITE; PS00034; PAIRED_BOX; 1.
KW   Transcription regulation; Paired box; Developmental protein;
KW   Nuclear protein; Disease mutation; Chromosomal translocation;
KW   Proto-oncogene; Alternative splicing; Polymorphism.
FT   DOMAIN       34    159       PAIRED BOX.
FT   DNA_BIND    219    278       HOMEOBOX.
FT   VARSPLIC    196    215       ASAPQSDEGSDIDSEPDLPL -> GKRWRLGRRTCWVTWRA
FT                                SAS (IN ISOFORM PAX3A).
FT   VARSPLIC    216    479       MISSING (IN ISOFORM PAX3A).
FT   VARSPLIC    196    206       ASAPQSDEGSD -> GKALVSGVSSH (IN ISOFORM
FT                                PAX3B).
FT   VARSPLIC    207    479       MISSING (IN ISOFORM PAX3B).
FT   VARIANT      45     45       F -> L (IN WS1).
FT                                /FTId=VAR_003790.
FT   VARIANT      47     47       N -> H (IN WS3).
FT                                /FTId=VAR_003791.
FT   VARIANT      47     47       N -> K (IN CDHS).
FT                                /FTId=VAR_003792.
FT   VARIANT      50     50       P -> L (IN WS1; IMPORTANT HEARING LOSS).
FT                                /FTId=VAR_003793.
FT   VARIANT      56     56       R -> L (IN WS1; ASSOCIATED WITH
FT                                MENINGOMYELOCELE).
FT                                /FTId=VAR_003794.
FT   VARIANT      59     59       I -> F (IN WS1).
FT                                /FTId=VAR_003795.
FT   VARIANT      59     59       I -> N (IN WS1).
FT                                /FTId=VAR_003796.
FT   VARIANT      60     60       V -> M (IN WS1).
FT                                /FTId=VAR_003797.
FT   VARIANT      62     62       M -> V (IN WS1).
FT                                /FTId=VAR_003798.
FT   VARIANT      63     67       MISSING (IN WS1).
FT                                /FTId=VAR_003799.
FT   VARIANT      81     81       G -> A (IN WS2).
FT                                /FTId=VAR_003800.
FT   VARIANT      84     84       S -> F (IN WS3).
FT                                /FTId=VAR_003801.
FT   VARIANT      85     85       K -> E (IN WS1).
FT                                /FTId=VAR_003802.
FT   VARIANT      99     99       G -> D (IN WS1).
FT                                /FTId=VAR_003803.
FT   VARIANT     238    238       F -> S (IN WS1).
FT                                /FTId=VAR_003804.
FT   VARIANT     265    265       V -> F (IN WS1).
FT                                /FTId=VAR_003805.
FT   VARIANT     271    271       R -> G (IN WS1).
FT                                /FTId=VAR_003806.
FT   VARIANT     315    315       T -> K.
FT                                /FTId=VAR_003807.
SQ   SEQUENCE   479 AA;  52967 MW;  8AFCA674E3ACB4FE CRC64;
     MTTLAGAVPR MMRPGPGQNY PRSGFPLEVS TPLGQGRVNQ LGGVFINGRP LPNHIRHKIV
     EMAHHGIRPC VISRQLRVSH GCVSKILCRY QETGSIRPGA IGGSKPKQVT TPDVEKKIEE
     YKRENPGMFS WEIRDKLLKD AVCDRNTVPS VSSISRILRS KFGKGEEEEA DLERKEAEES
     EKKAKHSIDG ILSERASAPQ SDEGSDIDSE PDLPLKRKQR RSRTTFTAEQ LEELERAFER
     THYPDIYTRE ELAQRAKLTE ARVQVWFSNR RARWRKQAGA NQLMAFNHLI PGGFPPTAMP
     TLPTYQLSET SYQPTSIPQA VSDPSSTVHR PQPLPPSTVH QSTIPSNPDS SSAYCLPSTR
     HGFSSYTDSF VPPSGPSNPM NPTIGNGLSP QVMGLLTNHG GVPHQPQTDY ALSPLTGGLE
     PTTTVSASCS QRLDHMKSLD SLPTSQSYCP PTYSTTGYSM DPVTGYQYGQ YGQSKPWTF
//
ID   PAX4_HUMAN     STANDARD;      PRT;   350 AA.
AC   O43316;
DT   15-DEC-1998 (Rel. 37, Created)
DT   15-DEC-1998 (Rel. 37, Last sequence update)
DT   30-MAY-2000 (Rel. 39, Last annotation update)
DE   PAIRED BOX PROTEIN PAX-4.
GN   PAX4.
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
RN   [1]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 98102804.
RA   Matsushita T., Yamaoka T., Otsuka S., Moritani M., Matsumoto T.,
RA   Itakura M.;
RT   "Molecular cloning of mouse paired-box-containing gene (Pax)-4 from
RT   an islet beta cell line and deduced sequence of human Pax-4.";
RL   Biochem. Biophys. Res. Commun. 242:176-180(1998).
CC   -!- FUNCTION: KEY REGULATOR OF PANCREATIC CELL DIFFERENTIATION AND
CC       DEVELOPMENT.
CC   -!- SUBCELLULAR LOCATION: NUCLEAR (BY SIMILARITY).
CC   -!- SIMILARITY: BELONGS TO THE PAIRED FAMILY OF HOMEOBOX PROTEINS.
CC   -!- SIMILARITY: CONTAINS A PAIRED BOX DOMAIN.
CC   --------------------------------------------------------------------------
CC   This SWISS-PROT entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use  by  non-profit  institutions as long  as its content  is  in  no  way
CC   modified and this statement is not removed.  Usage  by  and for commercial
CC   entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC   or send an email to license@isb-sib.ch).
CC   --------------------------------------------------------------------------
DR   EMBL; AB008913; BAA24506.1; -.
DR   MIM; 167413; -.
DR   INTERPRO; IPR001356; -.
DR   INTERPRO; IPR001523; -.
DR   PFAM; PF00292; PAX; 1.
DR   PFAM; PF00046; homeobox; 1.
DR   PRINTS; PR00027; PAIREDBOX.
DR   PROSITE; PS00027; HOMEOBOX_1; 1.
DR   PROSITE; PS50071; HOMEOBOX_2; 1.
DR   PROSITE; PS00034; PAIRED_BOX; 1.
KW   Paired box; Developmental protein; Nuclear protein; DNA-binding;
KW   Transcription regulation.
FT   DOMAIN        5    129       PAIRED BOX.
FT   DNA_BIND    170    229       HOMEOBOX.
SQ   SEQUENCE   350 AA;  37832 MW;  2C2343AF16AEAAAC CRC64;
     MHQDGISSMN QLGGLFVNGR PLPLDTRQQI VRLAVSGMRP CDISRILKVS NGCVSKILGR
     YYRTGVLEPK GIGGSKPRLA TPPVVARIAQ LKGECPALFA WEIQRQLCAE GLCTQDKTPS
     VSSINRVLRA LQEDQGLPCT RLRSPAVLAP AVLTPHSGSE TPRGTHPGTG HRNRTIFSPS
     QAEALEKEFQ RGQYPDSVAR GKLATATSLP EDTVRVWFSN RRAKWRRQEK LKWEMQLPGA
     SQGLTVPRVA PGIISAQQSP GSVPTAALPA LEPLGPSCYQ LCWATAPERC LSDTPPKACL
     KPCWDCGSFL LPVIAPSCVD VAWPCLDASL AHHLIGGAGK ATPTHFSHWP
//
ID   PAX5_HUMAN     STANDARD;      PRT;   391 AA.
AC   Q02548; O75933;
DT   01-OCT-1993 (Rel. 27, Created)
DT   01-OCT-1993 (Rel. 27, Last sequence update)
DT   30-MAY-2000 (Rel. 39, Last annotation update)
DE   PAIRED BOX PROTEIN PAX-5 (B-CELL SPECIFIC TRANSCRIPTION FACTOR)
DE   (BSAP).
GN   PAX5.
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
RN   [1]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 92387536.
RA   Adams B., Doerfler P., Aguzzi A., Kozmik Z., Urbanek P.,
RA   Maurer-Fogy I., Busslinger M.;
RT   "Pax-5 encodes the transcription factor BSAP and is expressed in B
RT   lymphocytes, the developing CNS, and adult testis.";
RL   Genes Dev. 6:1589-1607(1992).
RN   [2]
RP   SEQUENCE OF 62-197 FROM N.A.
RX   MEDLINE; 98416211.
RA   Verkoczy L.K., Berinstein N.L.;
RT   "Isolation of genes negatively or positively co-expressed with human
RT   recombination activating gene 1 (RAG1) by differential display PCR
RT   (DD RT-PCR).";
RL   Nucleic Acids Res. 26:4497-4507(1998).
CC   -!- FUNCTION: MAY PLAY AN IMPORTANT ROLE IN B-CELL DIFFERENTIATION AS
CC       WELL AS NEURAL DEVELOPMENT AND SPERMATOGENESIS. INVOLVED IN THE
CC       REGULATION OF THE CD19 GENE, A B-LYMPHOID-SPECIFIC TARGET GENE.
CC   -!- SUBUNIT: BINDS DNA AS A MONOMER.
CC   -!- SUBCELLULAR LOCATION: NUCLEAR.
CC   -!- DEVELOPMENTAL STAGE: EXPRESSED AT EARLY B-CELL DIFFERENTIATION,
CC       IN THE DEVELOPING CNS AND IN ADULT TESTIS.
CC   -!- PTM: O-GLYCOSYLATED (PROBABLE).
CC   -!- SIMILARITY: CONTAINS A PAIRED BOX DOMAIN.
CC   --------------------------------------------------------------------------
CC   This SWISS-PROT entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use  by  non-profit  institutions as long  as its content  is  in  no  way
CC   modified and this statement is not removed.  Usage  by  and for commercial
CC   entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC   or send an email to license@isb-sib.ch).
CC   --------------------------------------------------------------------------
DR   EMBL; M96944; AAA58397.1; -.
DR   EMBL; AF080573; AAC35286.1; -.
DR   PIR; A44063; A44063.
DR   HSSP; P06601; 1PDN.
DR   TRANSFAC; T00070; -.
DR   MIM; 167414; -.
DR   INTERPRO; IPR001523; -.
DR   PFAM; PF00292; PAX; 1.
DR   PRINTS; PR00027; PAIREDBOX.
DR   PROSITE; PS00034; PAIRED_BOX; 1.
KW   Paired box; Developmental protein; Nuclear protein; DNA-binding;
KW   Transcription regulation; Differentiation; Spermatogenesis;
KW   Neurogenesis; Glycoprotein.
FT   DOMAIN       16    140       PAIRED BOX.
FT   CONFLICT     99     99       I -> F (IN REF. 2).
FT   CONFLICT    141    143       TKV -> PKL (IN REF. 2).
SQ   SEQUENCE   391 AA;  42149 MW;  DB37E6EACD9F993A CRC64;
     MDLEKNYPTP RTSRTGHGGV NQLGGVFVNG RPLPDVVRQR IVELAHQGVR PCDISRQLRV
     SHGCVSKILG RYYETGSIKP GVIGGSKPKV ATPKVVEKIA EYKRQNPTMF AWEIRDRLLA
     ERVCDNDTVP SVSSINRIIR TKVQQPPNQP VPASSHSIVS TGSVTQVSSV STDSAGSSYS
     ISGILGITSP SADTNKRKRD EGIQESPVPN GHSLPGRDFL RKQMRGDLFT QQQLEVLDRV
     FERQHYSDIF TTTEPIKPEQ TTEYSAMASL AGGLDDMKAN LASPTPADIG SSVPGPQSYP
     IVTGRDLAST TLPGYPPHVP PAGQGSYSAP TLTGMVPGSE FSGSPYSHPQ YSSYNDSWRF
     PNPGLLGSPY YYSAAARGAA PPAAATAYDR H
//
ID   PAX6_HUMAN     STANDARD;      PRT;   422 AA.
AC   P26367; Q99413;
DT   01-AUG-1992 (Rel. 23, Created)
DT   15-JUL-1999 (Rel. 38, Last sequence update)
DT   15-JUL-1999 (Rel. 38, Last annotation update)
DE   PAIRED BOX PROTEIN PAX-6 (OCULORHOMBIN) (ANIRIDIA, TYPE II PROTEIN).
GN   PAX6 OR AN2.
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
RN   [1]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 92103673.
RA   Ton C.C.T., Hirvonen H., Miwa H., Weil M.M., Monaghan P., Jordan T.,
RA   van Heyningen V., Hastie N.D., Meijers-Heijboer H., Drechsler M.,
RA   Royer-Pokora B., Collins F., Swaroop A., Strong L.C., Saunders G.F.;
RT   "Positional cloning and characterization of a paired box- and
RT   homeobox-containing gene from the aniridia region.";
RL   Cell 67:1059-1074(1991).
RN   [2]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 94258210.
RA   Glaser T., Walton D.S., Maas R.L.;
RT   "Genomic structure, evolutionary conservation and aniridia mutations
RT   in the human PAX6 gene.";
RL   Nat. Genet. 2:232-239(1992).
RN   [3]
RP   SEQUENCE OF 5-422 FROM N.A.
RA   Wilkinson J.;
RL   Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   REVIEW ON VARIANTS.
RX   MEDLINE; 98141676.
RA   Prosser J., van Heyningen V.;
RT   "PAX6 mutations reviewed.";
RL   Hum. Mutat. 11:93-108(1998).
RN   [5]
RP   VARIANT AN TRP-208.
RX   MEDLINE; 93372853.
RA   Hanson I.M., Seawright A., Hardman K., Hodgson S., Zaletayev D.,
RA   Fekete G., van Heyningen V.;
RT   "PAX6 mutations in aniridia.";
RL   Hum. Mol. Genet. 2:915-920(1993).
RN   [6]
RP   VARIANT GLY-26.
RX   MEDLINE; 94214497.
RA   Hanson I.M., Fletcher J.M., Jordan T., Brown A., Taylor D.,
RA   Adams R.J., Punnet H.H., van Heyningen V.;
RT   "Mutations at the PAX6 locus are found in heterogeneous anterior
RT   segment malformations including Peters' anomaly.";
RL   Nat. Genet. 6:168-173(1994).
RN   [7]
RP   VARIANT CYS-128.
RX   MEDLINE; 96225435.
RA   Azuma N., Nishina S., Yanagisawa H., Okuyama T., Yamada M.;
RT   "PAX6 missense mutation in isolated foveal hypoplasia.";
RL   Nat. Genet. 13:141-142(1996).
RN   [8]
RP   VARIANTS GLY-26 AND AN ARG-87.
RX   MEDLINE; 97227282.
RA   Tang H.K., Chao L.-Y., Saunders G.F.;
RT   "Functional analysis of paired box missense mutations in the PAX6
RT   gene.";
RL   Hum. Mol. Genet. 6:381-386(1997).
RN   [9]
RP   VARIANT AN PRO-22--ARG-26 DEL.
RX   MEDLINE; 97428347.
RA   Axton R.A., Hanson I.M., Love J., Seawright A., Prosser J.,
RA   van Heyningen V.;
RT   "Combined SSCP/heteroduplex analysis in the screening for PAX6
RT   mutations.";
RL   Mol. Cell. Probes 11:287-292(1997).
RN   [10]
RP   VARIANT AN TRP-18.
RX   MEDLINE; 99006892.
RA   Wolf M.T.F., Lorenz B., Winterpacht A., Drechsler M., Schumacher V.,
RA   Royer-Pokora B., Blankenagel A., Zabel B., Wildhardt G.;
RT   "Ten novel mutations found in Aniridia.";
RL   Hum. Mutat. 12:304-313(1998).
RN   [11]
RP   VARIANT EYE MALFORMATIONS ARG-422.
RX   MEDLINE; 98199717.
RA   Azuma N., Yamada M.;
RT   "Missense mutation at the C terminus of the PAX6 gene in ocular
RT   anterior segment anomalies.";
RL   Invest. Ophthalmol. Vis. Sci. 39:828-830(1998).
RN   [12]
RP   VARIANTS AN SER-17; VAL-29; GLN-44 AND HIS-178.
RX   MEDLINE; 99072581.
RA   Azuma N., Hotta Y., Tanaka H., Yamada M.;
RT   "Missense mutations in the PAX6 gene in aniridia.";
RL   Invest. Ophthalmol. Vis. Sci. 39:2524-2528(1998).
RN   [13]
RP   VARIANT EYE MALFORMATIONS ASP-53.
RX   MEDLINE; 99375017.
RA   Azuma N., Yamaguchi Y., Handa H., Hayakawa M., Kanai A., Yamada M.;
RT   "Missense mutation in the alternative splice region of the PAX6 gene
RT   in eye anomalies.";
RL   Am. J. Hum. Genet. 65:656-663(1999).
RN   [14]
RP   VARIANTS AN SER-42; LEU-53; PRO-63; GLU-79 AND GLN-208.
RX   MEDLINE; 99250762.
RA   Groenskov K., Rosenberg T., Sand A., Broendum-Nielsen K.;
RT   "Mutational analysis of PAX6: 16 novel mutations including 5 missense
RT   mutations with a mild aniridia phenotype.";
RL   Eur. J. Hum. Genet. 7:274-286(1999).
RN   [15]
RP   VARIANTS AN P-33 AND P-43, VARIANT FH V-64, AND VARIANT EP D-126.
RX   MEDLINE; 99135896.
RA   Hanson I., Churchill A., Love J., Axton R., Moore T., Clarke M.,
RA   Meire F., van Heyningen V.;
RT   "Missense mutations in the most ancient residues of the PAX6 paired
RT   domain underlie a spectrum of human congenital eye malformations.";
RL   Hum. Mol. Genet. 8:165-172(1999).
RN   [16]
RP   VARIANTS AN SER-29; ARG-119; ALA-353.
RA   Wildhardt G.;
RL   Unpublished observations (APR-1999).
RN   [17]
RP   VARIANT AN ALA-37--PRO-39 DEL.
RA   Saunders G.F.;
RL   Unpublished observations (AUG-1999).
CC   -!- FUNCTION: MAY BE A TRANSCRIPTION FACTOR WITH IMPORTANT FUNCTIONS
CC       IN EYE AND NASAL DEVELOPMENT.
CC   -!- SUBCELLULAR LOCATION: NUCLEAR.
CC   -!- TISSUE SPECIFICITY: FETAL EYE, OLFACTORY BULBS, AND IN THE
CC       CEREBELLUM.
CC   -!- DEVELOPMENTAL STAGE: EXPRESSED IN THE DEVELOPING EYE AND BRAIN.
CC   -!- DISEASE: DEFECTS IN PAX6 ARE THE CAUSE OF ANIRIDIA (AN), TYPE II A
CC       BILATERAL PANOCULAR DISORDER CHARACTERIZED BY COMPLETE OR PARTIAL
CC       ABSENCE OF THE IRIS, ABSENCE OF THE FOVEA AND MALFORMATIONS OF THE
CC       LENS AND ANTERIOR CHAMBER. SEVERE AGE-RELATED CORNEAL DEGENERATION
CC       IS A FREQUENT COMPLICATION WHICH CONTRIBUTES TO A POOR VISUAL
CC       PROGNOSTIS IN AN. ABOUT ONE THIRD OF THE CASES ARE SPORADIC, AND
CC       TWO THIRDS ARE FAMILIAL, WITH AUTOSOMAL DOMINANT INHERITANCE, WITH
CC       HIGH PENETRANCE. NEARLY ONE THIRD OF SPORADIC AN PATIENTS DEVELOP
CC       WILMS TUMOR IN ASSOCIATION WITH GENITOURINARY ANOMALIES AND MENTAL
CC       RETARDATION (WAGR SYNDROME) AS A CONSEQUENCE OF HETEROZYGOUS
CC       (SUB)MICROSCOPIC DELETIONS OF CHROMOSOME 11P13.
CC   -!- DISEASE: DEFECTS IN PAX6 ARE THE CAUSE OF PETERS ANOMALY, A
CC       CONGENITAL DEFECT OF THE ANTERIOR CHAMBER OF THE EYE.
CC   -!- DISEASE: A MUTATION IN THE PAX6 HAS BEEN IDENTIFIED IN A CASE
CC       OF ECTOPIA PUPILLAE, A CONGENITAL EYE MALFORMATION IN WHICH THE
CC       PUPILS ARE DISPLACED FROM THEIR NORMAL CENTRAL POSITION.
CC   -!- DISEASE: DEFECTS IN PAX6 ARE RESPONSIBLE FOR OCULAR ANTERIOR
CC       SEGMENT ANOMALIES (AXENFELD ANOMALY).
CC   -!- SIMILARITY: BELONGS TO THE PAIRED FAMILY OF HOMEOBOX PROTEINS.
CC   -!- SIMILARITY: CONTAINS A PAIRED BOX DOMAIN.
CC   -!- DATABASE: NAME=PAX6 mutation db;
CC       WWW="http://www.hgu.mrc.ac.uk/Softdata/PAX6/".
CC   --------------------------------------------------------------------------
CC   This SWISS-PROT entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use  by  non-profit  institutions as long  as its content  is  in  no  way
CC   modified and this statement is not removed.  Usage  by  and for commercial
CC   entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC   or send an email to license@isb-sib.ch).
CC   --------------------------------------------------------------------------
DR   EMBL; M77844; AAA59963.1; -.
DR   EMBL; M77844; AAA59962.1; -.
DR   EMBL; M93650; AAA36416.1; -.
DR   EMBL; Z83307; CAB05885.1; -.
DR   PIR; A41644; A41644.
DR   HSSP; P06601; 1PDN.
DR   TRANSFAC; T01122; -.
DR   TRANSFAC; T01814; -.
DR   MIM; 106210; -.
DR   MIM; 109120; -.
DR   MIM; 129750; -.
DR   MIM; 136520; -.
DR   MIM; 148190; -.
DR   MIM; 261540; -.
DR   MIM; 604229; -.
DR   INTERPRO; IPR001356; -.
DR   INTERPRO; IPR001523; -.
DR   PFAM; PF00292; PAX; 1.
DR   PFAM; PF00046; homeobox; 1.
DR   PRINTS; PR00027; PAIREDBOX.
DR   PROSITE; PS00027; HOMEOBOX_1; 1.
DR   PROSITE; PS50071; HOMEOBOX_2; 1.
DR   PROSITE; PS00034; PAIRED_BOX; 1.
KW   Transcription regulation; Homeobox; DNA-binding; Nuclear protein;
KW   Developmental protein; Paired box; Disease mutation.
FT   DOMAIN        4    128       PAIRED BOX.
FT   DOMAIN      129    209       GLN/GLY-RICH.
FT   DNA_BIND    210    269       HOMEOBOX.
FT   DOMAIN      279    422       PRO/SER/THR-RICH.
FT   VARIANT      17     17       N -> S (IN AN).
FT                                /FTId=VAR_003808.
FT   VARIANT      18     18       G -> W (IN AN AND PETER'S ANOMALY).
FT                                /FTId=VAR_003809.
FT   VARIANT      22     26       MISSING (IN AN; SPORADIC FORM).
FT                                /FTId=VAR_008693.
FT   VARIANT      26     26       R -> G (IN PETER'S ANOMALY).
FT                                /FTId=VAR_003810.
FT   VARIANT      29     29       I -> S (IN AN; SPORADIC FORM).
FT                                /FTId=VAR_008694.
FT   VARIANT      29     29       I -> V (IN AN).
FT                                /FTId=VAR_003811.
FT   VARIANT      33     33       A -> P (IN AN; SPORADIC FORM).
FT                                /FTId=VAR_008695.
FT   VARIANT      37     39       MISSING (IN AN; SPORADIC FORM).
FT                                /FTId=VAR_008696.
FT   VARIANT      42     42       I -> S (IN AN; MILD).
FT                                /FTId=VAR_008697.
FT   VARIANT      43     43       S -> P (IN AN; SPORADIC FORM).
FT                                /FTId=VAR_008698.
FT   VARIANT      44     44       R -> Q (IN AN).
FT                                /FTId=VAR_003812.
FT   VARIANT      53     53       V -> L (IN AN; MILD).
FT                                /FTId=VAR_008699.
FT   VARIANT      53     53       V -> D (IN PETERS ANOMALY; CONGENITAL
FT                                CATARACT; AXENFELD ANOMALY AND FOVEAL
FT                                HYPOPLASIA; JAPANESE PEDIGREES).
FT                                /FTId=VAR_008700.
FT   VARIANT      63     63       T -> P (IN AN; MILD).
FT                                /FTId=VAR_008701.
FT   VARIANT      64     64       G -> V (IN FOVEAL HYPOPLASIA AND
FT                                PRESENILE CATARACT SYNDROME).
FT                                /FTId=VAR_008702.
FT   VARIANT      79     79       A -> E (IN AN; MILD).
FT                                /FTId=VAR_008703.
FT   VARIANT      87     87       I -> R (IN AN; LOSS OF ACTIVITY).
FT                                /FTId=VAR_003813.
FT   VARIANT     119    119       S -> R (IN AN; SPORADIC FORM).
FT                                /FTId=VAR_008704.
FT   VARIANT     126    126       V -> D (IN ECTOPIA PUPILLAE).
FT                                /FTId=VAR_008705.
FT   VARIANT     128    128       R -> C (IN ISOLATED FOVEAL HYPOPLASIA).
FT                                /FTId=VAR_003814.
FT   VARIANT     178    178       Q -> H (IN AN).
FT                                /FTId=VAR_003815.
FT   VARIANT     208    208       R -> W (IN AN).
FT                                /FTId=VAR_003816.
FT   VARIANT     208    208       R -> Q (IN AN; MILD).
FT                                /FTId=VAR_008706.
FT   VARIANT     353    353       S -> A (IN AN; FAMILIAL FORM).
FT                                /FTId=VAR_008707.
FT   VARIANT     422    422       Q -> R (IN OCULAR ANTERIOR SEGMENT
FT                                ANOMALIES).
FT                                /FTId=VAR_008708.
FT   CONFLICT    317    317       R -> L (IN REF. 1).
SQ   SEQUENCE   422 AA;  46683 MW;  C33CDD2C1B13C397 CRC64;
     MQNSHSGVNQ LGGVFVNGRP LPDSTRQKIV ELAHSGARPC DISRILQVSN GCVSKILGRY
     YETGSIRPRA IGGSKPRVAT PEVVSKIAQY KRECPSIFAW EIRDRLLSEG VCTNDNIPSV
     SSINRVLRNL ASEKQQMGAD GMYDKLRMLN GQTGSWGTRP GWYPGTSVPG QPTQDGCQQQ
     EGGGENTNSI SSNGEDSDEA QMRLQLKRKL QRNRTSFTQE QIEALEKEFE RTHYPDVFAR
     ERLAAKIDLP EARIQVWFSN RRAKWRREEK LRNQRRQASN TPSHIPISSS FSTSVYQPIP
     QPTTPVSSFT SGSMLGRTDT ALTNTYSALP PMPSFTMANN LPMQPPVPSQ TSSYSCMLPT
     SPSVNGRSYD TYTPPHMQTH MNSQPMGTSG TTSTGLISPG VSVPVQVPGS EPDMSQYWPR
     LQ
//
ID   PAX7_HUMAN     STANDARD;      PRT;   520 AA.
AC   P23759;
DT   01-NOV-1991 (Rel. 20, Created)
DT   30-MAY-2000 (Rel. 39, Last sequence update)
DT   30-MAY-2000 (Rel. 39, Last annotation update)
DE   PAIRED BOX PROTEIN PAX-7 (HUP1).
GN   PAX7 OR HUP1.
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
RN   [1]
RP   SEQUENCE FROM N.A., AND ALTERNATIVE SPLICING.
RX   MEDLINE; 97480728.
RA   Vorobyov E., Mertsalov I., Dockhorn-Dworniczak B., Dworniczak B.,
RA   Horst J.;
RT   "The genomic organization and full coding region of the human PAX7
RT   gene.";
RL   Genomics 45:168-174(1997).
RN   [2]
RP   SEQUENCE FROM N.A. (LONG FORM).
RA   Heath P.;
RL   Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   SEQUENCE OF 1-467 FROM N.A. (LONG FORM).
RX   MEDLINE; 95075634.
RA   Schaefer B.W., Czerny T., Bernasconi M., Genini M., Busslinger M.;
RT   "Molecular cloning and characterization of a human PAX-7 cDNA
RT   expressed in normal and neoplastic myocytes.";
RL   Nucleic Acids Res. 22:4574-4582(1994).
RN   [4]
RP   SEQUENCE OF 30-195 FROM N.A. (SHORT FORM).
RX   MEDLINE; 89305521.
RA   Burri M., Tromvoukis Y., Bopp D., Frigerio G., Noll M.;
RT   "Conservation of the paired domain in metazoans and its structure in
RT   three isolated human genes.";
RL   EMBO J. 8:1183-1190(1989).
CC   -!- FUNCTION: PROBABLE TRANSCRIPTION FACTOR. IT MAY HAVE A ROLE IN
CC       MYOGENESIS.
CC   -!- SUBUNIT: CAN BIND AS A HETERODIMER WITH PAX3.
CC   -!- SUBCELLULAR LOCATION: NUCLEAR.
CC   -!- ALTERNATIVE PRODUCTS: TWO ISOFORMS; A LONG FORM (SHOWN HERE), AND
CC       A SHORT FORM; ARE PRODUCED BY ALTERNATIVE SPLICING.
CC   -!- DISEASE: RHABDOMYOSARCOMA-2 (RMS2) IS CHARACTERIZED BY A
CC       CHROMOSOMAL TRANSLOCATION T(1;13)(P36;Q14) WHICH INVOLVES PAX7 AND
CC       FOXO1A. THE RESULTING PROTEIN IS A TRANSCRIPTIONAL ACTIVATOR.
CC   -!- SIMILARITY: BELONGS TO THE PAIRED FAMILY OF HOMEOBOX PROTEINS.
CC   -!- SIMILARITY: CONTAINS A PAIRED BOX DOMAIN.
CC   --------------------------------------------------------------------------
CC   This SWISS-PROT entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use  by  non-profit  institutions as long  as its content  is  in  no  way
CC   modified and this statement is not removed.  Usage  by  and for commercial
CC   entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC   or send an email to license@isb-sib.ch).
CC   --------------------------------------------------------------------------
DR   EMBL; X96743; CAA65520.1; -.
DR   EMBL; X96744; CAA65521.1; -.
DR   EMBL; X15042; CAA65521.1; JOINED.
DR   EMBL; X15250; CAA65521.1; JOINED.
DR   EMBL; X15251; CAA65521.1; JOINED.
DR   EMBL; X96745; CAA65521.1; JOINED.
DR   EMBL; X96746; CAA65521.1; JOINED.
DR   EMBL; X96747; CAA65521.1; JOINED.
DR   EMBL; X96748; CAA65521.1; JOINED.
DR   EMBL; X96744; CAA65522.1; -.
DR   EMBL; X15042; CAA65522.1; JOINED.
DR   EMBL; X15250; CAA65522.1; JOINED.
DR   EMBL; X15251; CAA65522.1; JOINED.
DR   EMBL; X96745; CAA65522.1; JOINED.
DR   EMBL; X96746; CAA65522.1; JOINED.
DR   EMBL; X96747; CAA65522.1; JOINED.
DR   EMBL; X96748; CAA65522.1; JOINED.
DR   EMBL; AL021528; CAA16432.1; -.
DR   EMBL; Z35141; CAA84513.1; -.
DR   PIR; S06959; S06959.
DR   HSSP; P06601; 1FJL.
DR   TRANSFAC; T00396; -.
DR   MIM; 167410; -.
DR   INTERPRO; IPR001356; -.
DR   INTERPRO; IPR001523; -.
DR   PFAM; PF00292; PAX; 1.
DR   PFAM; PF00046; homeobox; 1.
DR   PRINTS; PR00027; PAIREDBOX.
DR   PROSITE; PS00027; HOMEOBOX_1; 1.
DR   PROSITE; PS50071; HOMEOBOX_2; 1.
DR   PROSITE; PS00034; PAIRED_BOX; 1.
KW   Transcription regulation; Homeobox; DNA-binding; Nuclear protein;
KW   Developmental protein; Paired box; Chromosomal translocation;
KW   Proto-oncogene; Alternative splicing.
FT   DOMAIN       34    161       PAIRED BOX.
FT   DNA_BIND    217    276       HOMEOBOX.
FT   DOMAIN      340    346       POLY-ALA.
FT   VARSPLIC    151    152       MISSING (IN SHORT ISOFORM).
SQ   SEQUENCE   520 AA;  56896 MW;  3B0F8CC99D65699C CRC64;
     MAALPGTVPR MMRPAPGQNY PRTGFPLEVS TPLGQGRVNQ LGGVFINGRP LPNHIRHKIV
     EMAHHGIRPC VISRQLRVSH GCVSKILCRY QETGSIRPGA IGGSKPRQVA TPDVEKKIEE
     YKRENPGMFS WEIRDRLLKD GHCDRSTVPS GLVSSISRVL RIKFGKKEEE DEADKKEDDG
     EKKAKHSIDG ILGDKGNRLD EGSDVESEPD LPLKRKQRRS RTTFTAEQLE ELEKAFERTH
     YPDIYTREEL AQRTKLTEAR VQVWFSNRRA RWRKQAGANQ LAAFNHLLPG GFPPTGMPTL
     PPYQLPDSTY PTTTISQDGG STVHRPQPLP PSTMHQGGLA AAAAAADTSS AYGARHSFSS
     YSDSFMNPAA PSNHMNPVSN GLSPQVMSIL GNPSAVPPQP QADFSISPLH GGLDSATSIS
     ASCSQRADSI KPGDSLPTSQ AYCPPTYSTT GYSVDPVAGY QYGQYGQSEC LVPWASPVPI
     PSPTPRASCL FMESYKVVSG WGMSISQMEK LKSSQMEQFT
//
ID   PAX9_HUMAN     STANDARD;      PRT;   341 AA.
AC   P55771; Q99582; Q9UQR4;
DT   01-NOV-1997 (Rel. 35, Created)
DT   30-MAY-2000 (Rel. 39, Last sequence update)
DT   30-MAY-2000 (Rel. 39, Last annotation update)
DE   PAIRED BOX PROTEIN PAX-9.
GN   PAX9.
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
RN   [1]
RP   SEQUENCE FROM N.A.
RA   Egger C., Schorpp M., Boehm T.;
RT   "Evolutionary conservation of gene structure of the pax1/9 gene
RT   family.";
RL   Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   SEQUENCE OF 1-211 FROM N.A.
RX   MEDLINE; 95072651.
RA   Stapleton P., Weith A., Urbanek P., Kozmik Z., Busslinger M.;
RT   "Chromosomal localization of seven PAX genes and cloning of a novel
RT   family member, PAX-9.";
RL   Nat. Genet. 3:292-298(1993).
RN   [3]
RP   SEQUENCE OF 9-339 FROM N.A.
RC   TISSUE=OESOPHAGUS;
RX   MEDLINE; 97179475.
RA   Peters H., Schuster G., Neubueser A., Richter T., Hoefler H.;
RT   "Isolation of the Pax9 cDNA from adult human esophagus.";
RL   Mamm. Genome 8:62-64(1997).
CC   -!- FUNCTION: TRANSCRIPTION FACTOR ESSENTIAL FOR THE DEVELOPMENT OF A
CC       VARIETY OF ORGANS AND SKELETAL ELEMENTS (BY SIMILARITY).
CC   -!- SUBCELLULAR LOCATION: NUCLEAR.
CC   -!- SIMILARITY: BELONGS TO THE PAIRED FAMILY OF HOMEOBOX PROTEINS.
CC   -!- SIMILARITY: CONTAINS A PAIRED BOX DOMAIN.
CC   --------------------------------------------------------------------------
CC   This SWISS-PROT entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use  by  non-profit  institutions as long  as its content  is  in  no  way
CC   modified and this statement is not removed.  Usage  by  and for commercial
CC   entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC   or send an email to license@isb-sib.ch).
CC   --------------------------------------------------------------------------
DR   EMBL; AJ238381; CAB41533.1; -.
DR   EMBL; AJ238382; CAB41533.1; JOINED.
DR   EMBL; AJ238383; CAB41533.1; JOINED.
DR   EMBL; L09745; -; NOT_ANNOTATED_CDS.
DR   EMBL; X92850; CAA63436.1; -.
DR   HSSP; P06601; 1PDN.
DR   MIM; 167416; -.
DR   INTERPRO; IPR001523; -.
DR   PFAM; PF00292; PAX; 1.
DR   PRINTS; PR00027; PAIREDBOX.
DR   PROSITE; PS00034; PAIRED_BOX; 1.
KW   Transcription regulation; DNA-binding; Nuclear protein;
KW   Developmental protein; Paired box.
FT   DOMAIN        4    128       PAIRED BOX.
FT   CONFLICT    211    211       V -> G (IN REF. 2).
SQ   SEQUENCE   341 AA;  36310 MW;  F5E6B0BC991E7C1D CRC64;
     MEPAFGEVNQ LGGVFVNGRP LPNAIRLRIV ELAQLGIRPC DISRQLRVSH GCVSKILARY
     NETGSILPGA IGGSKPRVTT PTVVKHIRTY KQRDPGIFAW EIRDRLLADG VCDKYNVPSV
     SSISRILRNK IGNLAQQGHY DSYKQHQPTP QPALPYNHIY SYPSPITAAA AKVPTPPGVP
     AIPGSVAMPR TWPSSHSVTD ILGIRSITDQ VSDSSPYHSP KVEEWSSLGR NNFPAAAPHA
     VNGLEKGALE QEAKYGQAPN GLPAVGSFVS ASSMAPYPTP AQVSPYMTYS AAPSGYVAGH
     GWQHAGGTSL SPHNCDIPAS LAFKGMQAAR EGSHSVTASA L
//
ID   PAXI_HUMAN     STANDARD;      PRT;   557 AA.
AC   P49023;
DT   01-FEB-1996 (Rel. 33, Created)
DT   01-FEB-1996 (Rel. 33, Last sequence update)
DT   15-JUL-1998 (Rel. 36, Last annotation update)
DE   PAXILLIN.
GN   PXN.
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
RN   [1]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 95197488.
RA   Salgia R., Li J.-L., Lo S.H., Brunkhorst B., Kansas G.S.,
RA   Sobhany E.S., Sun Y., Pisick E., Hallek M., Ernst T., Tantravahi R.,
RA   Chen L.B., Griffin J.D.;
RT   "Molecular cloning of human paxillin, a focal adhesion protein
RT   phosphorylated by P210BCR/ABL.";
RL   J. Biol. Chem. 270:5039-5047(1995).
CC   -!- FUNCTION: CYTOSKELETAL PROTEIN INVOLVED IN ACTIN-MEMBRANE
CC       ATTACHMENT AT SITES OF CELL ADHESION TO THE EXTRACELLULAR MATRIX
CC       (FOCAL ADHESION). BINDS IN VITRO TO VINCULIN AS WELL AS TO THE SH3
CC       DOMAIN OF C-SRC AND, WHEN TYROSINE PHOSPHORYLATED, TO THE SH2
CC       DOMAIN OF V-CRK.
CC   -!- PTM: EXTENSIVE TYROSINE PHOSPHORYLATION OCCURS DURING INTEGRIN-
CC       MEDIATED CELL ADHESION, EMBRYONIC DEVELOPMENT, FIBROBLAST
CC       TRANSFORMATION AND FOLLOWING STIMULATION OF CELLS BY MITOGENS.
CC   -!- SIMILARITY: CONTAINS 4 LIM DOMAINS. THE LIM DOMAIN BINDS 2 ZINC
CC       IONS.
CC   --------------------------------------------------------------------------
CC   This SWISS-PROT entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use  by  non-profit  institutions as long  as its content  is  in  no  way
CC   modified and this statement is not removed.  Usage  by  and for commercial
CC   entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC   or send an email to license@isb-sib.ch).
CC   --------------------------------------------------------------------------
DR   EMBL; U14588; AAC50104.1; -.
DR   HSSP; P04006; 1IML.
DR   MIM; 602505; -.
DR   INTERPRO; IPR001781; -.
DR   INTERPRO; IPR001904; -.
DR   PFAM; PF00412; LIM; 4.
DR   PRINTS; PR00832; PAXILLIN.
DR   PROSITE; PS00478; LIM_DOMAIN_1; 4.
DR   PROSITE; PS50023; LIM_DOMAIN_2; 4.
KW   Cytoskeleton; Phosphorylation; LIM motif; Repeat; Metal-binding; Zinc.
FT   DOMAIN       46     53       PRO-RICH.
FT   MOD_RES     118    118       PHOSPHORYLATION (BY FAK) (BY SIMILARITY).
FT   DOMAIN      324    374       LIM.
FT   DOMAIN      383    433       LIM.
FT   DOMAIN      442    492       LIM.
FT   DOMAIN      501    551       LIM.
SQ   SEQUENCE   557 AA;  60936 MW;  B379BED63E8E63A5 CRC64;
     MDDLDALLAD LESTTSHISK RPVFLSEETP YSYPTGNHTY QEIAVPPPVP PPPSSEALNG
     TILDPLDQWQ PSGSRFIHQQ PQSSSPVYGS SAKTSSVSNP QDSVGSPCSR VGEEEHVYSF
     PNKQKSAEPS PTVMSTSLGS NLSELDRLLL ELNAVQHNPP GFPADEANSS PPLPGALSPL
     YGVPETNSPL GGKAGPLTKE KPKRNGGRGL EDVRPSVESL LDELESSVPS PVPAITVNQG
     EMSSPQRVTS TQQQTRISAS SATRELDELM ASLSDFKFMA QGKTGSSSPP GGPPKPGSQL
     DSMLGSLQSD LNKLGVATVA KGVCGACKKP IAGQVVTAMG KTWHPEHFVC THCQEEIGSR
     NFFERDGQPY CEKDYHNLFS PRCYYCNGPI LDKVVTALDR TWHPEHFFCA QCGAFFGPEG
     FHEKDGKAYC RKDYFDMFAP KCGGCARAIL ENYISALNTL WHPECFVCRE CFTPFVNGSF
     FEHDGQPYCE VHYHERRGSL CSGCQKPITG RCITAMAKKF HPEHFVCAFC LKQLNKGTFK
     EQNDKPYCQN CFLKLFC
//
ID   OPSD_XENLA     STANDARD;      PRT;   354 AA.
AC   P29403;
DT   01-APR-1993 (Rel. 25, Created)
DT   01-APR-1993 (Rel. 25, Last sequence update)
DT   15-JUL-1999 (Rel. 38, Last annotation update)
DE   RHODOPSIN.
GN   RHO.
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Amphibia; Batrachia; Anura; Mesobatrachia; Pipoidea; Pipidae;
OC   Xenopodinae; Xenopus.
RN   [1]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 93287804.
RA   Saha M.S., Grainger R.M.;
RT   "Early opsin expression in Xenopus embryos precedes photoreceptor
RT   differentiation.";
RL   Brain Res. Mol. Brain Res. 17:307-318(1993).
RN   [2]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 96216396.
RA   Batni S., Scalzetti L.C., Moody S.A., Knox B.E.;
RT   "Characterization of the Xenopus rhodopsin gene.";
RL   J. Biol. Chem. 271:3179-3186(1996).
CC   -!- FUNCTION: VISUAL PIGMENTS ARE THE LIGHT-ABSORBING MOLECULES THAT
CC       MEDIATE VISION. THEY CONSIST OF AN APOPROTEIN, OPSIN, COVALENTLY
CC       LINKED TO CIS-RETINAL.
CC   -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN.
CC   -!- TISSUE SPECIFICITY: ROD SHAPED PHOTORECEPTOR CELLS WHICH MEDIATES
CC       VISION IN DIM LIGHT.
CC   -!- PTM: SOME OR ALL OF THE CARBOXYL-TERMINAL SER OR THR RESIDUES MAY
CC       BE PHOSPHORYLATED.
CC   -!- SIMILARITY: BELONGS TO FAMILY 1 OF G-PROTEIN COUPLED RECEPTORS.
CC       OPSIN SUBFAMILY.
CC   --------------------------------------------------------------------------
CC   This SWISS-PROT entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use  by  non-profit  institutions as long  as its content  is  in  no  way
CC   modified and this statement is not removed.  Usage  by  and for commercial
CC   entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC   or send an email to license@isb-sib.ch).
CC   --------------------------------------------------------------------------
DR   EMBL; S62229; CAB32105.1; -.
DR   EMBL; L04692; AAB59950.1; -.
DR   EMBL; L07770; AAC42232.1; -.
DR   EMBL; U23808; AAC59901.1; -.
DR   PIR; S31473; S31473.
DR   GCRDB; GCR_0487; -.
DR   GCRDB; GCR_0497; -.
DR   GCRDB; GCR_0972; -.
DR   INTERPRO; IPR000276; -.
DR   INTERPRO; IPR000732; -.
DR   INTERPRO; IPR001760; -.
DR   PFAM; PF00001; 7tm_1; 1.
DR   PRINTS; PR00238; OPSIN.
DR   PRINTS; PR00579; RHODOPSIN.
DR   PROSITE; PS00237; G_PROTEIN_RECEPTOR; 1.
DR   PROSITE; PS00238; OPSIN; 1.
KW   Photoreceptor; Retinal protein; Transmembrane; Glycoprotein; Vision;
KW   Phosphorylation; Lipoprotein; Palmitate; G-protein coupled receptor.
FT   CARBOHYD      2      2       N-LINKED (GLCNAC...) (BY SIMILARITY).
FT   CARBOHYD     15     15       N-LINKED (GLCNAC...) (BY SIMILARITY).
FT   DOMAIN        1     36       EXTRACELLULAR.
FT   TRANSMEM     37     61       1 (POTENTIAL).
FT   DOMAIN       62     73       CYTOPLASMIC.
FT   TRANSMEM     74     98       2 (POTENTIAL).
FT   DOMAIN       99    113       EXTRACELLULAR.
FT   TRANSMEM    114    133       3 (POTENTIAL).
FT   DOMAIN      134    152       CYTOPLASMIC.
FT   TRANSMEM    153    176       4 (POTENTIAL).
FT   DOMAIN      177    202       EXTRACELLULAR.
FT   TRANSMEM    203    230       5 (POTENTIAL).
FT   DOMAIN      231    252       CYTOPLASMIC.
FT   TRANSMEM    253    276       6 (POTENTIAL).
FT   DOMAIN      277    284       EXTRACELLULAR.
FT   TRANSMEM    285    309       7 (POTENTIAL).
FT   DOMAIN      310    354       CYTOPLASMIC.
FT   BINDING     296    296       RETINAL CHROMOPHORE.
FT   LIPID       322    322       PALMITATE (BY SIMILARITY).
FT   LIPID       323    323       PALMITATE (BY SIMILARITY).
FT   DISULFID    110    187       BY SIMILARITY.
FT   CONFLICT    107    107       P -> Q (IN REF. 2).
FT   CONFLICT    137    137       I -> M (IN REF. 2).
FT   CONFLICT    241    241       L -> A (IN REF. 2).
SQ   SEQUENCE   354 AA;  39786 MW;  CD18F49EC63D8FFE CRC64;
     MNGTEGPNFY VPMSNKTGVV RSPFDYPQYY LAEPWQYSAL AAYMFLLILL GLPINFMTLF
     VTIQHKKLRT PLNYILLNLV FANHFMVLCG FTVTMYTSMH GYFIFGPTGC YIEGFFATLG
     GEVALWSLVV LAVERYIVVC KPMANFRFGE NHAIMGVAFT WIMALSCAAP PLFGWSRYIP
     EGMQCSCGVD YYTLKPEVNN ESFVIYMFIV HFTIPLIVIF FCYGRLLCTV KEAAAQQQES
     LTTQKAEKEV TRMVVIMVVF FLICWVPYAY VAFYIFTHQG SNFGPVFMTV PAFFAKSSAI
     YNPVIYIVLN KQFRNCLITT LCCGKNPFGD EDGSSAATSK TEASSVSSSQ VSPA
//
ID   OPS2_DROME     STANDARD;      PRT;   381 AA.
AC   P08099;
DT   01-AUG-1988 (Rel. 08, Created)
DT   01-AUG-1988 (Rel. 08, Last sequence update)
DT   01-DEC-1992 (Rel. 24, Last annotation update)
DE   OPSIN RH2 (OCELLAR OPSIN).
GN   RH2.
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Arthropoda; Tracheata; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha;
OC   Ephydroidea; Drosophilidae; Drosophila.
RN   [1]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 86133563.
RA   Cowman A.F., Zuker C.S., Rubin G.M.;
RT   "An opsin gene expressed in only one photoreceptor cell type of the
RT   Drosophila eye.";
RL   Cell 44:705-710(1986).
RN   [2]
RP   LOCALIZATION OF OPSIN RH2, AND ABSORPTION MAXIMA.
RX   MEDLINE; 88261498.
RA   Feiler R., Harris W.A., Kirschfeld K., Wehrhahn C., Zuker C.S.;
RT   "Targeted misexpression of a Drosophila opsin gene leads to altered
RT   visual function.";
RL   Nature 333:737-741(1988).
RN   [3]
RP   LOCALIZATION OF OPSIN RH2.
RX   MEDLINE; 88261503.
RA   Pollock J.A., Benzer S.;
RT   "Transcript localization of four opsin genes in the three visual
RT   organs of Drosophila; RH2 is ocellus specific.";
RL   Nature 333:779-782(1988).
CC   -!- FUNCTION: VISUAL PIGMENTS ARE THE LIGHT-ABSORBING MOLECULES THAT
CC       MEDIATE VISION. THEY CONSIST OF AN APOPROTEIN, OPSIN, COVALENTLY
CC       LINKED TO CIS-RETINAL.
CC   -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN.
CC   -!- PTM: SOME OR ALL OF THE CARBOXYL-TERMINAL SER OR THR RESIDUES MAY
CC       BE PHOSPHORYLATED.
CC   -!- MISCELLANEOUS: OPSIN RH2 IS THE PREDOMINANT OPSIN EXPRESSED IN THE
CC       DORSAL OCELLI.
CC   -!- MISCELLANEOUS: OPSIN RH2 HAS AN ABSORPTION MAXIMA AT 420 NM.
CC   -!- SIMILARITY: BELONGS TO FAMILY 1 OF G-PROTEIN COUPLED RECEPTORS.
CC       OPSIN SUBFAMILY.
CC   --------------------------------------------------------------------------
CC   This SWISS-PROT entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use  by  non-profit  institutions as long  as its content  is  in  no  way
CC   modified and this statement is not removed.  Usage  by  and for commercial
CC   entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC   or send an email to license@isb-sib.ch).
CC   --------------------------------------------------------------------------
DR   EMBL; M12896; AAA28734.1; -.
DR   PIR; A24058; OOFF2.
DR   GCRDB; GCR_0027; -.
DR   FLYBASE; FBgn0003248; Rh2.
DR   INTERPRO; IPR000276; -.
DR   INTERPRO; IPR001735; -.
DR   INTERPRO; IPR001760; -.
DR   PFAM; PF00001; 7tm_1; 1.
DR   PRINTS; PR00238; OPSIN.
DR   PRINTS; PR00576; OPSINRH1RH2.
DR   PROSITE; PS00237; G_PROTEIN_RECEPTOR; 1.
DR   PROSITE; PS00238; OPSIN; 1.
KW   Photoreceptor; Retinal protein; Transmembrane; Phosphorylation;
KW   Glycoprotein; G-protein coupled receptor; Vision.
FT   DOMAIN        1     56       EXTRACELLULAR.
FT   TRANSMEM     57     81       1 (POTENTIAL).
FT   DOMAIN       82     93       CYTOPLASMIC.
FT   TRANSMEM     94    119       2 (POTENTIAL).
FT   DOMAIN      120    133       EXTRACELLULAR.
FT   TRANSMEM    134    153       3 (POTENTIAL).
FT   DOMAIN      154    172       CYTOPLASMIC.
FT   TRANSMEM    173    196       4 (POTENTIAL).
FT   DOMAIN      197    220       EXTRACELLULAR.
FT   TRANSMEM    221    248       5 (POTENTIAL).
FT   DOMAIN      249    283       CYTOPLASMIC.
FT   TRANSMEM    284    307       6 (POTENTIAL).
FT   DOMAIN      308    314       EXTRACELLULAR.
FT   TRANSMEM    315    339       7 (POTENTIAL).
FT   DOMAIN      340    381       CYTOPLASMIC.
FT   CARBOHYD     27     27       N-LINKED (GLCNAC...) (PROBABLE).
FT   DISULFID    130    207       POTENTIAL.
FT   BINDING     326    326       RETINAL CHROMOPHORE.
SQ   SEQUENCE   381 AA;  42722 MW;  628322D228396F9D CRC64;
     MERSHLPETP FDLAHSGPRF QAQSSGNGSV LDNVLPDMAH LVNPYWSRFA PMDPMMSKIL
     GLFTLAIMII SCCGNGVVVY IFGGTKSLRT PANLLVLNLA FSDFCMMASQ SPVMIINFYY
     ETWVLGPLWC DIYAGCGSLF GCVSIWSMCM IAFDRYNVIV KGINGTPMTI KTSIMKILFI
     WMMAVFWTVM PLIGWSAYVP EGNLTACSID YMTRMWNPRS YLITYSLFVY YTPLFLICYS
     YWFIIAAVAA HEKAMREQAK KMNVKSLRSS EDCDKSAEGK LAKVALTTIS LWFMAWTPYL
     VICYFGLFKI DGLTPLTTIW GATFAKTSAV YNPIVYGISH PKYRIVLKEK CPMCVFGNTD
     EPKPDAPASD TETTSEADSK A
//
ID   OPS2_DROPS     STANDARD;      PRT;   381 AA.
AC   P28679;
DT   01-DEC-1992 (Rel. 24, Created)
DT   01-NOV-1995 (Rel. 32, Last sequence update)
DT   01-FEB-1996 (Rel. 33, Last annotation update)
DE   OPSIN RH2 (OCELLAR OPSIN).
GN   RH2.
OS   Drosophila pseudoobscura (Fruit fly).
OC   Eukaryota; Metazoa; Arthropoda; Tracheata; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha;
OC   Ephydroidea; Drosophilidae; Drosophila.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   STRAIN=APPLE HILL;
RX   MEDLINE; 93012921.
RA   Carulli J.P., Hartl D.L.;
RT   "Variable rates of evolution among Drosophila opsin genes.";
RL   Genetics 132:193-204(1992).
CC   -!- FUNCTION: VISUAL PIGMENTS ARE THE LIGHT-ABSORBING MOLECULES THAT
CC       MEDIATE VISION. THEY CONSIST OF AN APOPROTEIN, OPSIN, COVALENTLY
CC       LINKED TO CIS-RETINAL.
CC   -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN.
CC   -!- PTM: SOME OR ALL OF THE CARBOXYL-TERMINAL SER OR THR RESIDUES MAY
CC       BE PHOSPHORYLATED.
CC   -!- MISCELLANEOUS: OPSIN RH2 IS THE PREDOMINANT OPSIN EXPRESSED IN THE
CC       DORSAL OCELLI.
CC   -!- MISCELLANEOUS: OPSIN RH2 HAS AN ABSORPTION MAXIMA AT 420 NM.
CC   -!- SIMILARITY: BELONGS TO FAMILY 1 OF G-PROTEIN COUPLED RECEPTORS.
CC       OPSIN SUBFAMILY.
CC   --------------------------------------------------------------------------
CC   This SWISS-PROT entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use  by  non-profit  institutions as long  as its content  is  in  no  way
CC   modified and this statement is not removed.  Usage  by  and for commercial
CC   entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC   or send an email to license@isb-sib.ch).
CC   --------------------------------------------------------------------------
DR   EMBL; X65878; CAA46709.1; -.
DR   PIR; S24606; S24606.
DR   GCRDB; GCR_0625; -.
DR   FLYBASE; FBgn0012708; Dpse\Rh2.
DR   INTERPRO; IPR000276; -.
DR   INTERPRO; IPR001735; -.
DR   INTERPRO; IPR001760; -.
DR   PFAM; PF00001; 7tm_1; 1.
DR   PRINTS; PR00238; OPSIN.
DR   PRINTS; PR00576; OPSINRH1RH2.
DR   PROSITE; PS00237; G_PROTEIN_RECEPTOR; 1.
DR   PROSITE; PS00238; OPSIN; 1.
KW   Photoreceptor; Retinal protein; Transmembrane; Phosphorylation;
KW   Glycoprotein; G-protein coupled receptor; Vision.
FT   DOMAIN        1     56       EXTRACELLULAR.
FT   TRANSMEM     57     81       1 (POTENTIAL).
FT   DOMAIN       82     93       CYTOPLASMIC.
FT   TRANSMEM     94    119       2 (POTENTIAL).
FT   DOMAIN      120    133       EXTRACELLULAR.
FT   TRANSMEM    134    153       3 (POTENTIAL).
FT   DOMAIN      154    172       CYTOPLASMIC.
FT   TRANSMEM    173    196       4 (POTENTIAL).
FT   DOMAIN      197    220       EXTRACELLULAR.
FT   TRANSMEM    221    248       5 (POTENTIAL).
FT   DOMAIN      249    283       CYTOPLASMIC.
FT   TRANSMEM    284    307       6 (POTENTIAL).
FT   DOMAIN      308    314       EXTRACELLULAR.
FT   TRANSMEM    315    339       7 (POTENTIAL).
FT   DOMAIN      340    381       CYTOPLASMIC.
FT   CARBOHYD     27     27       N-LINKED (GLCNAC...) (PROBABLE).
FT   DISULFID    130    207       POTENTIAL.
FT   BINDING     326    326       RETINAL CHROMOPHORE.
SQ   SEQUENCE   381 AA;  42703 MW;  6C16369A88C5938E CRC64;
     MERSLLPEPP LAMALLGPRF EAQTGGNRSV LDNVLPDMAP LVNPHWSRFA PMDPTMSKIL
     GLFTLVILII SCCGNGVVVY IFGGTKSLRT PANLLVLNLA FSDFCMMASQ SPVMIINFYY
     ETWVLGPLWC DIYAACGSLF GCVSIWSMCM IAFDRYNVIV KGINGTPMTI KTSIMKIAFI
     WMMAVFWTIM PLIGWSSYVP EGNLTACSID YMTRQWNPRS YLITYSLFVY YTPLFMICYS
     YWFIIATVAA HEKAMRDQAK KMNVKSLRSS EDCDKSAENK LAKVALTTIS LWFMAWTPYL
     IICYFGLFKI DGLTPLTTIW GATFAKTSAV YNPIVYGISH PNDRLVLKEK CPMCVCGTTD
     EPKPDAPPSD TETTSEAESK D
//
ID   OPS2_HEMSA     STANDARD;      PRT;   377 AA.
AC   Q25158;
DT   01-NOV-1997 (Rel. 35, Created)
DT   01-NOV-1997 (Rel. 35, Last sequence update)
DT   01-NOV-1997 (Rel. 35, Last annotation update)
DE   COMPOUND EYE OPSIN BCRH2.
OS   Hemigrapsus sanguineus (Crab).
OC   Eukaryota; Metazoa; Arthropoda; Crustacea; Malacostraca;
OC   Eumalacostraca; Eucarida; Decapoda; Pleocyemata; Brachyura;
OC   Eubrachyura; Grapsoidea; Varunidae; Hemigrapsus.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   TISSUE=EYE;
RA   Sakamoto K., Hisatomi O., Tokunaga F., Eguchi E.;
RT   "Two opsins from the compound eye of the crab Hemigrapsus
RT   sanguineus.";
RL   J. Exp. Biol. 199:441-450(1996).
CC   -!- FUNCTION: VISUAL PIGMENTS ARE THE LIGHT-ABSORBING MOLECULES THAT
CC       MEDIATE VISION. THEY CONSIST OF AN APOPROTEIN, OPSIN, COVALENTLY
CC       LINKED TO CIS-RETINAL. THIS OPSIN PRODUCES VISUAL PIGMENTS WITH
CC       MAXIMAL ABSORPTION IN THE BLUE-GREEN REGION OF THE SPECTRUM.
CC   -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN.
CC   -!- TISSUE SPECIFICITY: EXPRESSED IN ALL OF THE SEVEN RETINULAR CELLS
CC       (R1-R7) FORMING THE MAIN RHABDOM IN EACH OMMATIDIUM.
CC   -!- PTM: SOME OR ALL OF THE CARBOXYL-TERMINAL SER OR THR RESIDUES MAY
CC       BE PHOSPHORYLATED (BY SIMILARITY).
CC   -!- SIMILARITY: BELONGS TO FAMILY 1 OF G-PROTEIN COUPLED RECEPTORS.
CC       OPSIN SUBFAMILY.
CC   --------------------------------------------------------------------------
CC   This SWISS-PROT entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use  by  non-profit  institutions as long  as its content  is  in  no  way
CC   modified and this statement is not removed.  Usage  by  and for commercial
CC   entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC   or send an email to license@isb-sib.ch).
CC   --------------------------------------------------------------------------
DR   EMBL; D50584; BAA09133.1; -.
DR   GCRDB; GCR_1067; -.
DR   INTERPRO; IPR000276; -.
DR   INTERPRO; IPR001760; -.
DR   PFAM; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR00238; OPSIN.
DR   PROSITE; PS00237; G_PROTEIN_RECEPTOR; 1.
DR   PROSITE; PS00238; OPSIN; 1.
KW   Photoreceptor; Retinal protein; Transmembrane; Glycoprotein; Vision;
KW   Phosphorylation; G-protein coupled receptor.
FT   DOMAIN        1     53       EXTRACELLULAR.
FT   TRANSMEM     54     78       1 (POTENTIAL).
FT   DOMAIN       79     90       CYTOPLASMIC.
FT   TRANSMEM     91    115       2 (POTENTIAL).
FT   DOMAIN      116    131       EXTRACELLULAR.
FT   TRANSMEM    132    151       3 (POTENTIAL).
FT   DOMAIN      152    170       CYTOPLASMIC.
FT   TRANSMEM    171    194       4 (POTENTIAL).
FT   DOMAIN      195    218       EXTRACELLULAR.
FT   TRANSMEM    219    246       5 (POTENTIAL).
FT   DOMAIN      247    281       CYTOPLASMIC.
FT   TRANSMEM    282    305       6 (POTENTIAL).
FT   DOMAIN      306    313       EXTRACELLULAR.
FT   TRANSMEM    314    338       7 (POTENTIAL).
FT   DOMAIN      339    377       CYTOPLASMIC.
FT   DISULFID    128    205       BY SIMILARITY.
FT   BINDING     325    325       RETINAL CHROMOPHORE (BY SIMILARITY).
FT   CARBOHYD      3      3       N-LINKED (GLCNAC...) (POTENTIAL).
SQ   SEQUENCE   377 AA;  42114 MW;  FD6CC2E0E199A256 CRC64;
     MTNATGPQMA YYGAASMDFG YPEGVSIVDF VRPEIKPYVH QHWYNYPPVN PMWHYLLGVI
     YLFLGTVSIF GNGLVIYLFN KSAALRTPAN ILVVNLALSD LIMLTTNVPF FTYNCFSGGV
     WMFSPQYCEI YACLGAITGV CSIWLLCMIS FDRYNIICNG FNGPKLTTGK AVVFALISWV
     IAIGCALPPF FGWGNYILEG ILDSCSYDYL TQDFNTFSYN IFIFVFDYFL PAAIIVFSYV
     FIVKAIFAHE AAMRAQAKKM NVSTLRSNEA DAQRAEIRIA KTALVNVSLW FICWTPYALI
     SLKGVMGDTS GITPLVSTLP ALLAKSCSCY NPFVYAISHP KYRLAITQHL PWFCVHETET
     KSNDDSQSNS TVAQDKA
//
ID   OPS2_LIMPO     STANDARD;      PRT;   376 AA.
AC   P35361;
DT   01-JUN-1994 (Rel. 29, Created)
DT   01-JUN-1994 (Rel. 29, Last sequence update)
DT   01-NOV-1997 (Rel. 35, Last annotation update)
DE   OCELLAR OPSIN.
OS   Limulus polyphemus (Atlantic horseshoe crab).
OC   Eukaryota; Metazoa; Arthropoda; Chelicerata; Merostomata; Xiphosura;
OC   Limulidae; Limulus.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   TISSUE=MEDIAN OCELLI;
RX   MEDLINE; 93317641.
RA   Smith W.C., Price D.A., Greenberg R.M., Battelle B.-A.;
RT   "Opsins from the lateral eyes and ocelli of the horseshoe crab,
RT   Limulus polyphemus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 90:6150-6154(1993).
CC   -!- FUNCTION: VISUAL PIGMENTS ARE THE LIGHT-ABSORBING MOLECULES THAT
CC       MEDIATE VISION. THEY CONSIST OF AN APOPROTEIN, OPSIN, COVALENTLY
CC       LINKED TO CIS-RETINAL.
CC   -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN.
CC   -!- TISSUE SPECIFICITY: OCELLAR CELLS; MEDIAN OCELLI.
CC   -!- PTM: SOME OR ALL OF THE CARBOXYL-TERMINAL SER OR THR RESIDUES MAY
CC       BE PHOSPHORYLATED (BY SIMILARITY).
CC   -!- MISCELLANEOUS: THIS OPSIN HAS AN ABSORPTION MAXIMA AT 530 NM.
CC   -!- SIMILARITY: BELONGS TO FAMILY 1 OF G-PROTEIN COUPLED RECEPTORS.
CC       OPSIN SUBFAMILY.
CC   --------------------------------------------------------------------------
CC   This SWISS-PROT entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use  by  non-profit  institutions as long  as its content  is  in  no  way
CC   modified and this statement is not removed.  Usage  by  and for commercial
CC   entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC   or send an email to license@isb-sib.ch).
CC   --------------------------------------------------------------------------
DR   EMBL; L03792; AAA28274.1; -.
DR   EMBL; L03782; AAA02499.1; -.
DR   PIR; A48197; A48197.
DR   GCRDB; GCR_0585; -.
DR   INTERPRO; IPR000276; -.
DR   INTERPRO; IPR001391; -.
DR   INTERPRO; IPR001760; -.
DR   PFAM; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR00238; OPSIN.
DR   PRINTS; PR00578; OPSINLTRLEYE.
DR   PROSITE; PS00237; G_PROTEIN_RECEPTOR; 1.
DR   PROSITE; PS00238; OPSIN; 1.
KW   Photoreceptor; Retinal protein; Transmembrane; Glycoprotein; Vision;
KW   Phosphorylation; G-protein coupled receptor.
FT   DOMAIN        1     46       EXTRACELLULAR.
FT   TRANSMEM     47     71       1 (POTENTIAL).
FT   DOMAIN       72     83       CYTOPLASMIC.
FT   TRANSMEM     84    108       2 (POTENTIAL).
FT   DOMAIN      109    123       EXTRACELLULAR.
FT   TRANSMEM    124    143       3 (POTENTIAL).
FT   DOMAIN      144    162       CYTOPLASMIC.
FT   TRANSMEM    163    186       4 (POTENTIAL).
FT   DOMAIN      187    210       EXTRACELLULAR.
FT   TRANSMEM    211    238       5 (POTENTIAL).
FT   DOMAIN      239    274       CYTOPLASMIC.
FT   TRANSMEM    275    298       6 (POTENTIAL).
FT   DOMAIN      299    306       EXTRACELLULAR.
FT   TRANSMEM    307    331       7 (POTENTIAL).
FT   DOMAIN      332    376       CYTOPLASMIC.
FT   DISULFID    120    197       BY SIMILARITY.
FT   BINDING     318    318       RETINAL CHROMOPHORE (BY SIMILARITY).
FT   CARBOHYD     17     17       N-LINKED (GLCNAC...) (POTENTIAL).
FT   CARBOHYD    193    193       N-LINKED (GLCNAC...) (POTENTIAL).
SQ   SEQUENCE   376 AA;  42111 MW;  FA9647C40531CBF8 CRC64;
     MANQLSYSSL GWPYQPNASV VDTMPKEMLY MIHEHWYAFP PMNPLWYSIL GVAMIILGII
     CVLGNGMVIY LMMTTKSLRT PTNLLVVNLA FSDFCMMAFM MPTMASNCFA ETWILGPFMC
     EVYGMAGSLF GCASIWSMVM ITLDRYNVIV RGMAAAPLTH KKATLLLLFV WIWSGGWTIL
     PFFGWSRYVP EGNLTSCTVD YLTKDWSSAS YVIIYGLAVY FLPLITMIYC YFFIVHAVAE
     HEKQLREQAK KMNVASLRAN ADQQKQSAEC RLAKVAMMTV GLWFMAWTPY LIIAWAGVFS
     SGTRLTPLAT IWGSVFAKAN SCYNPIVYGI SHPRYKAALY QRFPSLACGS GESGSDVKSE
     ASATMTMEEK PKSPEA
//
ID   OPS2_PATYE     STANDARD;      PRT;   399 AA.
AC   O15974;
DT   15-JUL-1998 (Rel. 36, Created)
DT   15-JUL-1998 (Rel. 36, Last sequence update)
DT   30-MAY-2000 (Rel. 39, Last annotation update)
DE   RHODOPSIN, G0-COUPLED (G0-RHODOPSIN).
GN   SCOP2.
OS   Patinopecten yessoensis (Ezo giant scallop) (Yesso scallop).
OC   Eukaryota; Metazoa; Mollusca; Bivalvia; Pteriomorphia; Pectinoida;
OC   Pectinoidea; Pectinidae; Patinopecten.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   TISSUE=EYE;
RX   MEDLINE; 97435252.
RA   Kojima D., Terakita A., Ishikawa T., Tsukahara Y., Maeda A.,
RA   Shichida Y.;
RT   "A novel Go-mediated phototransduction cascade in scallop visual
RT   cells.";
RL   J. Biol. Chem. 272:22979-22989(1997).
CC   -!- FUNCTION: VISUAL PIGMENTS ARE THE LIGHT-ABSORBING MOLECULES THAT
CC       MEDIATE VISION. THEY CONSIST OF AN APOPROTEIN, OPSIN, COVALENTLY
CC       LINKED TO CIS-RETINAL.
CC   -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN.
CC   -!- TISSUE SPECIFICITY: RETINA. EXPRESSED IN THE HYPERPOLARIZING CELL
CC       LAYER OF THE PHOTORECPTOR CELLS WITH ITS PHOTORECPTIVE REGION
CC       ADJACENT TO THE LENS.
CC   -!- PTM: SOME OR ALL OF THE CARBOXYL-TERMINAL SER OR THR RESIDUES MAY
CC       BE PHOSPHORYLATED (BY SIMILARITY).
CC   -!- SIMILARITY: BELONGS TO FAMILY 1 OF G-PROTEIN COUPLED RECEPTORS.
CC       OPSIN SUBFAMILY.
CC   --------------------------------------------------------------------------
CC   This SWISS-PROT entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use  by  non-profit  institutions as long  as its content  is  in  no  way
CC   modified and this statement is not removed.  Usage  by  and for commercial
CC   entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC   or send an email to license@isb-sib.ch).
CC   --------------------------------------------------------------------------
DR   EMBL; AB006455; BAA22218.1; -.
DR   INTERPRO; IPR000276; -.
DR   INTERPRO; IPR001760; -.
DR   PFAM; PF00001; 7tm_1; 1.
DR   PROSITE; PS00237; G_PROTEIN_RECEPTOR; FALSE_NEG.
DR   PROSITE; PS00238; OPSIN; 1.
KW   Photoreceptor; Retinal protein; Transmembrane; Glycoprotein; Vision;
KW   Phosphorylation; G-protein coupled receptor.
FT   DOMAIN        1     17       EXTRACELLULAR.
FT   TRANSMEM     18     43       1 (POTENTIAL).
FT   DOMAIN       44     55       CYTOPLASMIC.
FT   TRANSMEM     56     81       2 (POTENTIAL).
FT   DOMAIN       82     95       EXTRACELLULAR.
FT   TRANSMEM     96    115       3 (POTENTIAL).
FT   DOMAIN      116    134       CYTOPLASMIC.
FT   TRANSMEM    135    158       4 (POTENTIAL).
FT   DOMAIN      159    182       EXTRACELLULAR.
FT   TRANSMEM    183    210       5 (POTENTIAL).
FT   DOMAIN      211    240       CYTOPLASMIC.
FT   TRANSMEM    241    263       6 (POTENTIAL).
FT   DOMAIN      264    271       EXTRACELLULAR.
FT   TRANSMEM    272    295       7 (POTENTIAL).
FT   DOMAIN      296    399       CYTOPLASMIC.
FT   DISULFID     92    169       BY SIMILARITY.
FT   BINDING     282    282       RETINAL CHROMOPHORE.
FT   CARBOHYD      6      6       N-LINKED (GLCNAC...) (POTENTIAL).
SQ   SEQUENCE   399 AA;  45096 MW;  5AA6857ABC912100 CRC64;
     MPFPLNRTDT ALVISPSEFR IIGIFISICC IIGVLGNLLI IIVFAKRRSV RRPINFFVLN
     LAVSDLIVAL LGYPMTAASA FSNRWIFDNI GCKIYAFLCF NSGVISIMTH AALSFCRYII
     ICQYGYRKKI TQTTVLRTLF SIWSFAMFWT LSPLFGWSSY VIEVVPVSCS VNWYGHGLGD
     VSYTISVIVA VYVFPLSIIV FSYGMILQEK VCKDSRKNGI RAQQRYTPRF IQDIEQRVTF
     ISFLMMAAFM VAWTPYAIMS ALAIGSFNVE NSFAALPTLF AKASCAYNPF IYAFTNANFR
     DTVVEIMAPW TTRRVGVSTL PWPQVTYYPR RRTSAVNTTD IEFPDDNIFI VNSSVNGPTV
     KREKIVQRNP INVRLGIKIE PRDSRAATEN TFTADFSVI
//
ID   OPS2_SCHGR     STANDARD;      PRT;   380 AA.
AC   Q26495;
DT   01-NOV-1997 (Rel. 35, Created)
DT   01-NOV-1997 (Rel. 35, Last sequence update)
DT   15-JUL-1998 (Rel. 36, Last annotation update)
DE   OPSIN 2.
GN   LO2.
OS   Schistocerca gregaria (Desert locust).
OC   Eukaryota; Metazoa; Arthropoda; Tracheata; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Orthopteroidea; Orthoptera; Caelifera;
OC   Acridomorpha; Acridoidea; Acrididae; Schistocerca.
RN   [1]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 97301174.
RA   Towner P., Harris P., Wolstenholme A.J., Hill C., Worm K., Gartner W.;
RT   "Primary structure of locust opsins: a speculative model which may
RT   account for ultraviolet wavelength light detection.";
RL   Vision Res. 37:495-503(1997).
CC   -!- FUNCTION: VISUAL PIGMENTS ARE THE LIGHT-ABSORBING MOLECULES THAT
CC       MEDIATE VISION. THEY CONSIST OF AN APOPROTEIN, OPSIN, COVALENTLY
CC       LINKED TO CIS-RETINAL.
CC   -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN.
CC   -!- PTM: SOME OR ALL OF THE CARBOXYL-TERMINAL SER OR THR RESIDUES MAY
CC       BE PHOSPHORYLATED (BY SIMILARITY).
CC   -!- SIMILARITY: BELONGS TO FAMILY 1 OF G-PROTEIN COUPLED RECEPTORS.
CC       OPSIN SUBFAMILY.
CC   --------------------------------------------------------------------------
CC   This SWISS-PROT entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use  by  non-profit  institutions as long  as its content  is  in  no  way
CC   modified and this statement is not removed.  Usage  by  and for commercial
CC   entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC   or send an email to license@isb-sib.ch).
CC   --------------------------------------------------------------------------
DR   EMBL; X80072; CAA56378.1; -.
DR   INTERPRO; IPR000276; -.
DR   INTERPRO; IPR001760; -.
DR   PFAM; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR00238; OPSIN.
DR   PROSITE; PS00237; G_PROTEIN_RECEPTOR; 1.
DR   PROSITE; PS00238; OPSIN; 1.
KW   Photoreceptor; Retinal protein; Transmembrane; Phosphorylation;
KW   Glycoprotein; G-protein coupled receptor; Vision.
FT   DOMAIN        1     51       EXTRACELLULAR.
FT   TRANSMEM     52     76       1 (POTENTIAL).
FT   DOMAIN       77     88       CYTOPLASMIC.
FT   TRANSMEM     89    115       2 (POTENTIAL).
FT   DOMAIN      116    128       EXTRACELLULAR.
FT   TRANSMEM    129    148       3 (POTENTIAL).
FT   DOMAIN      149    166       CYTOPLASMIC.
FT   TRANSMEM    167    191       4 (POTENTIAL).
FT   DOMAIN      192    215       EXTRACELLULAR.
FT   TRANSMEM    216    243       5 (POTENTIAL).
FT   DOMAIN      244    279       CYTOPLASMIC.
FT   TRANSMEM    280    303       6 (POTENTIAL).
FT   DOMAIN      304    311       EXTRACELLULAR.
FT   TRANSMEM    312    336       7 (POTENTIAL).
FT   DOMAIN      337    380       CYTOPLASMIC.
FT   CARBOHYD      3      3       N-LINKED (GLCNAC...) (POTENTIAL).
FT   DISULFID    125    202       POTENTIAL.
FT   BINDING     323    323       RETINAL CHROMOPHORE (BY SIMILARITY).
SQ   SEQUENCE   380 AA;  42530 MW;  113504F71027C07A CRC64;
     MVNTTDFYPV PAAMAYESSV GLPLLGWNVP TEHLDLVHPH WRSFQVPNKY WHFGLAFVYF
     MLMCMSSLGN GIVLWIYATT KSIRTPSNMF IVNLALFDVL MLLEMPMLVV SSLFYQRPVG
     WELGCDIYAA LGSVAGIGSA INNAAIAFDR YRTISCPIDG RLTQGQVLAL IAGTWVWTLP
     FTLMPLLRIW SRFTAEGFLT TCSFDYLTDD EDTKVFVGCI FAWSYAFPLC LICCFYYRLI
     GAVREHEKML RDQAKKMNVK SLQSNADTEA QSAEIRIAKV ALTIFFLFLC SWTPYAVVAM
     IGAFGNRAAL TPLSTMIPAV TAKIVSCIDP WVYAINHPRF RAEVQKRMKW LHLGEDARSS
     KSDTSSTATD RTVGNVSASA
//
