ID   ODO2_FUGRU     STANDARD;      PRT;   409 AA.
AC   Q90512;
DT   01-NOV-1998 (REL. 37, CREATED)
DT   01-NOV-1998 (REL. 37, LAST SEQUENCE UPDATE)
DT   01-NOV-1998 (REL. 37, LAST ANNOTATION UPDATE)
DE   DIHYDROLIPOAMIDE SUCCINYLTRANSFERASE COMPONENT OF 2-OXOGLUTARATE
DE   DEHYDROGENASE COMPLEX PRECURSOR (EC 2.3.1.61) (E2) (E2K) (FRAGMENT).
GN   DLST.
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; 96202283.
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   PROC. NATL. ACAD. SCI. U.S.A. 93:1366-1369(1996).
CC   -!- FUNCTION: THE 2-OXOGLUTARATE DEHYDROGENASE COMPLEX CATALYZES THE
CC       OVERALL CONVERSION OF 2-OXOGLUTARATE TO SUCCINYL-COA & CO(2). IT
CC       CONTAINS MULTIPLE COPIES OF 3 ENZYMATIC COMPONENTS: 2-OXOGLUTARATE
CC       DEHYDROGENASE (E1), DIHYDROLIPOAMIDE SUCCINYLTRANSFERASE (E2) &
CC       LIPOAMIDE DEHYDROGENASE (E3) (BY SIMILARITY).
CC   -!- CATALYTIC ACTIVITY: SUCCINYL-COA + DIHYDROLIPOAMIDE = COA +
CC       S-SUCCINYLDIHYDROLIPOAMIDE.
CC   -!- COFACTOR: THE E2 COMPONENT CONTAINS ONE COVALENTLY-BOUND LIPOYL
CC       COFACTOR (BY SIMILARITY).
CC   -!- SUBUNIT: FORMS A 24-POLYPEPTIDE STRUCTURAL CORE WITH OCTAHEDRAL
CC       SYMMETRY (BY SIMILARITY).
CC   -!- SUBCELLULAR LOCATION: MITOCHONDRIAL (BY SIMILARITY).
CC   -!- SIMILARITY: TO OTHER SPECIES E2 COMPONENT.
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; U40758; G1117958; -.
DR   PROSITE; PS00189; LIPOYL; 1.
KW   GLYCOLYSIS; TRANSFERASE; ACYLTRANSFERASE; LIPOYL; MITOCHONDRION;
KW   TRANSIT PEPTIDE.
FT   NON_TER       1      1
FT   TRANSIT      <1     36       MITOCHONDRION (BY SIMILARITY).
FT   CHAIN        37    409       DIHYDROLIPOAMIDE SUCCINYLTRANSFERASE
FT                                COMPONENT (E2) OF 2-OXOGLUTARATE
FT                                DEHYDROGENASE COMPLEX.
FT   BINDING      79     79       LIPOYL (POTENTIAL).
FT   ACT_SITE    380    380       POTENTIAL.
FT   ACT_SITE    384    384       POTENTIAL.
FT   DOMAIN      133    139       POLY-PRO.
SQ   SEQUENCE   409 AA;  44111 MW;  E28C73F0 CRC32;
     SSVCRRLIFR TSRPGERASS QNSFHVRYFR TSVVHRDDLV TVKTPAFAES VTEGDVRWEK
     AVGDSVTEDE VVCEIETDKT SVQVPSPAAG VIEELLVPDG GKVEGGTPLF KLRKGAAAEA
     APSSVTEPVT AAPPPPPPPV SAPTAMPSVP PVPTQALQAK PVPAPTLPEP STLGGRGESR
     VKMSRMRLRI AQRLKEAQNT CAMLTTFNEV DMSNIQEMRT LHKDAFLKKH SIKLGFMSAF
     VKAAAHALTD QPAVNAVIDG ATNEIVYRDY VDISVAVATP KGLVVPVIRN VETMNFADIE
     RTINALGEKA RNNELAVEDM DGGTFTISNG GVFGSLFGTP IINPPQSAIL GMHGIFQRPV
     AVDGKAEIRP MMYVALTYDH RLVDGREAVT FLRKIKAAVE DPRALLLDM
//
ID   TM21_FUGRU     STANDARD;      PRT;   213 AA.
AC   Q90515;
DT   01-NOV-1998 (REL. 37, CREATED)
DT   01-NOV-1998 (REL. 37, LAST SEQUENCE UPDATE)
DT   01-NOV-1998 (REL. 37, LAST ANNOTATION UPDATE)
DE   TRANSMEMBRANE PROTEIN TMP21 PRECURSOR (S31III125).
GN   TMP21.
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; 96202283.
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   PROC. NATL. ACAD. SCI. U.S.A. 93:1366-1369(1996).
CC   -!- FUNCTION: INVOLVED IN VESICULAR PROTEIN TRAFFICKING (BY
CC       SIMILARITY).
CC   -!- SUBCELLULAR LOCATION: TYPE I MEMBRANE PROTEIN. GOLI CISTERNAE (BY
CC       SIMILARITY).
CC   -!- SIMILARITY: BELONGS TO THE EMP24/GP25L 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; U40761; G1117964; -.
KW   TRANSPORT; PROTEIN TRANSPORT; TRANSMEMBRANE; SIGNAL; GLYCOPROTEIN;
KW   GOLGI STACK.
FT   SIGNAL        1     19       POTENTIAL.
FT   CHAIN        20    213       TRANSMEMBRANE PROTEIN TMP21.
FT   DOMAIN       20    179       LUMENAL (POTENTIAL).
FT   TRANSMEM    180    200       POTENTIAL.
FT   DOMAIN      201    213       CYTOPLASMIC (POTENTIAL).
FT   CARBOHYD    173    173       POTENTIAL.
SQ   SEQUENCE   213 AA;  24653 MW;  6E22B0BB CRC32;
     MARLTALLFL PVLIESAFSI SFFLPVNTRK CLREEIHKDV LVTGEYEISE QVVTVHTSST
     VVGDGSIFKI TDSSSHTLYS KEDATKGKFA FTTEDYDMFE VCFESKCTGR VPDQLVNLDM
     KHGVEAKNYE EIAKVEKLKP LEVELRRLED LSESIVNDFA YMKKREEEMR DTNESTNTRV
     LYFSIFSMFC LIGLATWQVF YLRRFFKAKK LIE
//
