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UniProtKB/Swiss-Prot & UniProtKB/TrEMBL Publications

Figure 1. A sample entry from Swiss-Prot

ID   TNF5_HUMAN     STANDARD;      PRT;   261 AA.
AC   P29965;
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   CD40 LIGAND (CD40-L) (TNF-RELATED ACTIVATION PROTEIN) (TRAP) (T CELL
DE   ANTIGEN GP39) (CD154 ANTIGEN).
GN   TNFSF5 OR CD40LG OR CD40L OR TRAP.
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; 93076854.
RA   GRAF D., KORTHAEUER U., MAGES H.W., SENGER G., KROCZEK R.A.;
RT   "Cloning of TRAP, a ligand for CD40 on human T cells.";
RL   Eur. J. Immunol. 22:3191-3194(1992).
.. 6 references omitted
..
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 116-261.
RX   MEDLINE; 96131874.
RA   KARPSUSAS M., HSU Y.-M., WANG J.-H., THOMPSON J., LEDERMAN S.,
RA   CHESS L., THOMAS D.;
RT   "2-A crystal structure of an extracellular fragment of human CD40
RT   ligand.";
RL   Structure 3:1031-1039(1995).
RN   [8]
RP   3D-STRUCTURE MODELING OF COMPLEX WITH CD40.
RX   MEDLINE; 98266353.
RA   SINGH J., GARBER E., VAN VLIJMEN H., KARPSUSAS M., HSU Y.-M.,
RA   ZHENG Z., NAISMITH J.H., THOMAS D.;
RT   "The role of polar interactions in the molecular recognition of CD40L
RT   with its receptor CD40.";
RL   Protein Sci. 7:1124-1135(1998).
RN   [9]
.. 6 references omitted
..
RN   [14]
RP   VARIANTS HIGM1 ARG-36; CYS-140; SER-231; MET-254 AND GLY-227 DEL.
RX   MEDLINE; 97295077.
RA   NONOYAMA S., SHIMADZU M., TORU H., SEYAMA K., NUNOI H., NEUBAUER M.,
RA   YATA J.-I., OCH H.D.;
RT   "Mutations of the CD40 ligand gene in 13 Japanese patients with
RT   X-linked hyper-IgM syndrome.";
RL   Hum. Genet. 99:624-627(1997).
CC   -!- FUNCTION: MEDIATES B-CELL PROLIFERATION IN THE ABSENCE OF CO-
CC       STIMULUS AS WELL AS IGE PRODUCTION IN THE PRESENCE OF IL-4.
CC       INVOLVED IN IMMUNOGLOBULIN CLASS SWITCHING.
CC   -!- SUBUNIT: HOMOTRIMER.
CC   -!- SUBCELLULAR LOCATION: TYPE II MEMBRANE PROTEIN. ALSO EXISTS AS AN
CC       EXTRACELLULAR SOLUBLE FORM.
CC   -!- TISSUE SPECIFICITY: SPECIFICALLY EXPRESSED ON ACTIVATED CD4+
CC       T-LYMPHOCYTES.
CC   -!- DISEASE: DEFECTS IN CD40LG ARE THE CAUSE OF AN X-LINKED
CC       IMMUNODEFICIENCY WITH HYPER-IGM (HIGM1), AN IMMUNOGLOBULIN ISOTYPE
CC       SWITCH DEFECT CHARACTERIZED BY ELEVATED CONCENTRATIONS OF SERUM
CC       IGM AND DECREASED AMOUNTS OF ALL OTHER ISOTYPES. AFFECTED MALES
CC       PRESENT AT AN EARLY AGE (USUALLY WITHIN THE FIRST YEAR OF LIFE)
CC       RECURRENT BACTERIAL AND OPPORTUNISTIC INFECTIONS, INCLUDING
CC       PNEUMOCYSTIS CARINII PNEUMONIA AND INTRACTABLE DIARRHEA DUE TO
CC       CRYPTOSPORIDIUM INFECTION. DESPITE SUBSTITUTION TREATMENT WITH
CC       INTRAVENOUS IMMUNOGLOBULIN, THE OVERALL PROGNOSIS IS RATHER POOR,
CC       WITH A DEATH RATE OF ABOUT 10% BEFORE ADOLESCENCE.
CC   -!- SIMILARITY: BELONGS TO THE TUMOR NECROSIS FACTOR FAMILY.
CC   -!- DATABASE: name=CD40Lbase;
CC       NOTE=European CD40L defect database (mutation db);
CC       WWW="http://www.expasy.ch/cd40lbase/";
CC       FTP="ftp://ftp.expasy.ch/databases/cd40lbase".
CC   -!- DATABASE: name=PROW; NOTE=CD guide CD154 entry;
CC       WWW="http://www.ncbi.nlm.nih.gov/prow/cd/cd154.htm".
DR   EMBL; X68550; CAA48554.1; -.
DR   EMBL; Z15017; CAA78737.1; -.
DR   EMBL; X67878; CAA48077.1; -.
DR   EMBL; L07414; AAA35662.1; -.
DR   EMBL; D31797; BAA06599.1; -.
DR   EMBL; D31793; BAA06599.1; JOINED.
DR   EMBL; D31794; BAA06599.1; JOINED.
DR   EMBL; D31795; BAA06599.1; JOINED.
DR   EMBL; D31796; BAA06599.1; JOINED.
DR   PIR; S25684; S25684.
DR   PIR; S26694; S26694.
DR   PIR; S28017; S28017.
DR   PIR; S28852; S28852.
DR   PIR; JH0793; JH0793.
DR   PDB; 1ALY; 17-SEP-97.
DR   MIM; 308230; -.
DR   PFAM; PF00229; TNF; 1.
DR   PROSITE; PS00251; TNF_1; 1.
DR   PROSITE; PS50049; TNF_2; 1.
KW   Cytokine; Transmembrane; Glycoprotein; Signal-anchor; 3D-structure;
KW   Disease mutation; Polymorphism.
FT   DOMAIN        1     22       CYTOPLASMIC (POTENTIAL).
FT   TRANSMEM     23     46       SIGNAL-ANCHOR (TYPE-II MEMBRANE PROTEIN).
FT   DOMAIN       47    261       EXTRACELLULAR (POTENTIAL).
FT   DISULFID    178    218       POTENTIAL.
FT   CARBOHYD    240    240       POTENTIAL.
FT   VARIANT      36     36       M -> R (IN H1GM1). 
FT   VARIANT     123    123       A -> E (IN H1GM1). 
FT   VARIANT     126    126       V -> A (IN H1GM1). 
FT   VARIANT     128    129       SE -> RG (IN H1GM1). 
FT   VARIANT     140    140       W -> C (IN H1GM1). 
FT   VARIANT     140    140       W -> G (IN H1GM1). 
FT   VARIANT     140    140       W -> R (IN H1GM1). 
FT   VARIANT     144    144       G -> E (IN H1GM1). 
FT   VARIANT     155    155       L -> P (IN H1GM1). 
FT   VARIANT     211    211       T -> D (IN H1GM1). 
FT   VARIANT     219    219       G -> R. 
FT   VARIANT     227    227       G -> V (IN H1GM1). 
FT   VARIANT     227    227       MISSING (IN H1GM1). 
FT   VARIANT     231    231       L -> S (IN H1GM1). 
FT   VARIANT     235    235       A -> P (IN H1GM1). 
FT   VARIANT     254    254       T -> M (IN H1GM1). 
SQ   SEQUENCE    261 AA; 29273 MW; DC2AD21F CRC32; 
     MIETYNQTSP RSAATGLPIS MKIFMYLLTV FLITQMIGSA LFAVYLHRRL DKIEDERNLH
     EDFVFMKTIQ RCNTGERSLS LLNCEEIKSQ FEGFVKDIML NKEETKKENS FEMQKGDQNP
     QIAAHVISEA SSKTTSVLQW AEKGYYTMSN NLVTLENGKQ LTVKRQGLYY IYAQVTFCSN
     REASSQAPFI ASLCLKSPGR FERILLRAAN THSSAKPCGQ QSIHLGGVFE LQPGASVFVN
     VTDPSQVSHG TGFTSFGLLK L
//
 

Figure 2. A sample entry from TrEMBL

ID   Q31795         PRELIMINARY;   PRT;   475 AA.
AC   Q31795;
DT   01-NOV-1996 (TrEMBLrel. 01, Created)
DT   01-NOV-1996 (TrEMBLrel. 01, Last sequence update)
DT   01-SEP-1999 (TrEMBLrel. 12, Last annotation update)
DE   RIBULOSE BISPHOSPHATE CARBOXYLASE LARGE CHAIN (EC 4.1.1.39).
GN   RBCL.
OS   Anthoceros formosae.
OG   Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Anthocerotopsida;
OC   Anthocerotales; Anthocerotaceae; Anthoceros.
RN   [1]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 96184846.
RA   YOSHINAGA K., IINUMA H., MASUZAWA T., UEDA K.;
RT   "Extensive RNA editing of U to C in addition to C to U substitution
RT   in the rbcL transcripts of hornwort chloroplasts and the origin of
RT   RNA editing in green plants.";
RL   Nucleic Acids Res. 24:1008-1014(1996).
CC   -!- FUNCTION: RUBISCO CATALYSES TWO REACTIONS: THE CARBOXYLATION OF D-
CC       RIBULOSE 1,5-BISPHOSPHATE, THE PRIMARY EVENT IN PHOTOSYNTHETIC
CC       CARBON DIOXIDE FIXATION, AS WELL AS THE OXIDATIVE FRAGMENTATION OF
CC       THE PENTOSE SUBSTRATE IN THE PHOTORESPIRATION PROCESS. BOTH
CC       REACTIONS OCCUR SIMULTANEOUSLY AND IN COMPETITION AT THE SAME
CC       ACTIVE SITE.
CC   -!- CATALYTIC ACTIVITY: D-RIBULOSE 1,5-BISPHOSPHATE + CO(2) = 2 3-
CC       PHOSPHO-D-GLYCERATE.
CC   -!- CATALYTIC ACTIVITY: D-RIBULOSE 1,5-BISPHOSPHATE + O(2) = 3-
CC       PHOSPHO-D-GLYCERATE + 2-PHOSPHOGLYCOLATE.
CC   -!- SUBUNIT: 8 LARGE CHAINS + 8 SMALL CHAINS.
CC   -!- SUBCELLULAR LOCATION: CHLOROPLAST.
DR   EMBL; D43695; BAA07796.1; -.
DR   PROSITE; PS00157; RUBISCO_LARGE; 1.
DR   PFAM; PF00016; RuBisCO_large; 1.
DR   MENDEL; 21614; Antfo;rbcL;21614.
KW   Chloroplast; Photosynthesis; Carbon dioxide fixation;
KW   Photorespiration; Lyase; Oxidoreductase; Monooxygenase.
FT   ACT_SITE    202    202       BINDING OF CO(2) ACTIVATES THE ENZYME.
SQ   SEQUENCE   475 AA;  52352 MW;  FEE98D6C CRC32;
     MSPQTETKAG VGFKAGVKDY RLTHYTPDYE TKDTDILAAS XMTPXPGVPP EEAGAAVAAE
     SSTGTWTTVW TDGLTSLDRY KGRCYDIEPV AGEENQYIAY AAYSLDLFEE GSVTNMFTSI
     VGNVFGFKAL RASRLEDSRI PPAYSKTFQG PPHGIQVERD KSNKYGRPLL GCTIKPKLGL
     SAKNYGRAVY ECLRGGLDFT KDDENVNSQP FMRWRDRFLF VAEAISKSQA ETGEIKGHYL
     NATAGTCEEM MKRAHFAREL GMPIVMHDYL TGGFIANTTL ARYCRDNGLL LHIHRAMHAV
     TDRQRNHGIH FRVSAKASRM SGGDHIHPGT VVGKLEGECE VTLGFVDLPC DDYIEKDRSR
     GIYFTQDWVS MPGVLLVASG GIHVWHMPAL TEIFGDDSVL QFGGGTLGHP WGNAPGAVAN
     RVALEACVQA RNEGRDLARE GNDIIREASK WSPELAAACE VWKEIKFVFE TIDTL
//
 

Figure 3. The Production of TrEMBL

Image2

Figure 4. First level TrEMBLnew entries (after translation and entry creation)

ID   AAC51357 PRELIMINARY; PRT; 440 AA. 
AC   AAC51357; 
DT   31-JUN-1997 (EMBLrel. 51, Created) 
DT   31-JUN-1997 (EMBLrel. 51, Last sequence update) 
DT   31-JUN-1997 (EMBLrel. 51, Last annotation update) 
DE   GABA-A RECEPTOR PI SUBUNIT. 
OS   Homo sapiens (Human). 
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Mammalia; 
OC   Eutheria; Primates; Catarrhini; Hominidae; Homo. 
RN   [1] 
RP   SEQUENCE FROM N.A. 
RA   HEDBLOM E., KIRKNESS E.F.; 
RT   "A novel class of GABAA receptor subunit in tissues of the 
RT   reproductive system."; 
RL   J. Biol. Chem. 272:15346-15350(1997). 
DR   EMBL; U95367; AAC51357.1; -. 
SQ   SEQUENCE 440 AA; 50640 MW; 375043BA CRC32; 
     MNYSLHLAFV CLSLFTERMC IQGSQFNVEV GRSDKLSLPG FENLTAGYNK FLRPNFGGEP 
     VQIALTLDIA SISSISESNM DYTATIYLRQ RWMDQRLVFE GNKSFTLDAR LVEFLWVPDT 
     YIVESKKSFL HEVTVGNRLI RLFSNGTVLY ALRITTTVAC NMDLSKYPMD TQTCKLQLES 
     WGYDGNDVEF TWLRGNDSVR GLEHLRLAQY TIERYFTLVT RSQQETGNYT RLVLQFELRR 
     NVLYFILETY VPSTFLVVLS WVSFWISLDS VPARTCIGVT TVLSMTTLMI GSRTSLPNTN 
     CFIKAIDVYL GICFSFVFGA LLEYAVAHYS SLQQMAAKDR GTTKEVEEVS ITNIINSSIS 
     SFKRKISFAS IEISSDNVDY SDLTMKTSDK FKFVFREKMG RIVDYFTIQN PSNVDHYSKL 
     LFPLIFMLAN VFYWAYYMYF 
// 
ID   AAC24194 PRELIMINARY; PRT; 440 AA. 
AC   AAC24194; 
DT   31-JUN-1997 (EMBLrel. 51, Created) 
DT   31-JUN-1997 (EMBLrel. 51, Last sequence update) 
DT   31-JUN-1997 (EMBLrel. 51, Last annotation update) 
DE   GABA-A RECEPTOR PI SUBUNIT. 
GN   GABRP. 
OS   Homo sapiens (Human). 
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Mammalia; 
OC   Eutheria; Primates; Catarrhini; Hominidae; Homo. 
RN   [1] 
RP   SEQUENCE FROM N.A. 
RA   JOHNSON E.K., HEDBLOM E., KIRKNESS E.F.; 
RT   "Structure and localization of the gene encoding the human GABA-A 
RT   receptor pi subunit (GABRP)."; 
RL   Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases. 
DR   EMBL; AF009702; AAC24194.1; -. 
DR   EMBL; AF009694; AAC24194.1; JOINED. 
DR   EMBL; AF009695; AAC24194.1; JOINED. 
DR   EMBL; AF009696; AAC24194.1; JOINED. 
DR   EMBL; AF009697; AAC24194.1; JOINED. 
DR   EMBL; AF009698; AAC24194.1; JOINED. 
DR   EMBL; AF009699; AAC24194.1; JOINED. 
DR   EMBL; AF009700; AAC24194.1; JOINED. 
DR   EMBL; AF009701; AAC24194.1; JOINED. 
SQ   SEQUENCE 440 AA; 50640 MW; 375043BA CRC32; 
     MNYSLHLAFV CLSLFTERMC IQGSQFNVEV GRSDKLSLPG FENLTAGYNK FLRPNFGGEP 
     VQIALTLDIA SISSISESNM DYTATIYLRQ RWMDQRLVFE GNKSFTLDAR LVEFLWVPDT 
     YIVESKKSFL HEVTVGNRLI RLFSNGTVLY ALRITTTVAC NMDLSKYPMD TQTCKLQLES 
     WGYDGNDVEF TWLRGNDSVR GLEHLRLAQY TIERYFTLVT RSQQETGNYT RLVLQFELRR 
     NVLYFILETY VPSTFLVVLS WVSFWISLDS VPARTCIGVT TVLSMTTLMI GSRTSLPNTN 
     CFIKAIDVYL GICFSFVFGA LLEYAVAHYS SLQQMAAKDR GTTKEVEEVS ITNIINSSIS 
     SFKRKISFAS IEISSDNVDY SDLTMKTSDK FKFVFREKMG RIVDYFTIQN PSNVDHYSKL 
     LFPLIFMLAN VFYWAYYMYF 
// 
 

Figure 5. Second level TrEMBLnew entry (after merging)

ID   AAC51357 PRELIMINARY; PRT; 440 AA. 
AC   AAC51357; 
DT   31-JUN-1997 (EMBLrel. 51, Created) 
DT   31-JUN-1997 (EMBLrel. 51, Last sequence update) 
DT   31-JUN-1997 (EMBLrel. 51, Last annotation update) 
DE   GABA-A RECEPTOR PI SUBUNIT. 
GN   GABRP. 
OS   Homo sapiens (Human). 
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Mammalia; 
OC   Eutheria; Primates; Catarrhini; Hominidae; Homo. 
RN   [1] 
RP   SEQUENCE FROM N.A. 
RA   HEDBLOM E., KIRKNESS E.F.; 
RT   "A novel class of GABAA receptor subunit in tissues of the 
RT   reproductive system."; 
RL   J. Biol. Chem. 272:15346-15350(1997). 
RN   [2] 
RP   SEQUENCE FROM N.A. 
RA   JOHNSON E.K., HEDBLOM E., KIRKNESS E.F.; 
RT   "Structure and localization of the gene encoding the human GABA-A 
RT   receptor pi subunit (GABRP)."; 
RL   Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases. 
DR   EMBL; U95367; AAC51357.1; -. 
DR   EMBL; AF009702; AAC24194.1; -. 
DR   EMBL; AF009694; AAC24194.1; JOINED. 
DR   EMBL; AF009695; AAC24194.1; JOINED. 
DR   EMBL; AF009696; AAC24194.1; JOINED. 
DR   EMBL; AF009697; AAC24194.1; JOINED. 
DR   EMBL; AF009698; AAC24194.1; JOINED. 
DR   EMBL; AF009699; AAC24194.1; JOINED. 
DR   EMBL; AF009700; AAC24194.1; JOINED. 
DR   EMBL; AF009701; AAC24194.1; JOINED. 
SQ   SEQUENCE 440 AA; 50640 MW; 375043BA CRC32; 
     MNYSLHLAFV CLSLFTERMC IQGSQFNVEV GRSDKLSLPG FENLTAGYNK FLRPNFGGEP 
     VQIALTLDIA SISSISESNM DYTATIYLRQ RWMDQRLVFE GNKSFTLDAR LVEFLWVPDT 
     YIVESKKSFL HEVTVGNRLI RLFSNGTVLY ALRITTTVAC NMDLSKYPMD TQTCKLQLES 
     WGYDGNDVEF TWLRGNDSVR GLEHLRLAQY TIERYFTLVT RSQQETGNYT RLVLQFELRR 
     NVLYFILETY VPSTFLVVLS WVSFWISLDS VPARTCIGVT TVLSMTTLMI GSRTSLPNTN 
     CFIKAIDVYL GICFSFVFGA LLEYAVAHYS SLQQMAAKDR GTTKEVEEVS ITNIINSSIS 
     SFKRKISFAS IEISSDNVDY SDLTMKTSDK FKFVFREKMG RIVDYFTIQN PSNVDHYSKL 
     LFPLIFMLAN VFYWAYYMYF 
// 
 

Figure 6. Third level TrEMBLnew entriy (after complete post-processing): SP-TrEMBL

ID   O00591 PRELIMINARY; PRT; 440 AA. 
AC   O00591; 
DT   01-JUL-1997 (TrEMBLrel. 04, CREATED) 
DT   01-JUL-1997 (TrEMBLrel. 04, LAST SEQUENCE UPDATE) 
DT   01-JUL-1997 (TrEMBLrel. 04, LAST ANNOTATION UPDATE) 
DE   GABA-A RECEPTOR PI SUBUNIT. 
GN   GABRP. 
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; 97326112. 
RA   HEDBLOM E., KIRKNESS E.F.; 
RT   "A novel class of GABAA receptor subunit in tissues of the 
RT   reproductive system."; 
RL   J. Biol. Chem. 272:15346-15350(1997). 
RN   [2] 
RP   SEQUENCE FROM N.A. 
RA   JOHNSON E.K., HEDBLOM E., KIRKNESS E.F.; 
RT   "Structure and localization of the gene encoding the human GABA-A 
RT   receptor pi subunit (GABRP)."; 
RL   Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases. 
CC   -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (BY SIMILARITY). 
CC   -!- SIMILARITY: BELONGS TO THE LIGAND-GATED IONIC CHANNELS FAMILY. 
DR   EMBL; U95367; AAC51357.1; -. 
DR   EMBL; AF009702; AAC24194.1; -. 
DR   EMBL; AF009694; AAC24194.1; JOINED. 
DR   EMBL; AF009695; AAC24194.1; JOINED. 
DR   EMBL; AF009696; AAC24194.1; JOINED. 
DR   EMBL; AF009697; AAC24194.1; JOINED. 
DR   EMBL; AF009698; AAC24194.1; JOINED. 
DR   EMBL; AF009699; AAC24194.1; JOINED. 
DR   EMBL; AF009700; AAC24194.1; JOINED. 
DR   EMBL; AF009701; AAC24194.1; JOINED. 
DR   PROSITE; PS00236; NEUROTR_ION_CHANNEL; 1. 
DR   PFAM; PF00065; neur_chan; 2. 
KW   Postsynaptic membrane; Ionic channel; Glycoprotein; Transmembrane. 
SQ   SEQUENCE 440 AA; 50640 MW; 375043BA CRC32; 
     MNYSLHLAFV CLSLFTERMC IQGSQFNVEV GRSDKLSLPG FENLTAGYNK FLRPNFGGEP 
     VQIALTLDIA SISSISESNM DYTATIYLRQ RWMDQRLVFE GNKSFTLDAR LVEFLWVPDT 
     YIVESKKSFL HEVTVGNRLI RLFSNGTVLY ALRITTTVAC NMDLSKYPMD TQTCKLQLES 
     WGYDGNDVEF TWLRGNDSVR GLEHLRLAQY TIERYFTLVT RSQQETGNYT RLVLQFELRR 
     NVLYFILETY VPSTFLVVLS WVSFWISLDS VPARTCIGVT TVLSMTTLMI GSRTSLPNTN 
     CFIKAIDVYL GICFSFVFGA LLEYAVAHYS SLQQMAAKDR GTTKEVEEVS ITNIINSSIS 
     SFKRKISFAS IEISSDNVDY SDLTMKTSDK FKFVFREKMG RIVDYFTIQN PSNVDHYSKL 
     LFPLIFMLAN VFYWAYYMYF 
// 
 

Figure 7. A fully annotated Swiss-Prot entry: The ultimate fate of a TrEMBLnew entry 

ID   GAAP_HUMAN     STANDARD;      PRT;   440 AA.
AC   O00591;
DT   15-JUL-1999 (Rel. 38, Created)
DT   15-JUL-1999 (Rel. 38, Last sequence update)
DT   15-DEC-1999 (Rel. 39, Last annotation update)
DE   GAMMA-AMINOBUTYRIC-ACID RECEPTOR PI SUBUNIT PRECURSOR (GABA(A)
DE   RECEPTOR).
GN   GABRP.
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; 97326112.
RA   HEDBLOM E., KIRKNESS E.F.;
RT   "A novel class of GABAA receptor subunit in tissues of the
RT   reproductive system.";
RL   J. Biol. Chem. 272:15346-15350(1997).
RN   [2]
RP   SEQUENCE FROM N.A.
RA   JOHNSON E.K., HEDBLOM E., KIRKNESS E.F.;
RT   "Structure and localization of the gene encoding the human GABA-A
RT   receptor pi subunit (GABRP).";
RL   Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: GABA, THE MAJOR INHIBITORY NEUROTRANSMITTER IN THE
CC       VERTEBRATE BRAIN, MEDIATES NEURONAL INHIBITION BY BINDING TO THE
CC       GABA/BENZODIAZEPINE RECEPTOR AND OPENING AN INTEGRAL CHLORIDE
CC       CHANNEL. IN THE UTERUS, THE FUNCTION OF THE RECEPTOR APPEARS TO BE
CC       RELATED TO TISSUE CONTRACTILITY. THE BINDING OF THIS PI SUBUNIT
CC       WITH OTHER GABA(A) RECEPTOR SUBUNITS ALTERS THE SENSITIVITY OF
CC       RECOMBINANT RECEPTORS TO MODULATORY AGENTS SUCH AS PREGNANOLONE.
CC   -!- SUBUNIT: GENERALLY PENTAMERIC. THERE ARE FIVE TYPES OF GABA(A)
CC       RECEPTOR CHAINS: ALPHA, BETA, GAMMA, DELTA, AND EPSILON. A SIXTH
CC       CLASS OF SUBUNIT: RHO FORM HOMOMERIC GABA RECEPTORS THAT DO NOT
CC       APPEAR TO COEXIST WITH GABA(A) RECEPTOR SUBUNITS BUT WITH GABA(C)
CC       RECEPTOR SUBUNITS. SUBUNIT PI CAN ALSO BIND THIS COMPLEX.
CC   -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN.
CC   -!- TISSUE SPECIFICITY: MOST ABUNDANT IN THE UTERUS, ALSO EXPRESSED IN
CC       LUNG, THYMUS AND PROSTATE.
CC   -!- SIMILARITY: BELONGS TO THE LIGAND-GATED IONIC CHANNELS FAMILY.
CC   ----------------------------------------------------------------------- 
CC   This Swiss-Prot entry is copyright. It is produced through a  
CC   collaboration between the Swiss Institute of Bioinformatics and the  
CC   EMBL outstation - the European Bioinformatics Institute. There are no 
CC   restrictions on its use by non-profit institutions as long as its  
CC   content is in no way modified and this statement is not removed. Usage 
CC   by and for commercial entities requires a license agreement (See  
CC   http://www.isb-sib.ch/announce/ or send an email to  
CC   license@isb-sib.ch). 
CC   ----------------------------------------------------------------------- 
DR   EMBL; U95367; AAC51357.1; -.
DR   EMBL; AF009702; AAC24194.1; -.
DR   EMBL; AF009694; AAC24194.1; JOINED.
DR   EMBL; AF009695; AAC24194.1; JOINED.
DR   EMBL; AF009696; AAC24194.1; JOINED.
DR   EMBL; AF009697; AAC24194.1; JOINED.
DR   EMBL; AF009698; AAC24194.1; JOINED.
DR   EMBL; AF009699; AAC24194.1; JOINED.
DR   EMBL; AF009700; AAC24194.1; JOINED.
DR   EMBL; AF009701; AAC24194.1; JOINED.
DR   MIM; 602729; -.
DR   PFAM; PF00065; neur_chan; 2.
DR   PROSITE; PS00236; NEUROTR_ION_CHANNEL; 1.
KW   Postsynaptic membrane; Ionic channel; Glycoprotein; Signal;
KW   Multigene family; Transmembrane.
FT   SIGNAL        1     16       POTENTIAL.
FT   CHAIN        17    440       GAMMA-AMINOBUTYRIC-ACID RECEPTOR PI
FT                                SUBUNIT.
FT   DOMAIN       17    242       EXTRACELLULAR (PROBABLE).
FT   TRANSMEM    243    266       PROBABLE.
FT   TRANSMEM    270    292       PROBABLE.
FT   TRANSMEM    305    327       PROBABLE.
FT   DOMAIN      328    416       CYTOPLASMIC (PROBABLE).
FT   TRANSMEM    417    438       PROBABLE.
FT   DISULFID    160    174       BY SIMILARITY.
FT   CARBOHYD     43     43       POTENTIAL.
FT   CARBOHYD    102    102       POTENTIAL.
FT   CARBOHYD    145    145       POTENTIAL.
FT   CARBOHYD    196    196       POTENTIAL.
FT   CARBOHYD    228    228       POTENTIAL.
SQ   SEQUENCE   440 AA;  50640 MW;  375043BA CRC32;
     MNYSLHLAFV CLSLFTERMC IQGSQFNVEV GRSDKLSLPG FENLTAGYNK FLRPNFGGEP
     VQIALTLDIA SISSISESNM DYTATIYLRQ RWMDQRLVFE GNKSFTLDAR LVEFLWVPDT
     YIVESKKSFL HEVTVGNRLI RLFSNGTVLY ALRITTTVAC NMDLSKYPMD TQTCKLQLES
     WGYDGNDVEF TWLRGNDSVR GLEHLRLAQY TIERYFTLVT RSQQETGNYT RLVLQFELRR
     NVLYFILETY VPSTFLVVLS WVSFWISLDS VPARTCIGVT TVLSMTTLMI GSRTSLPNTN
     CFIKAIDVYL GICFSFVFGA LLEYAVAHYS SLQQMAAKDR GTTKEVEEVS ITNIINSSIS
     SFKRKISFAS IEISSDNVDY SDLTMKTSDK FKFVFREKMG RIVDYFTIQN PSNVDHYSKL
     LFPLIFMLAN VFYWAYYMYF
//
 

Figure 8. EDITtoTrEMBL

 
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Figure 9. A sample entry from GCRDb

###GCR_0087 HSPLMERE X13556 421 SEROTONIN A GENOMIC 
DATE_ADDED 930711 
DATE_MOD 980128 
FAMILY A 
GROUP 2 
IUPHAR 5HT1A-5-Hydroxytrptamine receptor 
ABBREV 5HT1A 
SPECIES Homo sapiens 
UNIQ Y Y Y M Y Y 39 Y Y 
REF%K Human gene for plasma membrane receptor 
REF%K GB X13556 
REF%K G-protein coupled receptor; glycoprotein; membrane protein; 
REF%K human 
REF%A B. K. Kobilka 
REF%A T. Frielle 
REF%A S. Collins 
REF%A T. Feng 
REF%A T. S. Kobilka 
REF%A U. Francke 
REF%A R. J. Lefkowitz 
REF%A M. G. Caron 
REF%T An intronless gene encoding a potential member of the family of receptors coupled to guanine nucleotide regulatory proteins 
REF%J Nature  
REF%V 329 
REF%P 75-79 
REF%D 1987 
>HSPLMERE X13556, 421 bases, 47192D6F  
MDVLSPGQGNNTTSPPAPFETGGNTTGISDVTVSYQVITSLLLGTLIFCA 
VLGNACVVAAIALERSLQNVANYLIGSLAVTDLMVSVLVLPMAALYQVLN 
KWTLGQVTCDLFIALDVLCCTSSILHLCAIALDRYWAITDPIDYVNKRTP 
RPRALISLTWLIGFLISIPPILGWRTPEDRSDPDACTISKDHGYTIYSTF 
GAFYIPLLLMLVLYGRIFRAARFRIRKTVKKVEKTGADTRHGASPAPQPK 
KSVNGESGSRNWRLGVESKAGGALCANGAVRQGDDGAALEVIEVHRVGNS 
KEHLPLPSEAGPTPCAPASFERKNERNAEAKRKMALARERKTVKTLGIIM 
GTFILCWLPFFIVALVLPFCESSCHMPTLLGAIINWLGYSNSLLNPVIYA 
YFNKDFQNAFKKIIKCNFCRQ 
ORF173..1438 
tgctcctcgg agataccctt cgccgaagca gtaagaactt cctgcttggg tctctgcatt 
cccttcctcc gaaacttccc aggagaaggg cggaagaccc caggggaagg ggcgaggcga 
atcttcgcgc tgctttttct tccctccccc ttcccgcgcc gggcgcgcag gcatggatgt 
gctcagccct ggtcagggca acaacaccac atcaccaccg gctccctttg agaccggcgg 
caacactact ggtatctccg acgtgaccgt cagctaccaa gtgatcacct ctctgctgct 
gggcacgctc atcttctgcg cggtgctggg caatgcgtgc gtggtggctg ccatcgcctt 
ggagcgctcc ctgcagaacg tggccaatta tcttattggc tctttggcgg tcaccgacct 
catggtgtcg gtgttggtgc tgcccatggc cgcgctgtat caggtgctca acaagtggac 
actgggccag gtaacctgcg acctgttcat cgccctcgac gtgctgtgct gcacctcatc 
catcttgcac ctgtgcgcca tcgcgctgga caggtactgg gccatcacgg accccatcga 
ctacgtgaac aagaggacgc cccggccgcg tgcgctcatc tcgctcactt ggcttattgg 
cttcctcatc tctatcccgc ccatcctggg ctggcgcacc ccggaagacc gctcggaccc 
cgacgcatgc accattagca aggatcatgg ctacactatc tattccacct ttggagcttt 
ctacatcccg ctgctgctca tgctggttct ctatgggcgc atattccgag ctgcgcgctt 
ccgcatccgc aagacggtca aaaaggtgga gaagaccgga gcggacaccc gccatggagc 
atctcccgcc ccgcagccca agaagagtgt gaatggagag tcggggagca ggaactggag 
gctgggcgtg gagagcaagg ctgggggtgc tctgtgcgcc aatggcgcgg tgaggcaagg 
tgacgatggc gccgccctgg aggtgatcga ggtgcaccga gtgggcaact ccaaagagca 
cttgcctctg cccagcgagg ctggtcctac cccttgtgcc cccgcctctt tcgagaggaa 
aaatgagcgc aacgccgagg cgaagcgcaa gatggccctg gcccgagaga ggaagacagt 
gaagacgctg ggcatcatca tgggcacctt catcctctgc tggctgccct tcttcatcgt 
ggctcttgtt ctgcccttct gcgagagcag ctgccacatg cccaccctgt tgggcgccat 
aatcaattgg ctgggctact ccaactctct gcttaacccc gtcatttacg catacttcaa 
caaggacttt caaaacgcgt ttaagaagat cattaagtgt aacttctgcc gccagtgatg 
acggaggagt agccggccag tcgaggctac aggatccgtc ccattcacta tgcttccccc 
aaccctaggg aatccacact taatataatt cgccacttct cctctttttc tctgctccgc 
tcacggcttg cagacctgg 
EXN unknown 
CHR unknown 
TYP
 

Figure 10. Representation of the InterPro data flow scheme, illustrating the route from the source database providers via the RDBMS to the end user.

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