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Database: UniProt/SWISS-PROT
Entry: DCE1_PANTR
LinkDB: DCE1_PANTR
Original site: DCE1_PANTR 
ID   DCE1_PANTR              Reviewed;         594 AA.
AC   Q5IS68;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   23-MAY-2018, entry version 80.
DE   RecName: Full=Glutamate decarboxylase 1;
DE            EC=4.1.1.15;
DE   AltName: Full=67 kDa glutamic acid decarboxylase;
DE            Short=GAD-67;
DE   AltName: Full=Glutamate decarboxylase 67 kDa isoform;
GN   Name=GAD1; Synonyms=GAD67;
OS   Pan troglodytes (Chimpanzee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Pan.
OX   NCBI_TaxID=9598;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=15620360; DOI=10.1016/j.cell.2004.11.040;
RA   Dorus S., Vallender E.J., Evans P.D., Anderson J.R., Gilbert S.L.,
RA   Mahowald M., Wyckoff G.J., Malcom C.M., Lahn B.T.;
RT   "Accelerated evolution of nervous system genes in the origin of Homo
RT   sapiens.";
RL   Cell 119:1027-1040(2004).
CC   -!- FUNCTION: Catalyzes the production of GABA.
CC   -!- CATALYTIC ACTIVITY: L-glutamate = 4-aminobutanoate + CO(2).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000305}.
DR   EMBL; AY665260; AAV74298.1; -; mRNA.
DR   RefSeq; NP_001029285.1; NM_001034113.1.
DR   RefSeq; XP_009441979.1; XM_009443704.1.
DR   RefSeq; XP_016804843.1; XM_016949354.1.
DR   UniGene; Ptr.3595; -.
DR   ProteinModelPortal; Q5IS68; -.
DR   SMR; Q5IS68; -.
DR   STRING; 9598.ENSPTRP00000021575; -.
DR   PaxDb; Q5IS68; -.
DR   Ensembl; ENSPTRT00000023393; ENSPTRP00000021575; ENSPTRG00000012626.
DR   GeneID; 468557; -.
DR   KEGG; ptr:468557; -.
DR   CTD; 2571; -.
DR   VGNC; VGNC:436; GAD1.
DR   eggNOG; KOG0629; Eukaryota.
DR   eggNOG; COG0076; LUCA.
DR   GeneTree; ENSGT00760000119205; -.
DR   HOGENOM; HOG000005382; -.
DR   HOVERGEN; HBG004980; -.
DR   InParanoid; Q5IS68; -.
DR   KO; K01580; -.
DR   OMA; FHKHFFQ; -.
DR   OrthoDB; EOG091G07ZU; -.
DR   TreeFam; TF314688; -.
DR   Proteomes; UP000002277; Chromosome 2B.
DR   Bgee; ENSPTRG00000012626; -.
DR   GO; GO:0043679; C:axon terminus; IEA:Ensembl.
DR   GO; GO:0005938; C:cell cortex; IEA:Ensembl.
DR   GO; GO:0060077; C:inhibitory synapse; IEA:Ensembl.
DR   GO; GO:0048786; C:presynaptic active zone; IEA:Ensembl.
DR   GO; GO:0004351; F:glutamate decarboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR   GO; GO:0035641; P:locomotory exploration behavior; IEA:Ensembl.
DR   GO; GO:0042136; P:neurotransmitter biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0035176; P:social behavior; IEA:Ensembl.
DR   Gene3D; 3.40.640.10; -; 1.
DR   InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR021115; Pyridoxal-P_BS.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   PROSITE; PS00392; DDC_GAD_HDC_YDC; 1.
PE   2: Evidence at transcript level;
KW   Complete proteome; Decarboxylase; Lyase;
KW   Neurotransmitter biosynthesis; Phosphoprotein; Pyridoxal phosphate;
KW   Reference proteome.
FT   CHAIN         1    594       Glutamate decarboxylase 1.
FT                                /FTId=PRO_0000146965.
FT   REGION      190    192       Substrate binding. {ECO:0000250}.
FT   BINDING     567    567       Substrate. {ECO:0000250}.
FT   MOD_RES      78     78       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P48318}.
FT   MOD_RES     405    405       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000250}.
SQ   SEQUENCE   594 AA;  66898 MW;  4C1EC330D766EC0B CRC64;
     MASSTPSSSA TSSNAGADPN TTNLRPTTYD TWCGVAHGCT RKLGLKICGF LQRTNSLEEK
     SRLVSAFKER QSSKNLLSCE NSDRDARFRR TETDFSNLFA RDLLPAKNGE EQTVQFLLEV
     VDILLNYVRK TFDRSTKVLD FHHPHQLLEG MEGFNLELSD HPESLEQILV DCRDTLKYGV
     RTGHPRFFNQ LSTGLDIIGL AGEWLTSTAN TNMFTYEIAP VFVLMEQITL KKMREIIGWS
     SKDGDGIFSP GGAISNMYSI MAARYKYFPE VKTKGMAAVP KLVLFTSEQS HYSIKKAGAA
     LGFGTDNVIL IKCNERGKII PADFEAKILE AKQKGYVPFY VNATAGTTVY GAFDPIQEIA
     DICEKYNLWL HVDAAWGGGL LMSRKHRHKL NGIERANSVT WNPHKMMGVL LQCSAILIKE
     KGILQGCNQM CAGYLFQPDK QYDVSYDTGD KAIQCGRHVD IFKFWLMWKA KGTVGFESQI
     NKCLELAEYL YAKIKNREEF EMVFNGEPEH TNVCFWYIPQ SLRGVPDSPQ RREKLHKVAP
     KIKALMMESG TTMVGYQPQG DKANFFRMVI SNPAATQSDI DFLIEEIERL GQDL
//
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