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Database: UniProt/SWISS-PROT
Entry: DCE1_PIG
LinkDB: DCE1_PIG
Original site: DCE1_PIG 
ID   DCE1_PIG                Reviewed;         594 AA.
AC   P48319;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   16-JAN-2019, entry version 103.
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   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
OC   Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   PubMed=7835711; DOI=10.1016/0378-1119(94)00713-3;
RA   Suzuki R., Asami N., Amann E., Wagatsuma M.;
RT   "Sequences of two porcine glutamic acid decarboxylases (65- and 67-kDa
RT   GAD).";
RL   Gene 152:257-260(1995).
CC   -!- FUNCTION: Catalyzes the production of GABA.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + L-glutamate = 4-aminobutanoate + CO2;
CC         Xref=Rhea:RHEA:17785, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:59888; EC=4.1.1.15;
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; D31849; BAA06636.1; -; mRNA.
DR   PIR; JC4065; JC4065.
DR   RefSeq; NP_999059.1; NM_213894.1.
DR   UniGene; Ssc.14526; -.
DR   ProteinModelPortal; P48319; -.
DR   SMR; P48319; -.
DR   STRING; 9823.ENSSSCP00000023541; -.
DR   PaxDb; P48319; -.
DR   PeptideAtlas; P48319; -.
DR   PRIDE; P48319; -.
DR   Ensembl; ENSSSCT00000026586; ENSSSCP00000023541; ENSSSCG00000022233.
DR   Ensembl; ENSSSCT00000066260; ENSSSCP00000051832; ENSSSCG00000022233.
DR   GeneID; 396928; -.
DR   KEGG; ssc:396928; -.
DR   CTD; 2571; -.
DR   eggNOG; KOG0629; Eukaryota.
DR   eggNOG; COG0076; LUCA.
DR   GeneTree; ENSGT00940000155526; -.
DR   HOVERGEN; HBG004980; -.
DR   InParanoid; P48319; -.
DR   KO; K01580; -.
DR   OMA; PTMVTSQ; -.
DR   OrthoDB; 810772at2759; -.
DR   TreeFam; TF314688; -.
DR   Reactome; R-SSC-888568; GABA synthesis.
DR   Reactome; R-SSC-888590; GABA synthesis, release, reuptake and degradation.
DR   Proteomes; UP000008227; Chromosome 15.
DR   Bgee; ENSSSCG00000022233; Expressed in 4 organ(s), highest expression level in prefrontal cortex.
DR   ExpressionAtlas; P48319; baseline and differential.
DR   Genevisible; P48319; SS.
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:0042136; P:neurotransmitter biosynthetic process; IEA:UniProtKB-KW.
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_0000146966.
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;  66895 MW;  42C7954A537862AF CRC64;
     MASSTPSSSA TSSNAGPDPN TTNLRPTTYD TWCGVAHGCT RKLGLKICGF LQRTNSLEEK
     SRLVSAFKER QSSKNLLSCE NSDRDGRFRR TETDFSNLFA RDLLPAKNGE EQTVQFLLEV
     VDILLNYVRK TFDRSTKVLD FHHPHQLLEG MEGFNLELSD HPESLEQILV DCRDTLKYGV
     RTGHPRFFNQ LSTGLDIIGL AGEWLTSTAN TNMFTYEIAP VFVLMEQITL KKMREIVGWS
     NKDGDGIFSP GGAISNMYSI MAARYKYFPE VKTKGMAAVP KLVLFTSEHS HYSIKKAGAA
     LGFGTDNVIL IKCNERGKII PADLEAKILE AKQKGYIPLY VNATAGTTVY GAFDPIQEIA
     DICEKYNLWL HVDAAWGGGL LMSRKHRHKL SGIERADSVT WNPHKMMGVL LQCSAILVKE
     KGILQGCNQM CAGYLFQPDK QYDVSYDTGD KAIQCGRHVD IFKFWLMWKA KGTVGFENQI
     NKCLELAEYL YAKIKNREEF EMVFDGEPEH TNVCFWYIPQ SLRGVPDSPE RREKLHRVAP
     KIKALMMESG TTMVGYQPQG DKANFFRMVI SNPAATQSDI DFLIEEIERL GQDL
//
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