GenomeNet

Database: UniProt/SWISS-PROT
Entry: DCE1_MOUSE
LinkDB: DCE1_MOUSE
Original site: DCE1_MOUSE 
ID   DCE1_MOUSE              Reviewed;         593 AA.
AC   P48318; O08685;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   13-DEC-2002, sequence version 2.
DT   13-FEB-2019, entry version 156.
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   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   PubMed=12106047; DOI=10.1111/j.1460-9568.1990.tb00412.x;
RA   Katarova Z., Szabo G., Mugnaini E., Greenspan R.;
RT   "Molecular identification of the 62 kd form of glutamic acid
RT   decarboxylase from the mouse.";
RL   Eur. J. Neurosci. 2:190-202(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/cJ;
RA   Aust G., Steinbrenner H., Thamm B., Rost A.K., Seissler J.;
RL   Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=ILS, and ISS;
RX   PubMed=11471062; DOI=10.1007/s00335-001-1001-x;
RA   Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J.,
RA   Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M.;
RT   "High-throughput sequence identification of gene coding variants
RT   within alcohol-related QTLs.";
RL   Mamm. Genome 12:657-663(2001).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Retina;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 198-403.
RC   TISSUE=Brain;
RX   PubMed=8243324; DOI=10.1210/endo.133.6.8243324;
RA   Faulkner-Jones B.E., Cram D.S., Kun J., Harrison L.C.;
RT   "Localization and quantitation of expression of two glutamate
RT   decarboxylase genes in pancreatic beta-cells and other peripheral
RT   tissues of mouse and rat.";
RL   Endocrinology 133:2962-2972(1993).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, and Liver;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and
RT   expression.";
RL   Cell 143:1174-1189(2010).
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; Z49976; CAA90277.1; -; mRNA.
DR   EMBL; Y12257; CAA72934.1; -; mRNA.
DR   EMBL; AF483492; AAL90766.1; -; mRNA.
DR   EMBL; AF483493; AAL90767.1; -; mRNA.
DR   EMBL; BC027059; AAH27059.1; -; mRNA.
DR   EMBL; S67453; -; NOT_ANNOTATED_CDS; mRNA.
DR   CCDS; CCDS16108.1; -.
DR   PIR; S61534; S61534.
DR   RefSeq; NP_032103.2; NM_008077.5.
DR   RefSeq; XP_006498828.1; XM_006498765.3.
DR   RefSeq; XP_006498829.1; XM_006498766.3.
DR   UniGene; Mm.272120; -.
DR   ProteinModelPortal; P48318; -.
DR   SMR; P48318; -.
DR   ComplexPortal; CPX-3061; Glutamate decarboxylase 1 complex.
DR   ComplexPortal; CPX-3064; Glutamate decarboxylase 1/2 complex.
DR   IntAct; P48318; 3.
DR   MINT; P48318; -.
DR   STRING; 10090.ENSMUSP00000092539; -.
DR   iPTMnet; P48318; -.
DR   PhosphoSitePlus; P48318; -.
DR   SwissPalm; P48318; -.
DR   PaxDb; P48318; -.
DR   PeptideAtlas; P48318; -.
DR   PRIDE; P48318; -.
DR   Ensembl; ENSMUST00000094934; ENSMUSP00000092539; ENSMUSG00000070880.
DR   GeneID; 14415; -.
DR   KEGG; mmu:14415; -.
DR   UCSC; uc008jzk.1; mouse.
DR   CTD; 2571; -.
DR   MGI; MGI:95632; Gad1.
DR   eggNOG; KOG0629; Eukaryota.
DR   eggNOG; COG0076; LUCA.
DR   GeneTree; ENSGT00940000155526; -.
DR   HOGENOM; HOG000005382; -.
DR   HOVERGEN; HBG004980; -.
DR   InParanoid; P48318; -.
DR   KO; K01580; -.
DR   OMA; PTMVTSQ; -.
DR   OrthoDB; 810772at2759; -.
DR   PhylomeDB; P48318; -.
DR   TreeFam; TF314688; -.
DR   BRENDA; 4.1.1.15; 3474.
DR   Reactome; R-MMU-888568; GABA synthesis.
DR   Reactome; R-MMU-888590; GABA synthesis, release, reuptake and degradation.
DR   PRO; PR:P48318; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   Bgee; ENSMUSG00000070880; Expressed in 208 organ(s), highest expression level in olfactory bulb.
DR   ExpressionAtlas; P48318; baseline and differential.
DR   Genevisible; P48318; MM.
DR   GO; GO:0030424; C:axon; IDA:MGI.
DR   GO; GO:0043679; C:axon terminus; IDA:MGI.
DR   GO; GO:0005938; C:cell cortex; IDA:MGI.
DR   GO; GO:0061202; C:clathrin-sculpted gamma-aminobutyric acid transport vesicle membrane; TAS:Reactome.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0060077; C:inhibitory synapse; IDA:MGI.
DR   GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR   GO; GO:0044306; C:neuron projection terminus; IDA:MGI.
DR   GO; GO:0048786; C:presynaptic active zone; IDA:MGI.
DR   GO; GO:0045202; C:synapse; IDA:MGI.
DR   GO; GO:0016595; F:glutamate binding; ISO:MGI.
DR   GO; GO:0004351; F:glutamate decarboxylase activity; ISO:MGI.
DR   GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
DR   GO; GO:0047485; F:protein N-terminus binding; ISO:MGI.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; ISO:MGI.
DR   GO; GO:0009449; P:gamma-aminobutyric acid biosynthetic process; ISO:MGI.
DR   GO; GO:0035641; P:locomotory exploration behavior; IMP:MGI.
DR   GO; GO:0042493; P:response to drug; IEA:Ensembl.
DR   GO; GO:0035176; P:social behavior; IMP:MGI.
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   1: Evidence at protein level;
KW   Complete proteome; Decarboxylase; Lyase;
KW   Neurotransmitter biosynthesis; Phosphoprotein; Pyridoxal phosphate;
KW   Reference proteome.
FT   CHAIN         1    593       Glutamate decarboxylase 1.
FT                                /FTId=PRO_0000146964.
FT   REGION      189    191       Substrate binding. {ECO:0000250}.
FT   BINDING     566    566       Substrate. {ECO:0000250}.
FT   MOD_RES      77     77       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     404    404       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000250}.
FT   CONFLICT    133    133       R -> H (in Ref. 1; CAA90277).
FT                                {ECO:0000305}.
FT   CONFLICT    234    234       E -> K (in Ref. 5; S67453).
FT                                {ECO:0000305}.
FT   CONFLICT    258    258       S -> T (in Ref. 1; CAA90277).
FT                                {ECO:0000305}.
FT   CONFLICT    360    360       D -> S (in Ref. 1; CAA90277).
FT                                {ECO:0000305}.
FT   CONFLICT    461    461       F -> N (in Ref. 1; CAA90277).
FT                                {ECO:0000305}.
FT   CONFLICT    554    554       G -> A (in Ref. 1; CAA90277).
FT                                {ECO:0000305}.
FT   CONFLICT    575    575       T -> S (in Ref. 1; CAA90277).
FT                                {ECO:0000305}.
FT   CONFLICT    583    583       I -> T (in Ref. 1; CAA90277).
FT                                {ECO:0000305}.
SQ   SEQUENCE   593 AA;  66648 MW;  82D1AAF216F25100 CRC64;
     MASSTPSPAT SSNAGADPNT TNLRPTTYDT WCGVAHGCTR KLGLKICGFL QRTNSLEEKS
     RLVSAFRERQ SSKNLLSCEN SDQGARFRRT ETDFSNLFAQ DLLPAKNGEE QTAQFLLEVV
     DILLNYVRKT FDRSTKVLDF HHPHQLLEGM EGFNLELSDH PESLEQILVD CRDTLKYGVR
     TGHPRFFNQL STGLDIIGLA GEWLTSTANT NMFTYEIAPV FVLMEQITLK KMREIVGWSN
     KDGDGIFSPG GAISNMYSIM AARYKYFPEV KTKGMAAVPK LVLFTSEHSH YSIKKAGAAL
     GFGTDNVILI KCNERGKIIP ADLEAKILDA KQKGYVPLYV NATAGTTVYG AFDPIQEIAD
     ICEKYNLWLH VDAAWGGGLL MSRKHRHKLS GIERANSVTW NPHKMMGVLL QCSAILVKEK
     GILQGCNQMC AGYLFQPDKQ YDVSYDTGDK AIQCGRHVDI FKFWLMWKAK GTVGFENQIN
     KCLELADYLY AKIKNREEFE MVFDGEPEHT NVCFWYIPQS LRGVPDSPER REKLHRVAPK
     IKALMMESGT TMVGYQPQGD KANFFRMVIS NPAATQSDID FLIEEIERLG QDL
//
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