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Glutamate decarboxylase 1 (EC 4.1.1.15) (67 kDa glutamic acid decarboxylase) (GAD-67) (Glutamate decarboxylase 67 kDa isoform)

 DCE1_MOUSE              Reviewed;         593 AA.
P48318; O08685;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
13-DEC-2002, sequence version 2.
07-JUN-2017, entry version 147.
RecName: Full=Glutamate decarboxylase 1;
EC=4.1.1.15;
AltName: Full=67 kDa glutamic acid decarboxylase;
Short=GAD-67;
AltName: Full=Glutamate decarboxylase 67 kDa isoform;
Name=Gad1; Synonyms=Gad67;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
PubMed=12106047; DOI=10.1111/j.1460-9568.1990.tb00412.x;
Katarova Z., Szabo G., Mugnaini E., Greenspan R.;
"Molecular identification of the 62 kd form of glutamic acid
decarboxylase from the mouse.";
Eur. J. Neurosci. 2:190-202(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=BALB/cJ;
Aust G., Steinbrenner H., Thamm B., Rost A.K., Seissler J.;
Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=ILS, and ISS;
PubMed=11471062; DOI=10.1007/s00335-001-1001-x;
Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J.,
Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M.;
"High-throughput sequence identification of gene coding variants
within alcohol-related QTLs.";
Mamm. Genome 12:657-663(2001).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Retina;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 198-403.
TISSUE=Brain;
PubMed=8243324; DOI=10.1210/endo.133.6.8243324;
Faulkner-Jones B.E., Cram D.S., Kun J., Harrison L.C.;
"Localization and quantitation of expression of two glutamate
decarboxylase genes in pancreatic beta-cells and other peripheral
tissues of mouse and rat.";
Endocrinology 133:2962-2972(1993).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, and Liver;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Catalyzes the production of GABA.
-!- CATALYTIC ACTIVITY: L-glutamate = 4-aminobutanoate + CO(2).
-!- COFACTOR:
Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
-!- SUBUNIT: Homodimer. {ECO:0000250}.
-!- SIMILARITY: Belongs to the group II decarboxylase family.
{ECO:0000305}.
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EMBL; Z49976; CAA90277.1; -; mRNA.
EMBL; Y12257; CAA72934.1; -; mRNA.
EMBL; AF483492; AAL90766.1; -; mRNA.
EMBL; AF483493; AAL90767.1; -; mRNA.
EMBL; BC027059; AAH27059.1; -; mRNA.
EMBL; S67453; -; NOT_ANNOTATED_CDS; mRNA.
CCDS; CCDS16108.1; -.
PIR; S61534; S61534.
RefSeq; NP_032103.2; NM_008077.5.
RefSeq; XP_006498828.1; XM_006498765.3.
RefSeq; XP_006498829.1; XM_006498766.3.
UniGene; Mm.272120; -.
ProteinModelPortal; P48318; -.
SMR; P48318; -.
IntAct; P48318; 3.
MINT; MINT-4092862; -.
STRING; 10090.ENSMUSP00000092539; -.
iPTMnet; P48318; -.
PhosphoSitePlus; P48318; -.
SwissPalm; P48318; -.
PaxDb; P48318; -.
PeptideAtlas; P48318; -.
PRIDE; P48318; -.
Ensembl; ENSMUST00000094934; ENSMUSP00000092539; ENSMUSG00000070880.
GeneID; 14415; -.
KEGG; mmu:14415; -.
UCSC; uc008jzk.1; mouse.
CTD; 2571; -.
MGI; MGI:95632; Gad1.
eggNOG; KOG0629; Eukaryota.
eggNOG; COG0076; LUCA.
GeneTree; ENSGT00760000119205; -.
HOGENOM; HOG000005382; -.
HOVERGEN; HBG004980; -.
InParanoid; P48318; -.
KO; K01580; -.
OMA; TVNPHKM; -.
OrthoDB; EOG091G07ZU; -.
PhylomeDB; P48318; -.
TreeFam; TF314688; -.
BRENDA; 4.1.1.15; 3474.
Reactome; R-MMU-888568; GABA synthesis.
Reactome; R-MMU-888590; GABA synthesis, release, reuptake and degradation.
PRO; PR:P48318; -.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000070880; -.
CleanEx; MM_GAD1; -.
ExpressionAtlas; P48318; baseline and differential.
Genevisible; P48318; MM.
GO; GO:0030424; C:axon; IDA:MGI.
GO; GO:0043679; C:axon terminus; IDA:MGI.
GO; GO:0005938; C:cell cortex; IDA:MGI.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0060077; C:inhibitory synapse; IDA:MGI.
GO; GO:0005622; C:intracellular; ISO:MGI.
GO; GO:0005739; C:mitochondrion; IDA:MGI.
GO; GO:0044306; C:neuron projection terminus; IDA:MGI.
GO; GO:0048786; C:presynaptic active zone; IDA:MGI.
GO; GO:0045202; C:synapse; IDA:MGI.
GO; GO:0016595; F:glutamate binding; IEA:Ensembl.
GO; GO:0004351; F:glutamate decarboxylase activity; ISO:MGI.
GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
GO; GO:0047485; F:protein N-terminus binding; IEA:Ensembl.
GO; GO:0030170; F:pyridoxal phosphate binding; IEA:Ensembl.
GO; GO:0009449; P:gamma-aminobutyric acid biosynthetic process; IEA:Ensembl.
GO; GO:0035641; P:locomotory exploration behavior; IMP:MGI.
GO; GO:0042136; P:neurotransmitter biosynthetic process; IEA:UniProtKB-KW.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0035176; P:social behavior; IMP:MGI.
Gene3D; 3.40.640.10; -; 1.
Gene3D; 3.90.1150.10; -; 1.
InterPro; IPR002129; PyrdxlP-dep_de-COase.
InterPro; IPR015424; PyrdxlP-dep_Trfase.
InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
InterPro; IPR015422; PyrdxlP-dep_Trfase_sub2.
InterPro; IPR021115; Pyridoxal-P_BS.
Pfam; PF00282; Pyridoxal_deC; 1.
SUPFAM; SSF53383; SSF53383; 1.
PROSITE; PS00392; DDC_GAD_HDC_YDC; 1.
1: Evidence at protein level;
Complete proteome; Decarboxylase; Lyase;
Neurotransmitter biosynthesis; Phosphoprotein; Pyridoxal phosphate;
Reference proteome.
CHAIN 1 593 Glutamate decarboxylase 1.
/FTId=PRO_0000146964.
REGION 189 191 Substrate binding. {ECO:0000250}.
BINDING 566 566 Substrate. {ECO:0000250}.
MOD_RES 77 77 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 404 404 N6-(pyridoxal phosphate)lysine.
{ECO:0000250}.
CONFLICT 133 133 R -> H (in Ref. 1; CAA90277).
{ECO:0000305}.
CONFLICT 234 234 E -> K (in Ref. 5; S67453).
{ECO:0000305}.
CONFLICT 258 258 S -> T (in Ref. 1; CAA90277).
{ECO:0000305}.
CONFLICT 360 360 D -> S (in Ref. 1; CAA90277).
{ECO:0000305}.
CONFLICT 461 461 F -> N (in Ref. 1; CAA90277).
{ECO:0000305}.
CONFLICT 554 554 G -> A (in Ref. 1; CAA90277).
{ECO:0000305}.
CONFLICT 575 575 T -> S (in Ref. 1; CAA90277).
{ECO:0000305}.
CONFLICT 583 583 I -> T (in Ref. 1; CAA90277).
{ECO:0000305}.
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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