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 03-AUG-2022, entry version 171.
DE RecName: Full=Glutamate decarboxylase 1;
DE EC=4.1.1.15 {ECO:0000269|PubMed:9177246};
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; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC 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 decarboxylase
RT 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 within
RT 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 project:
RT 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 decarboxylase
RT genes in pancreatic beta-cells and other peripheral tissues of mouse and
RT rat.";
RL Endocrinology 133:2962-2972(1993).
RN [6]
RP DISRUPTION PHENOTYPE, FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=9177246; DOI=10.1073/pnas.94.12.6496;
RA Asada H., Kawamura Y., Maruyama K., Kume H., Ding R.G., Kanbara N.,
RA Kuzume H., Sanbo M., Yagi T., Obata K.;
RT "Cleft palate and decreased brain gamma-aminobutyric acid in mice lacking
RT the 67-kDa isoform of glutamic acid decarboxylase.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:6496-6499(1997).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77, AND IDENTIFICATION BY
RP 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 expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Catalyzes the synthesis of the inhibitory neurotransmitter
CC gamma-aminobutyric acid (GABA) with pyridoxal 5'-phosphate as cofactor.
CC {ECO:0000269|PubMed:9177246}.
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 Evidence={ECO:0000269|PubMed:9177246};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17786;
CC Evidence={ECO:0000305|PubMed:9177246};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:9177246};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q99259}.
CC -!- DISRUPTION PHENOTYPE: Deficient mice die at birth with cleft palate and
CC apnea and exhibit reduced levels of glutamic acid decarboxylase and
CC gamma-aminobutyric acid in the cerebral cortex.
CC {ECO:0000269|PubMed:9177246}.
CC -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC {ECO:0000305}.
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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 AlphaFoldDB; P48318; -.
DR SMR; P48318; -.
DR BioGRID; 199814; 10.
DR ComplexPortal; CPX-3061; Glutamate decarboxylase 1 complex.
DR ComplexPortal; CPX-3064; Glutamate decarboxylase 1/2 complex.
DR IntAct; P48318; 1.
DR STRING; 10090.ENSMUSP00000092539; -.
DR iPTMnet; P48318; -.
DR PhosphoSitePlus; P48318; -.
DR SwissPalm; P48318; -.
DR PaxDb; P48318; -.
DR PeptideAtlas; P48318; -.
DR PRIDE; P48318; -.
DR ProteomicsDB; 279836; -.
DR ABCD; P48318; 2 sequenced antibodies.
DR Antibodypedia; 3831; 760 antibodies from 46 providers.
DR DNASU; 14415; -.
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 VEuPathDB; HostDB:ENSMUSG00000070880; -.
DR eggNOG; KOG0629; Eukaryota.
DR GeneTree; ENSGT00940000155526; -.
DR HOGENOM; CLU_011856_0_0_1; -.
DR InParanoid; P48318; -.
DR OMA; RHATYHA; -.
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 BioGRID-ORCS; 14415; 2 hits in 75 CRISPR screens.
DR PRO; PR:P48318; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; P48318; protein.
DR Bgee; ENSMUSG00000070880; Expressed in lateral septal nucleus and 191 other tissues.
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:0016831; F:carboxy-lyase activity; IBA:GO_Central.
DR GO; GO:0016595; F:glutamate binding; ISO:MGI.
DR GO; GO:0004351; F:glutamate decarboxylase activity; IMP:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0047485; F:protein N-terminus binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0030170; F:pyridoxal phosphate binding; ISO:MGI.
DR GO; GO:0009449; P:gamma-aminobutyric acid biosynthetic process; IMP:UniProtKB.
DR GO; GO:0006538; P:glutamate catabolic process; ISO:MGI.
DR GO; GO:0035641; P:locomotory exploration behavior; IMP:MGI.
DR GO; GO:0042136; P:neurotransmitter biosynthetic process; IMP:UniProtKB.
DR GO; GO:0018352; P:protein-pyridoxal-5-phosphate linkage; ISS:UniProtKB.
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 Decarboxylase; Lyase; Neurotransmitter biosynthesis; Phosphoprotein;
KW Pyridoxal phosphate; Reference proteome.
FT CHAIN 1..593
FT /note="Glutamate decarboxylase 1"
FT /id="PRO_0000146964"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 189..191
FT /ligand="4-aminobutanoate"
FT /ligand_id="ChEBI:CHEBI:59888"
FT /evidence="ECO:0000250|UniProtKB:Q99259"
FT BINDING 566
FT /ligand="4-aminobutanoate"
FT /ligand_id="ChEBI:CHEBI:59888"
FT /evidence="ECO:0000250|UniProtKB:Q99259"
FT MOD_RES 77
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 404
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:Q99259"
FT CONFLICT 133
FT /note="R -> H (in Ref. 1; CAA90277)"
FT /evidence="ECO:0000305"
FT CONFLICT 234
FT /note="E -> K (in Ref. 5; S67453)"
FT /evidence="ECO:0000305"
FT CONFLICT 258
FT /note="S -> T (in Ref. 1; CAA90277)"
FT /evidence="ECO:0000305"
FT CONFLICT 360
FT /note="D -> S (in Ref. 1; CAA90277)"
FT /evidence="ECO:0000305"
FT CONFLICT 461
FT /note="F -> N (in Ref. 1; CAA90277)"
FT /evidence="ECO:0000305"
FT CONFLICT 554
FT /note="G -> A (in Ref. 1; CAA90277)"
FT /evidence="ECO:0000305"
FT CONFLICT 575
FT /note="T -> S (in Ref. 1; CAA90277)"
FT /evidence="ECO:0000305"
FT CONFLICT 583
FT /note="I -> T (in Ref. 1; CAA90277)"
FT /evidence="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
