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Database: UniProt/SWISS-PROT UniProt/TrEMBL
Entry: DCE2_HUMAN Q5VZ30_HUMAN
LinkDB: DCE2_HUMAN Q5VZ30_HUMAN
Original site: DCE2_HUMAN Q5VZ30_HUMAN 
ID   DCE2_HUMAN              Reviewed;         585 AA.
AC   Q05329; Q9UD87;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   24-JAN-2024, entry version 191.
DE   RecName: Full=Glutamate decarboxylase 2 {ECO:0000305};
DE            EC=4.1.1.15 {ECO:0000305|PubMed:8999827};
DE   AltName: Full=65 kDa glutamic acid decarboxylase;
DE            Short=GAD-65;
DE   AltName: Full=Glutamate decarboxylase 65 kDa isoform;
GN   Name=GAD2 {ECO:0000312|HGNC:HGNC:4093}; Synonyms=GAD65;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Pancreatic islet;
RX   PubMed=1924293; DOI=10.1073/pnas.88.19.8337;
RA   Karlsen A.E., Hagopian W.A., Grubin C.E., Dube S., Disteche C.M.,
RA   Adler D.A., Barmeier H., Mathewes S., Grant F.J., Foster D., Lernmark A.;
RT   "Cloning and primary structure of a human islet isoform of glutamic acid
RT   decarboxylase from chromosome 10.";
RL   Proc. Natl. Acad. Sci. U.S.A. 88:8337-8341(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1549570; DOI=10.1073/pnas.89.6.2115;
RA   Bu D.-F., Erlander M.G., Hitz B.C., Tillakaratne N.J., Kaufman D.L.,
RA   Wagner-Mcpherson C.B., Evans G.A., Tobin A.J.;
RT   "Two human glutamate decarboxylases, 65-kDa GAD and 67-kDa GAD, are each
RT   encoded by a single gene.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:2115-2119(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8088791; DOI=10.1006/geno.1994.1246;
RA   Bu D.-F., Tobin A.J.;
RT   "The exon-intron organization of the genes (GAD1 and GAD2) encoding two
RT   human glutamate decarboxylases (GAD67 and GAD65) suggests that they derive
RT   from a common ancestral GAD.";
RL   Genomics 21:222-228(1994).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ARG-12; ASN-124; ARG-286
RP   AND GLN-375.
RG   NIEHS SNPs program;
RL   Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 6-585.
RC   TISSUE=Pancreas;
RX   PubMed=7680313; DOI=10.1111/j.1432-1033.1993.tb17698.x;
RA   Mauch L., Abney C.C., Berg H., Scherbaum W.A., Liedvogel B., Northemann W.;
RT   "Characterization of a linear epitope within the human pancreatic 64-kDa
RT   glutamic acid decarboxylase and its autoimmune recognition by sera from
RT   insulin-dependent diabetes mellitus patients.";
RL   Eur. J. Biochem. 212:597-603(1993).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 245-585.
RX   PubMed=8243826; DOI=10.2337/diab.42.12.1799;
RA   Kim J., Richter W., Aanstoot H.-J., Shi Y., Fu Q., Rajotte R., Warnock G.,
RA   Baekkeskov S.;
RT   "Differential expression of GAD65 and GAD67 in human, rat, and mouse
RT   pancreatic islets.";
RL   Diabetes 42:1799-1808(1993).
RN   [7]
RP   PHOSPHORYLATION AT SER-3; SER-6; SER-10 AND SER-13, BIOPHYSICOCHEMICAL
RP   PROPERTIES, CATALYTIC ACTIVITY, FUNCTION, AND MUTAGENESIS OF 3-SER--SER-13.
RX   PubMed=8999827; DOI=10.1074/jbc.272.3.1548;
RA   Namchuk M., Lindsay L., Turck C.W., Kanaani J., Baekkeskov S.;
RT   "Phosphorylation of serine residues 3, 6, 10, and 13 distinguishes membrane
RT   anchored from soluble glutamic acid decarboxylase 65 and is restricted to
RT   glutamic acid decarboxylase 65alpha.";
RL   J. Biol. Chem. 272:1548-1557(1997).
RN   [8]
RP   SUBCELLULAR LOCATION, AND PALMITOYLATION AT CYS-30 AND CYS-45.
RX   PubMed=12356867; DOI=10.1083/jcb.200205053;
RA   Kanaani J., El-Din El-Husseini A., Aguilera-Moreno A., Diacovo J.M.,
RA   Bredt D.S., Baekkeskov S.;
RT   "A combination of three distinct trafficking signals mediates axonal
RT   targeting and presynaptic clustering of GAD65.";
RL   J. Cell Biol. 158:1229-1238(2002).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 222-235 IN COMPLEX WITH MHC.
RX   PubMed=10775108; DOI=10.1126/science.288.5465.505;
RA   Corper A.L., Stratmann T., Apostolopoulos V., Scott C.A., Garcia K.C.,
RA   Kang A.S., Wilson I.A., Teyton L.;
RT   "A structural framework for deciphering the link between I-Ag7 and
RT   autoimmune diabetes.";
RL   Science 288:505-511(2000).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 88-584 IN COMPLEX WITH SUBSTRATE,
RP   SUBUNIT, AND COFACTOR.
RX   PubMed=17384644; DOI=10.1038/nsmb1228;
RA   Fenalti G., Law R.H.P., Buckle A.M., Langendorf C., Tuck K., Rosado C.J.,
RA   Faux N.G., Mahmood K., Hampe C.S., Banga J.P., Wilce M., Schmidberger J.,
RA   Rossjohn J., El-Kabbani O., Pike R.N., Smith A.I., Mackay I.R.,
RA   Rowley M.J., Whisstock J.C.;
RT   "GABA production by glutamic acid decarboxylase is regulated by a dynamic
RT   catalytic loop.";
RL   Nat. Struct. Mol. Biol. 14:280-286(2007).
CC   -!- FUNCTION: Catalyzes the production of GABA.
CC       {ECO:0000305|PubMed:8999827}.
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:0000305|PubMed:8999827};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17786;
CC         Evidence={ECO:0000305|PubMed:8999827};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000269|PubMed:17384644};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=2.15 mM for glutamate {ECO:0000269|PubMed:8999827};
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10775108,
CC       ECO:0000269|PubMed:17384644}.
CC   -!- INTERACTION:
CC       Q05329; Q8WTS1: ABHD5; NbExp=3; IntAct=EBI-9304251, EBI-2813554;
CC       Q05329; Q6RW13: AGTRAP; NbExp=3; IntAct=EBI-9304251, EBI-741181;
CC       Q05329; Q6RW13-2: AGTRAP; NbExp=3; IntAct=EBI-9304251, EBI-11522760;
CC       Q05329; P55056: APOC4; NbExp=3; IntAct=EBI-9304251, EBI-18302142;
CC       Q05329; Q3SXY8: ARL13B; NbExp=3; IntAct=EBI-9304251, EBI-11343438;
CC       Q05329; Q15041: ARL6IP1; NbExp=6; IntAct=EBI-9304251, EBI-714543;
CC       Q05329; Q5T9G4-2: ARMC12; NbExp=3; IntAct=EBI-9304251, EBI-36513937;
CC       Q05329; Q8WZ55: BSND; NbExp=3; IntAct=EBI-9304251, EBI-7996695;
CC       Q05329; Q06432: CACNG1; NbExp=3; IntAct=EBI-9304251, EBI-9686780;
CC       Q05329; Q96DZ9: CMTM5; NbExp=3; IntAct=EBI-9304251, EBI-2548702;
CC       Q05329; Q96DZ9-2: CMTM5; NbExp=3; IntAct=EBI-9304251, EBI-11522780;
CC       Q05329; Q7Z7G2: CPLX4; NbExp=3; IntAct=EBI-9304251, EBI-18013275;
CC       Q05329; Q8N8Q1: CYB561D1; NbExp=3; IntAct=EBI-9304251, EBI-12873482;
CC       Q05329; Q9BUN8: DERL1; NbExp=3; IntAct=EBI-9304251, EBI-398977;
CC       Q05329; Q96Q80: DERL3; NbExp=3; IntAct=EBI-9304251, EBI-12831318;
CC       Q05329; Q6ZPD8: DGAT2L6; NbExp=3; IntAct=EBI-9304251, EBI-12831978;
CC       Q05329; Q6E0U4: DMKN; NbExp=3; IntAct=EBI-9304251, EBI-7943171;
CC       Q05329; Q8N9I5: FADS6; NbExp=3; IntAct=EBI-9304251, EBI-3943864;
CC       Q05329; Q9NRY5: FAM114A2; NbExp=3; IntAct=EBI-9304251, EBI-10973142;
CC       Q05329; Q96GL9: FAM163A; NbExp=3; IntAct=EBI-9304251, EBI-11793142;
CC       Q05329; A8MV81: HIGD1C; NbExp=3; IntAct=EBI-9304251, EBI-12809676;
CC       Q05329; Q96B96: LDAF1; NbExp=6; IntAct=EBI-9304251, EBI-7055862;
CC       Q05329; Q9H400: LIME1; NbExp=3; IntAct=EBI-9304251, EBI-2830566;
CC       Q05329; Q969L2: MAL2; NbExp=6; IntAct=EBI-9304251, EBI-944295;
CC       Q05329; Q5EB52: MEST; NbExp=3; IntAct=EBI-9304251, EBI-1050204;
CC       Q05329; Q9HC36: MRM3; NbExp=3; IntAct=EBI-9304251, EBI-1045440;
CC       Q05329; Q96AL5: PBX3; NbExp=3; IntAct=EBI-9304251, EBI-741171;
CC       Q05329; O60664: PLIN3; NbExp=3; IntAct=EBI-9304251, EBI-725795;
CC       Q05329; Q8IZV5: RDH10; NbExp=3; IntAct=EBI-9304251, EBI-11913715;
CC       Q05329; Q6ZWK4: RHEX; NbExp=3; IntAct=EBI-9304251, EBI-18304046;
CC       Q05329; Q9NS64: RPRM; NbExp=3; IntAct=EBI-9304251, EBI-1052363;
CC       Q05329; O15126: SCAMP1; NbExp=3; IntAct=EBI-9304251, EBI-954338;
CC       Q05329; Q8N3Y7: SDR16C5; NbExp=3; IntAct=EBI-9304251, EBI-3923480;
CC       Q05329; Q96IW7: SEC22A; NbExp=3; IntAct=EBI-9304251, EBI-8652744;
CC       Q05329; O60906: SMPD2; NbExp=3; IntAct=EBI-9304251, EBI-12828299;
CC       Q05329; Q9NZD8: SPG21; NbExp=3; IntAct=EBI-9304251, EBI-742688;
CC       Q05329; Q6PIF2: SYCE2; NbExp=3; IntAct=EBI-9304251, EBI-11958386;
CC       Q05329; O43761: SYNGR3; NbExp=3; IntAct=EBI-9304251, EBI-11321949;
CC       Q05329; A0PK00: TMEM120B; NbExp=3; IntAct=EBI-9304251, EBI-10171534;
CC       Q05329; Q5BJH2-2: TMEM128; NbExp=3; IntAct=EBI-9304251, EBI-10694905;
CC       Q05329; Q9UBN6: TNFRSF10D; NbExp=3; IntAct=EBI-9304251, EBI-1044859;
CC       Q05329; Q86UF1: TSPAN33; NbExp=3; IntAct=EBI-9304251, EBI-12045841;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:12356867}.
CC       Cytoplasmic vesicle {ECO:0000269|PubMed:12356867}. Presynaptic cell
CC       membrane {ECO:0000269|PubMed:12356867}; Lipid-anchor
CC       {ECO:0000269|PubMed:12356867}. Golgi apparatus membrane
CC       {ECO:0000269|PubMed:12356867}; Peripheral membrane protein
CC       {ECO:0000269|PubMed:12356867}; Cytoplasmic side
CC       {ECO:0000269|PubMed:12356867}. Note=Associated to cytoplasmic vesicles.
CC       In neurons, cytosolic leaflet of Golgi membranes and presynaptic
CC       clusters.
CC   -!- PTM: Phosphorylated; which does not affect kinetic parameters or
CC       subcellular location. {ECO:0000269|PubMed:8999827}.
CC   -!- PTM: Palmitoylated; which is required for presynaptic clustering.
CC       {ECO:0000269|PubMed:12356867}.
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA49554.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC       URL="http://egp.gs.washington.edu/data/gad2/";
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DR   EMBL; M81882; AAA62367.1; -; mRNA.
DR   EMBL; M74826; AAA58491.1; -; mRNA.
DR   EMBL; AY340073; AAP88040.1; -; Genomic_DNA.
DR   EMBL; X69936; CAA49554.1; ALT_INIT; mRNA.
DR   EMBL; M70435; AAA52513.1; -; mRNA.
DR   CCDS; CCDS7149.1; -.
DR   PIR; A41935; A41292.
DR   RefSeq; NP_000809.1; NM_000818.2.
DR   RefSeq; NP_001127838.1; NM_001134366.1.
DR   PDB; 1ES0; X-ray; 2.60 A; B=207-220.
DR   PDB; 2OKK; X-ray; 2.30 A; A=88-584.
DR   PDBsum; 1ES0; -.
DR   PDBsum; 2OKK; -.
DR   AlphaFoldDB; Q05329; -.
DR   SMR; Q05329; -.
DR   BioGRID; 108846; 46.
DR   ComplexPortal; CPX-3033; Glutamate decarboxylase 2 complex.
DR   ComplexPortal; CPX-3065; Glutamate decarboxylase 1/2 complex.
DR   DIP; DIP-29293N; -.
DR   IntAct; Q05329; 41.
DR   STRING; 9606.ENSP00000365437; -.
DR   ChEMBL; CHEMBL2952; -.
DR   DrugBank; DB00142; Glutamic acid.
DR   iPTMnet; Q05329; -.
DR   PhosphoSitePlus; Q05329; -.
DR   SwissPalm; Q05329; -.
DR   BioMuta; GAD2; -.
DR   DMDM; 1352216; -.
DR   jPOST; Q05329; -.
DR   MassIVE; Q05329; -.
DR   PaxDb; 9606-ENSP00000365437; -.
DR   PeptideAtlas; Q05329; -.
DR   ProteomicsDB; 58319; -.
DR   ABCD; Q05329; 12 sequenced antibodies.
DR   Antibodypedia; 3635; 869 antibodies from 44 providers.
DR   DNASU; 2572; -.
DR   Ensembl; ENST00000259271.7; ENSP00000259271.3; ENSG00000136750.13.
DR   Ensembl; ENST00000376261.8; ENSP00000365437.3; ENSG00000136750.13.
DR   GeneID; 2572; -.
DR   KEGG; hsa:2572; -.
DR   MANE-Select; ENST00000376261.8; ENSP00000365437.3; NM_001134366.2; NP_001127838.1.
DR   AGR; HGNC:4093; -.
DR   CTD; 2572; -.
DR   DisGeNET; 2572; -.
DR   GeneCards; GAD2; -.
DR   HGNC; HGNC:4093; GAD2.
DR   HPA; ENSG00000136750; Tissue enriched (brain).
DR   MIM; 138275; gene.
DR   neXtProt; NX_Q05329; -.
DR   OpenTargets; ENSG00000136750; -.
DR   PharmGKB; PA28508; -.
DR   VEuPathDB; HostDB:ENSG00000136750; -.
DR   eggNOG; KOG0629; Eukaryota.
DR   GeneTree; ENSGT00940000157951; -.
DR   HOGENOM; CLU_011856_0_0_1; -.
DR   InParanoid; Q05329; -.
DR   OMA; VACTCDQ; -.
DR   OrthoDB; 888358at2759; -.
DR   PhylomeDB; Q05329; -.
DR   TreeFam; TF314688; -.
DR   BioCyc; MetaCyc:HS06208-MONOMER; -.
DR   BRENDA; 4.1.1.15; 2681.
DR   PathwayCommons; Q05329; -.
DR   Reactome; R-HSA-888568; GABA synthesis.
DR   Reactome; R-HSA-888590; GABA synthesis, release, reuptake and degradation.
DR   Reactome; R-HSA-9022927; MECP2 regulates transcription of genes involved in GABA signaling.
DR   SABIO-RK; Q05329; -.
DR   SignaLink; Q05329; -.
DR   SIGNOR; Q05329; -.
DR   BioGRID-ORCS; 2572; 12 hits in 1152 CRISPR screens.
DR   ChiTaRS; GAD2; human.
DR   EvolutionaryTrace; Q05329; -.
DR   GeneWiki; GAD2; -.
DR   GenomeRNAi; 2572; -.
DR   Pharos; Q05329; Tbio.
DR   PRO; PR:Q05329; -.
DR   Proteomes; UP000005640; Chromosome 10.
DR   RNAct; Q05329; Protein.
DR   Bgee; ENSG00000136750; Expressed in islet of Langerhans and 90 other cell types or tissues.
DR   ExpressionAtlas; Q05329; baseline and differential.
DR   Genevisible; Q05329; HS.
DR   GO; GO:0030424; C:axon; IEA:Ensembl.
DR   GO; GO:0061202; C:clathrin-sculpted gamma-aminobutyric acid transport vesicle membrane; TAS:Reactome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0098982; C:GABA-ergic synapse; IEA:Ensembl.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0060077; C:inhibitory synapse; IEA:Ensembl.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0042734; C:presynaptic membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030672; C:synaptic vesicle membrane; IEA:Ensembl.
DR   GO; GO:0016595; F:glutamate binding; IEA:Ensembl.
DR   GO; GO:0004351; F:glutamate decarboxylase activity; IBA:GO_Central.
DR   GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:Ensembl.
DR   GO; GO:0007268; P:chemical synaptic transmission; TAS:ProtInc.
DR   GO; GO:0009449; P:gamma-aminobutyric acid biosynthetic process; IBA:GO_Central.
DR   GO; GO:0006540; P:glutamate decarboxylation to succinate; IBA:GO_Central.
DR   GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR   CDD; cd06450; DOPA_deC_like; 1.
DR   Gene3D; 3.90.1150.170; -; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 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   PANTHER; PTHR45677:SF11; GLUTAMATE DECARBOXYLASE 2; 1.
DR   PANTHER; PTHR45677; GLUTAMATE DECARBOXYLASE-RELATED; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00392; DDC_GAD_HDC_YDC; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell membrane; Cell projection; Cytoplasm;
KW   Cytoplasmic vesicle; Decarboxylase; Golgi apparatus; Lipoprotein; Lyase;
KW   Membrane; Neurotransmitter biosynthesis; Palmitate; Phosphoprotein;
KW   Pyridoxal phosphate; Reference proteome; Synapse.
FT   CHAIN           1..585
FT                   /note="Glutamate decarboxylase 2"
FT                   /id="PRO_0000146968"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         181..183
FT                   /ligand="substrate"
FT   BINDING         558
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:17384644"
FT   MOD_RES         3
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:8999827"
FT   MOD_RES         6
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:8999827"
FT   MOD_RES         10
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:8999827"
FT   MOD_RES         13
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:8999827"
FT   MOD_RES         396
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT   LIPID           30
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000269|PubMed:12356867"
FT   LIPID           45
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000269|PubMed:12356867"
FT   VARIANT         12
FT                   /note="G -> R (in dbSNP:rs8190591)"
FT                   /evidence="ECO:0000269|Ref.4"
FT                   /id="VAR_018821"
FT   VARIANT         124
FT                   /note="K -> N (in dbSNP:rs8190600)"
FT                   /evidence="ECO:0000269|Ref.4"
FT                   /id="VAR_018822"
FT   VARIANT         153
FT                   /note="P -> Q (in dbSNP:rs2839672)"
FT                   /id="VAR_029176"
FT   VARIANT         232
FT                   /note="G -> E (in dbSNP:rs2839673)"
FT                   /id="VAR_029177"
FT   VARIANT         286
FT                   /note="K -> R (in dbSNP:rs8190671)"
FT                   /evidence="ECO:0000269|Ref.4"
FT                   /id="VAR_018823"
FT   VARIANT         326
FT                   /note="G -> A (in dbSNP:rs2839678)"
FT                   /id="VAR_029178"
FT   VARIANT         375
FT                   /note="R -> Q (in dbSNP:rs8190730)"
FT                   /evidence="ECO:0000269|Ref.4"
FT                   /id="VAR_018824"
FT   MUTAGEN         3..13
FT                   /note="SPGSGFWSFGS->APGAGFWAFGA: No effect on glutamate
FT                   decarboxylase activity."
FT                   /evidence="ECO:0000269|PubMed:8999827"
FT   HELIX           89..91
FT                   /evidence="ECO:0007829|PDB:2OKK"
FT   HELIX           94..96
FT                   /evidence="ECO:0007829|PDB:2OKK"
FT   HELIX           104..126
FT                   /evidence="ECO:0007829|PDB:2OKK"
FT   HELIX           138..144
FT                   /evidence="ECO:0007829|PDB:2OKK"
FT   HELIX           156..169
FT                   /evidence="ECO:0007829|PDB:2OKK"
FT   STRAND          178..183
FT                   /evidence="ECO:0007829|PDB:2OKK"
FT   HELIX           188..200
FT                   /evidence="ECO:0007829|PDB:2OKK"
FT   TURN            207..209
FT                   /evidence="ECO:0007829|PDB:2OKK"
FT   HELIX           211..228
FT                   /evidence="ECO:0007829|PDB:2OKK"
FT   HELIX           231..233
FT                   /evidence="ECO:0007829|PDB:2OKK"
FT   STRAND          235..242
FT                   /evidence="ECO:0007829|PDB:2OKK"
FT   HELIX           243..258
FT                   /evidence="ECO:0007829|PDB:2OKK"
FT   HELIX           262..265
FT                   /evidence="ECO:0007829|PDB:2OKK"
FT   HELIX           267..269
FT                   /evidence="ECO:0007829|PDB:2OKK"
FT   STRAND          273..278
FT                   /evidence="ECO:0007829|PDB:2OKK"
FT   HELIX           284..291
FT                   /evidence="ECO:0007829|PDB:2OKK"
FT   HELIX           296..298
FT                   /evidence="ECO:0007829|PDB:2OKK"
FT   STRAND          299..302
FT                   /evidence="ECO:0007829|PDB:2OKK"
FT   HELIX           312..324
FT                   /evidence="ECO:0007829|PDB:2OKK"
FT   STRAND          328..337
FT                   /evidence="ECO:0007829|PDB:2OKK"
FT   TURN            339..341
FT                   /evidence="ECO:0007829|PDB:2OKK"
FT   HELIX           347..357
FT                   /evidence="ECO:0007829|PDB:2OKK"
FT   STRAND          360..365
FT                   /evidence="ECO:0007829|PDB:2OKK"
FT   HELIX           368..373
FT                   /evidence="ECO:0007829|PDB:2OKK"
FT   TURN            375..377
FT                   /evidence="ECO:0007829|PDB:2OKK"
FT   HELIX           378..381
FT                   /evidence="ECO:0007829|PDB:2OKK"
FT   HELIX           384..386
FT                   /evidence="ECO:0007829|PDB:2OKK"
FT   STRAND          388..392
FT                   /evidence="ECO:0007829|PDB:2OKK"
FT   STRAND          405..411
FT                   /evidence="ECO:0007829|PDB:2OKK"
FT   HELIX           414..419
FT                   /evidence="ECO:0007829|PDB:2OKK"
FT   HELIX           435..437
FT                   /evidence="ECO:0007829|PDB:2OKK"
FT   HELIX           440..442
FT                   /evidence="ECO:0007829|PDB:2OKK"
FT   HELIX           452..486
FT                   /evidence="ECO:0007829|PDB:2OKK"
FT   STRAND          491..497
FT                   /evidence="ECO:0007829|PDB:2OKK"
FT   STRAND          500..502
FT                   /evidence="ECO:0007829|PDB:2OKK"
FT   STRAND          504..508
FT                   /evidence="ECO:0007829|PDB:2OKK"
FT   TURN            511..515
FT                   /evidence="ECO:0007829|PDB:2OKK"
FT   HELIX           523..526
FT                   /evidence="ECO:0007829|PDB:2OKK"
FT   HELIX           529..540
FT                   /evidence="ECO:0007829|PDB:2OKK"
FT   STRAND          544..550
FT                   /evidence="ECO:0007829|PDB:2OKK"
FT   STRAND          553..559
FT                   /evidence="ECO:0007829|PDB:2OKK"
FT   HELIX           568..581
FT                   /evidence="ECO:0007829|PDB:2OKK"
SQ   SEQUENCE   585 AA;  65411 MW;  0322509F0E2C32EE CRC64;
     MASPGSGFWS FGSEDGSGDS ENPGTARAWC QVAQKFTGGI GNKLCALLYG DAEKPAESGG
     SQPPRAAARK AACACDQKPC SCSKVDVNYA FLHATDLLPA CDGERPTLAF LQDVMNILLQ
     YVVKSFDRST KVIDFHYPNE LLQEYNWELA DQPQNLEEIL MHCQTTLKYA IKTGHPRYFN
     QLSTGLDMVG LAADWLTSTA NTNMFTYEIA PVFVLLEYVT LKKMREIIGW PGGSGDGIFS
     PGGAISNMYA MMIARFKMFP EVKEKGMAAL PRLIAFTSEH SHFSLKKGAA ALGIGTDSVI
     LIKCDERGKM IPSDLERRIL EAKQKGFVPF LVSATAGTTV YGAFDPLLAV ADICKKYKIW
     MHVDAAWGGG LLMSRKHKWK LSGVERANSV TWNPHKMMGV PLQCSALLVR EEGLMQNCNQ
     MHASYLFQQD KHYDLSYDTG DKALQCGRHV DVFKLWLMWR AKGTTGFEAH VDKCLELAEY
     LYNIIKNREG YEMVFDGKPQ HTNVCFWYIP PSLRTLEDNE ERMSRLSKVA PVIKARMMEY
     GTTMVSYQPL GDKVNFFRMV ISNPAATHQD IDFLIEEIER LGQDL
//
ID   Q5VZ30_HUMAN            Unreviewed;       585 AA.
AC   Q5VZ30;
DT   10-MAY-2005, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2005, sequence version 1.
DT   24-JAN-2024, entry version 153.
DE   RecName: Full=Glutamate decarboxylase 2 {ECO:0000256|ARBA:ARBA00040577};
DE            EC=4.1.1.15 {ECO:0000256|ARBA:ARBA00012421};
DE   AltName: Full=65 kDa glutamic acid decarboxylase {ECO:0000256|ARBA:ARBA00043203};
DE   AltName: Full=Glutamate decarboxylase 65 kDa isoform {ECO:0000256|ARBA:ARBA00041381};
GN   Name=GAD2 {ECO:0000313|EMBL:AAI26330.1};
GN   ORFNames=hCG_23434 {ECO:0000313|EMBL:EAW86102.1};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606 {ECO:0000313|EMBL:AAI26330.1};
RN   [1] {ECO:0000313|EMBL:EAW86102.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=11181995; DOI=10.1126/science.1058040;
RA   Venter J.C., Adams M.D., Myers E.W., Li P.W., Mural R.J., Sutton G.G.,
RA   Smith H.O., Yandell M., Evans C.A., Holt R.A., Gocayne J.D., Amanatides P.,
RA   Ballew R.M., Huson D.H., Wortman J.R., Zhang Q., Kodira C.D., Zheng X.H.,
RA   Chen L., Skupski M., Subramanian G., Thomas P.D., Zhang J.,
RA   Gabor Miklos G.L., Nelson C., Broder S., Clark A.G., Nadeau J.,
RA   McKusick V.A., Zinder N., Levine A.J., Roberts R.J., Simon M., Slayman C.,
RA   Hunkapiller M., Bolanos R., Delcher A., Dew I., Fasulo D., Flanigan M.,
RA   Florea L., Halpern A., Hannenhalli S., Kravitz S., Levy S., Mobarry C.,
RA   Reinert K., Remington K., Abu-Threideh J., Beasley E., Biddick K.,
RA   Bonazzi V., Brandon R., Cargill M., Chandramouliswaran I., Charlab R.,
RA   Chaturvedi K., Deng Z., Di Francesco V., Dunn P., Eilbeck K.,
RA   Evangelista C., Gabrielian A.E., Gan W., Ge W., Gong F., Gu Z., Guan P.,
RA   Heiman T.J., Higgins M.E., Ji R.R., Ke Z., Ketchum K.A., Lai Z., Lei Y.,
RA   Li Z., Li J., Liang Y., Lin X., Lu F., Merkulov G.V., Milshina N.,
RA   Moore H.M., Naik A.K., Narayan V.A., Neelam B., Nusskern D., Rusch D.B.,
RA   Salzberg S., Shao W., Shue B., Sun J., Wang Z., Wang A., Wang X., Wang J.,
RA   Wei M., Wides R., Xiao C., Yan C., Yao A., Ye J., Zhan M., Zhang W.,
RA   Zhang H., Zhao Q., Zheng L., Zhong F., Zhong W., Zhu S., Zhao S.,
RA   Gilbert D., Baumhueter S., Spier G., Carter C., Cravchik A., Woodage T.,
RA   Ali F., An H., Awe A., Baldwin D., Baden H., Barnstead M., Barrow I.,
RA   Beeson K., Busam D., Carver A., Center A., Cheng M.L., Curry L.,
RA   Danaher S., Davenport L., Desilets R., Dietz S., Dodson K., Doup L.,
RA   Ferriera S., Garg N., Gluecksmann A., Hart B., Haynes J., Haynes C.,
RA   Heiner C., Hladun S., Hostin D., Houck J., Howland T., Ibegwam C.,
RA   Johnson J., Kalush F., Kline L., Koduru S., Love A., Mann F., May D.,
RA   McCawley S., McIntosh T., McMullen I., Moy M., Moy L., Murphy B.,
RA   Nelson K., Pfannkoch C., Pratts E., Puri V., Qureshi H., Reardon M.,
RA   Rodriguez R., Rogers Y.H., Romblad D., Ruhfel B., Scott R., Sitter C.,
RA   Smallwood M., Stewart E., Strong R., Suh E., Thomas R., Tint N.N., Tse S.,
RA   Vech C., Wang G., Wetter J., Williams S., Williams M., Windsor S.,
RA   Winn-Deen E., Wolfe K., Zaveri J., Zaveri K., Abril J.F., Guigo R.,
RA   Campbell M.J., Sjolander K.V., Karlak B., Kejariwal A., Mi H., Lazareva B.,
RA   Hatton T., Narechania A., Diemer K., Muruganujan A., Guo N., Sato S.,
RA   Bafna V., Istrail S., Lippert R., Schwartz R., Walenz B., Yooseph S.,
RA   Allen D., Basu A., Baxendale J., Blick L., Caminha M., Carnes-Stine J.,
RA   Caulk P., Chiang Y.H., Coyne M., Dahlke C., Mays A., Dombroski M.,
RA   Donnelly M., Ely D., Esparham S., Fosler C., Gire H., Glanowski S.,
RA   Glasser K., Glodek A., Gorokhov M., Graham K., Gropman B., Harris M.,
RA   Heil J., Henderson S., Hoover J., Jennings D., Jordan C., Jordan J.,
RA   Kasha J., Kagan L., Kraft C., Levitsky A., Lewis M., Liu X., Lopez J.,
RA   Ma D., Majoros W., McDaniel J., Murphy S., Newman M., Nguyen T., Nguyen N.,
RA   Nodell M., Pan S., Peck J., Peterson M., Rowe W., Sanders R., Scott J.,
RA   Simpson M., Smith T., Sprague A., Stockwell T., Turner R., Venter E.,
RA   Wang M., Wen M., Wu D., Wu M., Xia A., Zandieh A., Zhu X.;
RT   "The sequence of the human genome.";
RL   Science 291:1304-1351(2001).
RN   [2] {ECO:0000313|EMBL:AAI26330.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain {ECO:0000313|EMBL:AAI26330.1};
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RA   Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H.,
RA   Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M.,
RA   Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M.,
RA   Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F.,
RA   Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T.,
RA   Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F.,
RA   Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E.,
RA   Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y.,
RA   Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E.,
RA   Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y.,
RA   Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W.,
RA   Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J.,
RA   Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA   Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J.,
RA   Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W.,
RA   Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J.,
RA   Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I.,
RA   Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U.,
RA   Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A.,
RA   Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.;
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   [3] {ECO:0000313|EMBL:EAW86102.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the production of GABA.
CC       {ECO:0000256|ARBA:ARBA00037048}.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|PIRSR:PIRSR602129-50, ECO:0000256|RuleBase:RU000382};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004193};
CC       Lipid-anchor {ECO:0000256|ARBA:ARBA00004193}. Cytoplasm, cytosol
CC       {ECO:0000256|ARBA:ARBA00004514}. Cytoplasmic vesicle
CC       {ECO:0000256|ARBA:ARBA00004541}. Golgi apparatus membrane
CC       {ECO:0000256|ARBA:ARBA00004255}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004255}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004255}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004635}; Lipid-anchor
CC       {ECO:0000256|ARBA:ARBA00004635}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004287}. Presynaptic cell membrane
CC       {ECO:0000256|ARBA:ARBA00037840}; Lipid-anchor
CC       {ECO:0000256|ARBA:ARBA00037840}. Vesicle
CC       {ECO:0000256|ARBA:ARBA00004373}.
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000256|ARBA:ARBA00009533, ECO:0000256|RuleBase:RU000382}.
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DR   EMBL; BC126327; AAI26328.1; -; mRNA.
DR   EMBL; BC126329; AAI26330.1; -; mRNA.
DR   EMBL; CH471072; EAW86102.1; -; Genomic_DNA.
DR   RefSeq; NP_000809.1; NM_000818.2.
DR   RefSeq; NP_001127838.1; NM_001134366.1.
DR   SMR; Q5VZ30; -.
DR   DrugBank; DB00114; Pyridoxal phosphate.
DR   Antibodypedia; 3635; 869 antibodies from 44 providers.
DR   DNASU; 2572; -.
DR   GeneID; 2572; -.
DR   KEGG; hsa:2572; -.
DR   UCSC; uc001isp.3; human.
DR   CTD; 2572; -.
DR   PharmGKB; PA28508; -.
DR   VEuPathDB; HostDB:ENSG00000136750; -.
DR   HOGENOM; CLU_011856_0_0_1; -.
DR   OMA; VACTCDQ; -.
DR   OrthoDB; 888358at2759; -.
DR   BioGRID-ORCS; 2572; 12 hits in 1152 CRISPR screens.
DR   ChiTaRS; GAD2; human.
DR   GenomeRNAi; 2572; -.
DR   ExpressionAtlas; Q5VZ30; baseline and differential.
DR   GO; GO:0030424; C:axon; IEA:Ensembl.
DR   GO; GO:0098982; C:GABA-ergic synapse; IEA:Ensembl.
DR   GO; GO:0060077; C:inhibitory synapse; IEA:Ensembl.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR   GO; GO:0030672; C:synaptic vesicle membrane; IEA:Ensembl.
DR   GO; GO:0016595; F:glutamate binding; IEA:Ensembl.
DR   GO; GO:0004351; F:glutamate decarboxylase activity; IEA:Ensembl.
DR   GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:Ensembl.
DR   GO; GO:0006540; P:glutamate decarboxylation to succinate; IEA:Ensembl.
DR   GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR   CDD; cd06450; DOPA_deC_like; 1.
DR   Gene3D; 3.90.1150.170; -; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 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   PANTHER; PTHR45677:SF11; GLUTAMATE DECARBOXYLASE 2; 1.
DR   PANTHER; PTHR45677; GLUTAMATE DECARBOXYLASE-RELATED; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00392; DDC_GAD_HDC_YDC; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW   Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW   Decarboxylase {ECO:0000256|ARBA:ARBA00022793};
KW   Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW   Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000382};
KW   Membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Palmitate {ECO:0000256|ARBA:ARBA00023139};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU000382}; Synapse {ECO:0000256|ARBA:ARBA00023018}.
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         396
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   585 AA;  65411 MW;  0322509F0E2C32EE CRC64;
     MASPGSGFWS FGSEDGSGDS ENPGTARAWC QVAQKFTGGI GNKLCALLYG DAEKPAESGG
     SQPPRAAARK AACACDQKPC SCSKVDVNYA FLHATDLLPA CDGERPTLAF LQDVMNILLQ
     YVVKSFDRST KVIDFHYPNE LLQEYNWELA DQPQNLEEIL MHCQTTLKYA IKTGHPRYFN
     QLSTGLDMVG LAADWLTSTA NTNMFTYEIA PVFVLLEYVT LKKMREIIGW PGGSGDGIFS
     PGGAISNMYA MMIARFKMFP EVKEKGMAAL PRLIAFTSEH SHFSLKKGAA ALGIGTDSVI
     LIKCDERGKM IPSDLERRIL EAKQKGFVPF LVSATAGTTV YGAFDPLLAV ADICKKYKIW
     MHVDAAWGGG LLMSRKHKWK LSGVERANSV TWNPHKMMGV PLQCSALLVR EEGLMQNCNQ
     MHASYLFQQD KHYDLSYDTG DKALQCGRHV DVFKLWLMWR AKGTTGFEAH VDKCLELAEY
     LYNIIKNREG YEMVFDGKPQ HTNVCFWYIP PSLRTLEDNE ERMSRLSKVA PVIKARMMEY
     GTTMVSYQPL GDKVNFFRMV ISNPAATHQD IDFLIEEIER LGQDL
//
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