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/"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 //
Ontology (19) GO (19) Disease (1) OMIM (1) Drug (2) DRUGBANK (1) CHEMBL-UP (1) Chemical reaction (2) KEGG ENZYME (1) SABIO-RK-UP (1) Gene (8) KEGG GENES (1) NCBI-Gene (1) HGNC (1) ENSEMBL-UP (5) Protein sequence (4) RefSeq(pep) (2) PMD (2) DNA sequence (5) EMBL (5) 3D Structure (2) PDB (2) Protein domain (6) InterPro (4) Pfam (1) PROSITE (1) Literature (9) PubMed (9) Enzyme (1) BRENDA (1) All databases (59)
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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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 //
Ontology (11) GO (11) Drug (1) DRUGBANK (1) Chemical reaction (1) KEGG ENZYME (1) Gene (2) KEGG GENES (1) NCBI-Gene (1) Protein sequence (2) RefSeq(pep) (2) DNA sequence (3) EMBL (3) Protein domain (6) InterPro (4) Pfam (1) PROSITE (1) Literature (2) PubMed (2) All databases (28)
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