ID G3WJK8_SARHA Unreviewed; 587 AA.
AC G3WJK8;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 63.
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|Ensembl:ENSSHAP00000015613.1};
OS Sarcophilus harrisii (Tasmanian devil) (Sarcophilus laniarius).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Metatheria; Dasyuromorphia; Dasyuridae; Sarcophilus.
OX NCBI_TaxID=9305 {ECO:0000313|Ensembl:ENSSHAP00000015613.1, ECO:0000313|Proteomes:UP000007648};
RN [1] {ECO:0000313|Ensembl:ENSSHAP00000015613.1, ECO:0000313|Proteomes:UP000007648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21709235; DOI=10.1073/pnas.1102838108;
RA Miller W., Hayes V.M., Ratan A., Petersen D.C., Wittekindt N.E., Miller J.,
RA Walenz B., Knight J., Qi J., Zhao F., Wang Q., Bedoya-Reina O.C.,
RA Katiyar N., Tomsho L.P., Kasson L.M., Hardie R.A., Woodbridge P.,
RA Tindall E.A., Bertelsen M.F., Dixon D., Pyecroft S., Helgen K.M.,
RA Lesk A.M., Pringle T.H., Patterson N., Zhang Y., Kreiss A., Woods G.M.,
RA Jones M.E., Schuster S.C.;
RT "Genetic diversity and population structure of the endangered marsupial
RT Sarcophilus harrisii (Tasmanian devil).";
RL Proc. Natl. Acad. Sci. U.S.A. 108:12348-12353(2011).
RN [2] {ECO:0000313|Ensembl:ENSSHAP00000015613.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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 RefSeq; XP_003771904.1; XM_003771856.1.
DR AlphaFoldDB; G3WJK8; -.
DR STRING; 9305.ENSSHAP00000015613; -.
DR Ensembl; ENSSHAT00000015741.2; ENSSHAP00000015613.1; ENSSHAG00000013305.2.
DR GeneID; 100920746; -.
DR KEGG; shr:100920746; -.
DR CTD; 2572; -.
DR eggNOG; KOG0629; Eukaryota.
DR GeneTree; ENSGT00940000157951; -.
DR HOGENOM; CLU_011856_0_0_1; -.
DR InParanoid; G3WJK8; -.
DR OMA; AGMVIFK; -.
DR OrthoDB; 888358at2759; -.
DR TreeFam; TF314688; -.
DR Proteomes; UP000007648; Unassembled WGS sequence.
DR GO; GO:0030424; C:axon; IEA:Ensembl.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042734; C:presynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016831; F:carboxy-lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
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 3: Inferred from homology;
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000007648};
KW Synapse {ECO:0000256|ARBA:ARBA00023018}.
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 398
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 587 AA; 65773 MW; B7E0FD32619CB0EE CRC64;
MASTGSGFWS FGSEDGSGDP ENPSTARAWC QVAQKFTGGI GNKLCALLYG DAEKPMETSG
SEKETQGSAD KKTVCTCNQK PCSCPKTDLN YACLHSTDLL PACNGEVATL SFLQDVMDIL
LQYVVKSFDR STKVIDFHYP NELLQEHNWE LADQPQTLEE ILSNCRTTLK YAIKTGHPRY
FNQLSTGLDM VGLAADWLTS TANTNMFTYE IAPVFVLLEY VTLRKMREIV GWPGGSGDGI
FSPGGAISNM YAMLIARFKM FPEVKEKGMA AIPRLVAFTS EHSHFSVKKG AAALGIGTDS
VILIKCDERG KMIPSDLERR IVEAKQKGFV PFLVSATAGT TVYGAFDPLL AIADICKKYK
IWMHVDAAWG GGLLMSRKHK WKLNGVERAN SVTWNPHKMM GVPLQCSALL VREEGLMQSC
NQMHASYLFQ QDKHYDLSYD TGDKALQCGR HVDVFKLWLM WRAKGTIGFE AQIDKCLELA
EYLYNLIKNR EGYEMVFDGK PQHTNVCFWY IPPSLRHLED NEERMSRLLK VAPVIKARMM
EYGTTMVSYQ PLGDKVNFFR MVISNPAATH QDIDFLIEEI ERLGQDL
//