ID D0VY26_9SAUR Unreviewed; 223 AA.
AC D0VY26;
DT 19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2010, sequence version 1.
DT 27-MAR-2024, entry version 33.
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};
DE Flags: Fragment;
GN Name=GAD2 {ECO:0000313|EMBL:BAI50378.1};
OS Leiolepis reevesii rubritaeniata.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Iguania; Acrodonta; Agamidae; Leiolepinae; Leiolepis.
OX NCBI_TaxID=596103 {ECO:0000313|EMBL:BAI50378.1};
RN [1] {ECO:0000313|EMBL:BAI50378.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Testis {ECO:0000313|EMBL:BAI50378.1};
RA Srikulnath K., Nishida C., Matsubara K., Uno Y., Thongpan A.,
RA Suputtitada S., Apisitwanich S., Matsuda Y.;
RT "Karyotypic evolution in squamate reptiles: comparative gene mapping
RT revealed highly conserved linkage homology between the butterfly lizard
RT (Leiolepis reevesii rubritaeniata, Agamidae, Lacertilia) and the Japanese
RT four-striped rat snake (Elaphe quadrivirgata, Colubridae, Serpentes).";
RL Chromosome Res. 17:975-986(2009).
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; AB490380; BAI50378.1; -; mRNA.
DR AlphaFoldDB; D0VY26; -.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
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 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 MOD_RES 193
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:BAI50378.1"
FT NON_TER 223
FT /evidence="ECO:0000313|EMBL:BAI50378.1"
SQ SEQUENCE 223 AA; 24669 MW; C24F8FC721A1F91B CRC64;
MFTYEIAPVF VLLEYVTLRK MREIVGWPGG AGDGIFSPGG AISNMYAMLI ARFKMFPEVK
EKGMAAIPRL VAFTSEHSHF SVKKGAAALG IGTDSVILIR CDERGKMIPS DLERRIIEAK
QKGFVPFLVS ATAGTTVYGA FDPLIAIADI CKKYKIWMHV DGAWGGGLLM SRKHRWKLNG
VERANSVTWN PHKMMGVPLQ CSALLVREEG LMQSCNQMHA SYL
//
