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Glutamate decarboxylase 2 (EC 4.1.1.15) (65 kDa glutamic acid decarboxylase) (GAD-65) (Glutamate decarboxylase 65 kDa isoform)

 DCE2_MOUSE              Reviewed;         585 AA.
P48320; O35519;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 1.
12-SEP-2018, entry version 148.
RecName: Full=Glutamate decarboxylase 2;
EC=4.1.1.15;
AltName: Full=65 kDa glutamic acid decarboxylase;
Short=GAD-65;
AltName: Full=Glutamate decarboxylase 65 kDa isoform;
Name=Gad2; Synonyms=Gad65;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=8218409; DOI=10.1016/0167-4781(93)90056-J;
Lee D.S., Tian J., Phan T., Kaufman D.L.;
"Cloning and sequence analysis of a murine cDNA encoding glutamate
decarboxylase (GAD65).";
Biochim. Biophys. Acta 1216:157-160(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=8954991; DOI=10.1006/bbrc.1996.1898;
Asada H., Kawamura Y., Maruyama K., Kume H., Ding R.G., Ji F.Y.,
Kanbara N., Kuzume H., Sanbo M., Yagi T., Obata K.;
"Mice lacking the 65 kDa isoform of glutamic acid decarboxylase
(GAD65) maintain normal levels of GAD67 and GABA in their brains but
are susceptible to seizures.";
Biochem. Biophys. Res. Commun. 229:891-895(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Eye;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 175-379.
TISSUE=Brain;
PubMed=8243324; DOI=10.1210/endo.133.6.8243324;
Faulkner-Jones B.E., Cram D.S., Kun J., Harrison L.C.;
"Localization and quantitation of expression of two glutamate
decarboxylase genes in pancreatic beta-cells and other peripheral
tissues of mouse and rat.";
Endocrinology 133:2962-2972(1993).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Catalyzes the production of GABA.
-!- CATALYTIC ACTIVITY: L-glutamate = 4-aminobutanoate + CO(2).
-!- COFACTOR:
Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
-!- SUBUNIT: Homodimer. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}.
Cytoplasmic vesicle {ECO:0000250}. Cell junction, synapse,
presynaptic cell membrane {ECO:0000250}; Lipid-anchor
{ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Peripheral
membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
Note=Associated to cytoplasmic vesicles. In neurons, cytosolic
leaflet of Golgi membranes and presynaptic clusters (By
similarity). {ECO:0000250}.
-!- PTM: Phosphorylated; which does not affect kinetic parameters or
subcellular location. {ECO:0000250}.
-!- PTM: Palmitoylated; which is required for presynaptic clustering.
{ECO:0000250}.
-!- SIMILARITY: Belongs to the group II decarboxylase family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; L16980; AAA93049.1; -; mRNA.
EMBL; D42051; BAA22893.1; -; mRNA.
EMBL; BC018380; AAH18380.1; -; mRNA.
EMBL; S67454; -; NOT_ANNOTATED_CDS; mRNA.
CCDS; CCDS15724.1; -.
PIR; S38533; S38533.
RefSeq; NP_032104.2; NM_008078.2.
UniGene; Mm.4784; -.
ProteinModelPortal; P48320; -.
SMR; P48320; -.
ComplexPortal; CPX-3062; Glutamate decarboxylase 2 complex.
ComplexPortal; CPX-3064; Glutamate decarboxylase 1/2 complex.
IntAct; P48320; 2.
MINT; P48320; -.
STRING; 10090.ENSMUSP00000028123; -.
iPTMnet; P48320; -.
PhosphoSitePlus; P48320; -.
SwissPalm; P48320; -.
PaxDb; P48320; -.
PeptideAtlas; P48320; -.
PRIDE; P48320; -.
Ensembl; ENSMUST00000028123; ENSMUSP00000028123; ENSMUSG00000026787.
GeneID; 14417; -.
KEGG; mmu:14417; -.
UCSC; uc008inj.1; mouse.
CTD; 2572; -.
MGI; MGI:95634; Gad2.
eggNOG; KOG0629; Eukaryota.
eggNOG; COG0076; LUCA.
GeneTree; ENSGT00760000119205; -.
HOGENOM; HOG000005382; -.
HOVERGEN; HBG004980; -.
InParanoid; P48320; -.
KO; K01580; -.
OMA; WRAKGTT; -.
OrthoDB; EOG091G07ZU; -.
PhylomeDB; P48320; -.
TreeFam; TF314688; -.
BRENDA; 4.1.1.15; 3474.
Reactome; R-MMU-888568; GABA synthesis.
Reactome; R-MMU-888590; GABA synthesis, release, reuptake and degradation.
ChiTaRS; Gad2; mouse.
PRO; PR:P48320; -.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000026787; Expressed in 161 organ(s), highest expression level in olfactory tubercle.
CleanEx; MM_GAD2; -.
ExpressionAtlas; P48320; baseline and differential.
Genevisible; P48320; MM.
GO; GO:0031225; C:anchored component of membrane; ISO:MGI.
GO; GO:0030424; C:axon; IDA:MGI.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0031410; C:cytoplasmic vesicle; ISO:MGI.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0060077; C:inhibitory synapse; ISO:MGI.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
GO; GO:0042734; C:presynaptic membrane; IEA:UniProtKB-SubCell.
GO; GO:0045202; C:synapse; IDA:MGI.
GO; GO:0030672; C:synaptic vesicle membrane; ISO:MGI.
GO; GO:0016595; F:glutamate binding; ISO:MGI.
GO; GO:0004351; F:glutamate decarboxylase activity; ISO:MGI.
GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
GO; GO:0030170; F:pyridoxal phosphate binding; ISO:MGI.
GO; GO:0006540; P:glutamate decarboxylation to succinate; ISO:MGI.
GO; GO:0042136; P:neurotransmitter biosynthetic process; IEA:UniProtKB-KW.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
Gene3D; 3.40.640.10; -; 1.
InterPro; IPR002129; PyrdxlP-dep_de-COase.
InterPro; IPR015424; PyrdxlP-dep_Trfase.
InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
InterPro; IPR021115; Pyridoxal-P_BS.
Pfam; PF00282; Pyridoxal_deC; 1.
SUPFAM; SSF53383; SSF53383; 1.
PROSITE; PS00392; DDC_GAD_HDC_YDC; 1.
1: Evidence at protein level;
Cell junction; Cell membrane; Complete proteome; Cytoplasm;
Cytoplasmic vesicle; Decarboxylase; Golgi apparatus; Lipoprotein;
Lyase; Membrane; Neurotransmitter biosynthesis; Palmitate;
Phosphoprotein; Pyridoxal phosphate; Reference proteome; Synapse.
CHAIN 1 585 Glutamate decarboxylase 2.
/FTId=PRO_0000146969.
REGION 181 183 Substrate binding. {ECO:0000250}.
BINDING 558 558 Substrate. {ECO:0000250}.
MOD_RES 3 3 Phosphoserine.
{ECO:0000250|UniProtKB:Q05329}.
MOD_RES 6 6 Phosphoserine.
{ECO:0000250|UniProtKB:Q05329}.
MOD_RES 10 10 Phosphoserine.
{ECO:0000250|UniProtKB:Q05329}.
MOD_RES 13 13 Phosphoserine.
{ECO:0000250|UniProtKB:Q05329}.
MOD_RES 396 396 N6-(pyridoxal phosphate)lysine.
{ECO:0000250}.
LIPID 30 30 S-palmitoyl cysteine. {ECO:0000250}.
LIPID 45 45 S-palmitoyl cysteine. {ECO:0000250}.
CONFLICT 259 259 F -> S (in Ref. 2; BAA22893).
{ECO:0000305}.
CONFLICT 319 319 I -> S (in Ref. 4; S67454).
{ECO:0000305}.
CONFLICT 325 325 K -> E (in Ref. 2; BAA22893).
{ECO:0000305}.
CONFLICT 499 499 P -> S (in Ref. 2; BAA22893).
{ECO:0000305}.
SEQUENCE 585 AA; 65224 MW; C2F486E85123B057 CRC64;
MASPGSGFWS FGSEDGSADP ENPGTARAWC QVAQKFTGGI GNKLCALLYG DSGKPAEGGG
SVTSRAATGK VACTCDQKPC NCPKGDVNYA FLHATDLLPA CDGERPTLAF LQDVMNILLQ
YVVKSFDRST KVIDFHYPNE LLQEYNWELA DQPQNLEEIL THCQTTLKYA IKTGHPRYFN
QLSTGLDMVG LAADWLTSTA NTNMFTYEIA PVFVLLEYVT LKKMREIIGW PGGSGDGIFS
PGGAISNMYA MLIARYKMFP EVKEKGMAAV PRLIAFTSEH SHFSLKKGAA ALGIGTDSVI
LIKCDERGKM IPSDLERRIL EVKQKGFVPF LVSATAGTTV YGAFDPLLAV ADICKKYKIW
MHVDAAWGGG LLMSRKHKWK LSGVERANSV TWNPHKMMGV PLQCSALLVR EEGLMQSCNQ
MHASYLFQQD KHYDLSYDTG DKALQCGRHV DVFKLWLMWR AKGTTGFEAH IDKCLELAEY
LYTIIKNREG YEMVFDGKPQ HTNVCFWFVP PSLRTLEDNE ERMSRLSKVA PVIKARMMEY
GTTMVSYQPL GDKVNFFRMV ISNPAATHQD IDFLIEEIER LGQDL


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