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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_RAT                Reviewed;         585 AA.
Q05683;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 1.
05-DEC-2018, entry version 133.
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;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Hippocampus;
PubMed=2069816; DOI=10.1016/0896-6273(91)90077-D;
Erlander M.G., Tillakaratne N.J., Feldblum S., Patel N., Tobin A.J.;
"Two genes encode distinct glutamate decarboxylases.";
Neuron 7:91-100(1991).
[2]
PROTEIN SEQUENCE OF 190-219; 225-266 AND 524-558.
TISSUE=Brain;
PubMed=3385490;
Chang Y.C., Gottlieb D.I.;
"Characterization of the proteins purified with monoclonal antibodies
to glutamic acid decarboxylase.";
J. Neurosci. 8:2123-2130(1988).
[3]
SUBCELLULAR LOCATION, AND PALMITOYLATION.
PubMed=1321158; DOI=10.1083/jcb.118.2.309;
Christgau S., Aanstoot H.-J., Schierbeck H., Begley K., Tullin S.,
Hejnaes K., Baekkeskov S.;
"Membrane anchoring of the autoantigen GAD65 to microvesicles in
pancreatic beta-cells by palmitoylation in the NH2-terminal domain.";
J. Cell Biol. 118:309-320(1992).
[4]
PALMITOYLATION AT CYS-30 AND CYS-45, AND MUTAGENESIS OF CYS-30;
CYS-45; CYS-73; CYS-75; CYS-80; CYS-82 AND CYS-101.
PubMed=8132714; DOI=10.1083/jcb.124.6.927;
Shi Y., Veit B., Baekkeskov S.;
"Amino acid residues 24-31 but not palmitoylation of cysteines 30 and
45 are required for membrane anchoring of glutamic acid decarboxylase,
GAD65.";
J. Cell Biol. 124:927-934(1994).
[5]
PHOSPHORYLATION AT SER-3; SER-6; SER-10 AND SER-13, AND
BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=8999827; DOI=10.1074/jbc.272.3.1548;
Namchuk M., Lindsay L., Turck C.W., Kanaani J., Baekkeskov S.;
"Phosphorylation of serine residues 3, 6, 10, and 13 distinguishes
membrane anchored from soluble glutamic acid decarboxylase 65 and is
restricted to glutamic acid decarboxylase 65alpha.";
J. Biol. Chem. 272:1548-1557(1997).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3 AND SER-13, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: Catalyzes the production of GABA.
-!- CATALYTIC ACTIVITY:
Reaction=H(+) + L-glutamate = 4-aminobutanoate + CO2;
Xref=Rhea:RHEA:17785, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
ChEBI:CHEBI:29985, ChEBI:CHEBI:59888; EC=4.1.1.15;
-!- COFACTOR:
Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=1.02 mM for glutamate {ECO:0000269|PubMed:8999827};
-!- 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: The N-terminus is blocked.
-!- PTM: Phosphorylated; which does not affect kinetic parameters or
subcellular location. {ECO:0000269|PubMed:8999827}.
-!- 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; M72422; AAA63488.1; -; mRNA.
PIR; JH0423; JH0423.
RefSeq; NP_036695.1; NM_012563.1.
UniGene; Rn.29951; -.
PDB; 3CUP; X-ray; 3.09 A; B=221-235.
PDBsum; 3CUP; -.
ProteinModelPortal; Q05683; -.
SMR; Q05683; -.
BioGrid; 246551; 1.
ComplexPortal; CPX-3063; Glutamate decarboxylase 1/2 complex.
ComplexPortal; CPX-3067; Glutamate decarboxylase 2 complex.
IntAct; Q05683; 1.
STRING; 10116.ENSRNOP00000024901; -.
BindingDB; Q05683; -.
iPTMnet; Q05683; -.
PhosphoSitePlus; Q05683; -.
SwissPalm; Q05683; -.
PaxDb; Q05683; -.
PRIDE; Q05683; -.
Ensembl; ENSRNOT00000024901; ENSRNOP00000024901; ENSRNOG00000018200.
GeneID; 24380; -.
KEGG; rno:24380; -.
UCSC; RGD:2653; rat.
CTD; 2572; -.
RGD; 2653; Gad2.
eggNOG; KOG0629; Eukaryota.
eggNOG; COG0076; LUCA.
GeneTree; ENSGT00940000157951; -.
HOGENOM; HOG000005382; -.
HOVERGEN; HBG004980; -.
InParanoid; Q05683; -.
KO; K01580; -.
OMA; ACACNQK; -.
OrthoDB; EOG091G07ZU; -.
PhylomeDB; Q05683; -.
TreeFam; TF314688; -.
Reactome; R-RNO-888568; GABA synthesis.
Reactome; R-RNO-888590; GABA synthesis, release, reuptake and degradation.
SABIO-RK; Q05683; -.
PRO; PR:Q05683; -.
Proteomes; UP000002494; Chromosome 17.
Bgee; ENSRNOG00000018200; Expressed in 2 organ(s), highest expression level in brain.
Genevisible; Q05683; RN.
GO; GO:0031225; C:anchored component of membrane; IDA:RGD.
GO; GO:0030424; C:axon; IEA:Ensembl.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0031410; C:cytoplasmic vesicle; IDA:RGD.
GO; GO:0005829; C:cytosol; IDA:RGD.
GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0060077; C:inhibitory synapse; IDA:MGI.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
GO; GO:0042734; C:presynaptic membrane; IEA:UniProtKB-SubCell.
GO; GO:0030672; C:synaptic vesicle membrane; IDA:RGD.
GO; GO:0016595; F:glutamate binding; IDA:RGD.
GO; GO:0004351; F:glutamate decarboxylase activity; IDA:RGD.
GO; GO:0046982; F:protein heterodimerization activity; IDA:RGD.
GO; GO:0030170; F:pyridoxal phosphate binding; IDA:RGD.
GO; GO:0007268; P:chemical synaptic transmission; TAS:RGD.
GO; GO:0006540; P:glutamate decarboxylation to succinate; IDA:RGD.
GO; GO:0042136; P:neurotransmitter biosynthetic process; IEA:UniProtKB-KW.
GO; GO:0042493; P:response to drug; IEP:RGD.
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;
3D-structure; Cell junction; Cell membrane; Complete proteome;
Cytoplasm; Cytoplasmic vesicle; Decarboxylase;
Direct protein sequencing; Golgi apparatus; Lipoprotein; Lyase;
Membrane; Neurotransmitter biosynthesis; Palmitate; Phosphoprotein;
Pyridoxal phosphate; Reference proteome; Synapse.
CHAIN 1 585 Glutamate decarboxylase 2.
/FTId=PRO_0000146971.
REGION 181 183 Substrate binding. {ECO:0000250}.
BINDING 558 558 Substrate. {ECO:0000250}.
MOD_RES 3 3 Phosphoserine.
{ECO:0000244|PubMed:22673903,
ECO:0000269|PubMed:8999827}.
MOD_RES 6 6 Phosphoserine.
{ECO:0000269|PubMed:8999827}.
MOD_RES 10 10 Phosphoserine.
{ECO:0000269|PubMed:8999827}.
MOD_RES 13 13 Phosphoserine.
{ECO:0000244|PubMed:22673903,
ECO:0000269|PubMed:8999827}.
MOD_RES 396 396 N6-(pyridoxal phosphate)lysine.
{ECO:0000250}.
LIPID 30 30 S-palmitoyl cysteine.
{ECO:0000269|PubMed:8132714}.
LIPID 45 45 S-palmitoyl cysteine.
{ECO:0000269|PubMed:8132714}.
MUTAGEN 30 30 C->A: Abolishes palmitoylation but not
membrane-association; when associates
with A-45. {ECO:0000269|PubMed:8132714}.
MUTAGEN 45 45 C->A: Abolishes palmitoylation but not
membrane-association; when associates
with A-30. {ECO:0000269|PubMed:8132714}.
MUTAGEN 73 73 C->S: No effect on palmitoylation.
{ECO:0000269|PubMed:8132714}.
MUTAGEN 75 75 C->S: No effect on palmitoylation.
{ECO:0000269|PubMed:8132714}.
MUTAGEN 80 80 C->S: No effect on palmitoylation.
{ECO:0000269|PubMed:8132714}.
MUTAGEN 82 82 C->S: No effect on palmitoylation.
{ECO:0000269|PubMed:8132714}.
MUTAGEN 101 101 C->S: No effect on palmitoylation.
{ECO:0000269|PubMed:8132714}.
CONFLICT 190 190 G -> V (in Ref. 2; AA sequence).
{ECO:0000305}.
SEQUENCE 585 AA; 65402 MW; C04040B7BA7B37D1 CRC64;
MASPGSGFWS FGSEDGSGDP ENPGTARAWC QVAQKFTGGI GNKLCALLYG DSEKPAESGG
SVTSRAATRK VACTCDQKPC SCPKGDVNYA LLHATDLLPA CEGERPTLAF 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 LNGVERANSV TWNPHKMMGV PLQCSALLVR EEGLMQSCNQ
MHASYLFQQD KHYDLSYDTG DKALQCGRHV DVFKLWLMWR AKGTTGFEAH IDKCLELAEY
LYNIIKNREG YEMVFDGKPQ HTNVCFWFVP PSLRVLEDNE ERMSRLSKVA PVIKARMMEY
GTTMVSYQPL GDKVNFFRMV ISNPAATHQD IDFLIEEIER LGQDL


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