DCE1_RAT
ID DCE1_RAT Reviewed; 593 AA.
AC P18088;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Glutamate decarboxylase 1;
DE EC=4.1.1.15 {ECO:0000269|PubMed:1924335};
DE AltName: Full=67 kDa glutamic acid decarboxylase;
DE Short=GAD-67;
DE AltName: Full=Glutamate decarboxylase 67 kDa isoform;
GN Name=Gad1; Synonyms=Gad67;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2170798; DOI=10.1016/0169-328x(90)90016-7;
RA Wyborski R.J., Bond R.W., Gottlieb D.I.;
RT "Characterization of a cDNA coding for rat glutamic acid decarboxylase.";
RL Brain Res. Mol. Brain Res. 8:193-198(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2299361; DOI=10.1111/j.1471-4159.1990.tb01928.x;
RA Julien J.F., Samama P., Mallet J.;
RT "Rat brain glutamic acid decarboxylase sequence deduced from a cloned
RT cDNA.";
RL J. Neurochem. 54:703-705(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, CATALYTIC ACTIVITY, AND
RP FUNCTION.
RX PubMed=1924335; DOI=10.1073/pnas.88.19.8754;
RA Michelsen B.K., Petersen J.S., Boel E., Moldrup A., Dyrberg T.,
RA Madsen O.D.;
RT "Cloning, characterization, and autoimmune recognition of rat islet
RT glutamic acid decarboxylase in insulin-dependent diabetes mellitus.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:8754-8758(1991).
CC -!- FUNCTION: Catalyzes the synthesis of the inhibitory neurotransmitter
CC gamma-aminobutyric acid (GABA) with pyridoxal 5'-phosphate as cofactor.
CC {ECO:0000269|PubMed:1924335}.
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:0000269|PubMed:1924335};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17786;
CC Evidence={ECO:0000305|PubMed:1924335};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:Q99259};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q99259}.
CC -!- TISSUE SPECIFICITY: Expressed in brain and pancreatic islets.
CC {ECO:0000269|PubMed:1924335}.
CC -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC {ECO:0000305}.
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DR EMBL; M34445; AAC42037.1; -; mRNA.
DR EMBL; X57572; CAA40800.1; -; mRNA.
DR EMBL; X57573; CAA40801.1; -; mRNA.
DR EMBL; M76177; AAA41184.1; -; mRNA.
DR PIR; A41367; A41367.
DR RefSeq; NP_058703.1; NM_017007.1.
DR RefSeq; XP_017446943.1; XM_017591454.1.
DR RefSeq; XP_017446944.1; XM_017591455.1.
DR AlphaFoldDB; P18088; -.
DR SMR; P18088; -.
DR BioGRID; 246550; 2.
DR ComplexPortal; CPX-3063; Glutamate decarboxylase 1/2 complex.
DR ComplexPortal; CPX-3066; Glutamate decarboxylase 1 complex.
DR IntAct; P18088; 2.
DR STRING; 10116.ENSRNOP00000000008; -.
DR ChEMBL; CHEMBL3758; -.
DR iPTMnet; P18088; -.
DR PhosphoSitePlus; P18088; -.
DR PaxDb; P18088; -.
DR PRIDE; P18088; -.
DR ABCD; P18088; 2 sequenced antibodies.
DR Ensembl; ENSRNOT00000000008; ENSRNOP00000000008; ENSRNOG00000000007.
DR GeneID; 24379; -.
DR KEGG; rno:24379; -.
DR UCSC; RGD:2652; rat.
DR CTD; 2571; -.
DR RGD; 2652; Gad1.
DR eggNOG; KOG0629; Eukaryota.
DR GeneTree; ENSGT00940000155526; -.
DR InParanoid; P18088; -.
DR OMA; RHATYHA; -.
DR OrthoDB; 810772at2759; -.
DR PhylomeDB; P18088; -.
DR TreeFam; TF314688; -.
DR Reactome; R-RNO-888568; GABA synthesis.
DR Reactome; R-RNO-888590; GABA synthesis, release, reuptake and degradation.
DR SABIO-RK; P18088; -.
DR PRO; PR:P18088; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000000007; Expressed in cerebellum and 6 other tissues.
DR ExpressionAtlas; P18088; baseline and differential.
DR Genevisible; P18088; RN.
DR GO; GO:0030424; C:axon; ISO:RGD.
DR GO; GO:0043679; C:axon terminus; ISO:RGD.
DR GO; GO:0005938; C:cell cortex; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0060077; C:inhibitory synapse; ISO:RGD.
DR GO; GO:0044306; C:neuron projection terminus; ISO:RGD.
DR GO; GO:0048786; C:presynaptic active zone; IDA:MGI.
DR GO; GO:0045202; C:synapse; ISO:RGD.
DR GO; GO:0016831; F:carboxy-lyase activity; IBA:GO_Central.
DR GO; GO:0016595; F:glutamate binding; IDA:RGD.
DR GO; GO:0004351; F:glutamate decarboxylase activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0047485; F:protein N-terminus binding; IPI:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IDA:RGD.
DR GO; GO:0009449; P:gamma-aminobutyric acid biosynthetic process; IDA:UniProtKB.
DR GO; GO:0006538; P:glutamate catabolic process; ISO:RGD.
DR GO; GO:0035641; P:locomotory exploration behavior; ISO:RGD.
DR GO; GO:0042136; P:neurotransmitter biosynthetic process; IDA:UniProtKB.
DR GO; GO:0018352; P:protein-pyridoxal-5-phosphate linkage; ISS:UniProtKB.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0035176; P:social behavior; ISO:RGD.
DR Gene3D; 3.40.640.10; -; 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 Pfam; PF00282; Pyridoxal_deC; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR PROSITE; PS00392; DDC_GAD_HDC_YDC; 1.
PE 1: Evidence at protein level;
KW Decarboxylase; Lyase; Neurotransmitter biosynthesis; Phosphoprotein;
KW Pyridoxal phosphate; Reference proteome.
FT CHAIN 1..593
FT /note="Glutamate decarboxylase 1"
FT /id="PRO_0000146967"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 189..191
FT /ligand="4-aminobutanoate"
FT /ligand_id="ChEBI:CHEBI:59888"
FT /evidence="ECO:0000250|UniProtKB:Q99259"
FT BINDING 566
FT /ligand="4-aminobutanoate"
FT /ligand_id="ChEBI:CHEBI:59888"
FT /evidence="ECO:0000250|UniProtKB:Q99259"
FT MOD_RES 77
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48318"
FT MOD_RES 404
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:Q99259"
FT CONFLICT 103
FT /note="L -> V (in Ref. 2; CAA40800)"
FT /evidence="ECO:0000305"
FT CONFLICT 284
FT /note="F -> S (in Ref. 2; CAA40800)"
FT /evidence="ECO:0000305"
FT CONFLICT 287..288
FT /note="EH -> AD (in Ref. 2; CAA40800)"
FT /evidence="ECO:0000305"
FT CONFLICT 344..345
FT /note="AG -> EA (in Ref. 2; CAA40800)"
FT /evidence="ECO:0000305"
FT CONFLICT 347
FT /note="T -> I (in Ref. 2; CAA40800)"
FT /evidence="ECO:0000305"
FT CONFLICT 352..353
FT /note="FD -> LE (in Ref. 2; CAA40800)"
FT /evidence="ECO:0000305"
FT CONFLICT 380
FT /note="L -> R (in Ref. 2; CAA40800)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 593 AA; 66640 MW; EF83239C30301F69 CRC64;
MASSTPSPAT SSNAGADPNT TNLRPTTYDT WCGVAHGCTR KLGLKICGFL QRTNSLEEKS
RLVSAFRERQ ASKNLLSCEN SDPGARFRRT ETDFSNLFAQ DLLPAKNGEE QTVQFLLEVV
DILLNYVRKT FDRSTKVLDF HHPHQLLEGM EGFNLELSDH PESLEQILVD CRDTLKYGVR
TGHPRFFNQL STGLDIIGLA GEWLTSTANT NMFTYEIAPV FVLMEQITLK KMREIIGWSN
KDGDGIFSPG GAISNMYSIM AARYKYFPEV KTKGMAAVPK LVLFTSEHSH YSIKKAGAAL
GFGTDNVILI KCNERGKIIP ADLEAKILDA KQKGFVPLYV NATAGTTVYG AFDPIQEIAD
ICEKYNLWLH VDAAWGGGLL MSRKHRHKLS GIERANSVTW NPHKMMGVLL QCSAILVKEK
GILQGCNQMC AGYLFQPDKQ YDVSYDTGDK AIQCGRHVDI FKFWLMWKAK GTVGFENQIN
KCLELAEYLY AKIKNREEFE MVFNGEPEHT NVCFWYIPQS LRGVPDSPER REKLHRVAPK
IKALMMESGT TMVGYQPQGD KANFFRMVIS NPAATQSDID FLIEEIERLG QDL
