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Database: UniProt/SWISS-PROT
Entry: DCE1_RAT
LinkDB: DCE1_RAT
Original site: 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   16-JAN-2019, entry version 141.
DE   RecName: Full=Glutamate decarboxylase 1;
DE            EC=4.1.1.15;
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; 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
RT   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].
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 production of GABA.
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   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC   -!- SUBUNIT: Homodimer.
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000305}.
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   UniGene; Rn.91245; -.
DR   ProteinModelPortal; P18088; -.
DR   SMR; P18088; -.
DR   BioGrid; 246550; 1.
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   Ensembl; ENSRNOT00000000008; ENSRNOP00000000008; ENSRNOG00000000007.
DR   Ensembl; ENSRNOT00000087712; ENSRNOP00000072778; 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   eggNOG; COG0076; LUCA.
DR   GeneTree; ENSGT00940000155526; -.
DR   HOGENOM; HOG000005382; -.
DR   HOVERGEN; HBG004980; -.
DR   InParanoid; P18088; -.
DR   KO; K01580; -.
DR   OMA; PTMVTSQ; -.
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 7 organ(s), highest expression level in brain.
DR   ExpressionAtlas; P18088; baseline and differential.
DR   Genevisible; P18088; RN.
DR   GO; GO:0043679; C:axon terminus; IEA:Ensembl.
DR   GO; GO:0005938; C:cell cortex; IEA:Ensembl.
DR   GO; GO:0060077; C:inhibitory synapse; IEA:Ensembl.
DR   GO; GO:0048786; C:presynaptic active zone; IDA:MGI.
DR   GO; GO:0016595; F:glutamate binding; IDA:RGD.
DR   GO; GO:0004351; F:glutamate decarboxylase activity; IDA:RGD.
DR   GO; GO:0046982; F:protein heterodimerization activity; IDA:RGD.
DR   GO; GO:0047485; F:protein N-terminus binding; IPI:RGD.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IDA:RGD.
DR   GO; GO:0009449; P:gamma-aminobutyric acid biosynthetic process; IDA:RGD.
DR   GO; GO:0035641; P:locomotory exploration behavior; IEA:Ensembl.
DR   GO; GO:0042493; P:response to drug; IEP:RGD.
DR   GO; GO:0035176; P:social behavior; IEA:Ensembl.
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   2: Evidence at transcript level;
KW   Complete proteome; Decarboxylase; Lyase;
KW   Neurotransmitter biosynthesis; Phosphoprotein; Pyridoxal phosphate;
KW   Reference proteome.
FT   CHAIN         1    593       Glutamate decarboxylase 1.
FT                                /FTId=PRO_0000146967.
FT   REGION      189    191       Substrate binding. {ECO:0000250}.
FT   BINDING     566    566       Substrate. {ECO:0000250}.
FT   MOD_RES      77     77       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P48318}.
FT   MOD_RES     404    404       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000250}.
FT   CONFLICT    103    103       L -> V (in Ref. 2; CAA40800).
FT                                {ECO:0000305}.
FT   CONFLICT    284    284       F -> S (in Ref. 2; CAA40800).
FT                                {ECO:0000305}.
FT   CONFLICT    287    288       EH -> AD (in Ref. 2; CAA40800).
FT                                {ECO:0000305}.
FT   CONFLICT    344    345       AG -> EA (in Ref. 2; CAA40800).
FT                                {ECO:0000305}.
FT   CONFLICT    347    347       T -> I (in Ref. 2; CAA40800).
FT                                {ECO:0000305}.
FT   CONFLICT    352    353       FD -> LE (in Ref. 2; CAA40800).
FT                                {ECO:0000305}.
FT   CONFLICT    380    380       L -> R (in Ref. 2; CAA40800).
FT                                {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
//
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