DCE2_CANLF
ID DCE2_CANLF Reviewed; 585 AA.
AC Q4PRC2; A0PA84;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Glutamate decarboxylase 2;
DE EC=4.1.1.15;
DE AltName: Full=65 kDa glutamic acid decarboxylase;
DE Short=GAD-65;
DE AltName: Full=Glutamate decarboxylase 65 kDa isoform;
GN Name=GAD2; Synonyms=GAD65;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RA Davison L.J., Weenink S.M., Christie M.R., Herrtage M.E., Catchpole B.;
RT "Autoantibodies to recombinant canine GAD65 in canine diabetes mellitus.";
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=18981669; DOI=10.1292/jvms.70.1107;
RA Arata S., Hashizume C., Kikusui T., Takeuchi Y., Mori Y.;
RT "Sequences of canine glutamate decarboxylase (GAD) 1 and GAD2 genes, and
RT variation of their genetic polymorphisms among five dog breeds.";
RL J. Vet. Med. Sci. 70:1107-1110(2008).
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. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Cytoplasmic
CC vesicle {ECO:0000250}. Presynaptic cell membrane {ECO:0000250}; Lipid-
CC anchor {ECO:0000250}. Golgi apparatus membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}; Cytoplasmic side
CC {ECO:0000250}. Note=Associated to cytoplasmic vesicles. In neurons,
CC cytosolic leaflet of Golgi membranes and presynaptic clusters (By
CC similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylated; which does not affect kinetic parameters or
CC subcellular location. {ECO:0000250}.
CC -!- PTM: Palmitoylated; which is required for presynaptic clustering.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC {ECO:0000305}.
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DR EMBL; DQ060442; AAY59421.1; -; mRNA.
DR EMBL; AB261623; BAF37948.1; -; mRNA.
DR RefSeq; NP_001070907.1; NM_001077439.1.
DR AlphaFoldDB; Q4PRC2; -.
DR SMR; Q4PRC2; -.
DR STRING; 9612.ENSCAFP00000006413; -.
DR PaxDb; Q4PRC2; -.
DR Ensembl; ENSCAFT00030027701; ENSCAFP00030024173; ENSCAFG00030014888.
DR Ensembl; ENSCAFT00845007030; ENSCAFP00845005606; ENSCAFG00845003895.
DR GeneID; 487107; -.
DR KEGG; cfa:487107; -.
DR CTD; 2572; -.
DR VEuPathDB; HostDB:ENSCAFG00845003895; -.
DR eggNOG; KOG0629; Eukaryota.
DR GeneTree; ENSGT00940000157951; -.
DR InParanoid; Q4PRC2; -.
DR OrthoDB; 810772at2759; -.
DR BRENDA; 4.1.1.15; 1153.
DR Proteomes; UP000002254; Chromosome 2.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IEA:Ensembl.
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:0004351; F:glutamate decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR GO; GO:0042136; P:neurotransmitter biosynthetic process; IEA:UniProtKB-KW.
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 Cell membrane; Cell projection; Cytoplasm; Cytoplasmic vesicle;
KW Decarboxylase; Golgi apparatus; Lipoprotein; Lyase; Membrane;
KW Neurotransmitter biosynthesis; Palmitate; Phosphoprotein;
KW Pyridoxal phosphate; Reference proteome; Synapse.
FT CHAIN 1..585
FT /note="Glutamate decarboxylase 2"
FT /id="PRO_0000231042"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 181..183
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 558
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 3
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q05329"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q05329"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q05329"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q05329"
FT MOD_RES 396
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT LIPID 30
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 45
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 585 AA; 65419 MW; 55BDA189F62922B2 CRC64;
MASPGSGFWS FGSEDGSGDP ENPSTARAWC QVAQKFTGGI GNKLCALLYG DAEKPAESGG
SEPPRATSRK AACACNQKPC SCPKAEVNYA FLHATDLLPA CDGERPTLAF LQDVMDILLQ
YVVKSFDRST KVIDFHYPNE LLQEYNWELA DQPQNLEEIL MHCQTTLKYA IKTGHPRYFN
QLSTGLDMVG LAADWLTSTA NTNMFTYEIA PVFVLLEYVT LKKMREIIGW PGGSGDGIFS
PGGAISNMYA MLIARFKMFP EVKEKGMAAV PRLIAFTSEH SHFSLKKGAA ALGIGTDSVI
LIKCDERGKM VPSDLERRIL EAKQKGFVPF LVSATAGTTV YGAFDPLLAV ADICKKYKIW
MHVDAAWGGG LLMSRKHKWK LSGVERANSV TWNPHKMMGV PLQCSALLVR EEGLMQSCNQ
MHASYLFQQD KHYDLSYDTG DKALQCGRHV DVFKLWLMWR AKGTTGFEAH IDKCLELAEY
LYSIIKNREG YEMVFDGKPQ HTNVCFWYVP PSLRVLEDNE ERMNRLSKVA PVIKARMMEY
GTTMVSYQPL GDKVNFFRMV ISNPAATHQD IDFLIEEIER LGQDL
