DCE2_PIG
ID DCE2_PIG Reviewed; 585 AA.
AC P48321; Q506P9;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 132.
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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=7835711; DOI=10.1016/0378-1119(94)00713-3;
RA Suzuki R., Asami N., Amann E., Wagatsuma M.;
RT "Sequences of two porcine glutamic acid decarboxylases (65- and 67-kDa
RT GAD).";
RL Gene 152:257-260(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Yu H., Li J.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
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; D31848; BAA06635.1; -; mRNA.
DR EMBL; AY973276; AAY28733.1; -; mRNA.
DR PIR; JC4064; JC4064.
DR RefSeq; NP_999060.2; NM_213895.2.
DR AlphaFoldDB; P48321; -.
DR SMR; P48321; -.
DR STRING; 9823.ENSSSCP00000011796; -.
DR PaxDb; P48321; -.
DR PeptideAtlas; P48321; -.
DR PRIDE; P48321; -.
DR Ensembl; ENSSSCT00005031130; ENSSSCP00005018983; ENSSSCG00005019284.
DR Ensembl; ENSSSCT00015104104; ENSSSCP00015043488; ENSSSCG00015077047.
DR Ensembl; ENSSSCT00030033461; ENSSSCP00030015102; ENSSSCG00030024058.
DR Ensembl; ENSSSCT00035101530; ENSSSCP00035043240; ENSSSCG00035074556.
DR Ensembl; ENSSSCT00040072051; ENSSSCP00040030774; ENSSSCG00040053194.
DR Ensembl; ENSSSCT00050014918; ENSSSCP00050006129; ENSSSCG00050011048.
DR Ensembl; ENSSSCT00065055175; ENSSSCP00065023975; ENSSSCG00065040350.
DR GeneID; 396929; -.
DR KEGG; ssc:396929; -.
DR CTD; 2572; -.
DR eggNOG; KOG0629; Eukaryota.
DR HOGENOM; CLU_011856_0_0_1; -.
DR InParanoid; P48321; -.
DR OrthoDB; 810772at2759; -.
DR TreeFam; TF314688; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR Genevisible; P48321; SS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:0016831; F:carboxy-lyase activity; IBA:GO_Central.
DR GO; GO:0004351; F:glutamate decarboxylase activity; IBA:GO_Central.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0009449; P:gamma-aminobutyric acid biosynthetic process; IBA:GO_Central.
DR GO; GO:0006540; P:glutamate decarboxylation to succinate; IBA:GO_Central.
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_0000146970"
FT REGION 1..24
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; 65388 MW; 4FF2810637671B6B CRC64;
MASPGSGFWS FGSEDGSGDP ENSGTARAWC QVAQKFTGGI GNKLCALLYG DAEKPAESGG
SQPPRTTSRK ATCACNQKPC NCPKAEVNYA FLHATDLLPA CDGERPTLAF LQDVMDILLQ
YVVKSFDRST KVIDFHYPNE LLQEYNWELA DQPQNLEEIL MHCQTTLKYA IKTGHPRYFN
QLSTGLDMVG LAADWLTSTA NTNMFTYEIA PVFVLLEYVT LKKMREIIGW PGGSGDGIFS
PGGAISNMYA MLIARFKMFP EVKEKGMAAV PRLIAFTSEH SHFSLKKGAA ALGIGTDSVI
LIKCDERGKM IPSDLERRIL EAKQKGFVPF LVSATAGTTV YGAFDPLLAV ADICKKYKIW
MHVDAAWGGG LLMSRKHKWK LSGVERANSV TWNPHKMMGV PLQCSALLVR EEGLMQSCNQ
MHASYLFQQD KHYDLSYDTG DKALQCGRHV DVFKLWLMWR AKGTTGFEAH IDKCLELAEY
LYNIIKNREG YEMVFDGKPQ HTNVCFWYVP PSLRVLDNNE ERMSRLSKVA PVIKARMMES
GTTMVSYQPL GDKVNFFRMV ISNPAATHQD IDFLIEEIER LGQDL
