GPX2_SAPAP
ID GPX2_SAPAP Reviewed; 190 AA.
AC Q4AEH7;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Glutathione peroxidase 2;
DE Short=GPx-2;
DE Short=GSHPx-2;
DE EC=1.11.1.9 {ECO:0000250|UniProtKB:P18283};
DE AltName: Full=Glutathione peroxidase-gastrointestinal;
DE Short=GPx-GI;
DE Short=GSHPx-GI;
GN Name=GPX2;
OS Sapajus apella (Brown-capped capuchin) (Cebus apella).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Cebinae; Sapajus.
OX NCBI_TaxID=9515;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=15967696; DOI=10.1016/j.cbpc.2005.05.002;
RA Fukuhara R., Kageyama T.;
RT "Structure, gene expression, and evolution of primate glutathione
RT peroxidases.";
RL Comp. Biochem. Physiol. 141B:428-436(2005).
CC -!- FUNCTION: Could play a major role in protecting mammals from the
CC toxicity of ingested organic hydroperoxides. Tert-butyl hydroperoxide,
CC cumene hydroperoxide and linoleic acid hydroperoxide but not
CC phosphatidycholine hydroperoxide, can act as acceptors.
CC {ECO:0000250|UniProtKB:P18283}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a hydroperoxide + 2 glutathione = an alcohol + glutathione
CC disulfide + H2O; Xref=Rhea:RHEA:62632, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:30879, ChEBI:CHEBI:35924, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:58297; Evidence={ECO:0000250|UniProtKB:P18283};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62633;
CC Evidence={ECO:0000250|UniProtKB:P18283};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 glutathione + H2O2 = glutathione disulfide + 2 H2O;
CC Xref=Rhea:RHEA:16833, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:57925, ChEBI:CHEBI:58297; EC=1.11.1.9;
CC Evidence={ECO:0000250|UniProtKB:P18283};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16834;
CC Evidence={ECO:0000250|UniProtKB:P18283};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 glutathione + tert-butyl hydroperoxide = glutathione
CC disulfide + H2O + tert-butanol; Xref=Rhea:RHEA:69412,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:45895, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:58297, ChEBI:CHEBI:64090;
CC Evidence={ECO:0000250|UniProtKB:P18283};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69413;
CC Evidence={ECO:0000250|UniProtKB:P18283};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cumene hydroperoxide + 2 glutathione = 2-phenylpropan-2-ol +
CC glutathione disulfide + H2O; Xref=Rhea:RHEA:69651, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:57925, ChEBI:CHEBI:58297, ChEBI:CHEBI:78673,
CC ChEBI:CHEBI:131607; Evidence={ECO:0000250|UniProtKB:P18283};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69652;
CC Evidence={ECO:0000250|UniProtKB:P18283};
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P18283}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P18283}.
CC -!- SIMILARITY: Belongs to the glutathione peroxidase family.
CC {ECO:0000305}.
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DR EMBL; AB121004; BAE17013.1; -; mRNA.
DR PeroxiBase; 3639; CapGPx02.
DR PRIDE; Q4AEH7; -.
DR Proteomes; UP000504640; Unplaced.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0004602; F:glutathione peroxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR CDD; cd00340; GSH_Peroxidase; 1.
DR InterPro; IPR000889; Glutathione_peroxidase.
DR InterPro; IPR029759; GPX_AS.
DR InterPro; IPR029760; GPX_CS.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR11592; PTHR11592; 1.
DR Pfam; PF00255; GSHPx; 1.
DR PIRSF; PIRSF000303; Glutathion_perox; 1.
DR PRINTS; PR01011; GLUTPROXDASE.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS00460; GLUTATHIONE_PEROXID_1; 1.
DR PROSITE; PS00763; GLUTATHIONE_PEROXID_2; 1.
DR PROSITE; PS51355; GLUTATHIONE_PEROXID_3; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Oxidoreductase; Peroxidase; Reference proteome; Selenocysteine.
FT CHAIN 1..190
FT /note="Glutathione peroxidase 2"
FT /id="PRO_0000066618"
FT ACT_SITE 40
FT /evidence="ECO:0000250"
FT NON_STD 40
FT /note="Selenocysteine"
SQ SEQUENCE 190 AA; 21909 MW; E63C54CEDBF62C94 CRC64;
MAFIAKSFYD LSAISLDGEK VDFNTFRGRA VLIENVASLU GTTTRDFTQL NELQCRFPRR
LVVLGFPCNQ FGHQENCQNE EILNSLKYVR PGGGYQPTFT LVQKCEVNGQ NEHPVFAYLK
DKLPYPHDDP FSLMTDPKFI IWSPVCRSDV AWNFEKFLIG PEGEPFRRYS RTFPTINIEP
DIKRLLKVAI
