GPX2_RAT
ID GPX2_RAT Reviewed; 190 AA.
AC P83645;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 3.
DT 03-AUG-2022, entry version 112.
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 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 {ECO:0000305};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-87.
RC STRAIN=Sprague-Dawley; TISSUE=Spinal ganglion;
RA Xiao H.S., Han Z.G., Zhang F.X., Huang Q.H., Lu Y.J., Bao L., Fu G.,
RA Guo C., Yan Q., Jin S.X., Zhu Z.D., Xu X.R., Li N.G., Chen Z., Zhang X.;
RT "Distinct gene expression profiles of rat dorsal root ganglion induced by
RT peripheral nerve axotomy.";
RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 80-190.
RC STRAIN=Sprague-Dawley; TISSUE=Ileum;
RX PubMed=8889548; DOI=10.1101/gr.6.9.791;
RA Bonaldo M.F., Lennon G., Soares M.B.;
RT "Normalization and subtraction: two approaches to facilitate gene
RT discovery.";
RL Genome Res. 6:791-806(1996).
RN [3] {ECO:0000305}
RP PROTEIN SEQUENCE OF 7-27; 91-101; 121-138; 140-168 AND 175-181, CATALYTIC
RP ACTIVITY, AND TISSUE SPECIFICITY.
RC STRAIN=CD Charles River {ECO:0000269|PubMed:9685647};
RC TISSUE=Gastrointestinal tract epithelium {ECO:0000269|PubMed:9685647};
RX PubMed=9685647; DOI=10.1016/s0304-4165(98)00032-4;
RA Esworthy R.S., Swiderek K.M., Ho Y.-S., Chu F.-F.;
RT "Selenium-dependent glutathione peroxidase-GI is a major glutathione
RT peroxidase activity in the mucosal epithelium of rodent intestine.";
RL Biochim. Biophys. Acta 1381:213-226(1998).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 -!- TISSUE SPECIFICITY: Mucosal epithelium of the gastrointestinal tract.
CC {ECO:0000269|PubMed:9685647}.
CC -!- SIMILARITY: Belongs to the glutathione peroxidase family.
CC {ECO:0000305}.
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DR EMBL; BG664050; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BQ196649; -; NOT_ANNOTATED_CDS; mRNA.
DR PeroxiBase; 3731; RnoGPx02.
DR iPTMnet; P83645; -.
DR PhosphoSitePlus; P83645; -.
DR UCSC; RGD:727780; rat.
DR RGD; 727780; Gpx2.
DR InParanoid; P83645; -.
DR PhylomeDB; P83645; -.
DR BRENDA; 1.11.1.9; 5301.
DR Reactome; R-RNO-2142712; Synthesis of 12-eicosatetraenoic acid derivatives.
DR Reactome; R-RNO-2142770; Synthesis of 15-eicosatetraenoic acid derivatives.
DR Reactome; R-RNO-3299685; Detoxification of Reactive Oxygen Species.
DR Reactome; R-RNO-5628897; TP53 Regulates Metabolic Genes.
DR PRO; PR:P83645; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0004602; F:glutathione peroxidase activity; IDA:RGD.
DR GO; GO:0004601; F:peroxidase activity; IBA:GO_Central.
DR GO; GO:0051702; P:biological process involved in interaction with symbiont; ISO:RGD.
DR GO; GO:0002862; P:negative regulation of inflammatory response to antigenic stimulus; ISO:RGD.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR GO; GO:0009609; P:response to symbiotic bacterium; ISO:RGD.
DR GO; GO:0001659; P:temperature homeostasis; ISO:RGD.
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 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Oxidoreductase; Peroxidase;
KW Reference proteome; Selenocysteine.
FT CHAIN 1..190
FT /note="Glutathione peroxidase 2"
FT /id="PRO_0000066624"
FT ACT_SITE 40
FT /evidence="ECO:0000250"
FT NON_STD 40
FT /note="Selenocysteine"
FT CONFLICT 91
FT /note="H -> P (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 190 AA; 22014 MW; 9A69384CBEF81E70 CRC64;
MAYIAKSFYD LSAIGLDGEK IDFNTFRGRA VLIENVASLU GTTTRDYTQL NELQCRFPRR
LVVLGFPCNQ FGHQENCQNE EILNSLKYVR HGGGFQPTFS LTQKCDVNGQ NQHPVFAYLK
DKLPYPYDDP FSLMTDPKLI IWSPVRRSDV SWNFEKFLIG PEGEPFRRYS RTFQTINIEP
DIKRLLKVAI
