GPX2_MOUSE
ID GPX2_MOUSE Reviewed; 190 AA.
AC Q9JHC0; Q3V2B2;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 3.
DT 25-MAY-2022, entry version 143.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129;
RX PubMed=8661011; DOI=10.1006/geno.1996.0227;
RA Chu F.-F., Esworthy R.S., Burmeister M.;
RT "The mouse glutathione peroxidase Gpx2 gene maps to chromosome 12; its
RT pseudogene Gpx2-ps maps to chromosome 7.";
RL Genomics 33:516-518(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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; U62658; AAD41533.1; -; Genomic_DNA.
DR EMBL; AK131940; BAE20886.1; -; mRNA.
DR EMBL; BC010823; AAH10823.1; -; mRNA.
DR EMBL; BC034335; AAH34335.1; -; mRNA.
DR EMBL; BC039658; AAH39658.1; -; mRNA.
DR EMBL; BC054848; AAH54848.2; -; mRNA.
DR CCDS; CCDS25996.1; -.
DR RefSeq; NP_109602.2; NM_030677.2.
DR STRING; 10090.ENSMUSP00000081012; -.
DR PeroxiBase; 3710; MmGPx02.
DR iPTMnet; Q9JHC0; -.
DR PhosphoSitePlus; Q9JHC0; -.
DR jPOST; Q9JHC0; -.
DR MaxQB; Q9JHC0; -.
DR PaxDb; Q9JHC0; -.
DR PeptideAtlas; Q9JHC0; -.
DR PRIDE; Q9JHC0; -.
DR ProteomicsDB; 271051; -.
DR DNASU; 14776; -.
DR GeneID; 14776; -.
DR KEGG; mmu:14776; -.
DR UCSC; uc007nys.1; mouse.
DR CTD; 2877; -.
DR MGI; MGI:106609; Gpx2.
DR eggNOG; KOG1651; Eukaryota.
DR InParanoid; Q9JHC0; -.
DR OrthoDB; 1483113at2759; -.
DR PhylomeDB; Q9JHC0; -.
DR TreeFam; TF105318; -.
DR Reactome; R-MMU-2142712; Synthesis of 12-eicosatetraenoic acid derivatives.
DR Reactome; R-MMU-2142770; Synthesis of 15-eicosatetraenoic acid derivatives.
DR Reactome; R-MMU-3299685; Detoxification of Reactive Oxygen Species.
DR Reactome; R-MMU-5628897; TP53 Regulates Metabolic Genes.
DR BioGRID-ORCS; 14776; 2 hits in 76 CRISPR screens.
DR ChiTaRS; Gpx2; mouse.
DR PRO; PR:Q9JHC0; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9JHC0; protein.
DR GO; GO:0005829; C:cytosol; TAS:MGI.
DR GO; GO:0004602; F:glutathione peroxidase activity; IMP:MGI.
DR GO; GO:0004601; F:peroxidase activity; IBA:GO_Central.
DR GO; GO:0051702; P:biological process involved in interaction with symbiont; IGI:MGI.
DR GO; GO:0002862; P:negative regulation of inflammatory response to antigenic stimulus; IGI:MGI.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR GO; GO:0009609; P:response to symbiotic bacterium; IGI:MGI.
DR GO; GO:0001659; P:temperature homeostasis; IGI:MGI.
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_0000066622"
FT ACT_SITE 40
FT NON_STD 40
FT /note="Selenocysteine"
FT CONFLICT 14
FT /note="I -> V (in Ref. 2; BAE20886)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 190 AA; 21990 MW; F66BDD7A431E1A6D CRC64;
MAYIAKSFYD LSAIGLDGEK IDFNTFRGRA VLIENVASLU GTTTRDYNQL NELQCRFPRR
LVVLGFPCNQ FGHQENCQNE EILNSLKYVR PGGGYQPTFS LTQKCDVNGQ NEHPVFAYLK
DKLPYPYDDP FSLMTDPKLI IWSPVRRSDV SWNFEKFLIG PEGEPFRRYS RSFQTINIEP
DIKRLLKVAI
