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 27-MAR-2024, entry version 150.
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;
DE AltName: Full=Phospholipid hydroperoxide glutathione peroxidase GPX2;
DE EC=1.11.1.12 {ECO:0000250|UniProtKB:P18283};
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: Catalyzes the reduction of hydroperoxides in a glutathione-
CC dependent manner thus regulating cellular redox homeostasis. Can reduce
CC small soluble hydroperoxides such as H2O2, cumene hydroperoxide and
CC tert-butyl hydroperoxide, as well as several fatty acid-derived
CC hydroperoxides. Cannot reduce phosphatidycholine hydroperoxide.
CC {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=a hydroperoxy polyunsaturated fatty acid + 2 glutathione = a
CC hydroxy polyunsaturated fatty acid + glutathione disulfide + H2O;
CC Xref=Rhea:RHEA:19057, ChEBI:CHEBI:15377, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:58297, ChEBI:CHEBI:131871, ChEBI:CHEBI:134019;
CC EC=1.11.1.12; Evidence={ECO:0000250|UniProtKB:P18283};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19058;
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 -!- CATALYTIC ACTIVITY:
CC Reaction=(13S)-hydroperoxy-(9Z,11E)-octadecadienoate + 2 glutathione =
CC (13S)-hydroxy-(9Z,11E)-octadecadienoate + glutathione disulfide +
CC H2O; Xref=Rhea:RHEA:48888, ChEBI:CHEBI:15377, ChEBI:CHEBI:57466,
CC ChEBI:CHEBI:57925, ChEBI:CHEBI:58297, ChEBI:CHEBI:90850;
CC Evidence={ECO:0000250|UniProtKB:P18283};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48889;
CC Evidence={ECO:0000250|UniProtKB:P18283};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5S)-hydroperoxy-(6E,8Z,11Z,14Z)-eicosatetraenoate + 2
CC glutathione = (5S)-hydroxy-(6E,8Z,11Z,14Z)-eicosatetraenoate +
CC glutathione disulfide + H2O; Xref=Rhea:RHEA:48620, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:57450, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297,
CC ChEBI:CHEBI:90632; Evidence={ECO:0000250|UniProtKB:P18283};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48621;
CC Evidence={ECO:0000250|UniProtKB:P18283};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(12R)-hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoate + 2
CC glutathione = (12R)-hydroxy-(5Z,8Z,10E,14Z)-eicosatetraenoate +
CC glutathione disulfide + H2O; Xref=Rhea:RHEA:76691, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:57925, ChEBI:CHEBI:58297, ChEBI:CHEBI:75230,
CC ChEBI:CHEBI:83343; Evidence={ECO:0000250|UniProtKB:P18283};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76692;
CC Evidence={ECO:0000250|UniProtKB:P18283};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoate + 2
CC glutathione = (15S)-hydroxy-(5Z,8Z,11Z,13E)-eicosatetraenoate +
CC glutathione disulfide + H2O; Xref=Rhea:RHEA:76695, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:57409, ChEBI:CHEBI:57446, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:58297; Evidence={ECO:0000250|UniProtKB:P18283};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76696;
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; 10090-ENSMUSP00000081012; -.
DR PeptideAtlas; Q9JHC0; -.
DR ProteomicsDB; 271051; -.
DR DNASU; 14776; -.
DR GeneID; 14776; -.
DR KEGG; mmu:14776; -.
DR UCSC; uc007nys.1; mouse.
DR AGR; MGI:106609; -.
DR CTD; 2877; -.
DR MGI; MGI:106609; Gpx2.
DR eggNOG; KOG1651; Eukaryota.
DR InParanoid; Q9JHC0; -.
DR OrthoDB; 67394at2759; -.
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 81 CRISPR screens.
DR ChiTaRS; Gpx2; mouse.
DR PRO; PR:Q9JHC0; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9JHC0; Protein.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0045171; C:intercellular bridge; ISO:MGI.
DR GO; GO:0072686; C:mitotic spindle; ISO:MGI.
DR GO; GO:0004602; F:glutathione peroxidase activity; IMP:MGI.
DR GO; GO:0047066; F:phospholipid-hydroperoxide glutathione peroxidase activity; ISO:MGI.
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 Gene3D; 3.40.30.10; Glutaredoxin; 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; GLUTATHIONE PEROXIDASE; 1.
DR PANTHER; PTHR11592:SF36; GLUTATHIONE PEROXIDASE 2; 1.
DR Pfam; PF00255; GSHPx; 1.
DR PIRSF; PIRSF000303; Glutathion_perox; 1.
DR PRINTS; PR01011; GLUTPROXDASE.
DR SUPFAM; SSF52833; Thioredoxin-like; 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 /evidence="ECO:0000250|UniProtKB:O70325"
FT NON_STD 40
FT /note="Selenocysteine"
FT /evidence="ECO:0000250|UniProtKB:O70325"
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
//
