ID G3V4J6_HUMAN Unreviewed; 78 AA.
AC G3V4J6;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=Glutathione peroxidase {ECO:0000256|RuleBase:RU000499};
GN Name=GPX2 {ECO:0000313|Ensembl:ENSP00000451844.1};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000451844.1, ECO:0000313|Proteomes:UP000005640};
RN [1] {ECO:0000313|Ensembl:ENSP00000451844.1, ECO:0000313|Proteomes:UP000005640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [2] {ECO:0000313|Ensembl:ENSP00000451844.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00043817};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76692;
CC Evidence={ECO:0000256|ARBA:ARBA00043817};
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:0000256|ARBA:ARBA00043784};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76696;
CC Evidence={ECO:0000256|ARBA:ARBA00043784};
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:0000256|ARBA:ARBA00043664};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48621;
CC Evidence={ECO:0000256|ARBA:ARBA00043664};
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:0000256|ARBA:ARBA00036108};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16834;
CC Evidence={ECO:0000256|ARBA:ARBA00036108};
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:0000256|ARBA:ARBA00035992};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69413;
CC Evidence={ECO:0000256|ARBA:ARBA00035992};
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:0000256|ARBA:ARBA00036755};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69652;
CC Evidence={ECO:0000256|ARBA:ARBA00036755};
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000256|ARBA:ARBA00004514}.
CC -!- SIMILARITY: Belongs to the glutathione peroxidase family.
CC {ECO:0000256|ARBA:ARBA00006926, ECO:0000256|RuleBase:RU000499}.
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DR EMBL; AL139022; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; G3V4J6; -.
DR SMR; G3V4J6; -.
DR MassIVE; G3V4J6; -.
DR MaxQB; G3V4J6; -.
DR PeptideAtlas; G3V4J6; -.
DR ProteomicsDB; 33251; -.
DR Ensembl; ENST00000557323.1; ENSP00000451844.1; ENSG00000176153.13.
DR UCSC; uc059clg.1; human.
DR HGNC; HGNC:4554; GPX2.
DR VEuPathDB; HostDB:ENSG00000176153; -.
DR GeneTree; ENSGT00940000160477; -.
DR HOGENOM; CLU_029507_6_2_1; -.
DR ChiTaRS; GPX2; human.
DR Proteomes; UP000005640; Chromosome 14.
DR Bgee; ENSG00000176153; Expressed in gall bladder and 144 other cell types or tissues.
DR ExpressionAtlas; G3V4J6; baseline and differential.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0004602; F:glutathione peroxidase activity; IEA:InterPro.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
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 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 1: Evidence at protein level;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU000499};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000256|RuleBase:RU000499};
KW Proteomics identification {ECO:0007829|MaxQB:G3V4J6,
KW ECO:0007829|PeptideAtlas:G3V4J6};
KW Reference proteome {ECO:0000313|Proteomes:UP000005640}.
SQ SEQUENCE 78 AA; 8917 MW; 0456B3DED203B23C CRC64;
MAFIAKSFYD LSAISLDGEK VDFNTFRGRA VLIENVASLC GTTTRDFTQL NELQCRFPRR
LVVLGFPCNQ FGHQERQK
//
