ID   GPX2_HUMAN              Reviewed;         190 AA.
AC   P18283; Q6PJ52; Q8WWI7; Q9NRP9;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 3.
DT   27-MAR-2024, entry version 206.
DE   RecName: Full=Glutathione peroxidase 2;
DE            Short=GPx-2;
DE            Short=GSHPx-2;
DE            EC=1.11.1.9 {ECO:0000269|PubMed:8428933};
DE   AltName: Full=Gastrointestinal glutathione peroxidase;
DE   AltName: Full=Glutathione peroxidase-gastrointestinal {ECO:0000303|PubMed:8428933};
DE            Short=GPx-GI {ECO:0000303|PubMed:8428933};
DE            Short=GSHPx-GI {ECO:0000303|PubMed:8428933};
DE   AltName: Full=Glutathione peroxidase-related protein 2;
DE            Short=GPRP-2;
DE   AltName: Full=Phospholipid hydroperoxide glutathione peroxidase GPX2 {ECO:0000303|PubMed:36608588};
DE            EC=1.11.1.12 {ECO:0000269|PubMed:36608588};
GN   Name=GPX2 {ECO:0000303|Ref.9, ECO:0000312|HGNC:HGNC:4554};
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   PubMed=2388849; DOI=10.1093/nar/18.15.4619;
RA   Akasaka M., Mizoguchi J., Takahashi K.;
RT   "A human cDNA sequence of a novel glutathione peroxidase-related protein.";
RL   Nucleic Acids Res. 18:4619-4619(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR
RP   LOCATION, TISSUE SPECIFICITY, AND SUBUNIT.
RC   TISSUE=Liver;
RX   PubMed=8428933; DOI=10.1016/s0021-9258(18)53812-6;
RA   Chu F.-F., Doroshow J.H., Esworthy R.S.;
RT   "Expression, characterization, and tissue distribution of a new cellular
RT   selenium-dependent glutathione peroxidase, GSHPx-GI.";
RL   J. Biol. Chem. 268:2571-2576(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT LEU-37.
RX   PubMed=10806356; DOI=10.1016/s0378-1119(00)00137-2;
RA   Kelner M.J., Bagnell R.D., Montoya M.A., Lanham K.A.;
RT   "Structural organization of the human gastrointestinal glutathione
RT   peroxidase (GPX2) promoter and 3'-nontranscribed region: transcriptional
RT   response to exogenous redox agents.";
RL   Gene 248:109-116(2000).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS LEU-126 AND CYS-146.
RG   NIEHS SNPs program;
RL   Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN   [5]
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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain, Prostate, and Urinary bladder;
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).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [8]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=36608588; DOI=10.1016/j.redox.2022.102593;
RA   Schwarz M., Loeser A., Cheng Q., Wichmann-Costaganna M., Schaedel P.,
RA   Werz O., Arner E.S., Kipp A.P.;
RT   "Side-by-side comparison of recombinant human glutathione peroxidases
RT   identifies overlapping substrate specificities for soluble
RT   hydroperoxides.";
RL   Redox Biol. 59:102593-102593(2023).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 4-188.
RG   Structural genomics consortium (SGC);
RT   "Crystal structure of the selenocysteine to cysteine mutant of human
RT   glutathione peroxidase 2 (GPX2).";
RL   Submitted (FEB-2009) to the PDB data bank.
CC   -!- FUNCTION: Catalyzes the reduction of hydroperoxides in a glutathione-
CC       dependent manner thus regulating cellular redox homeostasis
CC       (PubMed:8428933, PubMed:36608588). Can reduce small soluble
CC       hydroperoxides such as H2O2, cumene hydroperoxide and tert-butyl
CC       hydroperoxide, as well as several fatty acid-derived hydroperoxides
CC       (PubMed:8428933, PubMed:36608588). Cannot reduce phosphatidycholine
CC       hydroperoxide (PubMed:8428933). {ECO:0000269|PubMed:36608588,
CC       ECO:0000269|PubMed:8428933}.
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:0000269|PubMed:36608588, ECO:0000269|PubMed:8428933};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16834;
CC         Evidence={ECO:0000269|PubMed:8428933};
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:0000269|PubMed:36608588};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19058;
CC         Evidence={ECO:0000305|PubMed:36608588};
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:0000269|PubMed:36608588, ECO:0000269|PubMed:8428933};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69413;
CC         Evidence={ECO:0000269|PubMed:8428933};
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:0000269|PubMed:36608588,
CC         ECO:0000269|PubMed:8428933};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69652;
CC         Evidence={ECO:0000269|PubMed:8428933};
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:0000269|PubMed:36608588};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48889;
CC         Evidence={ECO:0000305|PubMed:36608588};
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:0000269|PubMed:36608588};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48621;
CC         Evidence={ECO:0000305|PubMed:36608588};
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:0000269|PubMed:36608588};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76692;
CC         Evidence={ECO:0000305|PubMed:36608588};
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:0000269|PubMed:36608588};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76696;
CC         Evidence={ECO:0000305|PubMed:36608588};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:8428933}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:8428933}.
CC   -!- TISSUE SPECIFICITY: Mostly in liver and gastrointestinal tract, not
CC       found in heart or kidney. {ECO:0000269|PubMed:8428933}.
CC   -!- SIMILARITY: Belongs to the glutathione peroxidase family.
CC       {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC       URL="http://egp.gs.washington.edu/data/gpx2/";
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DR   EMBL; X53463; CAB43534.1; -; mRNA.
DR   EMBL; X68314; CAA48394.1; -; mRNA.
DR   EMBL; AF199441; AAF74026.1; -; Genomic_DNA.
DR   EMBL; AY785560; AAV31780.1; -; Genomic_DNA.
DR   EMBL; AL139022; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC005277; AAH05277.1; -; mRNA.
DR   EMBL; BC016756; AAH16756.1; -; mRNA.
DR   EMBL; BC022820; AAH22820.2; -; mRNA.
DR   EMBL; BC067221; AAH67221.1; -; mRNA.
DR   CCDS; CCDS41964.1; -.
DR   PIR; A45207; A45207.
DR   RefSeq; NP_002074.2; NM_002083.3.
DR   PDB; 2HE3; X-ray; 2.10 A; A=4-188.
DR   PDBsum; 2HE3; -.
DR   SMR; P18283; -.
DR   BioGRID; 109135; 3.
DR   IntAct; P18283; 4.
DR   MINT; P18283; -.
DR   STRING; 9606.ENSP00000374265; -.
DR   DrugBank; DB09096; Benzoyl peroxide.
DR   DrugBank; DB00143; Glutathione.
DR   DrugBank; DB03310; Glutathione disulfide.
DR   PeroxiBase; 3601; HsGPx02.
DR   iPTMnet; P18283; -.
DR   PhosphoSitePlus; P18283; -.
DR   BioMuta; GPX2; -.
DR   DMDM; 172046064; -.
DR   jPOST; P18283; -.
DR   MassIVE; P18283; -.
DR   MaxQB; P18283; -.
DR   PaxDb; 9606-ENSP00000374265; -.
DR   PeptideAtlas; P18283; -.
DR   ProteomicsDB; 53556; -.
DR   Antibodypedia; 47304; 217 antibodies from 31 providers.
DR   DNASU; 2877; -.
DR   Ensembl; ENST00000389614.6; ENSP00000374265.5; ENSG00000176153.13.
DR   GeneID; 2877; -.
DR   KEGG; hsa:2877; -.
DR   MANE-Select; ENST00000389614.6; ENSP00000374265.5; NM_002083.4; NP_002074.2.
DR   UCSC; uc021ruq.3; human.
DR   AGR; HGNC:4554; -.
DR   CTD; 2877; -.
DR   DisGeNET; 2877; -.
DR   GeneCards; GPX2; -.
DR   HGNC; HGNC:4554; GPX2.
DR   HPA; ENSG00000176153; Tissue enhanced (gallbladder, intestine, liver, stomach, urinary bladder).
DR   MIM; 138319; gene.
DR   neXtProt; NX_P18283; -.
DR   OpenTargets; ENSG00000176153; -.
DR   PharmGKB; PA28950; -.
DR   VEuPathDB; HostDB:ENSG00000176153; -.
DR   eggNOG; KOG1651; Eukaryota.
DR   GeneTree; ENSGT00940000160477; -.
DR   HOGENOM; CLU_029507_2_0_1; -.
DR   InParanoid; P18283; -.
DR   OMA; NGEILNC; -.
DR   OrthoDB; 67394at2759; -.
DR   PhylomeDB; P18283; -.
DR   TreeFam; TF105318; -.
DR   BioCyc; MetaCyc:HS11006-MONOMER; -.
DR   BRENDA; 1.11.1.9; 2681.
DR   PathwayCommons; P18283; -.
DR   Reactome; R-HSA-2142688; Synthesis of 5-eicosatetraenoic acids.
DR   Reactome; R-HSA-2142712; Synthesis of 12-eicosatetraenoic acid derivatives.
DR   Reactome; R-HSA-2142770; Synthesis of 15-eicosatetraenoic acid derivatives.
DR   Reactome; R-HSA-3299685; Detoxification of Reactive Oxygen Species.
DR   Reactome; R-HSA-5628897; TP53 Regulates Metabolic Genes.
DR   SABIO-RK; P18283; -.
DR   SignaLink; P18283; -.
DR   BioGRID-ORCS; 2877; 29 hits in 1160 CRISPR screens.
DR   ChiTaRS; GPX2; human.
DR   EvolutionaryTrace; P18283; -.
DR   GeneWiki; GPX2_(gene); -.
DR   GenomeRNAi; 2877; -.
DR   Pharos; P18283; Tbio.
DR   PRO; PR:P18283; -.
DR   Proteomes; UP000005640; Chromosome 14.
DR   RNAct; P18283; Protein.
DR   Bgee; ENSG00000176153; Expressed in gall bladder and 144 other cell types or tissues.
DR   ExpressionAtlas; P18283; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
DR   GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR   GO; GO:0045171; C:intercellular bridge; IDA:HPA.
DR   GO; GO:0072686; C:mitotic spindle; IDA:HPA.
DR   GO; GO:0009055; F:electron transfer activity; TAS:UniProtKB.
DR   GO; GO:0004602; F:glutathione peroxidase activity; IDA:UniProtKB.
DR   GO; GO:0047066; F:phospholipid-hydroperoxide glutathione peroxidase activity; IDA:UniProtKB.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
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.
DR   Genevisible; P18283; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Oxidoreductase; Peroxidase; Reference proteome;
KW   Selenocysteine.
FT   CHAIN           1..190
FT                   /note="Glutathione peroxidase 2"
FT                   /id="PRO_0000066619"
FT   ACT_SITE        40
FT                   /evidence="ECO:0000250|UniProtKB:O70325"
FT   NON_STD         40
FT                   /note="Selenocysteine"
FT                   /evidence="ECO:0000250|UniProtKB:O70325"
FT   VARIANT         37
FT                   /note="A -> L (requires 2 nucleotide substitutions)"
FT                   /evidence="ECO:0000269|PubMed:10806356"
FT                   /id="VAR_003615"
FT   VARIANT         126
FT                   /note="P -> L (in dbSNP:rs17881652)"
FT                   /evidence="ECO:0000269|Ref.4"
FT                   /id="VAR_020916"
FT   VARIANT         146
FT                   /note="R -> C (in dbSNP:rs17880492)"
FT                   /evidence="ECO:0000269|Ref.4"
FT                   /id="VAR_020917"
FT   VARIANT         176
FT                   /note="I -> M"
FT                   /id="VAR_003616"
FT   CONFLICT        37
FT                   /note="A -> R (in Ref. 1; CAB43534)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        77
FT                   /note="C -> S (in Ref. 1; CAB43534)"
FT                   /evidence="ECO:0000305"
FT   HELIX           8..10
FT                   /evidence="ECO:0007829|PDB:2HE3"
FT   STRAND          12..15
FT                   /evidence="ECO:0007829|PDB:2HE3"
FT   STRAND          20..22
FT                   /evidence="ECO:0007829|PDB:2HE3"
FT   HELIX           23..26
FT                   /evidence="ECO:0007829|PDB:2HE3"
FT   STRAND          29..36
FT                   /evidence="ECO:0007829|PDB:2HE3"
FT   HELIX           43..56
FT                   /evidence="ECO:0007829|PDB:2HE3"
FT   TURN            58..60
FT                   /evidence="ECO:0007829|PDB:2HE3"
FT   STRAND          61..68
FT                   /evidence="ECO:0007829|PDB:2HE3"
FT   HELIX           79..81
FT                   /evidence="ECO:0007829|PDB:2HE3"
FT   HELIX           82..88
FT                   /evidence="ECO:0007829|PDB:2HE3"
FT   STRAND          98..102
FT                   /evidence="ECO:0007829|PDB:2HE3"
FT   STRAND          105..109
FT                   /evidence="ECO:0007829|PDB:2HE3"
FT   HELIX           114..122
FT                   /evidence="ECO:0007829|PDB:2HE3"
FT   HELIX           137..139
FT                   /evidence="ECO:0007829|PDB:2HE3"
FT   STRAND          156..159
FT                   /evidence="ECO:0007829|PDB:2HE3"
FT   STRAND          165..169
FT                   /evidence="ECO:0007829|PDB:2HE3"
FT   HELIX           175..178
FT                   /evidence="ECO:0007829|PDB:2HE3"
FT   HELIX           179..186
FT                   /evidence="ECO:0007829|PDB:2HE3"
SQ   SEQUENCE   190 AA;  21954 MW;  FC8C4E69C4DE83A0 CRC64;
     MAFIAKSFYD LSAISLDGEK VDFNTFRGRA VLIENVASLU GTTTRDFTQL NELQCRFPRR
     LVVLGFPCNQ FGHQENCQNE EILNSLKYVR PGGGYQPTFT LVQKCEVNGQ NEHPVFAYLK
     DKLPYPYDDP FSLMTDPKLI IWSPVRRSDV AWNFEKFLIG PEGEPFRRYS RTFPTINIEP
     DIKRLLKVAI
//