ID   GPX2_HYLLA              Reviewed;         190 AA.
AC   Q4AEH9;
DT   11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 2.
DT   27-MAR-2024, entry version 68.
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   Hylobates lar (Lar gibbon) (White-handed gibbon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hylobatidae;
OC   Hylobates.
OX   NCBI_TaxID=9580;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=15967696; DOI=10.1016/j.cbpc.2005.05.002;
RA   Fukuhara R., Kageyama T.;
RT   "Structure, gene expression, and evolution of primate glutathione
RT   peroxidases.";
RL   Comp. Biochem. Physiol. 141B:428-436(2005).
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; AB121002; BAE17011.1; -; mRNA.
DR   SMR; Q4AEH9; -.
DR   PeroxiBase; 3697; HlGPx02.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0004602; F:glutathione peroxidase activity; ISS:UniProtKB.
DR   GO; GO:0047066; F:phospholipid-hydroperoxide glutathione peroxidase activity; IEA:RHEA.
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.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Oxidoreductase; Peroxidase; Selenocysteine.
FT   CHAIN           1..190
FT                   /note="Glutathione peroxidase 2"
FT                   /id="PRO_0000066620"
FT   ACT_SITE        40
FT                   /evidence="ECO:0000250|UniProtKB:O70325"
FT   NON_STD         40
FT                   /note="Selenocysteine"
FT                   /evidence="ECO:0000250|UniProtKB:O70325"
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
//