ID   GPX4_SPIOL              Reviewed;         171 AA.
AC   O23814;
DT   27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 91.
DE   RecName: Full=Probable phospholipid hydroperoxide glutathione peroxidase;
DE            Short=PHGPx;
DE            EC=1.11.1.12;
OS   Spinacia oleracea (Spinach).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Caryophyllales; Chenopodiaceae; Chenopodioideae; Anserineae; Spinacia.
OX   NCBI_TaxID=3562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. King of Denmark;
RX   PubMed=9301122; DOI=10.1271/bbb.61.1379;
RA   Sugimoto M., Furui S., Suzuki Y.;
RT   "Molecular cloning and characterization of a cDNA encoding putative
RT   phospholipid hydroperoxide glutathione peroxidase from spinach.";
RL   Biosci. Biotechnol. Biochem. 61:1379-1381(1997).
CC   -!- FUNCTION: Protects cells and enzymes from oxidative damage, by
CC       catalyzing the reduction of hydrogen peroxide, lipid peroxides and
CC       organic hydroperoxide, by glutathione. {ECO:0000250|UniProtKB:O70325}.
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:P36968};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the glutathione peroxidase family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; D63425; BAA22194.1; -; mRNA.
DR   PIR; JC5619; JC5619.
DR   AlphaFoldDB; O23814; -.
DR   SMR; O23814; -.
DR   IntAct; O23814; 1.
DR   PeroxiBase; 2925; SoGPx06.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004602; F:glutathione peroxidase activity; IEA:InterPro.
DR   GO; GO:0047066; F:phospholipid-hydroperoxide glutathione peroxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
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   InterPro; IPR013766; Thioredoxin_domain.
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.
FT   CHAIN           1..171
FT                   /note="Probable phospholipid hydroperoxide glutathione
FT                   peroxidase"
FT                   /id="PRO_0000066635"
FT   ACT_SITE        44
FT                   /evidence="ECO:0000250|UniProtKB:P36968"
SQ   SEQUENCE   171 AA;  19048 MW;  0DA82AAB80BAD476 CRC64;
     MASDSSAQPK SVHEFVVRDA RGNDVDLSIY KGKVLLIVNV ASQCGLTNSN YTEMTELYEK
     YRELGLEILA FPCNQFGNQE PGSNEEVLEF ACTRFKAEYP IFDKVDVNGS NAAPIYKFLK
     SSKGGLFGDG LKWNFTKFLV DKDGNVVDRY APTTSPKSIE KDVKKLLGIQ K