ID   GPX4_MESCR              Reviewed;         170 AA.
AC   Q9LEF0;
DT   27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 78.
DE   RecName: Full=Probable phospholipid hydroperoxide glutathione peroxidase;
DE            Short=PHGPx;
DE            EC=1.11.1.12;
GN   Name=GPXMC1;
OS   Mesembryanthemum crystallinum (Common ice plant) (Cryophytum crystallinum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Caryophyllales; Aizoaceae; Mesembryanthemum;
OC   Mesembryanthemum subgen. Cryophytum.
OX   NCBI_TaxID=3544;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaf;
RA   Kiefer M., Cushman J.C., Ratajczak R., Haag-Kerwer A.;
RT   "A putative phospholipid hydroperoxide glutathione peroxidase from the
RT   common ice plant Mesembryanthemum crystallinum.";
RL   Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; AJ250951; CAB96145.1; -; mRNA.
DR   EMBL; AJ315976; CAC83045.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9LEF0; -.
DR   SMR; Q9LEF0; -.
DR   PeroxiBase; 2866; McGPx06.
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..170
FT                   /note="Probable phospholipid hydroperoxide glutathione
FT                   peroxidase"
FT                   /id="PRO_0000066632"
FT   ACT_SITE        44
FT                   /evidence="ECO:0000250|UniProtKB:P36968"
SQ   SEQUENCE   170 AA;  18917 MW;  10FBD855BBFC4798 CRC64;
     MASQSTDQPK SIHDFIVKDA RGNDVDLSIY KGKVLLIVNV ASQCGLTNSN YPELTKLYEQ
     YKDKGLEILA FPCNQFGNQE PGDNEQIMEF ACTRFKAEFP IFDKVDVNGS NAAPVYKYLK
     SSKGGLFGDG IKWNFTKFLV DRDGKVVDRY APTTSPASIE KDIKKLIGTS