ID   GPX4_CITSI              Reviewed;         167 AA.
AC   Q06652;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Probable phospholipid hydroperoxide glutathione peroxidase;
DE            Short=PHGPx;
DE            EC=1.11.1.12;
DE   AltName: Full=Salt-associated protein;
GN   Name=CSA;
OS   Citrus sinensis (Sweet orange) (Citrus aurantium var. sinensis).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Sapindales; Rutaceae; Aurantioideae; Citrus.
OX   NCBI_TaxID=2711;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX   PubMed=8467085; DOI=10.1007/bf00027124;
RA   Holland D., Ben-Hayyim G., Faltin Z., Camoin L., Strosberg A.D., Eshdat Y.;
RT   "Molecular characterization of salt-stress-associated protein in citrus:
RT   protein and cDNA sequence homology to mammalian glutathione peroxidases.";
RL   Plant Mol. Biol. 21:923-927(1993).
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   -!- INDUCTION: By salt stress.
CC   -!- SIMILARITY: Belongs to the glutathione peroxidase family.
CC       {ECO:0000305}.
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DR   EMBL; X66377; CAA47018.1; -; mRNA.
DR   PIR; S33618; S33618.
DR   AlphaFoldDB; Q06652; -.
DR   SMR; Q06652; -.
DR   STRING; 2711.XP_006476598.1; -.
DR   PeroxiBase; 2618; CsGPx06.
DR   PRIDE; Q06652; -.
DR   eggNOG; KOG1651; Eukaryota.
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   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; Oxidoreductase; Peroxidase;
KW   Stress response.
FT   CHAIN           1..167
FT                   /note="Probable phospholipid hydroperoxide glutathione
FT                   peroxidase"
FT                   /id="PRO_0000066627"
FT   ACT_SITE        41
FT                   /evidence="ECO:0000250|UniProtKB:P36968"
SQ   SEQUENCE   167 AA;  18596 MW;  DB6BBDDC363F3260 CRC64;
     MASQSKTSVH DFTVKDAKGQ DVDLSIYKGK LLLIVNVASQ CGLTNSNYTE LSQLYDKYKN
     QGLEILAFPC NQFGAQEPGD NEQIQEFACT RFKAEFPIFD KVDVNGDNAA PLYKHLKSSK
     GGLFGDSIKW NFSKFLVDKE GNVVERYAPT TSPLSIEKDI KKLLETA