ID   GPX4_ARATH              Reviewed;         170 AA.
AC   Q8L910;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=Probable glutathione peroxidase 4;
DE            EC=1.11.1.9;
GN   Name=GPX4; OrderedLocusNames=At2g48150; ORFNames=F11L15.5;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11910074; DOI=10.1126/science.1071006;
RA   Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA   Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA   Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA   Shinagawa A., Shinozaki K.;
RT   "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL   Science 296:141-145(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=14617062; DOI=10.1046/j.1365-313x.2003.01901.x;
RA   Rodriguez Milla M.A., Maurer A., Rodriguez Huete A., Gustafson J.P.;
RT   "Glutathione peroxidase genes in Arabidopsis are ubiquitous and regulated
RT   by abiotic stresses through diverse signaling pathways.";
RL   Plant J. 36:602-615(2003).
CC   -!- FUNCTION: May constitute a glutathione peroxidase-like protective
CC       system against oxidative stresses. {ECO:0000250}.
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   -!- SIMILARITY: Belongs to the glutathione peroxidase family.
CC       {ECO:0000305}.
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DR   EMBL; AC006072; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CP002685; AEC10946.1; -; Genomic_DNA.
DR   EMBL; AK118448; BAC43057.1; -; mRNA.
DR   EMBL; BT003735; AAO39963.1; -; mRNA.
DR   EMBL; AY088692; AAM67012.1; -; mRNA.
DR   RefSeq; NP_566128.1; NM_130382.2.
DR   AlphaFoldDB; Q8L910; -.
DR   SMR; Q8L910; -.
DR   STRING; 3702.AT2G48150.1; -.
DR   PeroxiBase; 2474; AtGPx04.
DR   PaxDb; Q8L910; -.
DR   PRIDE; Q8L910; -.
DR   ProteomicsDB; 220707; -.
DR   EnsemblPlants; AT2G48150.1; AT2G48150.1; AT2G48150.
DR   GeneID; 819427; -.
DR   Gramene; AT2G48150.1; AT2G48150.1; AT2G48150.
DR   KEGG; ath:AT2G48150; -.
DR   Araport; AT2G48150; -.
DR   TAIR; locus:2039346; AT2G48150.
DR   eggNOG; KOG1651; Eukaryota.
DR   HOGENOM; CLU_029507_0_1_1; -.
DR   InParanoid; Q8L910; -.
DR   OMA; YCGFTPQ; -.
DR   OrthoDB; 1483113at2759; -.
DR   PhylomeDB; Q8L910; -.
DR   BioCyc; ARA:AT2G48150-MON; -.
DR   PRO; PR:Q8L910; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q8L910; baseline and differential.
DR   Genevisible; Q8L910; AT.
DR   GO; GO:0005829; C:cytosol; HDA:TAIR.
DR   GO; GO:0012505; C:endomembrane system; IDA:TAIR.
DR   GO; GO:0004602; F:glutathione peroxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004601; F:peroxidase activity; IBA:GO_Central.
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   Oxidoreductase; Peroxidase; Reference proteome.
FT   CHAIN           1..170
FT                   /note="Probable glutathione peroxidase 4"
FT                   /id="PRO_0000066638"
FT   ACT_SITE        44
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   170 AA;  19300 MW;  963FD204BE596579 CRC64;
     MGASASVPER SVHQFTVKDS SGKDLNMSIY QGKVLLIVNV ASKCGFTETN YTQLTELYRK
     YKDQDFEILA FPCNQFLYQE PGTSQEAHEF ACERFKAEYP VFQKVRVNGQ NAAPIYKFLK
     ASKPTFLGSR IKWNFTKFLV GKDGLVIDRY GTMVTPLSIE KDIKKALEDA