ID   GPX2_ARATH              Reviewed;         169 AA.
AC   O04922;
DT   27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 151.
DE   RecName: Full=Probable glutathione peroxidase 2;
DE            EC=1.11.1.9;
GN   Name=GPX2; OrderedLocusNames=At2g31570; ORFNames=T9H9.9;
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 [MRNA].
RC   STRAIN=cv. Columbia;
RA   Turano F.J., Caldwell C.R., McMahon M.;
RT   "Glutathione peroxidase cDNA from Arabidopsis.";
RL   Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
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   [3]
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   [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, NOMENCLATURE, TISSUE SPECIFICITY, AND INDUCTION.
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).
RN   [7]
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH DJ1A.
RX   PubMed=20406884; DOI=10.1242/jcs.063222;
RA   Xu X.M., Lin H., Maple J., Bjoerkblom B., Alves G., Larsen J.P.,
RA   Moeller S.G.;
RT   "The Arabidopsis DJ-1a protein confers stress protection through cytosolic
RT   SOD activation.";
RL   J. Cell Sci. 123:1644-1651(2010).
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   -!- SUBUNIT: Interacts with DJ1A. {ECO:0000269|PubMed:20406884}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:20406884}.
CC       Nucleus {ECO:0000269|PubMed:20406884}.
CC   -!- TISSUE SPECIFICITY: Expressed in leaves, stems, flowers, green siliques
CC       and roots. {ECO:0000269|PubMed:14617062}.
CC   -!- INDUCTION: By salt stress and metals. Up-regulated by salicylic acid
CC       (SA). {ECO:0000269|PubMed:14617062}.
CC   -!- SIMILARITY: Belongs to the glutathione peroxidase family.
CC       {ECO:0000305}.
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DR   EMBL; U94495; AAB52725.1; -; mRNA.
DR   EMBL; AC007071; AAD24836.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC08562.1; -; Genomic_DNA.
DR   EMBL; AY058187; AAL25600.1; -; mRNA.
DR   EMBL; AY044330; AAK73271.1; -; mRNA.
DR   EMBL; AY098982; AAM19992.1; -; mRNA.
DR   EMBL; AY086518; AAM63517.1; -; mRNA.
DR   PIR; D84722; D84722.
DR   RefSeq; NP_180715.1; NM_128714.4.
DR   AlphaFoldDB; O04922; -.
DR   SMR; O04922; -.
DR   BioGRID; 3062; 3.
DR   IntAct; O04922; 2.
DR   MINT; O04922; -.
DR   STRING; 3702.AT2G31570.1; -.
DR   PeroxiBase; 2500; AtGPx02.
DR   iPTMnet; O04922; -.
DR   PaxDb; O04922; -.
DR   PRIDE; O04922; -.
DR   ProteomicsDB; 220705; -.
DR   EnsemblPlants; AT2G31570.1; AT2G31570.1; AT2G31570.
DR   GeneID; 817715; -.
DR   Gramene; AT2G31570.1; AT2G31570.1; AT2G31570.
DR   KEGG; ath:AT2G31570; -.
DR   Araport; AT2G31570; -.
DR   TAIR; locus:2065928; AT2G31570.
DR   eggNOG; KOG1651; Eukaryota.
DR   HOGENOM; CLU_029507_0_1_1; -.
DR   InParanoid; O04922; -.
DR   OMA; FPMMSKI; -.
DR   OrthoDB; 1483113at2759; -.
DR   PhylomeDB; O04922; -.
DR   BioCyc; ARA:AT2G31570-MON; -.
DR   PRO; PR:O04922; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; O04922; baseline and differential.
DR   Genevisible; O04922; AT.
DR   GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0005777; C:peroxisome; HDA:TAIR.
DR   GO; GO:0005886; C:plasma membrane; HDA: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:1901149; F:salicylic acid binding; HDA:TAIR.
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; Nucleus; Oxidoreductase; Peroxidase; Reference proteome;
KW   Stress response.
FT   CHAIN           1..169
FT                   /note="Probable glutathione peroxidase 2"
FT                   /id="PRO_0000066637"
FT   ACT_SITE        41
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   169 AA;  18945 MW;  23930B83A0AE3251 CRC64;
     MADESPKSIY DFTVKDIGGN DVSLDQYKGK TLLVVNVASK CGLTDANYKE LNVLYEKYKE
     QGLEILAFPC NQFLGQEPGN NEEIQQTVCT RFKAEFPIFD KVDVNGKNTA PLYKYLKAEK
     GGLLIDAIKW NFTKFLVSPD GKVLQRYSPR TSPLQFEKDI QTALGQASS