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   16-JUN-2009, entry version 68.
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; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; eurosids II; Brassicales; Brassicaceae; 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   MEDLINE=20083487; 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.,
RA   Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L.,
RA   Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H.,
RA   Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D.,
RA   Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M.,
RA   Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 402:761-768(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [4]
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   [5]
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
RT   regulated by abiotic stresses through diverse signaling pathways.";
RL   Plant J. 36:602-615(2003).
CC   -!- FUNCTION: May constitute a glutathionine peroxidase-like
CC       protective system against oxidative stresses.
CC   -!- CATALYTIC ACTIVITY: 2 glutathione + H(2)O(2) = glutathione
CC       disulfide + 2 H(2)O.
CC   -!- INTERACTION:
CC       Q9ZPS9:BRL1; NbExp=1; IntAct=EBI-2293817, EBI-2292728;
CC   -!- TISSUE SPECIFICITY: Expressed in leaves, stems, flowers, green
CC       siliques and roots.
CC   -!- INDUCTION: By salt stress and metals. Up-regulated by salicylic
CC       acid (SA).
CC   -!- SIMILARITY: Belongs to the glutathione peroxidase family.
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DR   EMBL; U94495; AAB52725.1; -; mRNA.
DR   EMBL; AC007071; AAD24836.1; -; 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   IPI; IPI00517494; -.
DR   PIR; D84722; D84722.
DR   RefSeq; NP_180715.1; -.
DR   UniGene; At.10210; -.
DR   HSSP; P00435; 1GP1.
DR   PeroxiBase; 2500; AtGPx02.
DR   PRIDE; O04922; -.
DR   GeneID; 817715; -.
DR   GenomeReviews; CT485783_GR; AT2G31570.
DR   KEGG; ath:AT2G31570; -.
DR   NMPDR; fig|3702.1.peg.10216; -.
DR   GeneFarm; 2049; 163.
DR   TAIR; At2g31570; -.
DR   OMA; O04922; ESPKSIY.
DR   BRENDA; 1.11.1.9; 302.
DR   ArrayExpress; O04922; -.
DR   GermOnline; AT2G31570; Arabidopsis thaliana.
DR   GO; GO:0005829; C:cytosol; NAS:TAIR.
DR   GO; GO:0004602; F:glutathione peroxidase activity; IEA:EC.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   InterPro; IPR000889; Glutathione_peroxidase.
DR   InterPro; IPR012335; Thioredoxin_fold.
DR   Gene3D; G3DSA:3.40.30.10; Thioredoxin_fold; 1.
DR   PANTHER; PTHR11592; Glut_peroxidase; 1.
DR   Pfam; PF00255; GSHPx; 1.
DR   PIRSF; PIRSF000303; Glutathion_perox; 1.
DR   PRINTS; PR01011; GLUTPROXDASE.
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   Complete proteome; Oxidoreductase; Peroxidase; Stress response.
FT   CHAIN         1    169       Probable glutathione peroxidase 2.
FT                                /FTId=PRO_0000066637.
FT   ACT_SITE     41     41       By similarity.
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
//