ID   GPX1_ARATH              Reviewed;         236 AA.
AC   P52032; O19985; O81717;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   27-MAR-2002, sequence version 2.
DT   04-NOV-2008, entry version 73.
DE   RecName: Full=Phospholipid hydroperoxide glutathione peroxidase 1, chloroplastic;
DE            Short=PHGPx;
DE            EC=1.11.1.12;
DE   Flags: Precursor;
GN   Name=GPX1; OrderedLocusNames=At2g25080; ORFNames=F13D4.40;
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   Gachotte D., Benveniste P.;
RT   "Cloning and sequencing of a glutathione peroxidase homologue from
RT   Arabidopsis thaliana.";
RL   (er) Plant Gene Register PGR95-133.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Columbia;
RX   MEDLINE=98345965; PubMed=9680987;
RA   Mullineaux P.M., Karpinski S., Jimenez A., Cleary S.P., Robinson C.,
RA   Creissen G.P.;
RT   "Identification of cDNAS encoding plastid-targeted glutathione
RT   peroxidase.";
RL   Plant J. 13:375-379(1998).
RN   [3]
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   [4]
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   [5]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   MEDLINE=22745486; PubMed=12766230; DOI=10.1074/mcp.M300030-MCP200;
RA   Ferro M., Salvi D., Brugiere S., Miras S., Kowalski S., Louwagie M.,
RA   Garin J., Joyard J., Rolland N.;
RT   "Proteomics of the chloroplast envelope membranes from Arabidopsis
RT   thaliana.";
RL   Mol. Cell. Proteomics 2:325-345(2003).
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
RT   regulated by abiotic stresses through diverse signaling pathways.";
RL   Plant J. 36:602-615(2003).
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 (By similarity).
CC   -!- CATALYTIC ACTIVITY: 2 glutathione + a lipid hydroperoxide =
CC       glutathione disulfide + lipid + 2 H(2)O.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma.
CC   -!- TISSUE SPECIFICITY: Expressed in leaves, stems, flowers, green
CC       siliques and seeds.
CC   -!- INDUCTION: By salt stress, osmotic stress, metals and heat
CC       treatment. Up-regulated by abscisic acid (ABA) and auxin.
CC   -!- SIMILARITY: Belongs to the glutathione peroxidase family.
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DR   EMBL; X89866; CAA61965.1; -; mRNA.
DR   EMBL; AJ000469; CAA04112.1; -; mRNA.
DR   EMBL; AY035153; AAK59657.1; -; mRNA.
DR   EMBL; AY063024; AAL34198.1; -; mRNA.
DR   PIR; A84644; A84644.
DR   PIR; S71250; S71250.
DR   RefSeq; NP_180080.1; -.
DR   UniGene; At.24670; -.
DR   HSSP; P00435; 1GP1.
DR   PeroxiBase; 2499; AtGPx01.
DR   GeneID; 817046; -.
DR   GenomeReviews; CT485783_GR; AT2G25080.
DR   KEGG; ath:AT2G25080; -.
DR   NMPDR; fig|3702.1.peg.9525; -.
DR   GeneFarm; 2047; 163.
DR   TAIR; At2g25080; -.
DR   ArrayExpress; P52032; -.
DR   GermOnline; AT2G25080; Arabidopsis thaliana.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-KW.
DR   GO; GO:0047066; F:phospholipid-hydroperoxide glutathione pero...; IEA:EC.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR000889; Glut_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   Chloroplast; Complete proteome; Oxidoreductase; Peroxidase; Plastid;
KW   Stress response; Transit peptide.
FT   TRANSIT       1     64       Chloroplast (Potential).
FT   CHAIN        65    236       Phospholipid hydroperoxide glutathione
FT                                peroxidase 1, chloroplastic.
FT                                /FTId=PRO_0000013086.
FT   ACT_SITE    111    111       By similarity.
FT   CONFLICT     18     18       V -> F (in Ref. 1; CAA61965).
FT   CONFLICT    236    236       A -> ELKNF (in Ref. 1).
SQ   SEQUENCE   236 AA;  26016 MW;  D676C0381526C37A CRC64;
     MVSMTTSSSS YGTFSTVVNS SRPNSSATFL VPSLKFSTGI SNFANLSNGF SLKSPINPGF
     LFKSRPFTVQ ARAAAEKTVH DFTVKDIDGK DVALNKFKGK VMLIVNVASR CGLTSSNYSE
     LSHLYEKYKT QGFEILAFPC NQFGFQEPGS NSEIKQFACT RFKAEFPIFD KVDVNGPSTA
     PIYEFLKSNA GGFLGGLIKW NFEKFLIDKK GKVVERYPPT TSPFQIEKDI QKLLAA
//