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 01-MAY-2013, entry version 109.
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; malvids; Brassicales; Brassicaceae; Camelineae; 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 PubMed=9680987; DOI=10.1046/j.1365-313X.1998.00052.x;
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 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 GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RG The Arabidopsis Information Resource (TAIR);
RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
RN [5]
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.,
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 [6]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RC STRAIN=cv. Wassilewskija;
RX 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 [7]
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; CP002685; AEC07655.1; -; Genomic_DNA.
DR EMBL; AY035153; AAK59657.1; -; mRNA.
DR EMBL; AY063024; AAL34198.1; -; mRNA.
DR IPI; IPI00520738; -.
DR PIR; A84644; A84644.
DR PIR; S71250; S71250.
DR RefSeq; NP_180080.1; NM_128065.4.
DR UniGene; At.24670; -.
DR ProteinModelPortal; P52032; -.
DR SMR; P52032; 77-234.
DR PeroxiBase; 2499; AtGPx01.
DR PaxDb; P52032; -.
DR PRIDE; P52032; -.
DR EnsemblPlants; AT2G25080.1; AT2G25080.1; AT2G25080.
DR GeneID; 817046; -.
DR KEGG; ath:AT2G25080; -.
DR GeneFarm; 2047; 163.
DR TAIR; At2g25080; -.
DR eggNOG; COG0386; -.
DR HOGENOM; HOG000277054; -.
DR InParanoid; P52032; -.
DR KO; K00432; -.
DR OMA; MASIYDF; -.
DR PhylomeDB; P52032; -.
DR ProtClustDB; PLN02399; -.
DR Genevestigator; P52032; -.
DR GermOnline; AT2G25080; Arabidopsis thaliana.
DR GO; GO:0009941; C:chloroplast envelope; IDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IDA:TAIR.
DR GO; GO:0004602; F:glutathione peroxidase activity; IEA:InterPro.
DR GO; GO:0047066; F:phospholipid-hydroperoxide glutathione peroxidase activity; IEA:EC.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR Gene3D; 3.40.30.10; -; 1.
DR InterPro; IPR000889; Glutathione_peroxidase.
DR InterPro; IPR012336; Thioredoxin-like_fold.
DR PANTHER; PTHR11592; PTHR11592; 1.
DR Pfam; PF00255; GSHPx; 1.
DR PIRSF; PIRSF000303; Glutathion_perox; 1.
DR PRINTS; PR01011; GLUTPROXDASE.
DR SUPFAM; SSF52833; Thiordxn-like_fd; 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 Chloroplast; Complete proteome; Oxidoreductase; Peroxidase; Plastid;
KW Reference proteome; 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
//
