ID   GPX6_ARATH              Reviewed;         232 AA.
AC   O48646; Q94BV3;
DT   27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2004, sequence version 2.
DT   16-JUN-2009, entry version 71.
DE   RecName: Full=Probable phospholipid hydroperoxide glutathione peroxidase 6, mitochondrial;
DE            Short=PHGPx;
DE            Short=AtGPX1;
DE            EC=1.11.1.12;
DE   Flags: Precursor;
GN   Name=GPX6; Synonyms=GPX1; OrderedLocusNames=At4g11600;
GN   ORFNames=T5C23.30;
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], TISSUE SPECIFICITY, AND INDUCTION.
RC   STRAIN=cv. Landsberg erecta;
RA   Bilodeau P., Luo M., Dennis E.S., Peacock W.J., Chaudhury A.M.;
RT   "Cloning of a cDNA encoding a putative glutathione peroxidase protein
RT   from Arabidopsis thaliana.";
RL   (er) Plant Gene Register PGR98-047.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   MEDLINE=20083488; PubMed=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G.,
RA   Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N.,
RA   Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M.,
RA   Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M.,
RA   Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T.,
RA   Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I.,
RA   Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P.,
RA   Langham S.-A., McCullagh B., Bilham L., Robben J.,
RA   van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F.,
RA   Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E.,
RA   Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P.,
RA   Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H.,
RA   De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R.,
RA   van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S.,
RA   Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R.,
RA   Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S.,
RA   Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H.,
RA   Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S.,
RA   Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A.,
RA   Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R.,
RA   Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S.,
RA   Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E.,
RA   Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A.,
RA   Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T.,
RA   Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C.,
RA   Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S.,
RA   Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K.,
RA   Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L.,
RA   Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J.,
RA   Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J.,
RA   Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D.,
RA   Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D.,
RA   Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C.,
RA   Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C.,
RA   Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R.,
RA   Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S.,
RA   Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A.,
RA   Chen E., Marra M.A., Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 402:769-777(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] OF 22-232.
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   NUCLEOTIDE SEQUENCE [MRNA] OF 31-232, AND INDUCTION.
RC   STRAIN=cv. Columbia;
RX   MEDLINE=98172218; PubMed=9511228; DOI=10.1266/ggs.72.311;
RA   Sugimoto M., Sakamoto W.;
RT   "Putative phospholipid hydroperoxide glutathione peroxidase gene from
RT   Arabidopsis thaliana induced by oxidative stress.";
RL   Genes Genet. Syst. 72:311-316(1997).
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: Mitochondrion (Potential).
CC   -!- TISSUE SPECIFICITY: Expressed at a low but detectable level in
CC       leaves, stems, and flowers, but at a higher level in siliques and
CC       even higher in roots. Predominantly expressed in seeds.
CC   -!- INDUCTION: By salt stress, osmotic stress, cold treatment, and
CC       metals. Up-regulated by salicylic acid (SA), jasmonic acid (JA),
CC       abscisic acid (ABA) and auxin.
CC   -!- SIMILARITY: Belongs to the glutathione peroxidase family.
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DR   EMBL; AF030132; AAC09173.1; ALT_INIT; mRNA.
DR   EMBL; AL049500; CAB39931.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AL161532; CAB78203.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AY039863; AAK63967.1; -; mRNA.
DR   EMBL; AY077655; AAL76133.1; -; mRNA.
DR   EMBL; AY088647; AAM66969.1; ALT_INIT; mRNA.
DR   EMBL; AB001568; BAA24226.1; ALT_INIT; mRNA.
DR   IPI; IPI00546280; -.
DR   PIR; T04207; T04207.
DR   RefSeq; NP_192897.2; -.
DR   UniGene; At.23184; -.
DR   HSSP; P00435; 1GP1.
DR   PeroxiBase; 2502; AtGPx06.
DR   PRIDE; O48646; -.
DR   GeneID; 826765; -.
DR   GenomeReviews; CT486007_GR; AT4G11600.
DR   KEGG; ath:AT4G11600; -.
DR   NMPDR; fig|3702.1.peg.18828; -.
DR   GeneFarm; 2055; 163.
DR   TAIR; At4g11600; -.
DR   OMA; O48646; SIKWNFS.
DR   BRENDA; 1.11.1.12; 302.
DR   ArrayExpress; O48646; -.
DR   GermOnline; AT4G11600; Arabidopsis thaliana.
DR   GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR   GO; GO:0005829; C:cytosol; TAS:TAIR.
DR   GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR   GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR   GO; GO:0004602; F:glutathione peroxidase activity; IEA:InterPro.
DR   GO; GO:0047066; F:phospholipid-hydroperoxide glutathione pero...; IEA:EC.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0046686; P:response to cadmium ion; IEP:TAIR.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   GO; GO:0009651; P:response to salt stress; IEP:TAIR.
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   2: Evidence at transcript level;
KW   Complete proteome; Mitochondrion; Oxidoreductase; Peroxidase;
KW   Stress response; Transit peptide.
FT   TRANSIT       1     54       Mitochondrion (Potential).
FT   CHAIN        55    232       Probable phospholipid hydroperoxide
FT                                glutathione peroxidase 6, mitochondrial.
FT                                /FTId=PRO_0000013088.
FT   ACT_SITE    105    105       By similarity.
FT   CONFLICT     30     30       S -> SSSS (in Ref. 1).
FT   CONFLICT     51     51       S -> Y (in Ref. 5).
SQ   SEQUENCE   232 AA;  25584 MW;  93F3084A8A331494 CRC64;
     MLRSSIRLLY IRRTSPLLRS LSSSSSSSSS KRFDSAKPLF NSHRIISLPI STTGAKLSRS
     EHSMAASSEP KSLYDFTVKD AKGNDVDLSI YKGKVLLIVN VASQCGLTNS NYTELAQLYE
     KYKGHGFEIL AFPCNQFGNQ EPGTNEEIVQ FACTRFKAEY PIFDKVDVNG DKAAPVYKFL
     KSSKGGLFGD GIKWNFAKFL VDKDGNVVDR FAPTTSPLSI EKDVKKLLGV TA
//