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UniProtKB/Swiss-Prot entry O48646


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name GPX6_ARATH
Primary accession number O48646
Secondary accession number Q94BV3
Integrated into Swiss-Prot on March 27, 2002
Sequence was last modified on May 10, 2004 (Sequence version 2)
Annotations were last modified on    December 16, 2008 (Entry version 65)
Name and origin of the protein
Protein name Probable phospholipid hydroperoxide glutathione peroxidase 6, mitochondrial [Precursor]
Synonyms PHGPx
AtGPX1
EC 1.11.1.12
Gene name
Name: GPX6
Synonyms: GPX1
OrderedLocusNames: At4g11600
ORFNames: T5C23.30
From
Arabidopsis thaliana (Mouse-ear cress) [TaxID: 3702] 
Taxonomy Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION.
STRAIN=cv. Landsberg erecta;
Bilodeau P., Luo M., Dennis E.S., Peacock W.J., Chaudhury A.M.;
"Cloning of a cDNA encoding a putative glutathione peroxidase protein from Arabidopsis thaliana.";
(er) Plant Gene Register PGR98-047.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
DOI=10.1038/47134; PubMed=10617198 [NCBI, ExPASy, EBI, Israel, Japan]
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.;
"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
Nature 402:769-777(1999).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
DOI=10.1126/science.1088305; PubMed=14593172 [NCBI, ExPASy, EBI, Israel, Japan]
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis genome.";
Science 302:842-846(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 22-232.
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.;
"Full-length cDNA from Arabidopsis thaliana.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 31-232, AND INDUCTION.
STRAIN=cv. Columbia;
DOI=10.1266/ggs.72.311; PubMed=9511228 [NCBI, ExPASy, EBI, Israel, Japan]
Sugimoto M., Sakamoto W.;
"Putative phospholipid hydroperoxide glutathione peroxidase gene from Arabidopsis thaliana induced by oxidative stress.";
Genes Genet. Syst. 72:311-316(1997).
[6]
GENE FAMILY, NOMENCLATURE, TISSUE SPECIFICITY, AND INDUCTION.
DOI=10.1046/j.1365-313X.2003.01901.x; PubMed=14617062 [NCBI, ExPASy, EBI, Israel, Japan]
Rodriguez Milla M.A., Maurer A., Rodriguez Huete A., Gustafson J.P.;
"Glutathione peroxidase genes in Arabidopsis are ubiquitous and regulated by abiotic stresses through diverse signaling pathways.";
Plant J. 36:602-615(2003).
Comments
  • FUNCTION: Protects cells and enzymes from oxidative damage, by catalyzing the reduction of hydrogen peroxide, lipid peroxides and organic hydroperoxide, by glutathione (By similarity).
  • CATALYTIC ACTIVITY: 2 glutathione + a lipid hydroperoxide = glutathione disulfide + lipid + 2 H2O.
  • SUBCELLULAR LOCATION: Mitochondrion (Potential).
  • TISSUE SPECIFICITY: Expressed at a low but detectable level in leaves, stems, and flowers, but at a higher level in siliques and even higher in roots. Predominantly expressed in seeds.
  • INDUCTION: By salt stress, osmotic stress, cold treatment, and metals. Up-regulated by salicylic acid (SA), jasmonic acid (JA), abscisic acid (ABA) and auxin.
  • SIMILARITY: Belongs to the glutathione peroxidase family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF030132; AAC09173.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL049500; CAB39931.1; ALT_INIT; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL161532; CAB78203.1; ALT_INIT; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY039863; AAK63967.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY077655; AAL76133.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY088647; AAM66969.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB001568; BAA24226.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T04207; T04207.
RefSeq NP_192897.2; -.
UniGene At.23184
3D structure databases
HSSP P00435; 1GP1. [HSSP ENTRY / PDB]
ModBase O48646.
Protein family/group databases
PeroxiBase 2502; AtGPx06.
Organism-specific databases
GeneFarm 2055; 163.
TAIR At4g11600; -.
Gene expression databases
ArrayExpress O48646; -.
GermOnline AT4G11600; Arabidopsis thaliana.
Ontologies
GO
GO:0009507; Cellular component: chloroplast (inferred from direct assay from TAIR).
GO:0005829; Cellular component: cytosol (traceable author statement from TAIR).
GO:0005739; Cellular component: mitochondrion (inferred from electronic annotation from UniProtKB-KW).
GO:0005886; Cellular component: plasma membrane (inferred from direct assay from TAIR).
GO:0004602; Molecular function: glutathione peroxidase activity (inferred from electronic annotation from InterPro).
GO:0047066; Molecular function: phospholipid-hydroperoxide glutathione peroxidase activity (inferred from electronic annotation from EC).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0046686; Biological process: response to cadmium ion (inferred from expression pattern from TAIR).
GO:0006979; Biological process: response to oxidative stress (inferred from electronic annotation from InterPro).
GO:0009651; Biological process: response to salt stress (inferred from expression pattern from TAIR).
QuickGo view.
Family and domain databases
InterPro IPR000889; Glut_peroxidase.
IPR001452; SH3.
IPR012335; Thioredoxin_fold.
Graphical view of domain structure.
Gene3D G3DSA:3.40.30.10; Thioredoxin_fold; 1.
PANTHER PTHR11592; Glut_peroxidase; 1.
Pfam PF00255; GSHPx; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000303; Glutathion_perox; 1.
PRINTS PR01011; GLUTPROXDASE.
PR00452; SH3DOMAIN.
PROSITE PS00460; GLUTATHIONE_PEROXID_1; 1.
PS00763; GLUTATHIONE_PEROXID_2; 1.
PS51355; GLUTATHIONE_PEROXID_3; 1.
PROSITE graphical view of domain structure (profiles).
Proteomics databases
PRIDE O48646; -.
Genome annotation databases
GeneID 826765; -.
GenomeReviews CT486007_GR; AT4G11600.
KEGG ath:AT4G11600; -.
NMPDR fig|3702.1.peg.18828; -.
Other
ProtoNet O48646.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Mitochondrion; Oxidoreductase; Peroxidase; Stress response; Transit peptide.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
TRANSIT   1    54  54     Mitochondrion (Potential). 
CHAIN   55   232  178     Probable phospholipid hydroperoxide glutathione peroxidase 6, mitochondrial. PRO_0000013088
ACT_SITE   105   105        By similarity. 
CONFLICT   30    30        S -> SSSS (in Ref. 1). 
CONFLICT   51    51        S -> Y (in Ref. 5). 
Sequence information
Length: 232 AA [This is the length of the unprocessed precursor] Molecular weight: 25584 Da [This is the MW of the unprocessed precursor] CRC64: 93F3084A8A331494 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MLRSSIRLLY IRRTSPLLRS LSSSSSSSSS KRFDSAKPLF NSHRIISLPI STTGAKLSRS 

        70         80         90        100        110        120 
EHSMAASSEP KSLYDFTVKD AKGNDVDLSI YKGKVLLIVN VASQCGLTNS NYTELAQLYE 

       130        140        150        160        170        180 
KYKGHGFEIL AFPCNQFGNQ EPGTNEEIVQ FACTRFKAEY PIFDKVDVNG DKAAPVYKFL 

       190        200        210        220        230 
KSSKGGLFGD GIKWNFAKFL VDKDGNVVDR FAPTTSPLSI EKDVKKLLGV TA 

O48646 in FASTA format

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