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UniProtKB/Swiss-Prot entry Q9SZ54


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

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Entry information
Entry name GPX7_ARATH
Primary accession number Q9SZ54
Secondary accession numbers None
Integrated into Swiss-Prot on January 10, 2006
Sequence was last modified on May 1, 2000 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 44)
Name and origin of the protein
Protein name Putative glutathione peroxidase 7, chloroplastic [Precursor]
Synonym EC 1.11.1.9
Gene name
Name: GPX7
OrderedLocusNames: At4g31870
ORFNames: F11C18.70
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 [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).
[2]
GENE FAMILY, AND NOMENCLATURE.
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
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
AL049607; CAB40757.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL161579; CAB79905.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T06309; T06309.
3D structure databases
HSSP P00435; 1GP1. [HSSP ENTRY / PDB]
ModBase Q9SZ54.
Protein family/group databases
PeroxiBase 2250; AtGPx07.
Organism-specific databases
GeneFarm 2057; 163.
TAIR At4g31870; -.
Gene expression databases
ArrayExpress Q9SZ54; -.
GermOnline AT4G31870; Arabidopsis thaliana.
Ontologies
GO
GO:0009507; Cellular component: chloroplast (inferred from electronic annotation from UniProtKB-KW).
GO:0004602; Molecular function: glutathione peroxidase activity (inferred from electronic annotation from InterPro).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0006979; Biological process: response to oxidative stress (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR000889; Glut_peroxidase.
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.
PRINTS PR01011; GLUTPROXDASE.
PROSITE PS00460; GLUTATHIONE_PEROXID_1; 1.
PS00763; GLUTATHIONE_PEROXID_2; 1.
PS51355; GLUTATHIONE_PEROXID_3; 1.
PROSITE graphical view of domain structure (profiles).
ProtoNet Q9SZ54.
Genome annotation databases
GenomeReviews CT486007_GR; AT4G31870.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Chloroplast; Complete proteome; Oxidoreductase; Peroxidase; Plastid; Transit peptide.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
TRANSIT   1    69  69     Chloroplast (Potential). 
CHAIN   70   230  161     Putative glutathione peroxidase 7, chloroplastic. PRO_0000045459
ACT_SITE   108   108        By similarity. 
Sequence information
Length: 230 AA [This is the length of the unprocessed precursor] Molecular weight: 25432 Da [This is the MW of the unprocessed precursor] CRC64: 7F1B51C819AC3602 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAFSYASFST PFNGFAANPS PITSAFLGPS LRFSTRTSKT RNPSNGVSVK SSNSHRFLVK 

        70         80         90        100        110        120 
SKNFSVYARA AAEKSVHDFT VKDIDGNDVS LDKFKGKPLL IVNVASRCGL TSSNYSELSQ 

       130        140        150        160        170        180 
LYEKYKNQGF EILAFPCNQF GGQEPGSNPE IKQFACTRFK AEFPIFDKVD VNGPSTAPIY 

       190        200        210        220        230 
KFLKSNAGGF LGDIIKWNFE KFLVDKKGKV VERYPPTTSP FQIEVPNSKL 

Q9SZ54 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

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