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UniProtKB/Swiss-Prot entry O59858


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

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Entry information
Entry name GPX1_SCHPO
Primary accession number O59858
Secondary accession numbers None
Integrated into Swiss-Prot on May 30, 2000
Sequence was last modified on August 1, 1998 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 59)
Name and origin of the protein
Protein name Glutathione peroxidase
Synonym EC 1.11.1.9
Gene name
Name: gpx1
ORFNames: SPBC32F12.03c
From
Schizosaccharomyces pombe (Fission yeast) [TaxID: 4896] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae; Schizosaccharomyces.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND INDUCTION.
STRAIN=JY741;
DOI=10.1002/(SICI)1097-0061(199908)15:11<1125::AID-YEA442>3.0.CO;2-Z; PubMed=10455235 [NCBI, ExPASy, EBI, Israel, Japan]
Yamada K., Nakagawa C.W., Mutoh N.;
"Schizosaccharomyces pombe homologue of glutathione peroxidase, which does not contain selenocysteine, is induced by several stresses and works as an antioxidant.";
Yeast 15:1125-1132(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 38366 / 972;
DOI=10.1038/nature724; PubMed=11859360 [NCBI, ExPASy, EBI, Israel, Japan]
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
"The genome sequence of Schizosaccharomyces pombe.";
Nature 415:871-880(2002).
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
AB012395; BAA25326.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CU329671; CAA19364.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T43376; T43376.
RefSeq NP_596146.1; -.
3D structure databases
HSSP P00435; 1GP1. [HSSP ENTRY / PDB]
ModBase O59858.
Protein family/group databases
PeroxiBase 3744; SpomGPx01.
Enzyme and pathway databases
BioCyc SPOM-XXX-01:SPOM-XXX-01-004182-MON; -.
Organism-specific databases
GeneDB_Spombe SPBC32F12.03c; -.
Gene expression databases
ArrayExpress O59858; -.
Ontologies
GO
GO:0005829; Cellular component: cytosol (inferred from direct assay from GeneDB_SPombe).
GO:0005634; Cellular component: nucleus (inferred from direct assay from GeneDB_SPombe).
GO:0004602; Molecular function: glutathione peroxidase activity (inferred from electronic annotation from InterPro).
GO:0033554; Biological process: cellular response to stress (inferred from expression pattern from GeneDB_SPombe).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0009408; Biological process: response to heat (inferred from expression pattern from GeneDB_SPombe).
GO:0042542; Biological process: response to hydrogen peroxide (inferred from genetic interaction from GeneDB_SPombe).
GO:0006970; Biological process: response to osmotic stress (inferred from expression pattern from GeneDB_SPombe).
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.
PIRSF PIRSF000303; Glutathion_perox; 1.
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).
Genome annotation databases
GeneID 2540222; -.
KEGG spo:SPBC32F12.03c; -.
NMPDR fig|4896.1.peg.2012; -.
Other
ProtoNet O59858.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Oxidoreductase; Peroxidase; Stress response.
Features
SEVIEWER logo Feature table viewer
KeyFrom  To Length Description FTId
CHAIN   1   158  158     Glutathione peroxidase. PRO_0000066644
ACT_SITE   36    36        By similarity. 
Sequence information
Length: 158 AA [This is the length of the unprocessed precursor] Molecular weight: 18061 Da [This is the MW of the unprocessed precursor] CRC64: 2D7009280B676876 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSHFYDLAPK DKDGNPFPFS NLKGKVVLVV NTASKCGFTP QYKGLEALYQ KYKDRGFIIL 

        70         80         90        100        110        120 
GFPCNQFGNQ EPGSDEEIAQ FCQKNYGVTF PVLAKINVNG DNVDPVYQFL KSQKKQLGLE 

       130        140        150 
RIKWNFEKFL VNRQGQVIER YSSISKPEHL ENDIESVL 

O59858 in FASTA format

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View entry in raw text format (no links)
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