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UniProtKB/Swiss-Prot entry P41921


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

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Entry information
Entry name GSHR_YEAST
Primary accession number P41921
Secondary accession numbers None
Integrated into Swiss-Prot on November 1, 1995
Sequence was last modified on October 1, 1996 (Sequence version 2)
Annotations were last modified on    November 25, 2008 (Entry version 81)
Name and origin of the protein
Protein name Glutathione reductase
Synonyms GRase
GR
EC 1.8.1.7
Gene name
Name: GLR1
OrderedLocusNames: YPL091W
ORFNames: LPG17W
From
Saccharomyces cerevisiae (Baker's yeast) [TaxID: 4932] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 17-483.
DOI=10.1016/0378-1119(95)00026-3; PubMed=7737505 [NCBI, ExPASy, EBI, Israel, Japan]
Collinson L.P., Dawes I.W.;
"Isolation, characterization and overexpression of the yeast gene, GLR1, encoding glutathione reductase.";
Gene 156:123-127(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204511 / S288c / AB972;
PubMed=9169875 [NCBI, ExPASy, EBI, Israel, Japan]
Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
Nature 387:103-105(1997).
[3]
NUCLEOTIDE SEQUENCE OF 20-483.
Aono M., Nakajima N.;
Submitted (AUG-1994) to the EMBL/GenBank/DDBJ databases.
[4]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02046; PubMed=14562106 [NCBI, ExPASy, EBI, Israel, Japan]
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-475, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M700468-MCP200; PubMed=18407956 [NCBI, ExPASy, EBI, Israel, Japan]
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
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
L35342; AAA92575.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U43281; AAB68208.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
D37871; BAA07109.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S61975; S61975.
RefSeq NP_015234.1; -.
3D structure databases
PDB
2HQM; X-ray; 2.40 A; A/B=14-483.[ExPASy / RCSB / EBI]
PDBsum 2HQM; -.
ModBase P41921.
Protein-protein interaction databases
DIP DIP:4020N; -.
IntAct P41921; -.
2D gel databases
COMPLUYEAST-2DPAGE P41921; -.
Organism-specific databases
CYGD YPL091w; -.
SGD S000006012; GLR1.
Yeast-GFP YPL091W.
Gene expression databases
GermOnline YPL091W; Saccharomyces cerevisiae.
Ontologies
GO
GO:0005739; Cellular component: mitochondrion (inferred from direct assay from SGD).
GO:0005634; Cellular component: nucleus (inferred from direct assay from SGD).
GO:0009055; Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0050660; Molecular function: FAD binding (inferred from electronic annotation from InterPro).
GO:0004362; Molecular function: glutathione-disulfide reductase activity (inferred from electronic annotation from InterPro).
GO:0050661; Molecular function: NADP binding (inferred from electronic annotation from InterPro).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0045454; Biological process: cell redox homeostasis (inferred from electronic annotation from InterPro).
GO:0006749; Biological process: glutathione metabolic process (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 mutant phenotype from SGD).
QuickGo view.
Family and domain databases
InterPro IPR013027; FAD_pyr_nucl-diS_OxRdtase.
IPR006322; Glut_reduct_1.
IPR000815; Hg_reductase.
IPR001100; Pyr_nuc-diS_OxRdtase.
IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
IPR012999; Pyr_OxRdtase_I_AS.
IPR001327; Pyr_OxRdtase_NAD_bd.
Graphical view of domain structure.
Gene3D G3DSA:3.30.390.30; Pyr_redox_dim; 1.
Pfam PF00070; Pyr_redox; 1.
PF07992; Pyr_redox_2; 1.
PF02852; Pyr_redox_dim; 1.
Pfam graphical view of domain structure.
PRINTS PR00368; FADPNR.
PR00945; HGRDTASE.
PR00411; PNDRDTASEI.
ProDom PD000139; FAD_pyr_redox; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR01421; gluta_reduc_1; 1.
PROSITE PS00076; PYRIDINE_REDOX_1; 1.
ProtoNet P41921.
Proteomic databases
PeptideAtlas P41921; -.
Genome annotation databases
Ensembl YPL091W; Saccharomyces cerevisiae. [Contig view]
GeneID 856014; -.
GenomeReviews U00094_GR; YPL091W.
KEGG sce:YPL091W; -.
NMPDR fig|4932.3.peg.6367; -.
Phylogenomic databases
HOGENOM P41921; -.
Other
LinkHub P41921; -.
NextBio 980908; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Complete proteome; Cytoplasm; FAD; Flavoprotein; NADP; Oxidoreductase; Phosphoprotein; Redox-active center.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   483  483     Glutathione reductase. PRO_0000067972
NP_BIND   53    61  9     FAD (By similarity). 
ACT_SITE   472   472        Proton acceptor (By similarity). 
MOD_RES   475   475        Phosphoserine. 
DISULFID   61    66        Redox-active (By similarity). 
CONFLICT   315   315        Q -> E (in Ref. 3; BAA07109). 
CONFLICT   428   428        C -> G (in Ref. 3; BAA07109). 
STRAND   23    29  7      
HELIX   33    44  12      
STRAND   49    55  7      
HELIX   59    64  6      
HELIX   66    82  17      
TURN   83    89  7      
HELIX   98   100  3      
HELIX   105   129  25      
STRAND   132   141  10      
STRAND   147   154  8      
STRAND   157   166  10      
STRAND   170   172  3      
HELIX   181   183  3      
HELIX   187   192  6      
STRAND   198   203  6      
HELIX   207   218  12      
STRAND   222   226  5      
STRAND   228   232  5      
HELIX   238   251  14      
STRAND   254   256  3      
STRAND   261   266  6      
STRAND   273   277  5      
STRAND   282   291  10      
STRAND   295   297  3      
HELIX   303   306  4      
STRAND   329   331  3      
HELIX   333   335  3      
HELIX   342   357  16      
HELIX   360   362  3      
STRAND   374   376  3      
STRAND   382   386  5      
HELIX   389   396  8      
HELIX   398   400  3      
STRAND   401   408  8      
HELIX   411   415  5      
STRAND   422   429  8      
TURN   430   433  4      
STRAND   434   442  9      
HELIX   445   457  13      
HELIX   462   466  5      
HELIX   476   480  5      
Sequence information
Length: 483 AA [This is the length of the unprocessed precursor] Molecular weight: 53441 Da [This is the MW of the unprocessed precursor] CRC64: 203BBB770120504A [This is a checksum on the sequence]
        10         20         30         40         50         60 
MLSATKQTFR SLQIRTMSTN TKHYDYLVIG GGSGGVASAR RAASYGAKTL LVEAKALGGT 

        70         80         90        100        110        120 
CVNVGCVPKK VMWYASDLAT RVSHANEYGL YQNLPLDKEH LTFNWPEFKQ KRDAYVHRLN 

       130        140        150        160        170        180 
GIYQKNLEKE KVDVVFGWAR FNKDGNVEVQ KRDNTTEVYS ANHILVATGG KAIFPENIPG 

       190        200        210        220        230        240 
FELGTDSDGF FRLEEQPKKV VVVGAGYIGI ELAGVFHGLG SETHLVIRGE TVLRKFDECI 

       250        260        270        280        290        300 
QNTITDHYVK EGINVHKLSK IVKVEKNVET DKLKIHMNDS KSIDDVDELI WTIGRKSHLG 

       310        320        330        340        350        360 
MGSENVGIKL NSHDQIIADE YQNTNVPNIY SLGDVVGKVE LTPVAIAAGR KLSNRLFGPE 

       370        380        390        400        410        420 
KFRNDKLDYE NVPSVIFSHP EAGSIGISEK EAIEKYGKEN IKVYNSKFTA MYYAMLSEKS 

       430        440        450        460        470        480 
PTRYKIVCAG PNEKVVGLHI VGDSSAEILQ GFGVAIKMGA TKADFDNCVA IHPTSAEELV 


TMR 

P41921 in FASTA format

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