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UniProtKB/Swiss-Prot entry P29509


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

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Entry information
Entry name TRXB1_YEAST
Primary accession number P29509
Secondary accession numbers None
Integrated into Swiss-Prot on April 1, 1993
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    November 25, 2008 (Entry version 89)
Name and origin of the protein
Protein name Thioredoxin reductase 1
Synonym EC 1.8.1.9
Gene name
Name: TRR1
OrderedLocusNames: YDR353W
ORFNames: D9476.5
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], AND PARTIAL PROTEIN SEQUENCE.
STRAIN=ATCC 200358 / YNN 295;
PubMed=7961686 [NCBI, ExPASy, EBI, Israel, Japan]
Chae H.Z., Chung S.J., Rhee S.G.;
"Thioredoxin-dependent peroxide reductase from yeast.";
J. Biol. Chem. 269:27670-27678(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204511 / S288c / AB972;
PubMed=9169867 [NCBI, ExPASy, EBI, Israel, Japan]
Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
Nature 387:75-78(1997).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
DOI=10.1101/gr.6037607; PubMed=17322287 [NCBI, ExPASy, EBI, Israel, Japan]
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.;
"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae.";
Genome Res. 17:536-543(2007).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 261-319.
DOI=10.1093/nar/14.16.6357; PubMed=2428012 [NCBI, ExPASy, EBI, Israel, Japan]
Furter R., Paravicini G., Aebi M., Braus G., Prantl F., Niederberger P., Huetter R.;
"The TRP4 gene of Saccharomyces cerevisiae: isolation and structural analysis.";
Nucleic Acids Res. 14:6357-6373(1986).
[5]
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).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; SER-94; THR-193; SER-279; SER-300 AND SER-303, 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
U10274; AAA64747.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U28372; AAB64789.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X04273; -; NOT_ANNOTATED_CDS; Genomic_DNA.[EMBL / GenBank / DDBJ]
AY557749; AAS56075.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S61150; S61150.
RefSeq NP_010640.1; -.
3D structure databases
HSSP Q39243; 1VDC. [HSSP ENTRY / PDB]
ModBase P29509.
Protein-protein interaction databases
DIP DIP:4319N; -.
IntAct P29509; -.
Organism-specific databases
CYGD YDR353w; -.
SGD S000002761; TRR1.
Yeast-GFP YDR353W.
Gene expression databases
GermOnline YDR353W; Saccharomyces cerevisiae.
Ontologies
GO
GO:0005829; Cellular component: cytosol (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:0008198; Molecular function: ferrous iron binding (inferred from direct assay from SGD).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0004791; Molecular function: thioredoxin-disulfide reductase activity (inferred from electronic annotation from InterPro).
GO:0045454; Biological process: cell redox homeostasis (inferred from direct assay from SGD).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0019430; Biological process: removal of superoxide radicals (inferred from electronic annotation from InterPro).
GO:0006979; Biological process: response to oxidative stress (inferred from genetic interaction from SGD).
QuickGo view.
Family and domain databases
InterPro IPR000759; Adrndx_reductase.
IPR013027; FAD_pyr_nucl-diS_OxRdtase.
IPR008255; Pyr_nucl-diS_OxRdtase_2_AS.
IPR001327; Pyr_OxRdtase_NAD_bd.
IPR000103; Pyridine_nuc-diS_OxRdtase_2.
IPR005982; Thioredox_reduct.
Graphical view of domain structure.
Pfam PF00070; Pyr_redox; 1.
PF07992; Pyr_redox_2; 1.
Pfam graphical view of domain structure.
PRINTS PR00419; ADXRDTASE.
PR00368; FADPNR.
PR00469; PNDRDTASEII.
ProDom PD000139; FAD_pyr_redox; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR01292; TRX_reduct; 1.
PROSITE PS00573; PYRIDINE_REDOX_2; 1.
ProtoNet P29509.
Proteomic databases
PeptideAtlas P29509; -.
Genome annotation databases
Ensembl YDR353W; Saccharomyces cerevisiae. [Contig view]
GeneID 851955; -.
GenomeReviews Z71256_GR; YDR353W.
KEGG sce:YDR353W; -.
NMPDR fig|4932.3.peg.1406; -.
Phylogenomic databases
HOGENOM P29509; -.
Other
LinkHub P29509; -.
NextBio 970056; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Cytoplasm; Direct protein sequencing; FAD; Flavoprotein; NADP; Oxidoreductase; Phosphoprotein; Redox-active center.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   319  318     Thioredoxin reductase 1. PRO_0000166770
NP_BIND   33    45  13     FAD (By similarity). 
NP_BIND   288   297  10     FAD (By similarity). 
MOD_RES   11    11        Phosphoserine. 
MOD_RES   94    94        Phosphoserine. 
MOD_RES   193   193        Phosphothreonine. 
MOD_RES   279   279        Phosphoserine. 
MOD_RES   300   300        Phosphoserine. 
MOD_RES   303   303        Phosphoserine. 
DISULFID   142   145        Redox-active (By similarity). 
CONFLICT   18    18        A -> V (in Ref. 1; AAA64747). 
CONFLICT   101   101        T -> A (in Ref. 1; AAA64747). 
CONFLICT   111   111        T -> A (in Ref. 1; AAA64747). 
CONFLICT   180   196        VFMLVRKDHLRASTIMQ -> CLCLSEKTICVLLPLCK (in Ref. 1; AAA64747). 
Sequence information
Length: 319 AA [This is the length of the unprocessed precursor] Molecular weight: 34238 Da [This is the MW of the unprocessed precursor] CRC64: 9F9E58A4BAD859E1 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MVHNKVTIIG SGPAAHTAAI YLARAEIKPI LYEGMMANGI AAGGQLTTTT EIENFPGFPD 

        70         80         90        100        110        120 
GLTGSELMDR MREQSTKFGT EIITETVSKV DLSSKPFKLW TEFNEDAEPV TTDAIILATG 

       130        140        150        160        170        180 
ASAKRMHLPG EETYWQKGIS ACAVCDGAVP IFRNKPLAVI GGGDSACEEA QFLTKYGSKV 

       190        200        210        220        230        240 
FMLVRKDHLR ASTIMQKRAE KNEKIEILYN TVALEAKGDG KLLNALRIKN TKKNEETDLP 

       250        260        270        280        290        300 
VSGLFYAIGH TPATKIVAGQ VDTDEAGYIK TVPGSSLTSV PGFFAAGDVQ DSKYRQAITS 

       310 
AGSGCMAALD AEKYLTSLE 

P29509 in FASTA format

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