ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry P38816


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

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name TRXB2_YEAST
Primary accession number P38816
Secondary accession numbers None
Integrated into Swiss-Prot on February 1, 1995
Sequence was last modified on February 1, 1995 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 79)
Name and origin of the protein
Protein name Thioredoxin reductase 2, mitochondrial [Precursor]
Synonym EC 1.8.1.9
Gene name
Name: TRR2
OrderedLocusNames: YHR106W
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 [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204511 / S288c / AB972;
PubMed=8091229 [NCBI, ExPASy, EBI, Israel, Japan]
Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z., Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T., Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J., Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L., St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P., Waterston R., Wilson R., Vaudin M.;
"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome VIII.";
Science 265:2077-2082(1994).
[2]
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).
[3]
CHARACTERIZATION.
DOI=10.1074/jbc.274.10.6366; PubMed=10037727 [NCBI, ExPASy, EBI, Israel, Japan]
Pedrajas J.R., Kosmidou E., Miranda-Vizuete A., Gustafsson J.-A., Wright A.P.H., Spyrou G.;
"Identification and functional characterization of a novel mitochondrial thioredoxin system in Saccharomyces cerevisiae.";
J. Biol. Chem. 274:6366-6373(1999).
[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).
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
U00059; AAB68856.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY557882; AAS56208.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S48948; S48948.
RefSeq NP_011974.1; -.
3D structure databases
HSSP Q39243; 1VDC. [HSSP ENTRY / PDB]
ModBase P38816.
Protein-protein interaction databases
DIP DIP:1942N; -.
IntAct P38816; -.
Organism-specific databases
CYGD YHR106w; -.
SGD S000001148; TRR2.
Yeast-GFP YHR106W.
Gene expression databases
GermOnline YHR106W; Saccharomyces cerevisiae.
Ontologies
GO
GO:0005739; Cellular component: mitochondrion (inferred from electronic annotation from UniProtKB-KW).
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:0004791; Molecular function: thioredoxin-disulfide reductase activity (inferred from electronic annotation from InterPro).
GO:0045454; Biological process: cell redox homeostasis (inferred by curator 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 mutant phenotype 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 P38816.
Proteomic databases
PeptideAtlas P38816; -.
Genome annotation databases
Ensembl YHR106W; Saccharomyces cerevisiae. [Contig view]
GeneID 856506; -.
GenomeReviews U00093_GR; YHR106W.
KEGG sce:YHR106W; -.
NMPDR fig|4932.3.peg.3135; -.
Phylogenomic databases
HOGENOM P38816; -.
Other
LinkHub P38816; -.
NextBio 982236; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; FAD; Flavoprotein; Mitochondrion; NADP; Oxidoreductase; Redox-active center; Transit peptide.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
TRANSIT   1    23  23     Mitochondrion (Potential). 
CHAIN   24   342  319     Thioredoxin reductase 2, mitochondrial. PRO_0000030303
NP_BIND   56    68  13     FAD (By similarity). 
NP_BIND   311   320  10     FAD (By similarity). 
DISULFID   165   168        Redox-active (By similarity). 
Sequence information
Length: 342 AA [This is the length of the unprocessed precursor] Molecular weight: 37087 Da [This is the MW of the unprocessed precursor] CRC64: 739F302AA0837A5A [This is a checksum on the sequence]
        10         20         30         40         50         60 
MIKHIVSPFR TNFVGISKSV LSRMIHHKVT IIGSGPAAHT AAIYLARAEM KPTLYEGMMA 

        70         80         90        100        110        120 
NGIAAGGQLT TTTDIENFPG FPESLSGSEL MERMRKQSAK FGTNIITETV SKVDLSSKPF 

       130        140        150        160        170        180 
RLWTEFNEDA EPVTTDAIIL ATGASAKRMH LPGEETYWQQ GISACAVCDG AVPIFRNKPL 

       190        200        210        220        230        240 
AVIGGGDSAC EEAEFLTKYA SKVYILVRKD HFRASVIMQR RIEKNPNIIV LFNTVALEAK 

       250        260        270        280        290        300 
GDGKLLNMLR IKNTKSNVEN DLEVNGLFYA IGHSPATDIV KGQVDEEETG YIKTVPGSSL 

       310        320        330        340 
TSVPGFFAAG DVQDSRYRQA VTSAGSGCIA ALDAERYLSA QE 

P38816 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

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

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ch flag SIB Switzerland Mirror sites: Australia  Brazil  Canada  China  Korea
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!