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Q04120 (TSA2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Peroxiredoxin TSA2
EC=1.11.1.15
Alternative name(s):
Cytoplasmic thiol peroxidase 2
Short name=cTPx 2
Thiol-specific antioxidant protein 2
Thioredoxin peroxidase 2
Gene names
Name:TSA2
Ordered Locus Names:YDR453C
ORF Names:D9461.38
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length196 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Reduces peroxides. May play an important role in eliminating peroxides generated during metabolism By similarity.

Catalytic activity

2 R'-SH + ROOH = R'-S-S-R' + H2O + ROH.

Subunit structure

Homodimer; disulfide-linked, upon oxidation By similarity.

Subcellular location

Cytoplasm.

Post-translational modification

The Cys-48-SH group is the primary site of oxidation by H2O2, and the oxidized Cys-48 (probably Cys-SOH) rapidly reacts with Cys-171-SH of the other subunit to form an intermolecular disulfide. This disulfide is subsequently reduced by thioredoxin.

Miscellaneous

Present with 4820 molecules/cell in log phase SD medium. Ref.4

Sequence similarities

Belongs to the AhpC/TSA family.

Contains 1 thioredoxin domain.

Ontologies

Keywords
   Cellular componentCytoplasm
   DomainRedox-active center
   Molecular functionAntioxidant
Oxidoreductase
Peroxidase
   PTMDisulfide bond
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processcell redox homeostasis

Inferred from direct assay. Source: SGD

cellular response to oxidative stress

Inferred from mutant phenotype. Source: SGD

   Cellular componentcytoplasm

Inferred from direct assay Ref.3. Source: SGD

   Molecular functionthioredoxin peroxidase activity

Inferred from direct assay Ref.3. Source: SGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 196195Peroxiredoxin TSA2
PRO_0000135096

Regions

Domain3 – 161159Thioredoxin

Sites

Active site481Cysteine sulfenic acid (-SOH) intermediate By similarity

Amino acid modifications

Disulfide bond48Interchain (with C-171); in linked form By similarity
Disulfide bond171Interchain (with C-48); in linked form By similarity

Experimental info

Mutagenesis481C → S: No activity. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q04120 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 43CC57C92081D745

FASTA19621,615
        10         20         30         40         50         60 
MVAEVQKQAP PFKKTAVVDG IFEEISLEKY KGKYVVLAFV PLAFSFVCPT EIVAFSDAAK 

        70         80         90        100        110        120 
KFEDQGAQVL FASTDSEYSL LAWTNLPRKD GGLGPVKVPL LADKNHSLSR DYGVLIEKEG 

       130        140        150        160        170        180 
IALRGLFIID PKGIIRHITI NDLSVGRNVN EALRLVEGFQ WTDKNGTVLP CNWTPGAATI 

       190 
KPDVKDSKEY FKNANN

« Hide

References

« Hide 'large scale' references
[1]"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
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. expand/collapse author list , 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.
Nature 387:75-78(1997) [PubMed: 9169867] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[2]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[3]"Distinct physiological functions of thiol peroxidase isoenzymes in Saccharomyces cerevisiae."
Park S.G., Cha M.-K., Jeong W., Kim I.-H.
J. Biol. Chem. 275:5723-5732(2000) [PubMed: 10681558] [Abstract]
Cited for: CHARACTERIZATION, MUTAGENESIS OF CYS-48.
[4]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed: 14562106] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U33007 Genomic DNA. Translation: AAB64886.1.
BK006938 Genomic DNA. Translation: DAA12288.1.
PIRS69732.
RefSeqNP_010741.1. NM_001180761.1.

3D structure databases

ProteinModelPortalQ04120.
SMRQ04120. Positions 3-195.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-4317N.
IntActQ04120. 12 interactions.
MINTMINT-535451.
STRINGQ04120.

Protein family/group databases

PeroxiBase4467. Sce2CysPrx02.

Proteomic databases

PeptideAtlasQ04120.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYDR453C; YDR453C; YDR453C.
GeneID852064.
KEGGsce:YDR453C.
NMPDRfig|4932.3.peg.1514.

Organism-specific databases

SGDS000002861. TSA2.

Phylogenomic databases

eggNOGfuNOG07930.
GeneTreeEFGT00050000006473.
HOGENOMHBG493509.
OMASERADEF.
OrthoDBEOG4SN4Z0.

Gene expression databases

ArrayExpressQ04120.
GenevestigatorQ04120.
GermOnlineYDR453C. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR000866. AhpC/TSA.
IPR024706. Peroxiredoxin_AhpC-typ.
IPR019479. Peroxiredoxin_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
Gene3DG3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.
KOK03386.
PfamPF10417. 1-cysPrx_C. 1 hit.
PF00578. AhpC-TSA. 1 hit.
[Graphical view]
PIRSFPIRSF000239. AHPC. 1 hit.
SUPFAMSSF52833. Thiordxn-like_fd. 1 hit.
PROSITEPS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio970346.

Entry information

Entry nameTSA2_YEAST
AccessionPrimary (citable) accession number: Q04120
Secondary accession number(s): D6VT78
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: December 14, 2011
This is version 98 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents