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P40553 (DOT5_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 111. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Peroxiredoxin DOT5

EC=1.11.1.15
Alternative name(s):
Disrupter of telomere silencing protein 5
Nuclear thiol peroxidase
Short name=nTPx
Thioredoxin reductase
Gene names
Name:DOT5
Ordered Locus Names:YIL010W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length215 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Has a role in telomere silencing, which is the repression of chromatin structure which leads to a stop in the transcription of nearby genes. Also has a role in the regulation of telomere length. Acts as an alkyl-hydroperoxide reductase in the nucleus during post-diauxic growth. Preferentially reduces alkyl-hydroperoxides rather than hydrogen preoxide. Acts as an antioxidant necessary for stationary phase survival. Ref.1 Ref.6 Ref.9

Catalytic activity

2 R'-SH + ROOH = R'-S-S-R' + H2O + ROH. Ref.5 Ref.6

Subunit structure

Monomer. Ref.10 Ref.12

Subcellular location

Nucleus. Chromosometelomere Potential Ref.5 Ref.7 Ref.9.

Induction

During the diauxic shift. In response to oxidative stress. Ref.6

Post-translational modification

The Cys-107-SH group is the primary site of oxidation, and the oxidized Cys-107 (probably Cys-SOH) rapidly reacts with Cys-112-SH to form an intramolecular disulfide. This disulfide is subsequently reduced by thioredoxin to restore the reduced active form of the enzyme By similarity.

Miscellaneous

Present with 1840 molecules/cell in log phase SD medium. Ref.8

Sequence similarities

Belongs to the AhpC/TSA family.

Contains 1 thioredoxin domain.

Biophysicochemical properties

pH dependence:

Optimum pH is 6.5. Ref.5

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 215215Peroxiredoxin DOT5
PRO_0000135152

Regions

Domain63 – 211149Thioredoxin

Sites

Active site1071Cysteine sulfenic acid (-SOH) intermediate Ref.6

Amino acid modifications

Modified residue301Phosphothreonine Ref.11
Disulfide bond107 ↔ 112Redox-active Ref.6

Experimental info

Mutagenesis1071C → S: No TPx activity, no effect on DOT activity. Ref.5 Ref.6 Ref.9
Mutagenesis1121C → S: No TPx activity, no effect on DOT activity. Ref.6 Ref.9

Secondary structure

............................ 215
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P40553 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: EB78A216891946C0

FASTA21524,120
        10         20         30         40         50         60 
MGEALRRSTR IAISKRMLEE EESKLAPIST PEVPKKKIKT GPKHNANQAV VQEANRSSDV 

        70         80         90        100        110        120 
NELEIGDPIP DLSLLNEDND SISLKKITEN NRVVVFFVYP RASTPGCTRQ ACGFRDNYQE 

       130        140        150        160        170        180 
LKKYAAVFGL SADSVTSQKK FQSKQNLPYH LLSDPKREFI GLLGAKKTPL SGSIRSHFIF 

       190        200        210 
VDGKLKFKRV KISPEVSVND AKKEVLEVAE KFKEE 

« Hide

References

« Hide 'large scale' references
[1]"Identification of high-copy disruptors of telomeric silencing in Saccharomyces cerevisiae."
Singer M.S., Kahana A., Wolf A.J., Meisinger L.L., Peterson S.E., Goggin C., Mahowald M., Gottschling D.E.
Genetics 150:613-632(1998) [PubMed: 9755194] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
[2]"The nucleotide sequence of Saccharomyces cerevisiae chromosome IX."
Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D., Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E., Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C. expand/collapse author list , Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V., Walsh S.V., Whitehead S., Barrell B.G.
Nature 387:84-87(1997) [PubMed: 9169870] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204511 / S288c / AB972.
[3]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae."
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. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed: 17322287] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[5]"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: CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-107.
[6]"Nuclear thiol peroxidase as a functional alkyl-hydroperoxide reductase necessary for stationary phase growth of Saccharomyces cerevisiae."
Cha M.-K., Choi Y.-S., Hong S.-K., Kim W.-C., No K.T., Kim I.-H.
J. Biol. Chem. 278:24636-24643(2003) [PubMed: 12730197] [Abstract]
Cited for: FUNCTION, ENZYME ACTIVITY, ACTIVE SITE, INDUCTION, DISULFIDE BOND, MUTAGENESIS OF CYS-107 AND CYS-112.
[7]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed: 14562095] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[8]"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].
[9]"Nuclear thioredoxin peroxidase Dot5 in Saccharomyces cerevisiae: roles in oxidative stress response and disruption of telomeric silencing."
Izawa S., Kuroki N., Inoue Y.
Appl. Microbiol. Biotechnol. 64:120-124(2004) [PubMed: 12925864] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-107 AND CYS-112.
[10]"Crystallization and preliminary X-ray analysis of a truncated mutant of yeast nuclear thiol peroxidase, a novel atypical 2-Cys peroxiredoxin."
Choi J., Choi S., Choi J., Cha M.-K., Kim I.-H., Shin W.
Acta Crystallogr. F 61:659-662(2005) [PubMed: 16511121] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, CRYSTALLIZATION, X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 57-215 OF MUTANT CYS-107 AND CYS-112, SUBUNIT.
[11]"A multidimensional chromatography technology for in-depth phosphoproteome analysis."
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-30, MASS SPECTROMETRY.
[12]"Crystal structure of the C107S/C112S mutant of yeast nuclear 2-Cys peroxiredoxin."
Choi J., Choi S., Chon J.K., Choi J., Cha M.-K., Kim I.-H., Shin W.
Proteins 61:1146-1149(2005) [PubMed: 16245326] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 57-215 OF MUTANT CYS-107 AND CYS-112, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z38113 Genomic DNA. Translation: CAA86239.1.
AY558298 Genomic DNA. Translation: AAS56624.1.
BK006942 Genomic DNA. Translation: DAA08535.1.
PIRS48445.
RefSeqNP_012255.1. NM_001179360.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2A4VX-ray1.80A57-215[»]
ProteinModelPortalP40553.
SMRP40553. Positions 59-214.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-4762N.
IntActP40553. 1 interaction.
MINTMINT-485714.
STRINGP40553.

Proteomic databases

PeptideAtlasP40553.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYIL010W; YIL010W; YIL010W.
GeneID854805.
KEGGsce:YIL010W.
NMPDRfig|4932.3.peg.1792.

Organism-specific databases

CYGDYIL010w.
SGDS000001272. DOT5.

Phylogenomic databases

eggNOGfuNOG09863.
GeneTreeEFGT00050000003088.
HOGENOMHBG493509.
OMAVESNGNE.
OrthoDBEOG4NPBCM.

Gene expression databases

ArrayExpressP40553.
GenevestigatorP40553.
GermOnlineYIL010W. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR000866. AhpC/TSA.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
Gene3DG3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.
KOK03564.
PfamPF00578. AhpC-TSA. 1 hit.
[Graphical view]
SUPFAMSSF52833. Thiordxn-like_fd. 1 hit.
PROSITEPS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio977622.

Entry information

Entry nameDOT5_YEAST
AccessionPrimary (citable) accession number: P40553
Secondary accession number(s): D6VVR9
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: January 25, 2012
This is version 111 of the entry and version 1 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

Yeast chromosome IX

Yeast (Saccharomyces cerevisiae) chromosome IX: entries and gene names

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families