Peroxiredoxin DOT5 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P40553 (DOT5_YEAST) Reviewed, UniProtKB/Swiss-Prot

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

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	215 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Chromosome › telomere 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

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Chromosome Nucleus Telomere
Domain	Redox-active center
Molecular function	Antioxidant Oxidoreductase Peroxidase
PTM	Disulfide bond Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cell redox homeostasis Inferred from mutant phenotype. Source: SGD regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	chromosome, telomeric region Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from direct assay Ref.5. Source: SGD
Molecular function	thioredoxin peroxidase activity Inferred from mutant phenotype. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 215

215

Peroxiredoxin DOT5

PRO_0000135152

Regions

Domain

63 – 211

149

Thioredoxin

Sites

Active site

107

Cysteine sulfenic acid (-SOH) intermediate Ref.6

Amino acid modifications

Modified residue

Phosphothreonine Ref.11

Disulfide bond

107 ↔ 112

Redox-active Ref.6

Experimental info

Mutagenesis

107

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

Mutagenesis

112

C → S: No TPx activity, no effect on DOT activity. Ref.6 Ref.9

Secondary structure

215

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P40553 [UniParc].

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

FASTA

215

24,120

        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' referencesShow '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. 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. 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.

PIR

S48445.

RefSeq

NP_012255.1. NM_001179360.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2A4V	X-ray	1.80	A	57-215	[»]

ProteinModelPortal

P40553.

SMR

P40553. Positions 59-214.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-4762N.

IntAct

P40553. 1 interaction.

MINT

MINT-485714.

STRING

P40553.

Proteomic databases

PeptideAtlas

P40553.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YIL010W; YIL010W; YIL010W.

GeneID

854805.

KEGG

sce:YIL010W.

NMPDR

fig|4932.3.peg.1792.

Organism-specific databases

CYGD

YIL010w.

SGD

S000001272. DOT5.

Phylogenomic databases

eggNOG

fuNOG09863.

GeneTree

EFGT00050000003088.

HOGENOM

HBG493509.

OMA

VESNGNE.

OrthoDB

EOG4NPBCM.

Gene expression databases

ArrayExpress

P40553.

Genevestigator

P40553.

GermOnline

YIL010W. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR000866. AhpC/TSA.
IPR012336. Thioredoxin-like_fold.
[Graphical view]

Gene3D

G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.

K03564.

Pfam

PF00578. AhpC-TSA. 1 hit.
[Graphical view]

SUPFAM

SSF52833. Thiordxn-like_fd. 1 hit.

PROSITE

PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

977622.

Entry information

Entry name

DOT5_YEAST

Accession

Primary (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 status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal 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

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents