Reviewed, UniProtKB/Swiss-Prot P40553 (DOT5_YEAST)

Names and origin

Protein names

Recommended name:
    Peroxiredoxin DOT5
    EC=1.11.1.15
Alternative name(s):
    Thioredoxin reductase
    Nuclear thiol peroxidase
      Short name=nTPx
    Disrupter of telomere silencing protein 5

Gene names

Name:	DOT5
Ordered Locus Names:	YIL010W

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	215 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
Catalytic activity	2 R'-SH + ROOH = R'-S-S-R' + H(2)O + ROH.
Subunit structure	Monomer.
Subcellular location	Nucleus. TelomerePotential.
Induction	During the diauxic shift. In response to oxidative stress.
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.
Sequence similarities	Belongs to the ahpC/TSA family. Contains 1 thioredoxin domain.
Biophysicochemical properties	pH dependence: Optimum pH is 6.5.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Chromosomal protein Nucleus Telomere
Domain	Redox-active center
Molecular function	Antioxidant Oxidoreductase Peroxidase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	cell redox homeostasis Ref.4 Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW response to oxidative stress Inferred from genetic interaction. Source: SGD
Cellular component	chromosome, telomeric region Inferred from electronic annotation. Source: UniProtKB-KW nucleus Ref.4 Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	thioredoxin peroxidase activity Ref.4 Inferred from direct assay. 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

1

Cysteine sulfenic acid (-SOH) intermediate

Amino acid modifications

Modified residue

30

1

Phosphothreonine

Disulfide bond

107 ↔ 112

Redox-active

Experimental info

Mutagenesis

107

1

C → S: No TPx activity, no effect on DOT activity

Mutagenesis

112

1

C → S: No TPx activity, no effect on DOT activity

Secondary structure

1

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215

Helix Strand Turn

Details...

Beta strand

73 – 75

3

Beta strand

81 – 83

3

Helix

84 – 90

7

Beta strand

92 – 98

7

Beta strand

100 – 104

5

Helix

105 – 121

17

Turn

122 – 124

3

Beta strand

126 – 132

7

Helix

135 – 145

11

Beta strand

148 – 153

6

Helix

158 – 163

6

Beta strand

166 – 171

6

Beta strand

176 – 181

6

Beta strand

184 – 191

8

Helix

194 – 211

18

Sequences

	Sequence		Length	Mass (Da)
	P40553-1 [UniParc]. Last modified February 1, 1995. Version 1. Checksum: EB78A216891946C0	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

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. , 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]	"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. , 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.
[4]	"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.
[5]	"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.
[6]	"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].
[7]	"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].
[8]	"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.
[9]	"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.
[10]	"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.
[11]	"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

EMBLGenBankDDBJ

Z38113 Genomic DNA. Translation: CAA86239.1.
AY558298 Genomic DNA. Translation: AAS56624.1.

PIR

S48445.

RefSeq

NP_012255.1.

3D structure databases

PDBMSD

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

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:4762N.

IntAct

P40553.

Proteomic databases

PeptideAtlas

P40553.

Genome annotation databases

Ensembl

YIL010W. Saccharomyces cerevisiae. [Contig view]

GeneID

854805.

GenomeReviews

Gene locus YIL010W in contig Z47047_GR.

KEGG

sce:YIL010W.

NMPDR

fig|4932.3.peg.1792.

Organism-specific databases

CYGD

YIL010w.

SGD

S000001272. DOT5.

Yeast-GFP

Search...

Phylogenomic databases

HOGENOM

P40553.

Gene expression databases

GermOnline

YIL010W. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR000866. AhpC-TSA.
IPR012335. Thioredoxin_fold.
[Graphical view]

Gene3D

G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.

Pfam

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

PROSITE

PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

LinkHub

P40553.

NextBio

977622.

Entry information

Entry name

DOT5_YEAST

Accession

Primary (citable) accession number: P40553

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	November 25, 2008
This is version 78 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)