[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION. PubMed=9755194 [NCBI, ExPASy, EBI, Israel, Japan] Singer M.S., Kahana A., Wolf A.J., Meisinger L.L., Peterson S.E., Goggin C., Mahowald M., Gottschling D.E.; "Identification of high-copy disruptors of telomeric silencing in Saccharomyces cerevisiae."; Genetics 150:613-632(1998).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=ATCC 204511 / S288c / AB972; PubMed=9169870 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX."; Nature 387:84-87(1997).
[3]	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).
[4]	CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND MUTAGENESIS OF CYS-107. DOI=10.1074/jbc.275.8.5723; PubMed=10681558 [NCBI, ExPASy, EBI, Israel, Japan] Park S.G., Cha M.-K., Jeong W., Kim I.-H.; "Distinct physiological functions of thiol peroxidase isoenzymes in Saccharomyces cerevisiae."; J. Biol. Chem. 275:5723-5732(2000).
[5]	FUNCTION, ENZYME ACTIVITY, ACTIVE SITE, INDUCTION, DISULFIDE BOND, AND MUTAGENESIS OF CYS-107 AND CYS-112. DOI=10.1074/jbc.M302628200; PubMed=12730197 [NCBI, ExPASy, EBI, Israel, Japan] Cha M.-K., Choi Y.-S., Hong S.-K., Kim W.-C., No K.T., Kim I.-H.; "Nuclear thiol peroxidase as a functional alkyl-hydroperoxide reductase necessary for stationary phase growth of Saccharomyces cerevisiae."; J. Biol. Chem. 278:24636-24643(2003).
[6]	SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. DOI=10.1038/nature02026; PubMed=14562095 [NCBI, ExPASy, EBI, Israel, Japan] Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.; "Global analysis of protein localization in budding yeast."; Nature 425:686-691(2003).
[7]	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).
[8]	FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF CYS-107 AND CYS-112. DOI=10.1007/s00253-003-1421-5; PubMed=12925864 [NCBI, ExPASy, EBI, Israel, Japan] Izawa S., Kuroki N., Inoue Y.; "Nuclear thioredoxin peroxidase Dot5 in Saccharomyces cerevisiae: roles in oxidative stress response and disruption of telomeric silencing."; Appl. Microbiol. Biotechnol. 64:120-124(2004).
[9]	IDENTIFICATION BY MASS SPECTROMETRY, CRYSTALLIZATION, X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 57-215 OF MUTANT CYS-107 AND CYS-112, AND SUBUNIT. DOI=10.1107/S1744309105016970; PubMed=16511121 [NCBI, ExPASy, EBI, Israel, Japan] Choi J., Choi S., Choi J., Cha M.-K., Kim I.-H., Shin W.; "Crystallization and preliminary X-ray analysis of a truncated mutant of yeast nuclear thiol peroxidase, a novel atypical 2-Cys peroxiredoxin."; Acta Crystallogr. F 61:659-662(2005).
[10]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-30, AND MASS SPECTROMETRY. DOI=10.1074/mcp.M700468-MCP200; PubMed=18407956 [NCBI, ExPASy, EBI, Israel, Japan] Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; "A multidimensional chromatography technology for in-depth phosphoproteome analysis."; Mol. Cell. Proteomics 7:1389-1396(2008).
[11]	X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 57-215 OF MUTANT CYS-107 AND CYS-112, AND SUBUNIT. DOI=10.1002/prot.20704; PubMed=16245326 [NCBI, ExPASy, EBI, Israel, Japan] Choi J., Choi S., Chon J.K., Choi J., Cha M.-K., Kim I.-H., Shin W.; "Crystal structure of the C107S/C112S mutant of yeast nuclear 2-Cys peroxiredoxin."; Proteins 61:1146-1149(2005).

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' + H₂O + ROH.
BIOPHYSICOCHEMICAL PROPERTIES:

pH dependence: Optimum pH is 6.5;
SUBUNIT: Monomer.
SUBCELLULAR LOCATION: Nucleus. Telomere (Potential).
INDUCTION: During the diauxic shift. In response to oxidative stress.
PTM: 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.
SIMILARITY: Belongs to the ahpC/TSA family.
SIMILARITY: Contains 1 thioredoxin domain.

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

Z38113; CAA86239.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY558298; AAS56624.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S48445; S48445.

RefSeq

NP_012255.1; -.

3D structure databases

PDB

2A4V; X-ray; 1.80 A; A=57-215.

[ExPASy / RCSB / EBI]

PDBsum

2A4V; -.

ModBase

P40553.

Protein-protein interaction databases

DIP

DIP:4762N; -.

IntAct

P40553; -.

Organism-specific databases

YIL010w; -.

S000001272; DOT5.

Gene expression databases

GermOnline

YIL010W; Saccharomyces cerevisiae.

Ontologies

GO:0000781;	Cellular component: chromosome, telomeric region (inferred from electronic annotation from UniProtKB-KW).
GO:0005634;	Cellular component: nucleus (inferred from electronic annotation from UniProtKB-KW).
GO:0008379;	Molecular function: thioredoxin peroxidase activity (inferred from direct assay from SGD).
GO:0045454;	Biological process: cell redox homeostasis (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0006355;	Biological process: regulation of transcription, DNA-dependent (inferred from electronic annotation from UniProtKB-KW).
GO:0006979;	Biological process: response to oxidative stress (inferred from genetic interaction from SGD).
QuickGo view.

Family and domain databases

InterPro

IPR000866; AhpC-TSA.
IPR012335; Thioredoxin_fold.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.30.10; Thioredoxin_fold; 1.

Pfam

PF00578; AhpC-TSA; 1.
Pfam graphical view of domain structure.

PROSITE

PS51352; THIOREDOXIN_2; 1.
PROSITE graphical view of domain structure (profiles).

ProtoNet

P40553.

Proteomic databases

PeptideAtlas

P40553; -.

Genome annotation databases

Ensembl

YIL010W; Saccharomyces cerevisiae. [Contig view]

854805; -.

Z47047_GR; YIL010W.

sce:YIL010W; -.

fig|4932.3.peg.1792; -.

Phylogenomic databases

HOGENOM

P40553; -.

Other

LinkHub

P40553; -.

NextBio

977622; -.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Antioxidant; Chromosomal protein; Complete proteome; Nucleus; Oxidoreductase; Peroxidase; Phosphoprotein; Redox-active center; Telomere; Transcription; Transcription regulation.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 215`	`215`	`Peroxiredoxin DOT5.`	`PRO_0000135152`
`DOMAIN`	`63 211`	`149`	`Thioredoxin.`
`ACT_SITE`	`107 107`		`Cysteine sulfenic acid (-SOH) intermediate.`
`MOD_RES`	`30 30`		`Phosphothreonine.`
`DISULFID`	`107 112`		`Redox-active.`
`MUTAGEN`	`107 107`		`C->S: No TPx activity, no effect on DOT activity.`
`MUTAGEN`	`112 112`		`C->S: No TPx activity, no effect on DOT activity.`
`STRAND`	`73 75`	`3`
`STRAND`	`81 83`	`3`
`HELIX`	`84 90`	`7`
`STRAND`	`92 98`	`7`
`STRAND`	`100 104`	`5`
`HELIX`	`105 121`	`17`
`TURN`	`122 124`	`3`
`STRAND`	`126 132`	`7`
`HELIX`	`135 145`	`11`
`STRAND`	`148 153`	`6`
`HELIX`	`158 163`	`6`
`STRAND`	`166 171`	`6`
`STRAND`	`176 181`	`6`
`STRAND`	`184 191`	`8`
`HELIX`	`194 211`	`18`

Sequence information

Length: 215 AA [This is the length of the unprocessed precursor]

Molecular weight: 24120 Da [This is the MW of the unprocessed precursor]

CRC64: EB78A216891946C0 [This is a checksum on the sequence]

        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

P40553 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 submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools