Reviewed,
UniProtKB/Swiss-Prot P40553 (DOT5_YEAST)
Last modified
November 25, 2008.
Version 78.
History...
Clusters with 100%,
90%,
50% identity |
Documents (4) |
Third-party data |
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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 |
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| 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 | |
| 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 reductionInferred from electronic annotation. Source: UniProtKB-KW regulation of transcription, DNA-dependentInferred from electronic annotation. Source: UniProtKB-KW response to oxidative stressInferred from genetic interaction. Source: SGD |
| Cellular component | chromosome, telomeric region Inferred from electronic annotation. Source: UniProtKB-KW nucleus Ref.4Inferred 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 | ||||||||||||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||||||||||||
| 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
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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. 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. 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 | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Z38113 Genomic DNA. Translation: CAA86239.1. AY558298 Genomic DNA. Translation: AAS56624.1. | |||||||||||||
| PIR | S48445. | ||||||||||||
| RefSeq | NP_012255.1. | ||||||||||||
3D structure databases | |||||||||||||
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| 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 |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | FPAP (Fungal Proteome Annotation Project) | ||||||||
Relevant documents
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |
| Yeast Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD |
| Yeast chromosome IX Yeast (Saccharomyces cerevisiae) chromosome IX: entries and gene names |

Clusters with


