DOT5_YEAST
ID DOT5_YEAST Reviewed; 215 AA.
AC P40553; D6VVR9;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Peroxiredoxin DOT5 {ECO:0000305};
DE Short=Prx;
DE EC=1.11.1.24 {ECO:0000269|PubMed:10681558, ECO:0000269|PubMed:12730197};
DE AltName: Full=Disrupter of telomere silencing protein 5 {ECO:0000303|PubMed:9755194};
DE AltName: Full=Nuclear thiol peroxidase {ECO:0000303|PubMed:10681558};
DE Short=nTPx {ECO:0000303|PubMed:10681558};
DE AltName: Full=Thioredoxin peroxidase;
DE AltName: Full=Thioredoxin-dependent peroxiredoxin DOT5 {ECO:0000305};
GN Name=DOT5 {ECO:0000303|PubMed:9755194};
GN OrderedLocusNames=YIL010W {ECO:0000312|SGD:S000001272};
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=9755194; DOI=10.1093/genetics/150.2.613;
RA Singer M.S., Kahana A., Wolf A.J., Meisinger L.L., Peterson S.E.,
RA Goggin C., Mahowald M., Gottschling D.E.;
RT "Identification of high-copy disruptors of telomeric silencing in
RT Saccharomyces cerevisiae.";
RL Genetics 150:613-632(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169870;
RA Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
RA Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL Nature 387:84-87(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION,
RP AND MUTAGENESIS OF CYS-107.
RX PubMed=10681558; DOI=10.1074/jbc.275.8.5723;
RA Park S.G., Cha M.-K., Jeong W., Kim I.-H.;
RT "Distinct physiological functions of thiol peroxidase isoenzymes in
RT Saccharomyces cerevisiae.";
RL J. Biol. Chem. 275:5723-5732(2000).
RN [6]
RP FUNCTION, ENZYME ACTIVITY, ACTIVE SITE, INDUCTION, DISULFIDE BOND, AND
RP MUTAGENESIS OF CYS-107 AND CYS-112.
RX PubMed=12730197; DOI=10.1074/jbc.m302628200;
RA Cha M.-K., Choi Y.-S., Hong S.-K., Kim W.-C., No K.T., Kim I.-H.;
RT "Nuclear thiol peroxidase as a functional alkyl-hydroperoxide reductase
RT necessary for stationary phase growth of Saccharomyces cerevisiae.";
RL J. Biol. Chem. 278:24636-24643(2003).
RN [7]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [8]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF CYS-107 AND CYS-112.
RX PubMed=12925864; DOI=10.1007/s00253-003-1421-5;
RA Izawa S., Kuroki N., Inoue Y.;
RT "Nuclear thioredoxin peroxidase Dot5 in Saccharomyces cerevisiae: roles in
RT oxidative stress response and disruption of telomeric silencing.";
RL Appl. Microbiol. Biotechnol. 64:120-124(2004).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY, CRYSTALLIZATION, X-RAY CRYSTALLOGRAPHY
RP (1.80 ANGSTROMS) OF 57-215 OF MUTANT CYS-107 AND CYS-112, AND SUBUNIT.
RX PubMed=16511121; DOI=10.1107/s1744309105016970;
RA Choi J., Choi S., Choi J., Cha M.-K., Kim I.-H., Shin W.;
RT "Crystallization and preliminary X-ray analysis of a truncated mutant of
RT yeast nuclear thiol peroxidase, a novel atypical 2-Cys peroxiredoxin.";
RL Acta Crystallogr. F 61:659-662(2005).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 57-215 OF MUTANT CYS-107 AND
RP CYS-112, AND SUBUNIT.
RX PubMed=16245326; DOI=10.1002/prot.20704;
RA Choi J., Choi S., Chon J.K., Choi J., Cha M.-K., Kim I.-H., Shin W.;
RT "Crystal structure of the C107S/C112S mutant of yeast nuclear 2-Cys
RT peroxiredoxin.";
RL Proteins 61:1146-1149(2005).
CC -!- FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of
CC hydrogen peroxide and organic hydroperoxides to water and alcohols,
CC respectively. Plays a role in cell protection against oxidative stress
CC by detoxifying peroxides and as sensor of hydrogen peroxide-mediated
CC signaling events. Has a role in telomere silencing, which is the
CC repression of chromatin structure which leads to a stop in the
CC transcription of nearby genes. Also has a role in the regulation of
CC telomere length. Acts as an alkyl-hydroperoxide reductase in the
CC nucleus during post-diauxic growth. Preferentially reduces alkyl-
CC hydroperoxides rather than hydrogen peroxide. Acts as an antioxidant
CC necessary for stationary phase survival. {ECO:0000269|PubMed:12730197,
CC ECO:0000269|PubMed:12925864, ECO:0000269|PubMed:9755194}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-dithiol + a hydroperoxide = [thioredoxin]-
CC disulfide + an alcohol + H2O; Xref=Rhea:RHEA:62620, Rhea:RHEA-
CC COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:29950, ChEBI:CHEBI:30879, ChEBI:CHEBI:35924,
CC ChEBI:CHEBI:50058; EC=1.11.1.24;
CC Evidence={ECO:0000269|PubMed:10681558, ECO:0000269|PubMed:12730197};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6.5. {ECO:0000269|PubMed:10681558};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:16245326,
CC ECO:0000269|PubMed:16511121}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10681558,
CC ECO:0000269|PubMed:12925864, ECO:0000269|PubMed:14562095}. Chromosome,
CC telomere {ECO:0000305}.
CC -!- INDUCTION: During the diauxic shift. In response to oxidative stress.
CC {ECO:0000269|PubMed:12730197}.
CC -!- MISCELLANEOUS: The active site is a conserved redox-active cysteine
CC residue, the peroxidatic cysteine (C(P)), which makes the nucleophilic
CC attack on the peroxide substrate. The peroxide oxidizes the C(P)-SH to
CC cysteine sulfenic acid (C(P)-SOH), which then reacts with another
CC cysteine residue, the resolving cysteine (C(R)), to form a disulfide
CC bridge. The disulfide is subsequently reduced by an appropriate
CC electron donor to complete the catalytic cycle. In this atypical 2-Cys
CC peroxiredoxin, C(R) is present in the same subunit to form an
CC intramolecular disulfide. The disulfide is subsequently reduced by
CC thioredoxin. {ECO:0000305|PubMed:12730197}.
CC -!- MISCELLANEOUS: Present with 1840 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the peroxiredoxin family. BCP/PrxQ subfamily.
CC {ECO:0000305}.
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DR EMBL; Z38113; CAA86239.1; -; Genomic_DNA.
DR EMBL; AY558298; AAS56624.1; -; Genomic_DNA.
DR EMBL; BK006942; DAA08535.1; -; Genomic_DNA.
DR PIR; S48445; S48445.
DR RefSeq; NP_012255.3; NM_001179360.3.
DR PDB; 2A4V; X-ray; 1.80 A; A=57-215.
DR PDBsum; 2A4V; -.
DR AlphaFoldDB; P40553; -.
DR SMR; P40553; -.
DR BioGRID; 34980; 65.
DR DIP; DIP-4762N; -.
DR IntAct; P40553; 1.
DR STRING; 4932.YIL010W; -.
DR iPTMnet; P40553; -.
DR MaxQB; P40553; -.
DR PaxDb; P40553; -.
DR PRIDE; P40553; -.
DR EnsemblFungi; YIL010W_mRNA; YIL010W; YIL010W.
DR GeneID; 854805; -.
DR KEGG; sce:YIL010W; -.
DR SGD; S000001272; DOT5.
DR VEuPathDB; FungiDB:YIL010W; -.
DR eggNOG; KOG0855; Eukaryota.
DR HOGENOM; CLU_042529_2_1_1; -.
DR InParanoid; P40553; -.
DR OMA; QVCGFQK; -.
DR BioCyc; YEAST:YIL010W-MON; -.
DR EvolutionaryTrace; P40553; -.
DR PRO; PR:P40553; -.
DR Proteomes; UP000002311; Chromosome IX.
DR RNAct; P40553; protein.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0008379; F:thioredoxin peroxidase activity; IDA:SGD.
DR GO; GO:0045454; P:cell redox homeostasis; IDA:SGD.
DR GO; GO:0034599; P:cellular response to oxidative stress; IGI:SGD.
DR InterPro; IPR000866; AhpC/TSA.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF00578; AhpC-TSA; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antioxidant; Chromosome; Disulfide bond; Nucleus;
KW Oxidoreductase; Peroxidase; Redox-active center; Reference proteome;
KW Telomere; Transcription; Transcription regulation.
FT CHAIN 1..215
FT /note="Peroxiredoxin DOT5"
FT /id="PRO_0000135152"
FT DOMAIN 63..211
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT REGION 20..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..59
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 107
FT /note="Cysteine sulfenic acid (-SOH) intermediate"
FT /evidence="ECO:0000269|PubMed:12730197"
FT DISULFID 107..112
FT /note="Redox-active"
FT /evidence="ECO:0000269|PubMed:12730197"
FT MUTAGEN 107
FT /note="C->S: No TPx activity, no effect on DOT activity."
FT /evidence="ECO:0000269|PubMed:10681558,
FT ECO:0000269|PubMed:12730197, ECO:0000269|PubMed:12925864"
FT MUTAGEN 112
FT /note="C->S: No TPx activity, no effect on DOT activity."
FT /evidence="ECO:0000269|PubMed:12730197,
FT ECO:0000269|PubMed:12925864"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:2A4V"
FT STRAND 81..83
FT /evidence="ECO:0007829|PDB:2A4V"
FT HELIX 84..90
FT /evidence="ECO:0007829|PDB:2A4V"
FT STRAND 92..98
FT /evidence="ECO:0007829|PDB:2A4V"
FT STRAND 100..104
FT /evidence="ECO:0007829|PDB:2A4V"
FT HELIX 105..121
FT /evidence="ECO:0007829|PDB:2A4V"
FT TURN 122..124
FT /evidence="ECO:0007829|PDB:2A4V"
FT STRAND 126..132
FT /evidence="ECO:0007829|PDB:2A4V"
FT HELIX 135..145
FT /evidence="ECO:0007829|PDB:2A4V"
FT STRAND 148..153
FT /evidence="ECO:0007829|PDB:2A4V"
FT HELIX 158..163
FT /evidence="ECO:0007829|PDB:2A4V"
FT STRAND 166..171
FT /evidence="ECO:0007829|PDB:2A4V"
FT STRAND 176..181
FT /evidence="ECO:0007829|PDB:2A4V"
FT STRAND 184..191
FT /evidence="ECO:0007829|PDB:2A4V"
FT HELIX 194..211
FT /evidence="ECO:0007829|PDB:2A4V"
SQ SEQUENCE 215 AA; 24120 MW; EB78A216891946C0 CRC64;
MGEALRRSTR IAISKRMLEE EESKLAPIST PEVPKKKIKT GPKHNANQAV VQEANRSSDV
NELEIGDPIP DLSLLNEDND SISLKKITEN NRVVVFFVYP RASTPGCTRQ ACGFRDNYQE
LKKYAAVFGL SADSVTSQKK FQSKQNLPYH LLSDPKREFI GLLGAKKTPL SGSIRSHFIF
VDGKLKFKRV KISPEVSVND AKKEVLEVAE KFKEE
