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Peroxiredoxin DOT5 (Prx) (EC 1.11.1.15) (Disrupter of telomere silencing protein 5) (Nuclear thiol peroxidase) (nTPx) (Thioredoxin peroxidase)

 DOT5_YEAST              Reviewed;         215 AA.
P40553; D6VVR9;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
01-FEB-1995, sequence version 1.
28-MAR-2018, entry version 160.
RecName: Full=Peroxiredoxin DOT5 {ECO:0000305};
Short=Prx;
EC=1.11.1.15 {ECO:0000269|PubMed:10681558, ECO:0000269|PubMed:12730197};
AltName: Full=Disrupter of telomere silencing protein 5 {ECO:0000303|PubMed:9755194};
AltName: Full=Nuclear thiol peroxidase {ECO:0000303|PubMed:10681558};
Short=nTPx {ECO:0000303|PubMed:10681558};
AltName: Full=Thioredoxin peroxidase;
Name=DOT5 {ECO:0000303|PubMed:9755194};
OrderedLocusNames=YIL010W {ECO:0000312|SGD:S000001272};
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
PubMed=9755194;
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 204508 / S288c;
PubMed=9169870;
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]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=17322287; DOI=10.1101/gr.6037607;
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).
[5]
CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
LOCATION, AND MUTAGENESIS OF CYS-107.
PubMed=10681558; DOI=10.1074/jbc.275.8.5723;
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).
[6]
FUNCTION, ENZYME ACTIVITY, ACTIVE SITE, INDUCTION, DISULFIDE BOND, AND
MUTAGENESIS OF CYS-107 AND CYS-112.
PubMed=12730197; DOI=10.1074/jbc.M302628200;
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).
[7]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=14562095; DOI=10.1038/nature02026;
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).
[8]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
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).
[9]
FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF CYS-107 AND
CYS-112.
PubMed=12925864; DOI=10.1007/s00253-003-1421-5;
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).
[10]
IDENTIFICATION BY MASS SPECTROMETRY, CRYSTALLIZATION, X-RAY
CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 57-215 OF MUTANT CYS-107 AND
CYS-112, AND SUBUNIT.
PubMed=16511121; DOI=10.1107/S1744309105016970;
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).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
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).
[12]
X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 57-215 OF MUTANT CYS-107 AND
CYS-112, AND SUBUNIT.
PubMed=16245326; DOI=10.1002/prot.20704;
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).
-!- FUNCTION: Thiol-specific peroxidase that catalyzes the reduction
of hydrogen peroxide and organic hydroperoxides to water and
alcohols, respectively. Plays a role in cell protection against
oxidative stress by detoxifying peroxides and as sensor of
hydrogen peroxide-mediated signaling events. 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
peroxide. Acts as an antioxidant necessary for stationary phase
survival. {ECO:0000269|PubMed:12730197,
ECO:0000269|PubMed:12925864, ECO:0000269|PubMed:9755194}.
-!- CATALYTIC ACTIVITY: 2 R'-SH + ROOH = R'-S-S-R' + H(2)O + ROH.
{ECO:0000269|PubMed:10681558, ECO:0000269|PubMed:12730197}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
pH dependence:
Optimum pH is 6.5. {ECO:0000269|PubMed:10681558};
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:16245326,
ECO:0000269|PubMed:16511121}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10681558,
ECO:0000269|PubMed:12925864, ECO:0000269|PubMed:14562095}.
Chromosome, telomere {ECO:0000305}.
-!- INDUCTION: During the diauxic shift. In response to oxidative
stress. {ECO:0000269|PubMed:12730197}.
-!- MISCELLANEOUS: The active site is a conserved redox-active
cysteine residue, the peroxidatic cysteine (C(P)), which makes the
nucleophilic attack on the peroxide substrate. The peroxide
oxidizes the C(P)-SH to cysteine sulfenic acid (C(P)-SOH), which
then reacts with another cysteine residue, the resolving cysteine
(C(R)), to form a disulfide bridge. The disulfide is subsequently
reduced by an appropriate electron donor to complete the catalytic
cycle. In this atypical 2-Cys peroxiredoxin, C(R) is present in
the same subunit to form an intramolecular disulfide. The
disulfide is subsequently reduced by thioredoxin.
{ECO:0000305|PubMed:12730197}.
-!- MISCELLANEOUS: Present with 1840 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the peroxiredoxin family. BCP/PrxQ
subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; Z38113; CAA86239.1; -; Genomic_DNA.
EMBL; AY558298; AAS56624.1; -; Genomic_DNA.
EMBL; BK006942; DAA08535.1; -; Genomic_DNA.
PIR; S48445; S48445.
RefSeq; NP_012255.3; NM_001179360.3.
PDB; 2A4V; X-ray; 1.80 A; A=57-215.
PDBsum; 2A4V; -.
ProteinModelPortal; P40553; -.
SMR; P40553; -.
BioGrid; 34980; 61.
DIP; DIP-4762N; -.
IntAct; P40553; 5.
STRING; 4932.YIL010W; -.
iPTMnet; P40553; -.
MaxQB; P40553; -.
PaxDb; P40553; -.
PRIDE; P40553; -.
EnsemblFungi; YIL010W; YIL010W; YIL010W.
GeneID; 854805; -.
KEGG; sce:YIL010W; -.
EuPathDB; FungiDB:YIL010W; -.
SGD; S000001272; DOT5.
HOGENOM; HOG000022344; -.
InParanoid; P40553; -.
KO; K03564; -.
OMA; VYPRAST; -.
OrthoDB; EOG092C5CGU; -.
BioCyc; YEAST:YIL010W-MONOMER; -.
EvolutionaryTrace; P40553; -.
PRO; PR:P40553; -.
Proteomes; UP000002311; Chromosome IX.
GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IDA:SGD.
GO; GO:0008379; F:thioredoxin peroxidase activity; IDA:SGD.
GO; GO:0045454; P:cell redox homeostasis; IDA:SGD.
GO; GO:0034599; P:cellular response to oxidative stress; IGI:SGD.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR000866; AhpC/TSA.
InterPro; IPR036249; Thioredoxin-like_sf.
InterPro; IPR013766; Thioredoxin_domain.
Pfam; PF00578; AhpC-TSA; 1.
SUPFAM; SSF52833; SSF52833; 1.
PROSITE; PS51352; THIOREDOXIN_2; 1.
1: Evidence at protein level;
3D-structure; Antioxidant; Chromosome; Complete proteome;
Disulfide bond; Nucleus; Oxidoreductase; Peroxidase;
Redox-active center; Reference proteome; Telomere; Transcription;
Transcription regulation.
CHAIN 1 215 Peroxiredoxin DOT5.
/FTId=PRO_0000135152.
DOMAIN 63 211 Thioredoxin. {ECO:0000255|PROSITE-
ProRule:PRU00691}.
ACT_SITE 107 107 Cysteine sulfenic acid (-SOH)
intermediate.
{ECO:0000269|PubMed:12730197}.
DISULFID 107 112 Redox-active.
{ECO:0000269|PubMed:12730197}.
MUTAGEN 107 107 C->S: No TPx activity, no effect on DOT
activity. {ECO:0000269|PubMed:10681558,
ECO:0000269|PubMed:12730197,
ECO:0000269|PubMed:12925864}.
MUTAGEN 112 112 C->S: No TPx activity, no effect on DOT
activity. {ECO:0000269|PubMed:12730197,
ECO:0000269|PubMed:12925864}.
STRAND 73 75 {ECO:0000244|PDB:2A4V}.
STRAND 81 83 {ECO:0000244|PDB:2A4V}.
HELIX 84 90 {ECO:0000244|PDB:2A4V}.
STRAND 92 98 {ECO:0000244|PDB:2A4V}.
STRAND 100 104 {ECO:0000244|PDB:2A4V}.
HELIX 105 121 {ECO:0000244|PDB:2A4V}.
TURN 122 124 {ECO:0000244|PDB:2A4V}.
STRAND 126 132 {ECO:0000244|PDB:2A4V}.
HELIX 135 145 {ECO:0000244|PDB:2A4V}.
STRAND 148 153 {ECO:0000244|PDB:2A4V}.
HELIX 158 163 {ECO:0000244|PDB:2A4V}.
STRAND 166 171 {ECO:0000244|PDB:2A4V}.
STRAND 176 181 {ECO:0000244|PDB:2A4V}.
STRAND 184 191 {ECO:0000244|PDB:2A4V}.
HELIX 194 211 {ECO:0000244|PDB:2A4V}.
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


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