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Histone deacetylase RPD3 (EC 3.5.1.98) (Transcriptional regulatory protein RPD3)

 RPD3_YEAST              Reviewed;         433 AA.
P32561; D6W0L7;
01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
01-OCT-1993, sequence version 1.
25-OCT-2017, entry version 176.
RecName: Full=Histone deacetylase RPD3;
EC=3.5.1.98;
AltName: Full=Transcriptional regulatory protein RPD3;
Name=RPD3; Synonyms=MOF6, REC3, SDI2, SDS6; OrderedLocusNames=YNL330C;
ORFNames=N0305;
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=1944291; DOI=10.1128/MCB.11.12.6317;
Vidal M., Gaber R.F.;
"RPD3 encodes a second factor required to achieve maximum positive and
negative transcriptional states in Saccharomyces cerevisiae.";
Mol. Cell. Biol. 11:6317-6327(1991).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 96604 / S288c / FY1679;
PubMed=8533474; DOI=10.1002/yea.320111010;
van Dyck L., Pascual-Ahuir A., Purnelle B., Goffeau A.;
"An 8.2 kb DNA segment from chromosome XIV carries the RPD3 and PAS8
genes as well as the Saccharomyces cerevisiae homologue of the
thiamine-repressed nmt1 gene and a chromosome III-duplicated gene for
a putative aryl-alcohol dehydrogenase.";
Yeast 11:987-991(1995).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169873;
Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F.,
Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M.,
Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N.,
Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D.,
Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A.,
Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A.,
Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C.,
Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M.,
Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J.,
Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L.,
Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M.,
Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P.,
Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A.,
Wambutt R., Wedler H., Zollner A., Hani J.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV
and its evolutionary implications.";
Nature 387:93-98(1997).
[4]
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).
[5]
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).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-201.
STRAIN=S288c / FY1676;
PubMed=7645347; DOI=10.1002/yea.320110606;
Maftahi M., Nicaud J.-M., Levesque H., Gaillardin C.;
"Sequencing analysis of a 15.4 kb fragment of yeast chromosome XIV
identifies the RPD3, PAS8 and KRE1 loci, five new open reading
frames.";
Yeast 11:567-572(1995).
[7]
FUNCTION.
STRAIN=ATCC 200060 / W303;
PubMed=8978024;
Vannier D., Balderes D., Shore D.;
"Evidence that the transcriptional regulators SIN3 and RPD3, and a
novel gene (SDS3) with similar functions, are involved in
transcriptional silencing in S. cerevisiae.";
Genetics 144:1343-1353(1996).
[8]
FUNCTION, AND IDENTIFICATION IN A HISTONE DEACETYLASE COMPLEX.
PubMed=8962081; DOI=10.1073/pnas.93.25.14503;
Rundlett S.E., Carmen A.A., Kobayashi R., Bavykin S., Turner B.M.,
Grunstein M.;
"HDA1 and RPD3 are members of distinct yeast histone deacetylase
complexes that regulate silencing and transcription.";
Proc. Natl. Acad. Sci. U.S.A. 93:14503-14508(1996).
[9]
INTERACTION WITH CPR6 AND CPR7.
PubMed=8873448;
DOI=10.1002/(SICI)1097-0061(199608)12:10<943::AID-YEA997>3.0.CO;2-3;
Duina A.A., Marsh J.A., Gaber R.F.;
"Identification of two CyP-40-like cyclophilins in Saccharomyces
cerevisiae, one of which is required for normal growth.";
Yeast 12:943-952(1996).
[10]
IDENTIFICATION IN THE RPD3 COMPLEX.
PubMed=9234741; DOI=10.1128/MCB.17.8.4852;
Kasten M.M., Dorland S., Stillman D.J.;
"A large protein complex containing the yeast Sin3p and Rpd3p
transcriptional regulators.";
Mol. Cell. Biol. 17:4852-4858(1997).
[11]
FUNCTION, AND MUTAGENESIS OF HIS-150; HIS-151 AND HIS-188.
PubMed=9512514; DOI=10.1101/gad.12.6.797;
Kadosh D., Struhl K.;
"Histone deacetylase activity of Rpd3 is important for transcriptional
repression in vivo.";
Genes Dev. 12:797-805(1998).
[12]
FUNCTION OF THE RPD3 COMPLEX.
PubMed=9710596; DOI=10.1128/MCB.18.9.5121;
Kadosh D., Struhl K.;
"Targeted recruitment of the Sin3-Rpd3 histone deacetylase complex
generates a highly localized domain of repressed chromatin in vivo.";
Mol. Cell. Biol. 18:5121-5127(1998).
[13]
DEACETYLATION OF HISTONE H4.
PubMed=9572144; DOI=10.1038/33952;
Rundlett S.E., Carmen A.A., Suka N., Turner B.M., Grunstein M.;
"Transcriptional repression by UME6 involves deacetylation of lysine 5
of histone H4 by RPD3.";
Nature 392:831-835(1998).
[14]
FUNCTION.
PubMed=10079324; DOI=10.1007/s002940050434;
Dora E.G., Rudin N., Martell J.R., Esposito M.S., Ramirez R.M.;
"RPD3 (REC3) mutations affect mitotic recombination in Saccharomyces
cerevisiae.";
Curr. Genet. 35:68-76(1999).
[15]
FUNCTION OF THE RPD3 COMPLEX.
PubMed=10388812;
Sun Z.-W., Hampsey M.;
"A general requirement for the Sin3-Rpd3 histone deacetylase complex
in regulating silencing in Saccharomyces cerevisiae.";
Genetics 152:921-932(1999).
[16]
FUNCTION.
PubMed=10359799; DOI=10.1073/pnas.96.12.6835;
Burgess S.M., Ajimura M., Kleckner N.;
"GCN5-dependent histone H3 acetylation and RPD3-dependent histone H4
deacetylation have distinct, opposing effects on IME2 transcription,
during meiosis and during vegetative growth, in budding yeast.";
Proc. Natl. Acad. Sci. U.S.A. 96:6835-6840(1999).
[17]
INTERACTION WITH CPR1 AND ESS1.
PubMed=10899127; DOI=10.1093/emboj/19.14.3739;
Arevalo-Rodriguez M., Cardenas M.E., Wu X., Hanes S.D., Heitman J.;
"Cyclophilin A and Ess1 interact with and regulate silencing by the
Sin3-Rpd3 histone deacetylase.";
EMBO J. 19:3739-3749(2000).
[18]
FUNCTION.
PubMed=11069890; DOI=10.1101/gad.829100;
Watson A.D., Edmondson D.G., Bone J.R., Mukai Y., Yu Y., Du W.,
Stillman D.J., Roth S.Y.;
"Ssn6-Tup1 interacts with class I histone deacetylases required for
repression.";
Genes Dev. 14:2737-2744(2000).
[19]
FUNCTION.
PubMed=10931932; DOI=10.1093/nar/28.16.3160;
Elkhaimi M., Kaadige M.R., Kamath D., Jackson J.C., Biliran H. Jr.,
Lopes J.M.;
"Combinatorial regulation of phospholipid biosynthetic gene expression
by the UME6, SIN3 and RPD3 genes.";
Nucleic Acids Res. 28:3160-3167(2000).
[20]
INTERACTION WITH CYC8.
PubMed=12234935; DOI=10.1093/emboj/cdf498;
Sandmeier J.J., French S., Osheim Y., Cheung W.L., Gallo C.M.,
Beyer A.L., Smith J.S.;
"RPD3 is required for the inactivation of yeast ribosomal DNA genes in
stationary phase.";
EMBO J. 21:4959-4968(2002).
[21]
DOMAIN, AND MUTAGENESIS OF TRP-322; GLU-325; GLY-327; LEU-328;
LEU-329; VAL-332; LEU-334; ASP-335; LEU-338 AND PRO-339.
PubMed=12110674; DOI=10.1074/jbc.M204640200;
Adachi N., Kimura A., Horikoshi M.;
"A conserved motif common to the histone acetyltransferase Esa1 and
the histone deacetylase Rpd3.";
J. Biol. Chem. 277:35688-35695(2002).
[22]
FUNCTION.
PubMed=12192044; DOI=10.1128/MCB.22.18.6458-6470.2002;
Deckert J., Struhl K.;
"Targeted recruitment of Rpd3 histone deacetylase represses
transcription by inhibiting recruitment of Swi/Snf, SAGA, and TATA
binding protein.";
Mol. Cell. Biol. 22:6458-6470(2002).
[23]
FUNCTION, AND DNA-BINDING.
PubMed=12089521; DOI=10.1038/ng907;
Kurdistani S.K., Robyr D., Tavazoie S., Grunstein M.;
"Genome-wide binding map of the histone deacetylase Rpd3 in yeast.";
Nat. Genet. 31:248-254(2002).
[24]
IDENTIFICATION IN THE RPD3 COMPLEX, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=12672825; DOI=10.1074/jbc.C300036200;
Nourani A., Howe L., Pray-Grant M.G., Workman J.L., Grant P.A.,
Cote J.;
"Opposite role of yeast ING family members in p53-dependent
transcriptional activation.";
J. Biol. Chem. 278:19171-19175(2003).
[25]
FUNCTION OF THE RPD3 COMPLEX.
PubMed=12808094; DOI=10.1128/MCB.23.13.4522-4531.2003;
Scott K.L., Plon S.E.;
"Loss of Sin3/Rpd3 histone deacetylase restores the DNA damage
response in checkpoint-deficient strains of Saccharomyces
cerevisiae.";
Mol. Cell. Biol. 23:4522-4531(2003).
[26]
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).
[27]
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).
[28]
INTERACTION WITH HAC1, AND FUNCTION OF THE RPD3 COMPLEX.
PubMed=15141165; DOI=10.1038/sj.emboj.7600233;
Schroeder M., Clark R., Liu C.Y., Kaufman R.J.;
"The unfolded protein response represses differentiation through the
RPD3-SIN3 histone deacetylase.";
EMBO J. 23:2281-2292(2004).
[29]
FUNCTION.
PubMed=15143171; DOI=10.1128/MCB.24.11.4769-4780.2004;
Aparicio J.G., Viggiani C.J., Gibson D.G., Aparicio O.M.;
"The Rpd3-Sin3 histone deacetylase regulates replication timing and
enables intra-S origin control in Saccharomyces cerevisiae.";
Mol. Cell. Biol. 24:4769-4780(2004).
[30]
FUNCTION.
PubMed=15456858; DOI=10.1128/MCB.24.20.8823-8833.2004;
Sabet N., Volo S., Yu C., Madigan J.P., Morse R.H.;
"Genome-wide analysis of the relationship between transcriptional
regulation by Rpd3p and the histone H3 and H4 amino termini in budding
yeast.";
Mol. Cell. Biol. 24:8823-8833(2004).
[31]
INTERACTION WITH HOG1, AND FUNCTION OF THE RPD3 COMPLEX.
PubMed=14737171; DOI=10.1038/nature02258;
De Nadal E., Zapater M., Alepuz P.M., Sumoy L., Mas G., Posas F.;
"The MAPK Hog1 recruits Rpd3 histone deacetylase to activate
osmoresponsive genes.";
Nature 427:370-374(2004).
[32]
FUNCTION OF THE RPD3 COMPLEX.
PubMed=14711989; DOI=10.1073/pnas.0304797101;
Jazayeri A., McAinsh A.D., Jackson S.P.;
"Saccharomyces cerevisiae Sin3p facilitates DNA double-strand break
repair.";
Proc. Natl. Acad. Sci. U.S.A. 101:1644-1649(2004).
[33]
IDENTIFICATION IN THE RPD3C(L) COMPLEX, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=16314178; DOI=10.1016/j.bbaexp.2005.09.005;
Carrozza M.J., Florens L., Swanson S.K., Shia W.-J., Anderson S.,
Yates J., Washburn M.P., Workman J.L.;
"Stable incorporation of sequence specific repressors Ash1 and Ume6
into the Rpd3L complex.";
Biochim. Biophys. Acta 1731:77-87(2005).
[34]
IDENTIFICATION IN THE RPD3C(L) AND RPD3C(S) COMPLEXES, IDENTIFICATION
BY MASS SPECTROMETRY, AND FUNCTION OF THE RPD3C(S) COMPLEX.
PubMed=16286008; DOI=10.1016/j.cell.2005.10.025;
Keogh M.-C., Kurdistani S.K., Morris S.A., Ahn S.H., Podolny V.,
Collins S.R., Schuldiner M., Chin K., Punna T., Thompson N.J.,
Boone C., Emili A., Weissman J.S., Hughes T.R., Strahl B.D.,
Grunstein M., Greenblatt J.F., Buratowski S., Krogan N.J.;
"Cotranscriptional set2 methylation of histone H3 lysine 36 recruits a
repressive Rpd3 complex.";
Cell 123:593-605(2005).
[35]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-394, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ADR376;
PubMed=17330950; DOI=10.1021/pr060559j;
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
Elias J.E., Gygi S.P.;
"Large-scale phosphorylation analysis of alpha-factor-arrested
Saccharomyces cerevisiae.";
J. Proteome Res. 6:1190-1197(2007).
[36]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-394 AND SER-408, AND
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).
[37]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-408, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
-!- FUNCTION: Catalytic component of the RPD3 histone deacetylase
(HDAC) complexes RPD3C(L) and RPD3C(S) responsible for the
deacetylation of lysine residues on the N-terminal part of the
core histones (H2A, H2B, H3 and H4). Histone deacetylation plays
an important role in transcriptional regulation, cell cycle
progression, DNA damage response, osmotic stress response and
developmental events. Is involved in rDNA and telomere silencing
and in double strand breaks repair. Required for both full
transcription repression and activation of many genes including
cell type-specific genes (STE6, TY2 and HO), cell differentiation-
specific genes (SPO13), genes that respond to external signals
(PHO5) and TRK2. The RPD3 complexes regulate also chromosomal
replication timing. {ECO:0000269|PubMed:10079324,
ECO:0000269|PubMed:10359799, ECO:0000269|PubMed:10388812,
ECO:0000269|PubMed:10931932, ECO:0000269|PubMed:11069890,
ECO:0000269|PubMed:12089521, ECO:0000269|PubMed:12192044,
ECO:0000269|PubMed:12808094, ECO:0000269|PubMed:14711989,
ECO:0000269|PubMed:14737171, ECO:0000269|PubMed:15141165,
ECO:0000269|PubMed:15143171, ECO:0000269|PubMed:15456858,
ECO:0000269|PubMed:16286008, ECO:0000269|PubMed:1944291,
ECO:0000269|PubMed:8962081, ECO:0000269|PubMed:8978024,
ECO:0000269|PubMed:9512514, ECO:0000269|PubMed:9710596}.
-!- CATALYTIC ACTIVITY: Hydrolysis of an N(6)-acetyl-lysine residue of
a histone to yield a deacetylated histone.
-!- SUBUNIT: Component of the RPD3C(L) complex composed of at least
ASH1, CTI6, DEP1, PHO23, RPD3, RXT2, RXT3, SAP30, SDS3, SIN3, UME1
and UME6. Component of the RPD3C(S) complex composed of at least
EAF3, RCO1, RPD3, SIN3, and UME1. Interacts with cyclophilins
CPR1, CPR6 and CPR7, with the kinase HOG1, and with ESS1, CYC8 and
HAC1. {ECO:0000269|PubMed:10899127, ECO:0000269|PubMed:12234935,
ECO:0000269|PubMed:12672825, ECO:0000269|PubMed:14737171,
ECO:0000269|PubMed:15141165, ECO:0000269|PubMed:16286008,
ECO:0000269|PubMed:16314178, ECO:0000269|PubMed:8873448,
ECO:0000269|PubMed:8962081, ECO:0000269|PubMed:9234741}.
-!- INTERACTION:
P53691:CPR6; NbExp=2; IntAct=EBI-15864, EBI-5429;
P47103:CPR7; NbExp=2; IntAct=EBI-15864, EBI-5436;
P14922:CYC8; NbExp=6; IntAct=EBI-15864, EBI-18215;
Q03213:HOT1; NbExp=3; IntAct=EBI-15864, EBI-27376;
P38255:RXT2; NbExp=5; IntAct=EBI-15864, EBI-21537;
P22579:SIN3; NbExp=10; IntAct=EBI-15864, EBI-17160;
P16649:TUP1; NbExp=2; IntAct=EBI-15864, EBI-19654;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
Nucleus {ECO:0000269|PubMed:14562095}.
-!- DOMAIN: The ESA1-RPD3 (ER) motif is common to ESA1 and RPD3 and is
required for ESA1 histone acetyl-transferase (HAT) activity and
RPD3 histone deacetylase (HDAC) activity.
{ECO:0000269|PubMed:12110674}.
-!- MISCELLANEOUS: Present with 3850 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the histone deacetylase family. HD type 1
subfamily. {ECO:0000305}.
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EMBL; S66438; AAB20328.1; -; Genomic_DNA.
EMBL; X83226; CAA58228.1; -; Genomic_DNA.
EMBL; Z46259; CAA86368.1; -; Genomic_DNA.
EMBL; Z71605; CAA96262.1; -; Genomic_DNA.
EMBL; Z71606; CAA96263.1; -; Genomic_DNA.
EMBL; AY692813; AAT92832.1; -; Genomic_DNA.
EMBL; BK006947; DAA10233.1; -; Genomic_DNA.
PIR; S22284; S22284.
RefSeq; NP_014069.1; NM_001183168.1.
ProteinModelPortal; P32561; -.
SMR; P32561; -.
BioGrid; 35511; 960.
DIP; DIP-681N; -.
IntAct; P32561; 59.
MINT; MINT-614075; -.
STRING; 4932.YNL330C; -.
iPTMnet; P32561; -.
MaxQB; P32561; -.
PRIDE; P32561; -.
EnsemblFungi; YNL330C; YNL330C; YNL330C.
GeneID; 855386; -.
KEGG; sce:YNL330C; -.
EuPathDB; FungiDB:YNL330C; -.
SGD; S000005274; RPD3.
GeneTree; ENSGT00530000062889; -.
HOGENOM; HOG000225180; -.
InParanoid; P32561; -.
KO; K06067; -.
OMA; KRVCYFF; -.
OrthoDB; EOG092C1END; -.
BioCyc; YEAST:G3O-33314-MONOMER; -.
Reactome; R-SCE-3214815; HDACs deacetylate histones.
Reactome; R-SCE-4551638; SUMOylation of chromatin organization proteins.
Reactome; R-SCE-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
PRO; PR:P32561; -.
Proteomes; UP000002311; Chromosome XIV.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0000118; C:histone deacetylase complex; IDA:SGD.
GO; GO:0034399; C:nuclear periphery; IDA:SGD.
GO; GO:0033698; C:Rpd3L complex; IDA:SGD.
GO; GO:0032221; C:Rpd3S complex; IDA:SGD.
GO; GO:0070822; C:Sin3-type complex; IDA:SGD.
GO; GO:0004407; F:histone deacetylase activity; IDA:SGD.
GO; GO:0032041; F:NAD-dependent histone deacetylase activity (H3-K14 specific); IEA:UniProtKB-EC.
GO; GO:0003713; F:transcription coactivator activity; IMP:SGD.
GO; GO:0003714; F:transcription corepressor activity; IMP:SGD.
GO; GO:0070932; P:histone H3 deacetylation; IMP:SGD.
GO; GO:0070933; P:histone H4 deacetylation; IMP:SGD.
GO; GO:0061188; P:negative regulation of chromatin silencing at rDNA; IMP:SGD.
GO; GO:0061186; P:negative regulation of chromatin silencing at silent mating-type cassette; IMP:SGD.
GO; GO:0031939; P:negative regulation of chromatin silencing at telomere; IDA:SGD.
GO; GO:0045128; P:negative regulation of reciprocal meiotic recombination; IMP:SGD.
GO; GO:0016479; P:negative regulation of transcription from RNA polymerase I promoter; IMP:SGD.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IMP:SGD.
GO; GO:0051038; P:negative regulation of transcription involved in meiotic cell cycle; IMP:SGD.
GO; GO:0016239; P:positive regulation of macroautophagy; IMP:SGD.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IMP:SGD.
GO; GO:0034503; P:protein localization to nucleolar rDNA repeats; IMP:SGD.
GO; GO:0030174; P:regulation of DNA-dependent DNA replication initiation; IMP:SGD.
GO; GO:0000083; P:regulation of transcription involved in G1/S transition of mitotic cell cycle; IGI:SGD.
GO; GO:0000117; P:regulation of transcription involved in G2/M transition of mitotic cell cycle; IGI:SGD.
GO; GO:0001302; P:replicative cell aging; IMP:SGD.
GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IGI:SGD.
GO; GO:0061587; P:transfer RNA gene-mediated silencing; IMP:SGD.
Gene3D; 3.40.800.20; -; 1.
InterPro; IPR000286; His_deacetylse.
InterPro; IPR003084; His_deacetylse_1.
InterPro; IPR023801; His_deacetylse_dom.
InterPro; IPR037138; His_deacetylse_dom_sf.
InterPro; IPR023696; Ureohydrolase_domain.
PANTHER; PTHR10625; PTHR10625; 1.
Pfam; PF00850; Hist_deacetyl; 1.
PIRSF; PIRSF037913; His_deacetylse_1; 1.
PRINTS; PR01270; HDASUPER.
PRINTS; PR01271; HISDACETLASE.
SUPFAM; SSF52768; SSF52768; 1.
1: Evidence at protein level;
Chromatin regulator; Complete proteome; Cytoplasm; Hydrolase; Nucleus;
Phosphoprotein; Reference proteome; Repressor; Transcription;
Transcription regulation.
CHAIN 1 433 Histone deacetylase RPD3.
/FTId=PRO_0000114724.
REGION 19 331 Histone deacetylase.
MOTIF 320 340 ESA1-RPD3 motif.
ACT_SITE 151 151 {ECO:0000305}.
MOD_RES 394 394 Phosphothreonine.
{ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:18407956}.
MOD_RES 408 408 Phosphoserine.
{ECO:0000244|PubMed:18407956,
ECO:0000244|PubMed:19779198}.
MUTAGEN 150 150 H->A: Impairs histone deacetylase
activity and transcription repression.
{ECO:0000269|PubMed:9512514}.
MUTAGEN 151 151 H->A: Impairs histone deacetylase
activity and transcription repression.
{ECO:0000269|PubMed:9512514}.
MUTAGEN 188 188 H->A: Impairs histone deacetylase
activity and transcription repression.
{ECO:0000269|PubMed:9512514}.
MUTAGEN 322 322 W->A: Reduces strongly HDAC activity.
{ECO:0000269|PubMed:12110674}.
MUTAGEN 325 325 E->A: Reduces strongly HDAC activity.
{ECO:0000269|PubMed:12110674}.
MUTAGEN 327 327 G->A: Reduces strongly HDAC activity.
{ECO:0000269|PubMed:12110674}.
MUTAGEN 328 328 L->A: Reduces strongly HDAC activity.
{ECO:0000269|PubMed:12110674}.
MUTAGEN 329 329 L->A: Reduces strongly HDAC activity.
{ECO:0000269|PubMed:12110674}.
MUTAGEN 332 332 V->A: Reduces strongly HDAC activity.
{ECO:0000269|PubMed:12110674}.
MUTAGEN 334 334 L->A: Reduces strongly HDAC activity.
{ECO:0000269|PubMed:12110674}.
MUTAGEN 335 335 D->A: Reduces strongly HDAC activity.
{ECO:0000269|PubMed:12110674}.
MUTAGEN 338 338 L->A: Reduces strongly HDAC activity.
{ECO:0000269|PubMed:12110674}.
MUTAGEN 339 339 P->A: Reduces strongly HDAC activity.
{ECO:0000269|PubMed:12110674}.
SEQUENCE 433 AA; 48904 MW; 34FFD72A7E7425DB CRC64;
MVYEATPFDP ITVKPSDKRR VAYFYDADVG NYAYGAGHPM KPHRIRMAHS LIMNYGLYKK
MEIYRAKPAT KQEMCQFHTD EYIDFLSRVT PDNLEMFKRE SVKFNVGDDC PVFDGLYEYC
SISGGGSMEG AARLNRGKCD VAVNYAGGLH HAKKSEASGF CYLNDIVLGI IELLRYHPRV
LYIDIDVHHG DGVEEAFYTT DRVMTCSFHK YGEFFPGTGE LRDIGVGAGK NYAVNVPLRD
GIDDATYRSV FEPVIKKIME WYQPSAVVLQ CGGDSLSGDR LGCFNLSMEG HANCVNYVKS
FGIPMMVVGG GGYTMRNVAR TWCFETGLLN NVVLDKDLPY NEYYEYYGPD YKLSVRPSNM
FNVNTPEYLD KVMTNIFANL ENTKYAPSVQ LNHTPRDAED LGDVEEDSAE AKDTKGGSQY
ARDLHVEHDN EFY


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