GENTAUR Molecular Products.

 RPD3_YEAST              Reviewed;         433 AA.
 P32561; D6W0L7;
 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
 01-OCT-1993, sequence version 1.
 18-JUL-2018, entry version 184.
 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;
     Q08923:CTI6; NbExp=9; IntAct=EBI-15864, EBI-33349;
     P14922:CYC8; NbExp=6; IntAct=EBI-15864, EBI-18215;
     Q12432:EAF3; NbExp=11; IntAct=EBI-15864, EBI-6281;
     Q03214:ECM5; NbExp=5; IntAct=EBI-15864, EBI-27382;
     Q02784:GRX5; NbExp=3; IntAct=EBI-15864, EBI-29427;
     Q03213:HOT1; NbExp=3; IntAct=EBI-15864, EBI-27376;
     P47018:MTC1; NbExp=8; IntAct=EBI-15864, EBI-26065;
     P50947:PHO23; NbExp=9; IntAct=EBI-15864, EBI-28808;
     Q04779:RCO1; NbExp=12; IntAct=EBI-15864, EBI-28153;
     P38255:RXT2; NbExp=11; IntAct=EBI-15864, EBI-21537;
     P38429:SAP30; NbExp=7; IntAct=EBI-15864, EBI-27570;
     P40505:SDS3; NbExp=4; IntAct=EBI-15864, EBI-16809;
     P22579:SIN3; NbExp=27; IntAct=EBI-15864, EBI-17160;
     P16649:TUP1; NbExp=2; IntAct=EBI-15864, EBI-19654;
     Q03010:UME1; NbExp=10; IntAct=EBI-15864, EBI-20070;
 -!- 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; 1032.
 ComplexPortal; CPX-1372; SNT2C histone deacetylase complex.
 ComplexPortal; CPX-1851; Rpd3S histone deacetylase complex.
 ComplexPortal; CPX-1852; RPD3L histone deacetylase complex.
 DIP; DIP-681N; -.
 IntAct; P32561; 90.
 MINT; P32561; -.
 STRING; 4932.YNL330C; -.
 iPTMnet; P32561; -.
 MaxQB; P32561; -.
 PaxDb; P32561; -.
 PRIDE; P32561; -.
 EnsemblFungi; YNL330C; YNL330C; YNL330C.
 GeneID; 855386; -.
 KEGG; sce:YNL330C; -.
 EuPathDB; FungiDB:YNL330C; -.
 SGD; S000005274; RPD3.
 GeneTree; ENSGT00910000144047; -.
 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 by RNA polymerase I; IMP:SGD.
 GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; 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 by RNA polymerase II; 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_dom_sf.
 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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