SDS3_YEAST
ID SDS3_YEAST Reviewed; 327 AA.
AC P40505; D6VVK2;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Transcriptional regulatory protein SDS3;
DE AltName: Full=Suppressor of defective silencing protein 3;
GN Name=SDS3; OrderedLocusNames=YIL084C;
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.
RC STRAIN=ATCC 200060 / W303;
RX PubMed=8978024; DOI=10.1093/genetics/144.4.1343;
RA Vannier D., Balderes D., Shore D.;
RT "Evidence that the transcriptional regulators SIN3 and RPD3, and a novel
RT gene (SDS3) with similar functions, are involved in transcriptional
RT silencing in S. cerevisiae.";
RL Genetics 144:1343-1353(1996).
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 FUNCTION, AND IDENTIFICATION IN THE RPD3 COMPLEX.
RX PubMed=10655212; DOI=10.1093/genetics/154.2.573;
RA Dorland S., Deegenaars M.L., Stillman D.J.;
RT "Roles for the Saccharomyces cerevisiae SDS3, CBK1 and HYM1 genes in
RT transcriptional repression by SIN3.";
RL Genetics 154:573-586(2000).
RN [6]
RP FUNCTION, AND IDENTIFICATION IN THE RPD3 COMPLEX.
RX PubMed=11024051; DOI=10.1074/jbc.m005730200;
RA Lechner T., Carrozza M.J., Yu Y., Grant P.A., Eberharter A., Vannier D.,
RA Brosch G., Stillman D.J., Shore D., Workman J.L.;
RT "Sds3 (suppressor of defective silencing 3) is an integral component of the
RT yeast Sin3[middle dot]Rpd3 histone deacetylase complex and is required for
RT histone deacetylase activity.";
RL J. Biol. Chem. 275:40961-40966(2000).
RN [7]
RP FUNCTION.
RX PubMed=11405640; DOI=10.1007/s004380100447;
RA Vannier D., Damay P., Shore D.;
RT "A role for Sds3p, a component of the Rpd3p/Sin3p deacetylase complex, in
RT maintaining cellular integrity in Saccharomyces cerevisiae.";
RL Mol. Genet. Genomics 265:560-568(2001).
RN [8]
RP IDENTIFICATION IN THE RPD3 COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=12672825; DOI=10.1074/jbc.c300036200;
RA Nourani A., Howe L., Pray-Grant M.G., Workman J.L., Grant P.A., Cote J.;
RT "Opposite role of yeast ING family members in p53-dependent transcriptional
RT activation.";
RL J. Biol. Chem. 278:19171-19175(2003).
RN [9]
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 [10]
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 [11]
RP IDENTIFICATION IN THE RPD3C(L) COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=16314178; DOI=10.1016/j.bbaexp.2005.09.005;
RA Carrozza M.J., Florens L., Swanson S.K., Shia W.-J., Anderson S., Yates J.,
RA Washburn M.P., Workman J.L.;
RT "Stable incorporation of sequence specific repressors Ash1 and Ume6 into
RT the Rpd3L complex.";
RL Biochim. Biophys. Acta 1731:77-87(2005).
RN [12]
RP IDENTIFICATION IN THE RPD3C(L) COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=16286008; DOI=10.1016/j.cell.2005.10.025;
RA Keogh M.-C., Kurdistani S.K., Morris S.A., Ahn S.H., Podolny V.,
RA Collins S.R., Schuldiner M., Chin K., Punna T., Thompson N.J., Boone C.,
RA Emili A., Weissman J.S., Hughes T.R., Strahl B.D., Grunstein M.,
RA Greenblatt J.F., Buratowski S., Krogan N.J.;
RT "Cotranscriptional set2 methylation of histone H3 lysine 36 recruits a
RT repressive Rpd3 complex.";
RL Cell 123:593-605(2005).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-166 AND SER-211, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Component of the RPD3C(L) histone deacetylase complex (HDAC)
CC responsible for the deacetylation of lysine residues on the N-terminal
CC part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation
CC gives a tag for epigenetic repression and plays an important role in
CC transcriptional regulation, cell cycle progression and developmental
CC events. SDS3 is required for the HDAC activity of the complex and for
CC the RPD3-SIN3 association. {ECO:0000269|PubMed:10655212,
CC ECO:0000269|PubMed:11024051, ECO:0000269|PubMed:11405640,
CC ECO:0000269|PubMed:8978024}.
CC -!- SUBUNIT: Component of the RPD3C(L) complex composed of at least ASH1,
CC CTI6, DEP1, PHO23, RPD3, RXT2, RXT3, SAP30, SDS3, SIN3, UME1 and UME6.
CC {ECO:0000269|PubMed:10655212, ECO:0000269|PubMed:11024051,
CC ECO:0000269|PubMed:12672825, ECO:0000269|PubMed:16286008,
CC ECO:0000269|PubMed:16314178}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 105 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SDS3 family. {ECO:0000305}.
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DR EMBL; U62525; AAB40993.1; -; Genomic_DNA.
DR EMBL; Z46728; CAA86710.1; -; Genomic_DNA.
DR EMBL; AY692879; AAT92898.1; -; Genomic_DNA.
DR EMBL; BK006942; DAA08468.1; -; Genomic_DNA.
DR PIR; S49796; S49796.
DR RefSeq; NP_012182.1; NM_001179432.1.
DR AlphaFoldDB; P40505; -.
DR SMR; P40505; -.
DR BioGRID; 34908; 803.
DR ComplexPortal; CPX-1852; RPD3L histone deacetylase complex.
DR DIP; DIP-2706N; -.
DR IntAct; P40505; 21.
DR MINT; P40505; -.
DR STRING; 4932.YIL084C; -.
DR iPTMnet; P40505; -.
DR MaxQB; P40505; -.
DR PaxDb; P40505; -.
DR PRIDE; P40505; -.
DR EnsemblFungi; YIL084C_mRNA; YIL084C; YIL084C.
DR GeneID; 854725; -.
DR KEGG; sce:YIL084C; -.
DR SGD; S000001346; SDS3.
DR VEuPathDB; FungiDB:YIL084C; -.
DR eggNOG; KOG4466; Eukaryota.
DR HOGENOM; CLU_067595_1_0_1; -.
DR InParanoid; P40505; -.
DR OMA; CKEKLYE; -.
DR BioCyc; YEAST:G3O-31346-MON; -.
DR Reactome; R-SCE-3214815; HDACs deacetylate histones.
DR PRO; PR:P40505; -.
DR Proteomes; UP000002311; Chromosome IX.
DR RNAct; P40505; protein.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0033698; C:Rpd3L complex; IDA:SGD.
DR GO; GO:0070210; C:Rpd3L-Expanded complex; HDA:SGD.
DR GO; GO:0070822; C:Sin3-type complex; IBA:GO_Central.
DR GO; GO:0042826; F:histone deacetylase binding; IBA:GO_Central.
DR GO; GO:0043709; P:cell adhesion involved in single-species biofilm formation; IMP:SGD.
DR GO; GO:0031507; P:heterochromatin assembly; IMP:SGD.
DR GO; GO:0016575; P:histone deacetylation; IMP:SGD.
DR GO; GO:0061188; P:negative regulation of ribosomal DNA heterochromatin assembly; IMP:SGD.
DR GO; GO:0061186; P:negative regulation of silent mating-type cassette heterochromatin assembly; IMP:SGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:0006334; P:nucleosome assembly; IC:ComplexPortal.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:0061408; P:positive regulation of transcription from RNA polymerase II promoter in response to heat stress; IMP:SGD.
DR GO; GO:2000217; P:regulation of invasive growth in response to glucose limitation; IMP:SGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IC:ComplexPortal.
DR InterPro; IPR013907; Sds3.
DR PANTHER; PTHR21964; PTHR21964; 1.
DR Pfam; PF08598; Sds3; 1.
DR SMART; SM01401; Sds3; 1.
PE 1: Evidence at protein level;
KW Chromatin regulator; Coiled coil; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; Transcription; Transcription regulation.
FT CHAIN 1..327
FT /note="Transcriptional regulatory protein SDS3"
FT /id="PRO_0000097654"
FT REGION 151..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 268..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 61..135
FT /evidence="ECO:0000255"
FT COMPBIAS 151..186
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..240
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 166
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 211
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 327 AA; 37625 MW; 4A6186E68BFE0CC7 CRC64;
MAIQKVSNKD LSRKDKRRFN IESKVNKIYQ NFYSERDNQY KDRLTALQTD LTSLHQGDNG
QYARQVRDLE EERDLELVRL RLFEEYRVSR SGIEFQEDIE KAKAEHEKLI KLCKERLYSS
IEQKIKKLQE ERLLMDVANV HSYAMNYSRP QYQKNTRSHT VSGWDSSSNE YGRDTANESA
TDTGAGNDRR TLRRRNASKD TRGNNNNQDE SDFQTGNGSG SNGHGSRQGS QFPHFNNLTY
KSGMNSDSDF LQGINEGTDL YAFLFGEKNP KDNANGNEKK KNRGAQRYST KTAPPLQSLK
PDEVTEDISL IRELTGQPPA PFRLRSD
