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   27-MAR-2024, entry version 182.
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   PDB; 8GA8; EM; 3.50 A; H=1-327.
DR   PDB; 8HPO; EM; 2.60 A; D=1-327.
DR   PDBsum; 8GA8; -.
DR   PDBsum; 8HPO; -.
DR   AlphaFoldDB; P40505; -.
DR   EMDB; EMD-29892; -.
DR   EMDB; EMD-34935; -.
DR   SMR; P40505; -.
DR   BioGRID; 34908; 810.
DR   ComplexPortal; CPX-1852; RPD3L histone deacetylase complex.
DR   DIP; DIP-2706N; -.
DR   IntAct; P40505; 21.
DR   MINT; P40505; -.
DR   STRING; 4932.YIL084C; -.
DR   GlyGen; P40505; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P40505; -.
DR   MaxQB; P40505; -.
DR   PaxDb; 4932-YIL084C; -.
DR   PeptideAtlas; P40505; -.
DR   EnsemblFungi; YIL084C_mRNA; YIL084C; YIL084C.
DR   GeneID; 854725; -.
DR   KEGG; sce:YIL084C; -.
DR   AGR; SGD:S000001346; -.
DR   SGD; S000001346; SDS3.
DR   VEuPathDB; FungiDB:YIL084C; -.
DR   eggNOG; KOG4466; Eukaryota.
DR   HOGENOM; CLU_067595_1_0_1; -.
DR   InParanoid; P40505; -.
DR   OMA; VANAHSY; -.
DR   OrthoDB; 2724749at2759; -.
DR   BioCyc; YEAST:G3O-31346-MONOMER; -.
DR   Reactome; R-SCE-3214815; HDACs deacetylate histones.
DR   BioGRID-ORCS; 854725; 0 hits in 10 CRISPR screens.
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 formation; IMP:SGD.
DR   GO; GO:0061188; P:negative regulation of rDNA heterochromatin formation; IMP:SGD.
DR   GO; GO:0061186; P:negative regulation of silent mating-type cassette heterochromatin formation; IMP:SGD.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:SGD.
DR   GO; GO:0006334; P:nucleosome assembly; NAS:ComplexPortal.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; 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; NAS:ComplexPortal.
DR   InterPro; IPR013907; Sds3.
DR   PANTHER; PTHR21964; BREAST CANCER METASTASIS-SUPPRESSOR 1; 1.
DR   PANTHER; PTHR21964:SF39; TRANSCRIPTIONAL REGULATORY PROTEIN SDS3; 1.
DR   Pfam; PF08598; Sds3; 1.
DR   SMART; SM01401; Sds3; 1.
PE   1: Evidence at protein level;
KW   3D-structure; 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"
FT   HELIX           15..34
FT                   /evidence="ECO:0007829|PDB:8HPO"
FT   TURN            36..38
FT                   /evidence="ECO:0007829|PDB:8HPO"
FT   HELIX           41..54
FT                   /evidence="ECO:0007829|PDB:8HPO"
FT   HELIX           62..140
FT                   /evidence="ECO:0007829|PDB:8HPO"
FT   HELIX           301..315
FT                   /evidence="ECO:0007829|PDB:8HPO"
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
//