RSC3_YEAST
ID RSC3_YEAST Reviewed; 885 AA.
AC Q06639; D6VST2;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=Chromatin structure-remodeling complex protein RSC3;
DE AltName: Full=Remodel the structure of chromatin complex subunit 3;
GN Name=RSC3; OrderedLocusNames=YDR303C; ORFNames=D9740.13;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [2]
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 [3]
RP PROTEIN SEQUENCE OF 137-151, IDENTIFICATION IN THE RSC COMPLEX, FUNCTION OF
RP THE RSC COMPLEX, HETEROMERIC COMPLEX FORMATION WITH RSC30, AND MUTAGENESIS
RP OF CYS-14.
RX PubMed=11336698; DOI=10.1016/s1097-2765(01)00219-2;
RA Angus-Hill M.L., Schlichter A., Roberts D., Erdjument-Bromage H.,
RA Tempst P., Cairns B.R.;
RT "A Rsc3/Rsc30 zinc cluster dimer reveals novel roles for the chromatin
RT remodeler RSC in gene expression and cell cycle control.";
RL Mol. Cell 7:741-751(2001).
RN [4]
RP FUNCTION OF THE RSC COMPLEX, AND COMPOSITION OF THE RSC COMPLEX.
RX PubMed=8980231; DOI=10.1016/s0092-8674(00)81820-6;
RA Cairns B.R., Lorch Y., Li Y., Zhang M., Lacomis L., Erdjument-Bromage H.,
RA Tempst P., Du J., Laurent B.C., Kornberg R.D.;
RT "RSC, an essential, abundant chromatin-remodeling complex.";
RL Cell 87:1249-1260(1996).
RN [5]
RP FUNCTION OF THE RSC COMPLEX.
RX PubMed=10025404; DOI=10.1016/s0092-8674(00)80551-6;
RA Lorch Y., Zhang M., Kornberg R.D.;
RT "Histone octamer transfer by a chromatin-remodeling complex.";
RL Cell 96:389-392(1999).
RN [6]
RP FUNCTION OF THE RSC COMPLEX.
RX PubMed=10329629; DOI=10.1093/emboj/18.10.2836;
RA Moreira J.M.A., Holmberg S.;
RT "Transcriptional repression of the yeast CHA1 gene requires the chromatin-
RT remodeling complex RSC.";
RL EMBO J. 18:2836-2844(1999).
RN [7]
RP COMPOSITION OF THE RSC COMPLEX.
RX PubMed=10619019; DOI=10.1016/s1097-2765(00)80382-2;
RA Cairns B.R., Schlichter A., Erdjument-Bromage H., Tempst P., Kornberg R.D.,
RA Winston F.;
RT "Two functionally distinct forms of the RSC nucleosome-remodeling complex,
RT containing essential AT hook, BAH, and bromodomains.";
RL Mol. Cell 4:715-723(1999).
RN [8]
RP FUNCTION OF THE RSC COMPLEX.
RX PubMed=12183366; DOI=10.1101/gad.995002;
RA Saha A., Wittmeyer J., Cairns B.R.;
RT "Chromatin remodeling by RSC involves ATP-dependent DNA translocation.";
RL Genes Dev. 16:2120-2134(2002).
RN [9]
RP FUNCTION OF THE RSC COMPLEX.
RX PubMed=12072455; DOI=10.1093/genetics/161.2.575;
RA Chai B., Hsu J.-M., Du J., Laurent B.C.;
RT "Yeast RSC function is required for organization of the cellular
RT cytoskeleton via an alternative PKC1 pathway.";
RL Genetics 161:575-584(2002).
RN [10]
RP FUNCTION OF THE RSC COMPLEX, SUBCELLULAR LOCATION, AND INTERACTION OF THE
RP RSC COMPLEX WITH HISTONES.
RX PubMed=12697820; DOI=10.1128/mcb.23.9.3202-3215.2003;
RA Hsu J.-M., Huang J., Meluh P.B., Laurent B.C.;
RT "The yeast RSC chromatin-remodeling complex is required for kinetochore
RT function in chromosome segregation.";
RL Mol. Cell. Biol. 23:3202-3215(2003).
RN [11]
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 [12]
RP FUNCTION, AND INTERACTION WITH LDB7 AND NPL6.
RX PubMed=16204215; DOI=10.1534/genetics.105.047589;
RA Wilson B., Erdjument-Bromage H., Tempst P., Cairns B.R.;
RT "The RSC chromatin remodeling complex bears an essential fungal-specific
RT protein module with broad functional roles.";
RL Genetics 172:795-809(2006).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-236, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95 AND SER-236, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-236, AND IDENTIFICATION BY
RP 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).
CC -!- FUNCTION: Component of the chromatin structure-remodeling complex
CC (RSC), which is involved in transcription regulation and nucleosome
CC positioning. RSC is responsible for the transfer of a histone octamer
CC from a nucleosome core particle to naked DNA. The reaction requires ATP
CC and involves an activated RSC-nucleosome intermediate. Remodeling
CC reaction also involves DNA translocation, DNA twist and conformational
CC change. As a reconfigurer of centromeric and flanking nucleosomes, RSC
CC complex is required both for proper kinetochore function in chromosome
CC segregation and, via a PKC1-dependent signaling pathway, for
CC organization of the cellular cytoskeleton. This subunit is required for
CC transcription of ribosomal protein genes and genes involved in the
CC integrity of the cell wall, and also for proper metaphase progression.
CC Together with HTL1, LDB7, NPL6, RSC30 components, defines a fungal-
CC specific module within the RSC complex that plays a role in many
CC cellular functions including the maintenance of cell wall integrity.
CC {ECO:0000269|PubMed:10025404, ECO:0000269|PubMed:10329629,
CC ECO:0000269|PubMed:11336698, ECO:0000269|PubMed:12072455,
CC ECO:0000269|PubMed:12183366, ECO:0000269|PubMed:12697820,
CC ECO:0000269|PubMed:16204215, ECO:0000269|PubMed:8980231}.
CC -!- SUBUNIT: Forms a heteromer with RSC30. Interacts with LDB7 and NPL6.
CC Component of the two forms of the RSC complex composed of at least
CC either RSC1 or RSC2, and ARP7, ARP9, LDB7, NPL6, RSC3, RSC30, RSC4,
CC RSC58, RSC6, RSC8, RSC9, SFH1, STH1, HTL1 and probably RTT102. The
CC complexes interact with histone and histone variant components of
CC centromeric chromatin. Component of a fungal-specific module (HTL1-
CC LDB7-NPL6-RSC3-RSC30) within the RSC complex.
CC {ECO:0000269|PubMed:11336698, ECO:0000269|PubMed:12697820,
CC ECO:0000269|PubMed:16204215}.
CC -!- INTERACTION:
CC Q06639; P38781: RSC30; NbExp=5; IntAct=EBI-22058, EBI-24549;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00227,
CC ECO:0000269|PubMed:12697820}. Note=Localizes to centromeric and
CC flanking chromatin. Association with these loci is dependent on STH1.
CC -!- MISCELLANEOUS: Present with 1750 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; U28374; AAB64739.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12142.1; -; Genomic_DNA.
DR PIR; S61189; S61189.
DR RefSeq; NP_010589.3; NM_001180611.3.
DR PDB; 6K15; EM; 3.40 A; K=1-885.
DR PDB; 6KW3; EM; 7.13 A; K=1-885.
DR PDB; 6KW4; EM; 7.55 A; K=1-885.
DR PDB; 6KW5; EM; 10.13 A; K=1-885.
DR PDB; 6V8O; EM; 3.07 A; G=1-885.
DR PDB; 6V92; EM; 20.00 A; G=1-885.
DR PDBsum; 6K15; -.
DR PDBsum; 6KW3; -.
DR PDBsum; 6KW4; -.
DR PDBsum; 6KW5; -.
DR PDBsum; 6V8O; -.
DR PDBsum; 6V92; -.
DR AlphaFoldDB; Q06639; -.
DR SMR; Q06639; -.
DR BioGRID; 32355; 138.
DR ComplexPortal; CPX-1888; RSC chromatin remodelling complex, variant RSC2.
DR ComplexPortal; CPX-1889; RSC chromatin remodelling complex, variant RSC1.
DR DIP; DIP-5867N; -.
DR IntAct; Q06639; 70.
DR MINT; Q06639; -.
DR STRING; 4932.YDR303C; -.
DR iPTMnet; Q06639; -.
DR MaxQB; Q06639; -.
DR PaxDb; Q06639; -.
DR PRIDE; Q06639; -.
DR EnsemblFungi; YDR303C_mRNA; YDR303C; YDR303C.
DR GeneID; 851897; -.
DR KEGG; sce:YDR303C; -.
DR SGD; S000002711; RSC3.
DR VEuPathDB; FungiDB:YDR303C; -.
DR eggNOG; ENOG502QWTJ; Eukaryota.
DR GeneTree; ENSGT00940000176763; -.
DR HOGENOM; CLU_017671_0_0_1; -.
DR InParanoid; Q06639; -.
DR OMA; NYCWRHL; -.
DR BioCyc; YEAST:G3O-29863-MON; -.
DR PRO; PR:Q06639; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q06639; protein.
DR GO; GO:0000785; C:chromatin; IC:ComplexPortal.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0016586; C:RSC-type complex; IDA:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:InterPro.
DR GO; GO:0043565; F:sequence-specific DNA binding; HDA:SGD.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006338; P:chromatin remodeling; IDA:SGD.
DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IC:ComplexPortal.
DR GO; GO:0006337; P:nucleosome disassembly; IDA:SGD.
DR GO; GO:0033262; P:regulation of nuclear cell cycle DNA replication; IGI:SGD.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IDA:SGD.
DR CDD; cd00067; GAL4; 1.
DR Gene3D; 4.10.240.10; -; 1.
DR InterPro; IPR001138; Zn2-C6_fun-type_DNA-bd.
DR InterPro; IPR036864; Zn2-C6_fun-type_DNA-bd_sf.
DR Pfam; PF00172; Zn_clus; 1.
DR SMART; SM00066; GAL4; 1.
DR SUPFAM; SSF57701; SSF57701; 1.
DR PROSITE; PS00463; ZN2_CY6_FUNGAL_1; 1.
DR PROSITE; PS50048; ZN2_CY6_FUNGAL_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chromatin regulator; Direct protein sequencing; DNA-binding;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Zinc.
FT CHAIN 1..885
FT /note="Chromatin structure-remodeling complex protein RSC3"
FT /id="PRO_0000114973"
FT DNA_BIND 14..42
FT /note="Zn(2)-C6 fungal-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
FT MOD_RES 95
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 236
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MUTAGEN 14
FT /note="C->G: Complete inactivation."
FT /evidence="ECO:0000269|PubMed:11336698"
FT STRAND 157..160
FT /evidence="ECO:0007829|PDB:6V8O"
FT HELIX 174..195
FT /evidence="ECO:0007829|PDB:6V8O"
SQ SEQUENCE 885 AA; 101720 MW; 2DB1D529E2686A0A CRC64;
MDIRGRKMKK PPACVQCRKR KIGCDRVKPI CGNCMKHNKM DCFYPDVPGQ YVPSSSSSSN
TRQVANGPYL NSYYASRRVS KETAALLQKN PELASLEQIR EYNTRLQLLN AQNQLNNRSS
AANATLNQQH TQYIPKSVPS LESKPVTSAN ESSTPLNWVQ GPAIFHMLTS PYTQDEIINH
EMNFLKGRLL ELQEITGKKI TGVNLDLKQD SSAQMQSSHS NRNQEEFLTI KKRKLSEDGV
TDGDGKPIPE SERRPHLNEF KDLDPQFLDT NKVFNVFNSA ISEEGRNRLW LLPKNINKSS
IFQIQYLIER DPFLFKFFND LNILIETQFN GPLHDLVASR NSIERNSGIS QILKFPSQSI
TQTLINKYLS TITETNSILP ILKPKRLLPI VEQLFPSNTI NKPNSKDFET IFQVFSVTND
QLLNLGFITL CLLILFESLN STVLIPLRDD EHLQLFNVLF NYLPLLKSNL TTLRFEIEKR
SMCNIETLRF ISLWKYYQFV MDTSSSSSFV IDYDEDMHMA CLLSLNHETQ NQSHILTWNF
IFKNYCWRHL FLGQLPLLMS EPFTNSTPII DPLLNNDFEL IDFEVNLMKY LQSKDQQLSI
DKIIQLIKLL KNKNIEVSQG CLTTPSIINN IMDSLIYRNS MLYLNFYLLL QFETLKNYAK
FNEILEDFLE LSRETLFFVF SNLANIKFAG HEFTFINKSI VVLQTLVLML LALYQRSFDS
SKRTNDANEI SEQTDIHSNN DNSKRIKNKN VIHLIINKIA MLLSDYTKNC KKQNKLIENL
IIKIKTISKY IKNLEENKVT TSADSNYSIN NGFSGISAEQ LIKLNHELSK ISESLIKTDF
YEQRKNSTVS NGVLGAAAPV DSDANSDTFG LTKENFNEVF EAIRS
