RSC30_YEAST
ID RSC30_YEAST Reviewed; 883 AA.
AC P38781; D3DL05;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Chromatin structure-remodeling complex protein RSC30;
DE AltName: Full=Remodel the structure of chromatin complex subunit 30;
GN Name=RSC30; OrderedLocusNames=YHR056C;
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=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
RN [2]
RP SEQUENCE REVISION TO N-TERMINUS.
RA Fisk D., Cherry J.M.;
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
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 PROTEIN SEQUENCE OF 28-37, IDENTIFICATION IN THE RSC COMPLEX, FUNCTION OF
RP THE RSC COMPLEX, HETEROMERIC COMPLEX FORMATION WITH RSC3, AND MUTAGENESIS
RP OF CYS-15.
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 [5]
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 [6]
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 [7]
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 [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 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 [12]
RP FUNCTION, AND INTERACTION WITH 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 IDENTIFICATION BY 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 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-150, 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).
RN [16]
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 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. Together with HTL1, LDB7, NPL6, RSC3
CC components, defines a fungal-specific module within the RSC complex
CC that plays a role in many cellular functions including the maintenance
CC of cell wall integrity. {ECO:0000269|PubMed:10025404,
CC ECO:0000269|PubMed:10329629, ECO:0000269|PubMed:11336698,
CC ECO:0000269|PubMed:12072455, ECO:0000269|PubMed:12183366,
CC ECO:0000269|PubMed:12697820, ECO:0000269|PubMed:16204215,
CC ECO:0000269|PubMed:8980231}.
CC -!- SUBUNIT: Forms a heteromer with RSC3. Interacts with NPL6. Component of
CC the two forms of the RSC complex composed of at least either RSC1 or
CC RSC2, and ARP7, ARP9, LDB7, NPL6, RSC3, RSC30, RSC4, RSC58, RSC6, RSC8,
CC RSC9, SFH1, STH1, HTL1 and probably RTT102. The complexes interact with
CC histone and histone variant components of centromeric chromatin.
CC Component of a fungal-specific module (HTL1-LDB7-NPL6-RSC3-RSC30)
CC within the RSC complex. {ECO:0000269|PubMed:11336698,
CC ECO:0000269|PubMed:12697820, ECO:0000269|PubMed:16204215}.
CC -!- INTERACTION:
CC P38781; Q06639: RSC3; NbExp=5; IntAct=EBI-24549, EBI-22058;
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.
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DR EMBL; U00061; AAB68385.2; -; Genomic_DNA.
DR EMBL; BK006934; DAA06749.1; -; Genomic_DNA.
DR RefSeq; NP_011923.2; NM_001179186.2.
DR PDB; 6K15; EM; 3.40 A; C=1-883.
DR PDB; 6KW3; EM; 7.13 A; C=1-883.
DR PDB; 6KW4; EM; 7.55 A; C=1-883.
DR PDB; 6KW5; EM; 10.13 A; C=1-883.
DR PDB; 6V8O; EM; 3.07 A; S=1-883.
DR PDB; 6V92; EM; 20.00 A; S=1-883.
DR PDBsum; 6K15; -.
DR PDBsum; 6KW3; -.
DR PDBsum; 6KW4; -.
DR PDBsum; 6KW5; -.
DR PDBsum; 6V8O; -.
DR PDBsum; 6V92; -.
DR AlphaFoldDB; P38781; -.
DR SMR; P38781; -.
DR BioGRID; 36488; 42.
DR ComplexPortal; CPX-1888; RSC chromatin remodelling complex, variant RSC2.
DR ComplexPortal; CPX-1889; RSC chromatin remodelling complex, variant RSC1.
DR DIP; DIP-4275N; -.
DR IntAct; P38781; 27.
DR STRING; 4932.YHR056C; -.
DR iPTMnet; P38781; -.
DR MaxQB; P38781; -.
DR PaxDb; P38781; -.
DR PRIDE; P38781; -.
DR TopDownProteomics; P38781; -.
DR EnsemblFungi; YHR056C_mRNA; YHR056C; YHR056C.
DR GeneID; 856453; -.
DR KEGG; sce:YHR056C; -.
DR SGD; S000001098; RSC30.
DR VEuPathDB; FungiDB:YHR056C; -.
DR eggNOG; ENOG502QWTJ; Eukaryota.
DR GeneTree; ENSGT00940000176763; -.
DR HOGENOM; CLU_017671_0_0_1; -.
DR OMA; DICHINQ; -.
DR BioCyc; YEAST:G3O-31110-MON; -.
DR PRO; PR:P38781; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P38781; protein.
DR GO; GO:0000785; C:chromatin; IC:ComplexPortal.
DR GO; GO:0016586; C:RSC-type complex; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006338; P:chromatin remodeling; IC:ComplexPortal.
DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IDA:SGD.
DR GO; GO:0006337; P:nucleosome disassembly; IDA:SGD.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:SGD.
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..883
FT /note="Chromatin structure-remodeling complex protein
FT RSC30"
FT /id="PRO_0000114974"
FT DNA_BIND 14..45
FT /note="Zn(2)-C6 fungal-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
FT REGION 121..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 241..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..153
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..267
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 150
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MUTAGEN 15
FT /note="C->G: Complete inactivation."
FT /evidence="ECO:0000269|PubMed:11336698"
FT STRAND 198..203
FT /evidence="ECO:0007829|PDB:6V8O"
FT HELIX 205..226
FT /evidence="ECO:0007829|PDB:6V8O"
SQ SEQUENCE 883 AA; 101335 MW; E8542445950FAA93 CRC64;
MMDMQVRKVR KPPACTQCRK RKIGCDRAKP ICGNCVKYNK PDCFYPDGPG KMVAVPSASG
MSTHGNGQGS NHFSQGNGVN QKNVMIQTQY PIMQTSIEAF NFSFNPSVDT AMQWTKAASY
QNNNTNNNTA PRQNSSTVSS NVHGNTIVRS DSPDVPSMDQ IREYNTRLQL VNAQSFDYTD
NPYSFNVGIN QDSAVFDLMT SPFTQEEVLI KEIDFLKNKL LDLQSLQLKS LKEKSNLNAD
NTTANKINKT GENSKKGKVD GKRAGFDHQT SRTSQSSQKY FTALTITDVQ SLVQVKPLKD
TPNYLFTKNF IIFRDHYLFK FYNILHDICH INQFKVSPPN NKNHQQYMEV CKVNFPPKAI
IIETLNSESL NNLNIEEFLP IFDKTLLLEF VHNSFPNGDT CPSFSTVDLP LSQLTKLGEL
TVLLLLLNDS MTLFNKQAIN NHVSALMNNL RLIRSQITLI NLEYYDQETI KFIAITKFYE
SLYMHDDHKS SLDEDLSCLL SFQIKDFKLF HFLKKMYYSR HSLLGQSSFM VPAAENLSPI
PASIDTNDIP LIANDLKLLE TQAKLINILQ GVPFYLPVNL TKIESLLETL TMGVSNTVDL
YFHDNEVRKE WKDTLNFINT IVYTNFFLFV QNESSLSMAV QHSSNNNKTS NSERCAKDLM
KIISNMHIFY SITFNFIFPI KSIKSFSSGN NRFHSNGKEF LFANHFIEIL QNFIAITFAI
FQRCEVILYD EFYKNLSNEE INVQLLLIHD KILEILKKIE IIVSFLRDEM NSNGSFKSIK
GFNKVLNLIK YMLRFSKKKQ NFARNSDNNN VTDYSQSAKN KNVLLKFPVS ELNRIYLKFK
EISDFLMERE VVQRSIIIDK DLESDNLGIT TANFNDFYDA FYN
