RSC7_YEAST
ID RSC7_YEAST Reviewed; 435 AA.
AC P32832; D6VZR4;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Chromatin structure-remodeling complex subunit RSC7;
DE AltName: Full=Nuclear protein localization protein 6;
DE AltName: Full=Remodel the structure of chromatin complex subunit 7;
GN Name=NPL6; Synonyms=RSC7; OrderedLocusNames=YMR091C; ORFNames=YM9582.16C;
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].
RA Chiang A.N., Silver P.A.;
RT "An acidic protein important for nuclear protein localization.";
RL Submitted (AUG-1992) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(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 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 [5]
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 [6]
RP FUNCTION, IDENTIFICATION IN THE RSC COMPLEX, AND INTERACTION WITH ARP7;
RP ARP9; RSC3; RSC8; RSC30 AND STH1.
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 [7]
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86, AND IDENTIFICATION BY
RP 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 [9]
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. Together with HTL1, LDB7,
CC RSC3, RSC30 components, defines a fungal-specific module within the RSC
CC complex that plays a role in many cellular functions including the
CC maintenance of cell wall integrity. Acidic protein important for
CC nuclear protein localization. {ECO:0000269|PubMed:16204215}.
CC -!- SUBUNIT: Interacts with ARP7, ARP9, RSC3, RSC8, RSC30 and STH1.
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:16204215}.
CC -!- INTERACTION:
CC P32832; P02829: HSP82; NbExp=2; IntAct=EBI-12202, EBI-8659;
CC P32832; P43609: RSC8; NbExp=7; IntAct=EBI-12202, EBI-23005;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 3510 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the RSC7/SWP82 family. RSC7 subfamily.
CC {ECO:0000305}.
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DR EMBL; M98434; AAA34817.1; -; Genomic_DNA.
DR EMBL; Z49259; CAA89238.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09988.1; -; Genomic_DNA.
DR PIR; S30792; S30792.
DR RefSeq; NP_013809.1; NM_001182591.1.
DR PDB; 6K15; EM; 3.40 A; F=1-435.
DR PDB; 6KW3; EM; 7.13 A; F=1-435.
DR PDB; 6KW4; EM; 7.55 A; F=1-435.
DR PDB; 6KW5; EM; 10.13 A; F=1-435.
DR PDB; 6TDA; EM; 15.00 A; M=1-435.
DR PDB; 6V8O; EM; 3.07 A; E=1-435.
DR PDB; 6V92; EM; 20.00 A; E=1-435.
DR PDBsum; 6K15; -.
DR PDBsum; 6KW3; -.
DR PDBsum; 6KW4; -.
DR PDBsum; 6KW5; -.
DR PDBsum; 6TDA; -.
DR PDBsum; 6V8O; -.
DR PDBsum; 6V92; -.
DR AlphaFoldDB; P32832; -.
DR SMR; P32832; -.
DR BioGRID; 35266; 148.
DR ComplexPortal; CPX-1888; RSC chromatin remodelling complex, variant RSC2.
DR ComplexPortal; CPX-1889; RSC chromatin remodelling complex, variant RSC1.
DR DIP; DIP-1477N; -.
DR IntAct; P32832; 62.
DR MINT; P32832; -.
DR STRING; 4932.YMR091C; -.
DR iPTMnet; P32832; -.
DR MaxQB; P32832; -.
DR PaxDb; P32832; -.
DR PRIDE; P32832; -.
DR EnsemblFungi; YMR091C_mRNA; YMR091C; YMR091C.
DR GeneID; 855116; -.
DR KEGG; sce:YMR091C; -.
DR SGD; S000004697; NPL6.
DR VEuPathDB; FungiDB:YMR091C; -.
DR eggNOG; ENOG502QW07; Eukaryota.
DR GeneTree; ENSGT00390000012364; -.
DR HOGENOM; CLU_022149_1_0_1; -.
DR InParanoid; P32832; -.
DR OMA; STNWLYQ; -.
DR BioCyc; YEAST:G3O-32791-MON; -.
DR PRO; PR:P32832; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P32832; 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:SGD.
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:0006368; P:transcription elongation from RNA polymerase II promoter; IDA:SGD.
DR InterPro; IPR013933; CRC_Rsc7/Swp82.
DR Pfam; PF08624; CRC_subunit; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chromatin regulator; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..435
FT /note="Chromatin structure-remodeling complex subunit RSC7"
FT /id="PRO_0000057945"
FT REGION 1..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 248..435
FT /note="Functional region; able to complement all NPL6 null
FT allele phenotypes"
FT COMPBIAS 32..65
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..94
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 86
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT HELIX 319..342
FT /evidence="ECO:0007829|PDB:6V8O"
FT TURN 343..345
FT /evidence="ECO:0007829|PDB:6V8O"
FT STRAND 346..351
FT /evidence="ECO:0007829|PDB:6V8O"
FT TURN 352..355
FT /evidence="ECO:0007829|PDB:6V8O"
FT STRAND 356..360
FT /evidence="ECO:0007829|PDB:6V8O"
FT TURN 361..363
FT /evidence="ECO:0007829|PDB:6V8O"
FT STRAND 368..373
FT /evidence="ECO:0007829|PDB:6V8O"
FT STRAND 377..380
FT /evidence="ECO:0007829|PDB:6K15"
FT STRAND 384..391
FT /evidence="ECO:0007829|PDB:6V8O"
FT TURN 393..396
FT /evidence="ECO:0007829|PDB:6V8O"
FT HELIX 401..403
FT /evidence="ECO:0007829|PDB:6V8O"
FT HELIX 407..410
FT /evidence="ECO:0007829|PDB:6V8O"
FT HELIX 416..432
FT /evidence="ECO:0007829|PDB:6V8O"
SQ SEQUENCE 435 AA; 49651 MW; 57B416BFB340422B CRC64;
MSDSEGGLAS EVEHEKRSRS TSNRPNYAID TEDLDIDEND ENEDDDYREE EANEGVNEEE
ISDEEEQINK SGRNKRRHVD EEEDLSEDKG VTRSRNRSKF KKPVFPGIDD AEENLNPLKV
VNEEYVLPDD PEGETKITAD GDLLGGREFL VRTFTLTEKG NRKFMLATEP ARIVGFRDSY
LFFQTHPNLY KFILNQTQKN DLIDRGVLPY SYRNRQIALV TARGVFKEFG AKIIRGGKHI
TDDYYASELR TKGNVIEGKL AGDPIDKSAR ALETMMYPAS ENGINPAKNQ VEFFEHRPHG
HMSNSNIIAS GSKLSSTNWL YQHSAACSRF NSDLFYDRVK VLLVDQQGLR DAYTNILHIP
ESTQSTTVLG WRRSKNDSPS DTSIVYETVI HDNDLNKPKT GLSEIPKEIY EDVVDEDVLR
AITEQQNFEK CNEYI
