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   27-MAR-2024, entry version 186.
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;
GN   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   EMDB; EMD-0777; -.
DR   EMDB; EMD-0778; -.
DR   EMDB; EMD-0779; -.
DR   EMDB; EMD-10465; -.
DR   EMDB; EMD-21107; -.
DR   EMDB; EMD-21114; -.
DR   EMDB; EMD-9905; -.
DR   SMR; P32832; -.
DR   BioGRID; 35266; 166.
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; 4932-YMR091C; -.
DR   PeptideAtlas; P32832; -.
DR   EnsemblFungi; YMR091C_mRNA; YMR091C; YMR091C.
DR   GeneID; 855116; -.
DR   KEGG; sce:YMR091C; -.
DR   AGR; SGD:S000004697; -.
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   OrthoDB; 2787924at2759; -.
DR   BioCyc; YEAST:G3O-32791-MONOMER; -.
DR   BioGRID-ORCS; 855116; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P32832; -.
DR   Proteomes; UP000002311; Chromosome XIII.
DR   RNAct; P32832; Protein.
DR   GO; GO:0000785; C:chromatin; NAS:ComplexPortal.
DR   GO; GO:0005634; C:nucleus; HDA:SGD.
DR   GO; GO:0016586; C:RSC-type complex; IDA:SGD.
DR   GO; GO:0031490; F:chromatin DNA binding; IBA:GO_Central.
DR   GO; GO:0006338; P:chromatin remodeling; IDA:SGD.
DR   GO; GO:0006337; P:nucleosome disassembly; IDA:SGD.
DR   GO; GO:0006368; P:transcription elongation by RNA polymerase II; IDA:SGD.
DR   InterPro; IPR013933; CRC_Rsc7/Swp82.
DR   PANTHER; PTHR22597:SF3; CHROMATIN STRUCTURE-REMODELING COMPLEX SUBUNIT RSC7; 1.
DR   PANTHER; PTHR22597; POLYCOMB GROUP PROTEIN; 1.
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
//