LDB7_YEAST
ID LDB7_YEAST Reviewed; 180 AA.
AC P38210; D6VPZ4;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Chromatin structure-remodeling complex protein RSC14;
DE AltName: Full=Low dye-binding protein 7;
DE AltName: Full=Remodel the structure of chromatin complex subunit 14;
GN Name=LDB7; Synonyms=RSC14; OrderedLocusNames=YBL006C; ORFNames=YBL0322;
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].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=1441753; DOI=10.1002/yea.320080909;
RA Delaveau T., Jacq C., Perea J.;
RT "Sequence of a 12.7 kb segment of yeast chromosome II identifies a PDR-like
RT gene and several new open reading frames.";
RL Yeast 8:761-768(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
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 IDENTIFICATION OF FRAMESHIFT.
RX PubMed=12748633; DOI=10.1038/nature01644;
RA Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.;
RT "Sequencing and comparison of yeast species to identify genes and
RT regulatory elements.";
RL Nature 423:241-254(2003).
RN [5]
RP FUNCTION.
RX PubMed=14587103; DOI=10.1002/yea.1032;
RA Conde R., Pablo G., Cueva R., Larriba G.;
RT "Screening for new yeast mutants affected in mannosylphosphorylation of
RT cell wall mannoproteins.";
RL Yeast 20:1189-1211(2003).
RN [6]
RP FUNCTION, IDENTIFICATION IN THE RSC COMPLEX, AND INTERACTION WITH ARP9;
RP RSC3 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).
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, NPL6,
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. May be involved in the transfer of
CC mannosylphosphate (MP) groups into N-linked oligosaccharides.
CC {ECO:0000269|PubMed:14587103, ECO:0000269|PubMed:16204215}.
CC -!- SUBUNIT: Interacts with STH1, RSC3 and ARP9. Component of the two forms
CC of the RSC complex composed of at least either RSC1 or RSC2, and ARP7,
CC ARP9, LDB7, NPL6, RSC3, RSC30, RSC4, RSC58, RSC6, RSC8, RSC9, SFH1,
CC STH1, HTL1 and probably RTT102. The complexes interact with histone and
CC histone variant components of centromeric chromatin. Component of a
CC fungal-specific module (HTL1-LDB7-NPL6-RSC3-RSC30) within the RSC
CC complex. {ECO:0000269|PubMed:16204215}.
CC -!- INTERACTION:
CC P38210; P32597: STH1; NbExp=2; IntAct=EBI-21189, EBI-18410;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB23992.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA84825.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; S47695; AAB23992.1; ALT_FRAME; Genomic_DNA.
DR EMBL; Z35767; CAA84825.1; ALT_FRAME; Genomic_DNA.
DR EMBL; BK006936; DAA07114.1; -; Genomic_DNA.
DR PIR; S41221; S41221.
DR RefSeq; NP_009547.2; NM_001178246.1.
DR PDB; 6V8O; EM; 3.07 A; D=1-180.
DR PDB; 6V92; EM; 20.00 A; D=1-180.
DR PDBsum; 6V8O; -.
DR PDBsum; 6V92; -.
DR AlphaFoldDB; P38210; -.
DR SMR; P38210; -.
DR BioGRID; 32693; 156.
DR ComplexPortal; CPX-1888; RSC chromatin remodelling complex, variant RSC2.
DR ComplexPortal; CPX-1889; RSC chromatin remodelling complex, variant RSC1.
DR DIP; DIP-3927N; -.
DR IntAct; P38210; 6.
DR STRING; 4932.YBL006C; -.
DR iPTMnet; P38210; -.
DR MaxQB; P38210; -.
DR PaxDb; P38210; -.
DR PRIDE; P38210; -.
DR EnsemblFungi; YBL006C_mRNA; YBL006C; YBL006C.
DR GeneID; 852277; -.
DR KEGG; sce:YBL006C; -.
DR SGD; S000000102; LDB7.
DR VEuPathDB; FungiDB:YBL006C; -.
DR eggNOG; ENOG502S2JC; Eukaryota.
DR HOGENOM; CLU_1366073_0_0_1; -.
DR InParanoid; P38210; -.
DR OMA; STDFAHY; -.
DR BioCyc; YEAST:G3O-28912-MON; -.
DR PRO; PR:P38210; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38210; protein.
DR GO; GO:0000785; C:chromatin; IC:ComplexPortal.
DR GO; GO:0016586; C:RSC-type complex; IDA:UniProtKB.
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; IPR013895; Rsc14.
DR Pfam; PF08586; Rsc14; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chromatin regulator; Nucleus; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..180
FT /note="Chromatin structure-remodeling complex protein
FT RSC14"
FT /id="PRO_0000076230"
FT HELIX 8..17
FT /evidence="ECO:0007829|PDB:6V8O"
FT HELIX 28..34
FT /evidence="ECO:0007829|PDB:6V8O"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:6V8O"
FT HELIX 73..78
FT /evidence="ECO:0007829|PDB:6V8O"
FT STRAND 85..88
FT /evidence="ECO:0007829|PDB:6V8O"
FT HELIX 94..98
FT /evidence="ECO:0007829|PDB:6V8O"
FT HELIX 102..112
FT /evidence="ECO:0007829|PDB:6V8O"
FT HELIX 116..124
FT /evidence="ECO:0007829|PDB:6V8O"
SQ SEQUENCE 180 AA; 19792 MW; 9A4F882DB7AA1EC9 CRC64;
MSGSNMGYYD VLAGLSALEK SSQVVFSATE LQQLTQQSHA TDKGIEGSEN SKAKVSKPKR
VAVHGYLGGK VSLADAAQVE YEVGHSLLGS YVPRQQLEAL SSVDFSHHFH RTLECKAALE
THDVFLAGAG QLSLPFQSHI ESPRNSEAKR KRKVIICKRC QSRFIGSHRR SQLREHACVD
