ARP9_YEAST
ID ARP9_YEAST Reviewed; 467 AA.
AC Q05123; D6VZK8;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Actin-like protein ARP9;
DE AltName: Full=Chromatin structure-remodeling complex protein ARP9;
DE AltName: Full=SWI/SNF complex component ARP9;
GN Name=ARP9; Synonyms=SWP59; OrderedLocusNames=YMR033W; ORFNames=YM9973.07;
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=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 [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 16-37 AND 459-467, FUNCTION, AND IDENTIFICATION IN THE
RP RSC AND SWI/SNF COMPLEXES.
RX PubMed=9844636; DOI=10.1016/s1097-2765(00)80162-8;
RA Cairns B.R., Erdjument-Bromage H., Tempst P., Winston F., Kornberg R.D.;
RT "Two actin-related proteins are shared functional components of the
RT chromatin-remodeling complexes RSC and SWI/SNF.";
RL Mol. Cell 2:639-651(1998).
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 GENE NAME.
RX PubMed=9290209;
RX DOI=10.1002/(sici)1097-0061(19970915)13:11<1053::aid-yea164>3.0.co;2-4;
RA Poch O., Winsor B.;
RT "Who's who among the Saccharomyces cerevisiae actin-related proteins? A
RT classification and nomenclature proposal for a large family.";
RL Yeast 13:1053-1058(1997).
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 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 [9]
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 [10]
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 [11]
RP FUNCTION, HETERODIMERIC COMPLEX FORMATION WITH ARP7 WITHIN THE RSC COMPLEX,
RP AND MUTAGENESIS OF GLY-337 AND GLY-338.
RX PubMed=12805231; DOI=10.1093/emboj/cdg296;
RA Szerlong H., Saha A., Cairns B.R.;
RT "The nuclear actin-related proteins Arp7 and Arp9: a dimeric module that
RT cooperates with architectural proteins for chromatin remodeling.";
RL EMBO J. 22:3175-3187(2003).
RN [12]
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 [13]
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 [14]
RP 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).
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 involved in
CC transcriptional regulation. Heterodimer of ARP9 and ARP7 functions with
CC HMG box proteins to facilitate proper chromatin architecture.
CC Heterodimer formation is necessary for assembly into RSC complex. Part
CC of the SWI/SNF complex, an ATP-dependent chromatin remodeling complex,
CC is required for the positive and negative regulation of gene expression
CC of a large number of genes. It changes chromatin structure by altering
CC DNA-histone contacts within a nucleosome, leading eventually to a
CC change in nucleosome position, thus facilitating or repressing binding
CC of gene-specific transcription factors. {ECO:0000269|PubMed:10025404,
CC ECO:0000269|PubMed:10329629, ECO:0000269|PubMed:12072455,
CC ECO:0000269|PubMed:12183366, ECO:0000269|PubMed:12697820,
CC ECO:0000269|PubMed:12805231, ECO:0000269|PubMed:8980231,
CC ECO:0000269|PubMed:9844636}.
CC -!- SUBUNIT: Forms a heterodimer with ARP7. 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 the SWI/SNF global transcription
CC activator complex. The 1.14 MDa SWI/SNF complex is composed of 11
CC different subunits: one copy each of SWI1, SNF2/SWI2, SNF5,
CC SNF12/SWP73, ARP7/SWP61, ARP9/SWP59; two copies each of SWI3, SNF6,
CC SNF11, SWP82; and three copies of TAF14/SWP29.
CC {ECO:0000269|PubMed:12697820, ECO:0000269|PubMed:16204215,
CC ECO:0000269|PubMed:9844636}.
CC -!- INTERACTION:
CC Q05123; Q12406: ARP7; NbExp=6; IntAct=EBI-2972, EBI-2962;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12697820}.
CC Note=Localizes to centromeric and flanking chromatin. Association with
CC these loci is dependent on STH1.
CC -!- MISCELLANEOUS: Present with 1790 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the actin family. {ECO:0000305}.
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DR EMBL; Z49213; CAA89149.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09932.1; -; Genomic_DNA.
DR PIR; S53950; S53950.
DR RefSeq; NP_013747.1; NM_001182530.1.
DR PDB; 3WEE; X-ray; 3.10 A; A=1-467.
DR PDB; 4I6M; X-ray; 2.80 A; B=1-467.
DR PDB; 5TGC; X-ray; 3.25 A; B/E=1-467.
DR PDB; 6KW3; EM; 7.13 A; g=1-467.
DR PDB; 6KW4; EM; 7.55 A; g=1-467.
DR PDB; 6KW5; EM; 10.13 A; g=1-467.
DR PDB; 6TDA; EM; 15.00 A; U=1-467.
DR PDB; 6UXW; EM; 8.96 A; Q=1-467.
DR PDB; 6V92; EM; 20.00 A; B=1-467.
DR PDB; 6VZ4; EM; 3.90 A; M=1-467.
DR PDB; 6VZG; EM; 4.20 A; M=1-467.
DR PDB; 7C4J; EM; 2.89 A; L=1-467.
DR PDB; 7EGP; EM; 6.90 A; N=1-467.
DR PDBsum; 3WEE; -.
DR PDBsum; 4I6M; -.
DR PDBsum; 5TGC; -.
DR PDBsum; 6KW3; -.
DR PDBsum; 6KW4; -.
DR PDBsum; 6KW5; -.
DR PDBsum; 6TDA; -.
DR PDBsum; 6UXW; -.
DR PDBsum; 6V92; -.
DR PDBsum; 6VZ4; -.
DR PDBsum; 6VZG; -.
DR PDBsum; 7C4J; -.
DR PDBsum; 7EGP; -.
DR AlphaFoldDB; Q05123; -.
DR SMR; Q05123; -.
DR BioGRID; 35205; 355.
DR ComplexPortal; CPX-1150; SWI/SNF chromatin remodelling complex.
DR ComplexPortal; CPX-1888; RSC chromatin remodelling complex, variant RSC2.
DR ComplexPortal; CPX-1889; RSC chromatin remodelling complex, variant RSC1.
DR DIP; DIP-6709N; -.
DR IntAct; Q05123; 62.
DR MINT; Q05123; -.
DR STRING; 4932.YMR033W; -.
DR MaxQB; Q05123; -.
DR PaxDb; Q05123; -.
DR PRIDE; Q05123; -.
DR DNASU; 855049; -.
DR EnsemblFungi; YMR033W_mRNA; YMR033W; YMR033W.
DR GeneID; 855049; -.
DR KEGG; sce:YMR033W; -.
DR SGD; S000004636; ARP9.
DR VEuPathDB; FungiDB:YMR033W; -.
DR eggNOG; KOG0676; Eukaryota.
DR HOGENOM; CLU_052064_0_0_1; -.
DR InParanoid; Q05123; -.
DR OMA; RYIFEKT; -.
DR BioCyc; YEAST:G3O-32738-MON; -.
DR Reactome; R-SCE-3214858; RMTs methylate histone arginines.
DR PRO; PR:Q05123; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; Q05123; protein.
DR GO; GO:0000785; C:chromatin; IC:ComplexPortal.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0016586; C:RSC-type complex; IDA:UniProtKB.
DR GO; GO:0016514; C:SWI/SNF complex; IDA:UniProtKB.
DR GO; GO:0005198; F:structural molecule activity; IMP:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IGI:UniProtKB.
DR GO; GO:0006338; P:chromatin remodeling; IDA:UniProtKB.
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:1905168; P:positive regulation of double-strand break repair via homologous recombination; IC:ComplexPortal.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:ComplexPortal.
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 InterPro; IPR004000; Actin.
DR InterPro; IPR043129; ATPase_NBD.
DR PANTHER; PTHR11937; PTHR11937; 1.
DR Pfam; PF00022; Actin; 1.
DR SMART; SM00268; ACTIN; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Chromatin regulator; Direct protein sequencing; Nucleus;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..467
FT /note="Actin-like protein ARP9"
FT /id="PRO_0000089129"
FT MUTAGEN 337
FT /note="G->V: Impaired heterodimerization with ARP7; when
FT associated with L-338."
FT /evidence="ECO:0000269|PubMed:12805231"
FT MUTAGEN 338
FT /note="G->L: Impaired heterodimerization with ARP7; when
FT associated with V-337."
FT /evidence="ECO:0000269|PubMed:12805231"
FT HELIX 6..8
FT /evidence="ECO:0007829|PDB:4I6M"
FT STRAND 10..14
FT /evidence="ECO:0007829|PDB:4I6M"
FT STRAND 16..24
FT /evidence="ECO:0007829|PDB:4I6M"
FT STRAND 27..29
FT /evidence="ECO:0007829|PDB:4I6M"
FT STRAND 35..39
FT /evidence="ECO:0007829|PDB:4I6M"
FT STRAND 41..45
FT /evidence="ECO:0007829|PDB:4I6M"
FT STRAND 51..56
FT /evidence="ECO:0007829|PDB:4I6M"
FT HELIX 58..60
FT /evidence="ECO:0007829|PDB:4I6M"
FT STRAND 62..65
FT /evidence="ECO:0007829|PDB:4I6M"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:5TGC"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:4I6M"
FT HELIX 76..98
FT /evidence="ECO:0007829|PDB:4I6M"
FT TURN 101..106
FT /evidence="ECO:0007829|PDB:4I6M"
FT STRAND 111..115
FT /evidence="ECO:0007829|PDB:4I6M"
FT HELIX 121..133
FT /evidence="ECO:0007829|PDB:4I6M"
FT STRAND 139..144
FT /evidence="ECO:0007829|PDB:4I6M"
FT HELIX 145..152
FT /evidence="ECO:0007829|PDB:4I6M"
FT STRAND 157..164
FT /evidence="ECO:0007829|PDB:4I6M"
FT STRAND 169..175
FT /evidence="ECO:0007829|PDB:4I6M"
FT TURN 181..183
FT /evidence="ECO:0007829|PDB:4I6M"
FT STRAND 185..188
FT /evidence="ECO:0007829|PDB:4I6M"
FT HELIX 191..201
FT /evidence="ECO:0007829|PDB:4I6M"
FT HELIX 207..214
FT /evidence="ECO:0007829|PDB:4I6M"
FT HELIX 224..228
FT /evidence="ECO:0007829|PDB:3WEE"
FT STRAND 229..232
FT /evidence="ECO:0007829|PDB:3WEE"
FT STRAND 251..254
FT /evidence="ECO:0007829|PDB:3WEE"
FT HELIX 276..278
FT /evidence="ECO:0007829|PDB:4I6M"
FT STRAND 282..285
FT /evidence="ECO:0007829|PDB:4I6M"
FT STRAND 291..294
FT /evidence="ECO:0007829|PDB:4I6M"
FT HELIX 296..299
FT /evidence="ECO:0007829|PDB:4I6M"
FT HELIX 303..317
FT /evidence="ECO:0007829|PDB:4I6M"
FT HELIX 323..329
FT /evidence="ECO:0007829|PDB:4I6M"
FT STRAND 333..337
FT /evidence="ECO:0007829|PDB:4I6M"
FT HELIX 338..341
FT /evidence="ECO:0007829|PDB:4I6M"
FT HELIX 345..357
FT /evidence="ECO:0007829|PDB:4I6M"
FT HELIX 363..372
FT /evidence="ECO:0007829|PDB:4I6M"
FT HELIX 379..386
FT /evidence="ECO:0007829|PDB:3WEE"
FT STRAND 401..403
FT /evidence="ECO:0007829|PDB:4I6M"
FT HELIX 417..422
FT /evidence="ECO:0007829|PDB:4I6M"
FT TURN 425..427
FT /evidence="ECO:0007829|PDB:4I6M"
FT HELIX 428..440
FT /evidence="ECO:0007829|PDB:4I6M"
FT STRAND 448..450
FT /evidence="ECO:0007829|PDB:4I6M"
FT HELIX 451..457
FT /evidence="ECO:0007829|PDB:4I6M"
FT HELIX 458..464
FT /evidence="ECO:0007829|PDB:4I6M"
SQ SEQUENCE 467 AA; 53074 MW; EE1AB154A906420E CRC64;
MAPFRQDSIL IIYPRSQTTL VQFGLNEETF TVPELEIPTQ IYRTTRQDGS YTYHSTNKDN
KAELIKPIQN GEIIDISAFT QFLRLIFVSI LSDRANKNQD AFEAELSNIP LLLITHHSWS
QSDLEIITQY VFESLEINNL IQLPASLAAT YSMISLQNCC IIDVGTHHTD IIPIVDYAQL
DHLVSSIPMG GQSINDSLKK LLPQWDDDQI ESLKKSPIFE VLSDDAKKLS SFDFGNENED
EDEGTLNVAE IITSGRDTRE VLEERERGQK VKNVKNSDLE FNTFWDEKGN EIKVGKQRFQ
GCNNLIKNIS NRVGLTLDNI DDINKAKAVW ENIIIVGGTT SISGFKEALL GQLLKDHLII
EPEEEKSKRE EEAKSVLPAA TKKKSKFMTN STAFVPTIEY VQCPTVIKLA KYPDYFPEWK
KSGYSEIIFL GAQIVSKQIF THPKDTFYIT REKYNMKGPA ALWDVQF
