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 27-MAR-2024, entry version 179. 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; GN 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 EMDB; EMD-0777; -. DR EMDB; EMD-0778; -. DR EMDB; EMD-0779; -. DR EMDB; EMD-10465; -. DR EMDB; EMD-20934; -. DR EMDB; EMD-21114; -. DR EMDB; EMD-21484; -. DR EMDB; EMD-21489; -. DR EMDB; EMD-30285; -. DR EMDB; EMD-31137; -. DR SMR; Q05123; -. DR BioGRID; 35205; 367. 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; 4932-YMR033W; -. DR PeptideAtlas; Q05123; -. DR DNASU; 855049; -. DR EnsemblFungi; YMR033W_mRNA; YMR033W; YMR033W. DR GeneID; 855049; -. DR KEGG; sce:YMR033W; -. DR AGR; SGD:S000004636; -. 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 OrthoDB; 2641150at2759; -. DR BioCyc; YEAST:G3O-32738-MONOMER; -. DR Reactome; R-SCE-114608; Platelet degranulation. DR Reactome; R-SCE-2029482; Regulation of actin dynamics for phagocytic cup formation. DR Reactome; R-SCE-5626467; RHO GTPases activate IQGAPs. DR Reactome; R-SCE-5663213; RHO GTPases Activate WASPs and WAVEs. DR Reactome; R-SCE-9013418; RHOBTB2 GTPase cycle. DR BioGRID-ORCS; 855049; 1 hit in 10 CRISPR screens. DR PRO; PR:Q05123; -. DR Proteomes; UP000002311; Chromosome XIII. DR RNAct; Q05123; Protein. DR GO; GO:0000785; C:chromatin; NAS: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:0006337; P:nucleosome disassembly; IDA:SGD. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:SGD. DR GO; GO:0006355; P:regulation of DNA-templated transcription; IMP:UniProtKB. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:ComplexPortal. DR GO; GO:0006368; P:transcription elongation by RNA polymerase II; IDA:SGD. DR Gene3D; 3.30.420.40; -; 2. DR Gene3D; 3.90.640.60; -; 1. DR InterPro; IPR004000; Actin. DR InterPro; IPR043129; ATPase_NBD. DR PANTHER; PTHR11937; ACTIN; 1. DR PANTHER; PTHR11937:SF46; ACTIN-42A-RELATED; 1. DR Pfam; PF00022; Actin; 1. DR SMART; SM00268; ACTIN; 1. DR SUPFAM; SSF53067; Actin-like ATPase domain; 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 //