ARP7_YEAST
ID ARP7_YEAST Reviewed; 477 AA.
AC Q12406; D6W444;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Actin-related protein 7;
DE AltName: Full=Actin-like protein ARP7;
DE AltName: Full=Chromatin structure-remodeling complex protein ARP7;
DE AltName: Full=SWI/SNF complex component ARP7;
GN Name=ARP7; Synonyms=SWP61; OrderedLocusNames=YPR034W; ORFNames=YP9367.14;
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=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(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 184-196; 217-232 AND 289-297, FUNCTION, IDENTIFICATION
RP IN THE RSC AND SWI/SNF COMPLEXES, AND MUTAGENESIS OF ALA-19; SER-33;
RP GLY-396 AND GLU-411.
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 ARP9 WITHIN THE RSC COMPLEX,
RP AND MUTAGENESIS OF ALA-19; SER-33 AND GLU-411.
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 3D-STRUCTURE MODELING OF THE SWI/SNF COMPLEX, AND ELECTRON MICROSCOPY OF
RP THE SWI/SNF COMPLEX.
RX PubMed=12524530; DOI=10.1038/nsb888;
RA Smith C.L., Horowitz-Scherer R., Flanagan J.F., Woodcock C.L.,
RA Peterson C.L.;
RT "Structural analysis of the yeast SWI/SNF chromatin remodeling complex.";
RL Nat. Struct. Biol. 10:141-145(2003).
RN [15]
RP INTERACTION WITH 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 ARP7 and ARP9 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 ARP9. Interacts with NPL6. Component
CC of the two forms of the RSC complex composed of at least either RSC1 or
CC RSC2, and ARP7, ARP9, LDB7, NPL6, RSC3, RSC30, RSC4, RSC58, RSC6, RSC8,
CC RSC9, SFH1, STH1, HTL1 and probably RTT102. The complexes interact with
CC histone and histone variant components of centromeric chromatin.
CC Component of the SWI/SNF global transcription activator complex. The
CC 1.14 MDa SWI/SNF complex is composed of 11 different subunits: one copy
CC each of SWI1, SNF2/SWI2, SNF5, SNF12/SWP73, ARP7/SWP61, ARP9/SWP59; two
CC copies each of SWI3, SNF6, SNF11, SWP82; and three copies of
CC TAF14/SWP29. {ECO:0000269|PubMed:12697820, ECO:0000269|PubMed:16204215,
CC ECO:0000269|PubMed:9844636}.
CC -!- INTERACTION:
CC Q12406; Q05123: ARP9; NbExp=6; IntAct=EBI-2962, EBI-2972;
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 1360 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; Z71255; CAA94984.1; -; Genomic_DNA.
DR EMBL; Z49274; CAA89288.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11460.1; -; Genomic_DNA.
DR PIR; S54508; S54508.
DR RefSeq; NP_015359.1; NM_001184131.1.
DR PDB; 3WEE; X-ray; 3.10 A; B=1-477.
DR PDB; 4I6M; X-ray; 2.80 A; A=1-477.
DR PDB; 5TGC; X-ray; 3.25 A; A/D=1-477.
DR PDB; 6KW3; EM; 7.13 A; f=1-477.
DR PDB; 6KW4; EM; 7.55 A; f=1-477.
DR PDB; 6KW5; EM; 10.13 A; f=1-477.
DR PDB; 6TDA; EM; 15.00 A; T=1-477.
DR PDB; 6UXW; EM; 8.96 A; P=1-477.
DR PDB; 6V92; EM; 20.00 A; A=1-477.
DR PDB; 6VZ4; EM; 3.90 A; L=1-477.
DR PDB; 6VZG; EM; 4.20 A; L=1-477.
DR PDB; 7C4J; EM; 2.89 A; K=1-477.
DR PDB; 7EGP; EM; 6.90 A; M=1-477.
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; Q12406; -.
DR SMR; Q12406; -.
DR BioGRID; 36212; 327.
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-6351N; -.
DR IntAct; Q12406; 61.
DR MINT; Q12406; -.
DR STRING; 4932.YPR034W; -.
DR iPTMnet; Q12406; -.
DR MaxQB; Q12406; -.
DR PaxDb; Q12406; -.
DR PRIDE; Q12406; -.
DR EnsemblFungi; YPR034W_mRNA; YPR034W; YPR034W.
DR GeneID; 856146; -.
DR KEGG; sce:YPR034W; -.
DR SGD; S000006238; ARP7.
DR VEuPathDB; FungiDB:YPR034W; -.
DR eggNOG; KOG0679; Eukaryota.
DR HOGENOM; CLU_566415_0_0_1; -.
DR InParanoid; Q12406; -.
DR OMA; WDRQFGA; -.
DR BioCyc; YEAST:G3O-34193-MON; -.
DR Reactome; R-SCE-3214858; RMTs methylate histone arginines.
DR PRO; PR:Q12406; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q12406; protein.
DR GO; GO:0000785; C:chromatin; IC:ComplexPortal.
DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IBA:GO_Central.
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:0003682; F:chromatin binding; IBA:GO_Central.
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:0043967; P:histone H4 acetylation; IBA:GO_Central.
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 DisProt; DP00874; -.
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..477
FT /note="Actin-related protein 7"
FT /id="PRO_0000089122"
FT MUTAGEN 19
FT /note="A->P: Impaired heterodimerization with ARP9.
FT Temperature-sensitive phenotype. Moderate suppressor of Ty
FT phenotype."
FT /evidence="ECO:0000269|PubMed:12805231,
FT ECO:0000269|PubMed:9844636"
FT MUTAGEN 33
FT /note="S->F: Impaired heterodimerization with ARP9.
FT Temperature-sensitive phenotype. Moderate suppressor of Ty
FT phenotype."
FT /evidence="ECO:0000269|PubMed:12805231,
FT ECO:0000269|PubMed:9844636"
FT MUTAGEN 396
FT /note="G->V: Temperature-sensitive phenotype. Moderate
FT suppressor of Ty phenotype."
FT /evidence="ECO:0000269|PubMed:9844636"
FT MUTAGEN 411
FT /note="E->K: Impaired heterodimerization with ARP9.
FT Temperature-sensitive phenotype. Moderate suppressor of Ty
FT phenotype."
FT /evidence="ECO:0000269|PubMed:12805231,
FT ECO:0000269|PubMed:9844636"
FT STRAND 8..12
FT /evidence="ECO:0007829|PDB:4I6M"
FT STRAND 14..21
FT /evidence="ECO:0007829|PDB:4I6M"
FT STRAND 24..26
FT /evidence="ECO:0007829|PDB:4I6M"
FT STRAND 28..37
FT /evidence="ECO:0007829|PDB:4I6M"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:3WEE"
FT STRAND 45..48
FT /evidence="ECO:0007829|PDB:3WEE"
FT HELIX 51..59
FT /evidence="ECO:0007829|PDB:4I6M"
FT STRAND 66..71
FT /evidence="ECO:0007829|PDB:4I6M"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:3WEE"
FT HELIX 80..93
FT /evidence="ECO:0007829|PDB:4I6M"
FT TURN 99..101
FT /evidence="ECO:0007829|PDB:3WEE"
FT STRAND 104..108
FT /evidence="ECO:0007829|PDB:4I6M"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:3WEE"
FT HELIX 116..127
FT /evidence="ECO:0007829|PDB:4I6M"
FT TURN 128..131
FT /evidence="ECO:0007829|PDB:4I6M"
FT STRAND 134..140
FT /evidence="ECO:0007829|PDB:4I6M"
FT HELIX 141..147
FT /evidence="ECO:0007829|PDB:4I6M"
FT TURN 148..150
FT /evidence="ECO:0007829|PDB:4I6M"
FT STRAND 152..159
FT /evidence="ECO:0007829|PDB:4I6M"
FT STRAND 164..170
FT /evidence="ECO:0007829|PDB:4I6M"
FT HELIX 176..178
FT /evidence="ECO:0007829|PDB:4I6M"
FT HELIX 186..197
FT /evidence="ECO:0007829|PDB:4I6M"
FT HELIX 198..200
FT /evidence="ECO:0007829|PDB:4I6M"
FT HELIX 217..225
FT /evidence="ECO:0007829|PDB:4I6M"
FT HELIX 227..234
FT /evidence="ECO:0007829|PDB:4I6M"
FT HELIX 243..261
FT /evidence="ECO:0007829|PDB:4I6M"
FT HELIX 283..285
FT /evidence="ECO:0007829|PDB:4I6M"
FT STRAND 287..292
FT /evidence="ECO:0007829|PDB:4I6M"
FT HELIX 293..295
FT /evidence="ECO:0007829|PDB:4I6M"
FT STRAND 297..302
FT /evidence="ECO:0007829|PDB:4I6M"
FT HELIX 303..314
FT /evidence="ECO:0007829|PDB:4I6M"
FT HELIX 316..318
FT /evidence="ECO:0007829|PDB:4I6M"
FT STRAND 321..323
FT /evidence="ECO:0007829|PDB:5TGC"
FT HELIX 325..327
FT /evidence="ECO:0007829|PDB:4I6M"
FT HELIX 329..338
FT /evidence="ECO:0007829|PDB:4I6M"
FT TURN 339..342
FT /evidence="ECO:0007829|PDB:4I6M"
FT HELIX 344..347
FT /evidence="ECO:0007829|PDB:3WEE"
FT STRAND 351..353
FT /evidence="ECO:0007829|PDB:5TGC"
FT HELIX 381..388
FT /evidence="ECO:0007829|PDB:4I6M"
FT STRAND 391..396
FT /evidence="ECO:0007829|PDB:4I6M"
FT HELIX 397..400
FT /evidence="ECO:0007829|PDB:4I6M"
FT HELIX 404..415
FT /evidence="ECO:0007829|PDB:4I6M"
FT STRAND 423..425
FT /evidence="ECO:0007829|PDB:3WEE"
FT HELIX 429..433
FT /evidence="ECO:0007829|PDB:4I6M"
FT HELIX 435..444
FT /evidence="ECO:0007829|PDB:4I6M"
FT HELIX 449..451
FT /evidence="ECO:0007829|PDB:4I6M"
FT STRAND 454..456
FT /evidence="ECO:0007829|PDB:4I6M"
FT HELIX 457..463
FT /evidence="ECO:0007829|PDB:4I6M"
SQ SEQUENCE 477 AA; 53810 MW; 8E105921576FA213 CRC64;
MTLNRKCVVI HNGSHRTVAG FSNVELPQCI IPSSYIKRTD EGGEAEFIFG TYNMIDAAAE
KRNGDEVYTL VDSQGLPYNW DALEMQWRYL YDTQLKVSPE ELPLVITMPA TNGKPDMAIL
ERYYELAFDK LNVPVFQIVI EPLAIALSMG KSSAFVIDIG ASGCNVTPII DGIVVKNAVV
RSKFGGDFLD FQVHERLAPL IKEENDMENM ADEQKRSTDV WYEASTWIQQ FKSTMLQVSE
KDLFELERYY KEQADIYAKQ QEQLKQMDQQ LQYTALTGSP NNPLVQKKNF LFKPLNKTLT
LDLKECYQFA EYLFKPQLIS DKFSPEDGLG PLMAKSVKKA GASINSMKAN TSTNPNGLGT
SHINTNVGDN NSTASSSNIS PEQVYSLLLT NVIITGSTSL IEGMEQRIIK ELSIRFPQYK
LTTFANQVMM DRKIQGWLGA LTMANLPSWS LGKWYSKEDY ETLKRDRKQS QATNATN
