Q12406 (ARP7_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Actin-related protein 7

Alternative name(s):
Actin-like protein ARP7
Chromatin structure-remodeling complex protein ARP7
SWI/SNF complex component ARP7

Gene names

Name:	ARP7
Synonyms:	SWP61
Ordered Locus Names:	YPR034W
ORF Names:	YP9367.14

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	477 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Component of the chromatin structure remodeling complex (RSC), which is involved in transcription regulation and nucleosome positioning. RSC is responsible for the transfer of a histone octamer from a nucleosome core particle to naked DNA. The reaction requires ATP and involves an activated RSC-nucleosome intermediate. Remodeling reaction also involves DNA translocation, DNA twist and conformational change. As a reconfigurer of centromeric and flanking nucleosomes, RSC complex is required both for proper kinetochore function in chromosome segregation and, via a PKC1-dependent signaling pathway, for organization of the cellular cytoskeleton. This subunit is involved in transcriptional regulation. Heterodimer of ARP7 and ARP9 functions with HMG box proteins to facilitate proper chromatin architecture. Heterodimer formation is necessary for assembly into RSC complex. Part of the SWI/SNF complex, an ATP-dependent chromatin remodeling complex, is required for the positive and negative regulation of gene expression of a large number of genes. It changes chromatin structure by altering DNA-histone contacts within a nucleosome, leading eventually to a change in nucleosome position, thus facilitating or repressing binding of gene-specific transcription factors. Ref.3 Ref.4 Ref.6 Ref.7 Ref.9 Ref.10 Ref.11 Ref.12
Subunit structure	Forms a heterodimer with ARP9. Interacts with NPL6. Component of the two forms of the RSC complex composed of at least either RSC1 or RSC2, and ARP7, ARP9, LDB7, NPL6, RSC3, RSC30, RSC4, RSC58, RSC6, RSC8, RSC9, SFH1, STH1, HTL1 and probably RTT102. The complexes interact with histone and histone variant components of centromeric chromatin. Component of the SWI/SNF global transcription activator complex. The 1.14 MDa SWI/SNF complex is composed of 11 different subunits: one copy each of SWI1, SNF2/SWI2, SNF5, SNF12/SWP73, ARP7/SWP61, ARP9/SWP59; two copies each of SWI3, SNF6, SNF11, SWP82; and three copies of TAF14/SWP29. Ref.3 Ref.12 Ref.15
Subcellular location	Nucleus. Note: Localizes to centromeric and flanking chromatin. Association with these loci is dependent on STH1. Ref.12
Miscellaneous	Present with 1360 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the actin family.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Molecular function	Chromatin regulator
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	ATP-dependent chromatin remodeling Inferred from direct assay Ref.6Ref.9. Source: UniProtKB nucleosome disassembly Inferred from direct assay PubMed 16492771. Source: SGD nucleosome mobilization Inferred from direct assay PubMed 17496903. Source: SGD positive regulation of transcription from RNA polymerase II promoter Inferred from mutant phenotype PubMed 9726966. Source: SGD transcription elongation from RNA polymerase II promoter Inferred from direct assay PubMed 17081996. Source: SGD
Cellular_component	RSC complex Inferred from direct assay Ref.3. Source: UniProtKB SWI/SNF complex Inferred from direct assay Ref.3. Source: UniProtKB
Molecular_function	structural molecule activity Inferred from mutant phenotype Ref.3. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ARP9	Q05123	5	EBI-2962,EBI-2972

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 477

477

Actin-related protein 7

PRO_0000089122

Experimental info

Mutagenesis

19

1

A → P: Impaired heterodimerization with ARP9. Temperature-sensitive phenotype. Moderate suppressor of Ty phenotype. Ref.3 Ref.11

Mutagenesis

33

1

S → F: Impaired heterodimerization with ARP9. Temperature-sensitive phenotype. Moderate suppressor of Ty phenotype. Ref.3 Ref.11

Mutagenesis

396

1

G → V: Temperature-sensitive phenotype. Moderate suppressor of Ty phenotype. Ref.3

Mutagenesis

411

1

E → K: Impaired heterodimerization with ARP9. Temperature-sensitive phenotype. Moderate suppressor of Ty phenotype. Ref.3 Ref.11

Secondary structure

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477

Helix Strand Turn

Details...

Beta strand

8 – 12

5

Beta strand

14 – 21

8

Beta strand

24 – 26

3

Beta strand

28 – 37

10

Helix

51 – 59

9

Beta strand

66 – 71

6

Helix

80 – 93

14

Beta strand

104 – 108

5

Helix

116 – 127

12

Turn

128 – 131

4

Beta strand

134 – 140

7

Helix

141 – 147

7

Turn

148 – 150

3

Beta strand

152 – 159

8

Beta strand

164 – 170

7

Helix

176 – 178

3

Helix

186 – 197

12

Helix

198 – 200

3

Helix

217 – 225

9

Helix

227 – 234

8

Helix

243 – 261

19

Helix

283 – 285

3

Beta strand

287 – 292

6

Helix

293 – 295

3

Beta strand

297 – 302

6

Helix

303 – 314

12

Helix

316 – 318

3

Helix

325 – 327

3

Helix

329 – 338

10

Turn

339 – 342

4

Helix

381 – 388

8

Beta strand

391 – 396

6

Helix

397 – 400

4

Helix

404 – 415

12

Helix

429 – 433

5

Helix

435 – 444

10

Helix

449 – 451

3

Beta strand

454 – 456

3

Helix

457 – 463

7

Sequences

	Sequence		Length	Mass (Da)
	Q12406 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 8E105921576FA213	FASTA	477	53,810
	10 20 30 40 50 60 MTLNRKCVVI HNGSHRTVAG FSNVELPQCI IPSSYIKRTD EGGEAEFIFG TYNMIDAAAE 70 80 90 100 110 120 KRNGDEVYTL VDSQGLPYNW DALEMQWRYL YDTQLKVSPE ELPLVITMPA TNGKPDMAIL 130 140 150 160 170 180 ERYYELAFDK LNVPVFQIVI EPLAIALSMG KSSAFVIDIG ASGCNVTPII DGIVVKNAVV 190 200 210 220 230 240 RSKFGGDFLD FQVHERLAPL IKEENDMENM ADEQKRSTDV WYEASTWIQQ FKSTMLQVSE 250 260 270 280 290 300 KDLFELERYY KEQADIYAKQ QEQLKQMDQQ LQYTALTGSP NNPLVQKKNF LFKPLNKTLT 310 320 330 340 350 360 LDLKECYQFA EYLFKPQLIS DKFSPEDGLG PLMAKSVKKA GASINSMKAN TSTNPNGLGT 370 380 390 400 410 420 SHINTNVGDN NSTASSSNIS PEQVYSLLLT NVIITGSTSL IEGMEQRIIK ELSIRFPQYK 430 440 450 460 470 LTTFANQVMM DRKIQGWLGA LTMANLPSWS LGKWYSKEDY ETLKRDRKQS QATNATN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI." Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M. , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J. Nature 387:103-105(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[2]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[3]	"Two actin-related proteins are shared functional components of the chromatin-remodeling complexes RSC and SWI/SNF." Cairns B.R., Erdjument-Bromage H., Tempst P., Winston F., Kornberg R.D. Mol. Cell 2:639-651(1998) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 184-196; 217-232 AND 289-297, FUNCTION, IDENTIFICATION IN THE RSC AND SWI/SNF COMPLEXES, MUTAGENESIS OF ALA-19; SER-33; GLY-396 AND GLU-411.
[4]	"RSC, an essential, abundant chromatin-remodeling complex." Cairns B.R., Lorch Y., Li Y., Zhang M., Lacomis L., Erdjument-Bromage H., Tempst P., Du J., Laurent B.C., Kornberg R.D. Cell 87:1249-1260(1996) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION OF THE RSC COMPLEX, COMPOSITION OF THE RSC COMPLEX.
[5]	"Who's who among the Saccharomyces cerevisiae actin-related proteins? A classification and nomenclature proposal for a large family." Poch O., Winsor B. Yeast 13:1053-1058(1997) [PubMed] [Europe PMC] [Abstract] Cited for: GENE NAME.
[6]	"Histone octamer transfer by a chromatin-remodeling complex." Lorch Y., Zhang M., Kornberg R.D. Cell 96:389-392(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION OF THE RSC COMPLEX.
[7]	"Transcriptional repression of the yeast CHA1 gene requires the chromatin-remodeling complex RSC." Moreira J.M.A., Holmberg S. EMBO J. 18:2836-2844(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION OF THE RSC COMPLEX.
[8]	"Two functionally distinct forms of the RSC nucleosome-remodeling complex, containing essential AT hook, BAH, and bromodomains." Cairns B.R., Schlichter A., Erdjument-Bromage H., Tempst P., Kornberg R.D., Winston F. Mol. Cell 4:715-723(1999) [PubMed] [Europe PMC] [Abstract] Cited for: COMPOSITION OF THE RSC COMPLEX.
[9]	"Chromatin remodeling by RSC involves ATP-dependent DNA translocation." Saha A., Wittmeyer J., Cairns B.R. Genes Dev. 16:2120-2134(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION OF THE RSC COMPLEX.
[10]	"Yeast RSC function is required for organization of the cellular cytoskeleton via an alternative PKC1 pathway." Chai B., Hsu J.-M., Du J., Laurent B.C. Genetics 161:575-584(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION OF THE RSC COMPLEX.
[11]	"The nuclear actin-related proteins Arp7 and Arp9: a dimeric module that cooperates with architectural proteins for chromatin remodeling." Szerlong H., Saha A., Cairns B.R. EMBO J. 22:3175-3187(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, HETERODIMERIC COMPLEX FORMATION WITH ARP9 WITHIN THE RSC COMPLEX, MUTAGENESIS OF ALA-19; SER-33 AND GLU-411.
[12]	"The yeast RSC chromatin-remodeling complex is required for kinetochore function in chromosome segregation." Hsu J.-M., Huang J., Meluh P.B., Laurent B.C. Mol. Cell. Biol. 23:3202-3215(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION OF THE RSC COMPLEX, SUBCELLULAR LOCATION, INTERACTION OF THE RSC COMPLEX WITH HISTONES.
[13]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[14]	"Structural analysis of the yeast SWI/SNF chromatin remodeling complex." Smith C.L., Horowitz-Scherer R., Flanagan J.F., Woodcock C.L., Peterson C.L. Nat. Struct. Biol. 10:141-145(2003) [PubMed] [Europe PMC] [Abstract] Cited for: 3D-STRUCTURE MODELING OF THE SWI/SNF COMPLEX, ELECTRON MICROSCOPY OF THE SWI/SNF COMPLEX.
[15]	"The RSC chromatin remodeling complex bears an essential fungal-specific protein module with broad functional roles." Wilson B., Erdjument-Bromage H., Tempst P., Cairns B.R. Genetics 172:795-809(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH NPL6.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Z71255 Genomic DNA. Translation: CAA94984.1.
Z49274 Genomic DNA. Translation: CAA89288.1.
BK006949 Genomic DNA. Translation: DAA11460.1.

PIR

S54508.

RefSeq

NP_015359.1. NM_001184131.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
4I6M	X-ray	2.80	A	1-477	[»]

ProteinModelPortal

Q12406.

SMR

Q12406. Positions 8-191.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-6351N.

IntAct

Q12406. 56 interactions.

MINT

MINT-686249.

STRING

4932.YPR034W.

Proteomic databases

PaxDb

Q12406.

PeptideAtlas

Q12406.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YPR034W; YPR034W; YPR034W.

GeneID

856146.

KEGG

sce:YPR034W.

Organism-specific databases

CYGD

YPR034w.

SGD

S000006238. ARP7.

Phylogenomic databases

eggNOG

COG5277.

HOGENOM

HOG000034072.

KO

K11767.

OMA

GMEQRII.

OrthoDB

EOG49631T.

Enzyme and pathway databases

BioCyc

YEAST:G3O-34193-MONOMER.

Gene expression databases

Genevestigator

Q12406.

GermOnline

YPR034W. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR004000. Actin-related.
[Graphical view]

PANTHER

PTHR11937. PTHR11937. 1 hit.

Pfam

PF00022. Actin. 1 hit.
[Graphical view]

SMART

SM00268. ACTIN. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

981268.

Entry information

Entry name

ARP7_YEAST

Accession

Primary (citable) accession number: Q12406
Secondary accession number(s): D6W444

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1996
Last modified:	May 29, 2013
This is version 112 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program