Q12386 (ARP8_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Actin-like protein ARP8

Gene names

Name:	ARP8
Ordered Locus Names:	YOR141C
ORF Names:	YOR3348C

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	881 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Probably involved in transcription regulation via its interaction with the INO80 complex, a chromatin remodeling complex. Exhibits low basal ATPase activity, and unable to polymerize. Strongly prefer nucleosomes and H3-H4 tetramers over H2A-H2B dimers, suggesting it may act as a nucleosome recognition module within the complex. Ref.9
Subunit structure	Component of the chromatin-remodeling INO80 complex, at least composed of ARP4, ARP5, ARP8, RVB1, RVB2, TAF14, NHP10, IES1, IES3, IES4, IES6, ACT1, IES2, IES5 and INO80. Exists as monomers and dimers, but the dimer is most probably the biologically relevant form required for stable interactions with histones that exploits the twofold symmetry of the nucleosome core By similarity. Ref.5 Ref.9
Subcellular location	Nucleus. Cytoplasm › cytoskeleton.
Miscellaneous	Present with 1010 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the actin family.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Cytoplasm Cytoskeleton Nucleus
Ligand	ATP-binding Nucleotide-binding
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	chromatin remodeling Inferred from mutant phenotype Ref.5. Source: SGD mitotic recombination Inferred from mutant phenotype PubMed 17320816. Source: SGD regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW response to DNA damage stimulus Inferred from mutant phenotype PubMed 17320816. Source: SGD transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	Ino80 complex Inferred from physical interaction PubMed 10952318. Source: SGD cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW cytoskeleton Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW mRNA binding Inferred from direct assay PubMed 20844764. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 881

881

Actin-like protein ARP8

PRO_0000089128

Regions

Nucleotide binding

502 – 505

4

ATP By similarity

Compositional bias

22 – 27

6

Poly-Asp

Amino acid modifications

Modified residue

65

1

Phosphoserine Ref.7 Ref.8

Modified residue

70

1

Phosphoserine Ref.8

Modified residue

230

1

Phosphoserine Ref.8

Modified residue

235

1

Phosphothreonine Ref.8

Modified residue

320

1

Phosphoserine Ref.8

Secondary structure

1

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881

Helix Strand Turn

Details...

Helix

265 – 267

3

Beta strand

268 – 272

5

Beta strand

275 – 281

7

Beta strand

285 – 287

3

Beta strand

289 – 293

5

Beta strand

295 – 298

4

Helix

299 – 301

3

Beta strand

305 – 307

3

Helix

321 – 341

21

Helix

352 – 354

3

Beta strand

357 – 360

4

Beta strand

367 – 370

4

Helix

386 – 390

5

Turn

394 – 396

3

Beta strand

397 – 400

4

Beta strand

402 – 404

3

Helix

418 – 433

16

Beta strand

434 – 437

4

Helix

442 – 447

6

Beta strand

449 – 454

6

Helix

460 – 472

13

Beta strand

477 – 483

7

Helix

484 – 491

8

Beta strand

498 – 503

6

Beta strand

508 – 514

7

Helix

520 – 522

3

Beta strand

524 – 527

4

Helix

530 – 543

14

Helix

556 – 569

14

Helix

574 – 576

3

Beta strand

579 – 586

8

Beta strand

589 – 591

3

Beta strand

593 – 602

10

Helix

603 – 609

7

Helix

610 – 612

3

Helix

615 – 619

5

Helix

628 – 631

4

Turn

640 – 642

3

Helix

651 – 657

7

Helix

662 – 664

3

Helix

668 – 686

19

Helix

703 – 716

14

Helix

720 – 722

3

Helix

723 – 727

5

Beta strand

730 – 734

5

Helix

735 – 738

4

Helix

742 – 753

12

Turn

757 – 759

3

Helix

763 – 778

16

Beta strand

786 – 788

3

Turn

793 – 797

5

Helix

798 – 817

20

Helix

838 – 840

3

Helix

841 – 849

9

Helix

853 – 858

6

Helix

862 – 868

7

Helix

869 – 874

6

Sequences

	Sequence		Length	Mass (Da)
	Q12386 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 8174851B6B077A19	FASTA	881	100,209
	10 20 30 40 50 60 MSQEEAESSI IYEEPIDIPL EDDDDEDELE EENSVPLSSQ ADQENAENES DDSVDNVVGS 70 80 90 100 110 120 ETPRSVTGLS VDPRDVADEE DEDEEGEDED EDEDDNDVDN EDENDNDNAN ENENELGSSR 130 140 150 160 170 180 DKRAPPAVQT SKRYKKYPKL DPAKAPPGKK VPLHLLEKRR LGRIKAAEEF AKTLKKIGIE 190 200 210 220 230 240 KVETTTLPAT GLFQPLMLIN QKNYSSDYLK KDDQIFALRD RKFLRNNNTS QISSTNTPDV 250 260 270 280 290 300 IDLKSLPHSE ASAAPLNDEI DLNDPTATIV IHPGSNSIKI GFPKDDHPVV VPNCVAVPKK 310 320 330 340 350 360 WLDLENSEHV ENVCLQREQS EEFNNIKSEM EKNFRERMRY YKRKVPGNAH EQVVSFNENS 370 380 390 400 410 420 KPEIISEKND PSPIEWIFDD SKLYYGSDAL RCVDEKFVIR KPFRGGSFNV KSPYYKSLAE 430 440 450 460 470 480 LISDVTKLLE HALNSETLNV KPTKFNQYKV VLVIPDIFKK SHVETFIRVL LTELQFQAVA 490 500 510 520 530 540 IIQESLATCY GAGISTSTCV VNIGAAETRI ACVDEGTVLE HSAITLDYGG DDITRLFALF 550 560 570 580 590 600 LLQSDFPLQD WKIDSKHGWL LAERLKKNFT TFQDADVAVQ LYNFMNRSPN QPTEKYEFKL 610 620 630 640 650 660 FDEVMLAPLA LFFPQIFKLI RTSSHKNSSL EFQLPESRDL FTNELNDWNS LSQFESKEGN 670 680 690 700 710 720 LYCDLNDDLK ILNRILDAHN IIDQLQDKPE NYGNTLKENF APLEKAIVQS IANASITADV 730 740 750 760 770 780 TRMNSFYSNI LIVGGSSKIP ALDFILTDRI NIWRPSLLSS ASFPQFYKKL TKEIKDLEGH 790 800 810 820 830 840 YVNAPDKTED ENKQILQAQI KEKIVEELEE QHQNIEHQNG NEHIFPVSII PPPRDMNPAL 850 860 870 880 IIWKGASVLA QIKLVEELFI TNSDWDVHGS RILQYKCIFT Y

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"DNA sequencing and analysis of 130 kb from yeast chromosome XV." Voss H., Benes V., Andrade M.A., Valencia A., Rechmann S., Teodoru C., Schwager C., Paces V., Sander C., Ansorge W. Yeast 13:655-672(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XV." Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D. , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K. Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"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.
[5]	"Involvement of actin-related proteins in ATP-dependent chromatin remodeling." Shen X., Ranallo R., Choi E., Wu C. Mol. Cell 12:147-155(2003) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE INO80 COMPLEX, MASS SPECTROMETRY.
[6]	"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].
[7]	"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae." Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P. J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65, MASS SPECTROMETRY. Strain: ADR376.
[8]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65; SER-70; SER-230; THR-235 AND SER-320, MASS SPECTROMETRY.
[9]	"Interactions between the nucleosome histone core and Arp8 in the INO80 chromatin remodeling complex." Saravanan M., Wuerges J., Bose D., McCormack E.A., Cook N.J., Zhang X., Wigley D.B. Proc. Natl. Acad. Sci. U.S.A. 109:20883-20888(2012) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 248-881, ELECTRON MICROSCOPY, FUNCTION, SUBUNIT.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X94335 Genomic DNA. Translation: CAA64058.1.
Z75049 Genomic DNA. Translation: CAA99341.1.
BK006948 Genomic DNA. Translation: DAA10913.1.

PIR

S67026.

RefSeq

NP_014784.1. NM_001183560.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
4AM6	X-ray	2.70	A/B	248-881	[»]
4AM7	X-ray	3.25	A/B	248-881	[»]

ProteinModelPortal

Q12386.

SMR

Q12386. Positions 259-881.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-6706N.

IntAct

Q12386. 27 interactions.

MINT

MINT-659970.

STRING

4932.YOR141C.

Proteomic databases

PaxDb

Q12386.

PeptideAtlas

Q12386.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YOR141C; YOR141C; YOR141C.

GeneID

854309.

KEGG

sce:YOR141C.

Organism-specific databases

CYGD

YOR141c.

SGD

S000005667. ARP8.

Phylogenomic databases

eggNOG

COG5277.

GeneTree

ENSGT00390000001763.

HOGENOM

HOG000246531.

KO

K11673.

OMA

TFQDADI.

OrthoDB

EOG4D29Z6.

Gene expression databases

Genevestigator

Q12386.

GermOnline

YOR141C. 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

976325.

Entry information

Entry name

ARP8_YEAST

Accession

Primary (citable) accession number: Q12386
Secondary accession number(s): D6W2J7

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1996
Last modified:	May 1, 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