Reviewed, UniProtKB/Swiss-Prot P32381 (ARP2_YEAST)

Names and origin

Protein names

Recommended name:
    Actin-related protein 2
Alternative name(s):
    Actin-like protein ARP2
      Short name=Actin-like protein 2

Gene names

Name:	ARP2
Synonyms:	ACT2
Ordered Locus Names:	YDL029W
ORF Names:	D2778

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	391 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Functions as ATP-binding component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks. Seems to contact the pointed end of the daughter actin filament By similarity.
Subunit structure	Component of the Arp2/3 complex composed of ARP2, ARP3, ARC40/p41-ARC, ARC35/p34-ARC, ARC18/p21-ARC, ARC19/p20-ARC and ARC16/p16-ARC.
Subcellular location	Cytoplasm › cytoskeleton › actin patch. Ref.3 Ref.5
Miscellaneous	Present with 6650 molecules/cell in log phase SD medium. Ref.6
Sequence similarities	Belongs to the actin family. ARP2 subfamily.

Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton
Ligand	ATP-binding Actin-binding Nucleotide-binding
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	ATP catabolic process Inferred from mutant phenotype. Source: SGD Arp2/3 complex-mediated actin nucleation Inferred from mutant phenotype. Source: SGD ascospore wall assembly Inferred from mutant phenotype. Source: SGD establishment of mitochondrion localization Inferred from mutant phenotype. Source: SGD mitochondrion inheritance Ref.5 Inferred from mutant phenotype. Source: SGD
Cellular component	Arp2/3 protein complex Inferred from direct assay. Source: SGD actin cortical patch Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrion Ref.5 Inferred from direct assay. Source: SGD
Molecular function	ATP binding Inferred from direct assay. Source: SGD ATPase activity Inferred from mutant phenotype. Source: SGD actin binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
	P43582	1	EBI-2927,EBI-22766
	Q12156	1	EBI-2927,EBI-30371
ARC35	P53731	1	EBI-2927,EBI-2770
ARC40	P38328	1	EBI-2927,EBI-2777
ARO8	P53090	1	EBI-2927,EBI-2042933
ARP3	P47117	1	EBI-2927,EBI-2933
DBP5	P20449	1	EBI-2927,EBI-5617
ESS1	P22696	1	EBI-2927,EBI-6679
GLN1	P32288	1	EBI-2927,EBI-7665
INO1	P11986	1	EBI-2927,EBI-9257
IPP1	P00817	1	EBI-2927,EBI-9338
LAS17	Q12446	2	EBI-2927,EBI-10022
MYO5	Q04439	1	EBI-2927,EBI-11687
PGM2	P37012	1	EBI-2927,EBI-13296
PRP40	P33203	1	EBI-2927,EBI-701
RNR1	P21524	1	EBI-2927,EBI-15234
RNR2	P09938	1	EBI-2927,EBI-15240
RSP5	P39940	1	EBI-2927,EBI-16219
SET2	P46995	1	EBI-2927,EBI-16985
URN1	Q06525	1	EBI-2927,EBI-35138
VRP1	P37370	1	EBI-2927,EBI-20502

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 391	391	Actin-related protein 2		PRO_0000089077
Regions
	Nucleotide binding	159 – 161	3	ATP By similarity
	Nucleotide binding	213 – 217	5	ATP By similarity
	Nucleotide binding	304 – 309	6	ATP By similarity
Amino acid modifications
	Modified residue	46	1	Phosphoserine Ref.7
	Modified residue	66	1	Phosphotyrosine Ref.7

Sequences

	Sequence		Length	Mass (Da)
	P32381-1 [UniParc]. Last modified October 1, 1993. Version 1. Checksum: 4C9E8952B477A1B9	FASTA	391	44,074
	10 20 30 40 50 60 MDPHNPIVLD QGTGFVKIGR AGENFPDYTF PSIVGRPILR AEERASVATP LKDIMIGDEA 70 80 90 100 110 120 SEVRSYLQIS YPMENGIIKN WTDMELLWDY AFFEQMKLPS TSNGKILLTE PPMNPLKNRE 130 140 150 160 170 180 KMCEVMFEKY DFGGVYVAIQ AVLALYAQGL SSGVVVDSGD GVTHIVPVYE SVVLSHLTRR 190 200 210 220 230 240 LDVAGRDVTR HLIDLLSRRG YAFNRTADFE TVRQIKEKLC YVSYDLDLDT KLARETTALV 250 260 270 280 290 300 ESYELPDGRT IKVGQERFEA PECLFQPGLV DVEQPGVGEL LFNTVQSADV DIRSSLYKAI 310 320 330 340 350 360 VLSGGSSMYP GLPSRLEKEL KQLWFSRVLH NDPSRLDKFK VRIEDPPRRK HMVFIGGAVL 370 380 390 ASIMADKDHM WLSKQEWQES GPSAMTKFGP R

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"New yeast actin-like gene required late in the cell cycle." Schwob E., Martin R.P. Nature 355:179-182(1992) [PubMed: 1729653] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 26109 / X2180.
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV." Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T. , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P. Nature 387:75-78(1997) [PubMed: 9169867] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[3]	"The complex containing actin-related proteins Arp2 and Arp3 is required for the motility and integrity of yeast actin patches." Winter D., Podtelejnikov A.V., Mann M., Li R. Curr. Biol. 7:519-529(1997) [PubMed: 9210376] [Abstract] Cited for: IDENTIFICATION IN THE ARP2/3 COMPLEX, SUBCELLULAR LOCATION.
[4]	Erratum Winter D., Podtelejnikov A.V., Mann M., Li R. Curr. Biol. 7:R593-R593(1997)
[5]	"Arp2/3 complex and actin dynamics are required for actin-based mitochondrial motility in yeast." Boldogh I.R., Yang H.C., Nowakowski W.D., Karmon S.L., Hays L.G., Yates J.R. III, Pon L.A. Proc. Natl. Acad. Sci. U.S.A. 98:3162-3167(2001) [PubMed: 11248049] [Abstract] Cited for: SUBCELLULAR LOCATION.
[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: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[7]	"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: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46 AND TYR-66, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X61502 Genomic DNA. Translation: CAA43718.1. Z71781 Genomic DNA. Translation: CAA96460.1. Z74077 Genomic DNA. Translation: CAA98588.1.
PIR	S20225.
RefSeq	NP_010255.1.
3D structure databases
HSSP	HSSP built from PDB template 1K8K based on UniProtKB P32391.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:2217N.
IntAct	P32381. 70 interactions.
STRING	P32381.
Proteomic databases
PeptideAtlas	P32381.
PRIDE	P32381.
Genome annotation databases
Ensembl	YDL029W; YDL029W; YDL029W; Saccharomyces cerevisiae. [Genome view]
GeneID	851532.
GenomeReviews	Gene locus YDL029W in contig Z71256_GR.
KEGG	sce:YDL029W.
NMPDR	fig|4932.3.peg.995.
Organism-specific databases
CYGD	YDL029w.
SGD	S000002187. ARP2.
Phylogenomic databases
HOGENOM	P32381.
OMA	SMVGRPI.
Gene expression databases
ArrayExpress	P32381.
Genevestigator	P32381.
GermOnline	YDL029W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR004000. Actin-like. [Graphical view]
PANTHER	PTHR11937. Actin_like. 1 hit.
Pfam	PF00022. Actin. 1 hit. [Graphical view]
PRINTS	PR00190. ACTIN.
SMART	SM00268. ACTIN. 1 hit. [Graphical view]
PROSITE	PS01132. ACTINS_ACT_LIKE. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	968926.

Entry information

Entry name

ARP2_YEAST

Accession

Primary (citable) accession number: P32381

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	October 1, 1993
Last modified:	November 3, 2009
This is version 85 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)