Reviewed, UniProtKB/Swiss-Prot P32390 (ARP3_SCHPO)

Names and origin

Protein names

Recommended name:
    Actin-related protein 3
Alternative name(s):
    Actin-like protein 3

Gene names

Name:	act2
ORF Names:	SPAC630.03

Organism

Schizosaccharomyces pombe (Fission yeast) [Complete proteome]

Taxonomic identifier

4896 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	427 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. May be involved in cytokinesis.
Subunit structure	Component of the Arp2/3 complex composed of arp2, act2, arc1/p41-ARC, arc2/p34-ARC, arc3/p21-ARC, arc4/p20-ARC and arc5/p16-ARC.
Subcellular location	Cytoplasm › cytoskeleton › actin patch.
Sequence similarities	Belongs to the actin family. ARP3 subfamily.

Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton
Ligand	ATP-binding Actin-binding Nucleotide-binding
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	cytokinesis, contractile ring formation Inferred from mutant phenotype. Source: GeneDB_SPombe establishment or maintenance of cell polarity Inferred from mutant phenotype. Source: GeneDB_SPombe regulation of actin filament polymerization Inferred from electronic annotation. Source: InterPro
Cellular component	actin cortical patch Inferred from direct assay. Source: GeneDB_SPombe cytosol Inferred from direct assay. Source: GeneDB_SPombe
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW actin binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 427

427

Actin-related protein 3

PRO_0000089088

Secondary structure

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427

Helix Strand Turn

Details...

Beta strand

8 – 10

3

Helix

79 – 82

4

Helix

102 – 114

13

Helix

121 – 123

3

Beta strand

126 – 130

5

Helix

136 – 146

11

Turn

147 – 150

4

Beta strand

156 – 159

4

Helix

160 – 166

7

Helix

167 – 170

4

Beta strand

171 – 173

3

Beta strand

183 – 185

3

Beta strand

191 – 194

4

Beta strand

207 – 210

4

Helix

215 – 222

8

Helix

235 – 244

10

Helix

251 – 257

7

Helix

285 – 288

4

Helix

290 – 293

4

Helix

296 – 298

3

Helix

307 – 316

10

Helix

320 – 323

4

Beta strand

330 – 333

4

Helix

347 – 354

8

Turn

383 – 387

5

Helix

392 – 395

4

Helix

406 – 411

6

Helix

415 – 417

3

Sequences

	Sequence		Length	Mass (Da)
	P32390-1 [UniParc]. Last modified October 1, 1993. Version 1. Checksum: C7909FFEE544789B	FASTA	427	47,373
	10 20 30 40 50 60 MASFNVPIIM DNGTGYSKLG YAGNDAPSYV FPTVIATRSA GASSGPAVSS KPSYMASKGS 70 80 90 100 110 120 GHLSSKRATE DLDFFIGNDA LKKASAGYSL DYPIRHGQIE NWDHMERFWQ QSLFKYLRCE 130 140 150 160 170 180 PEDHYFLLTE PPLNPPENRE NTAEIMFESF NCAGLYIAVQ AVLALAASWT SSKVTDRSLT 190 200 210 220 230 240 GTVVDSGDGV THIIPVAEGY VIGSSIKTMP LAGRDVTYFV QSLLRDRNEP DSSLKTAERI 250 260 270 280 290 300 KEECCYVCPD IVKEFSRFDR EPDRYLKYAS ESITGHSTTI DVGFERFLAP EIFFNPEIAS 310 320 330 340 350 360 SDFLTPLPEL VDNVVQSSPI DVRKGLYKNI VLSGGSTLFK NFGNRLQRDL KRIVDERIHR 370 380 390 400 410 420 SEMLSGAKSG GVDVNVISHK RQRNAVWFGG SLLAQTPEFG SYCHTKADYE EYGASIARRY QIFGNSL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of act2, an essential gene in the fission yeast Schizosaccharomyces pombe that encodes a protein related to actin." Lees-Miller J.P., Henry G., Helfman D.M. Proc. Natl. Acad. Sci. U.S.A. 89:80-83(1992) [PubMed: 1729722] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 38366 / 972.
[3]	"A mutant of arp2p causes partial disassembly of the Arp2/3 complex and loss of cortical actin function in fission yeast." Morrell J.L., Morphew M., Gould K.L. Mol. Biol. Cell 10:4201-4215(1999) [PubMed: 10588653] [Abstract] Cited for: IDENTIFICATION IN THE ARP2/3 COMPLEX.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

M81068 Genomic DNA. No translation available.
CU329670 Genomic DNA. Translation: CAB52725.1.

PIR

A41790.

RefSeq

NP_592898.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3DWL	X-ray	3.78	A/B	1-427	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

P32390.

Genome annotation databases

GeneID

2543233.

GenomeReviews

Gene locus act2 in contig CU329670_GR.

KEGG

spo:SPAC630.03.

NMPDR

fig|4896.1.peg.2868.

Organism-specific databases

GeneDB_Spombe

SPAC630.03.

Phylogenomic databases

OMA

RVEPEDH

OrthoDB

EOG95MPNF

Gene expression databases

ArrayExpress

P32390.

Family and domain databases

InterPro

IPR004000. Actin-like.
IPR015623. Arp3.
[Graphical view]

PANTHER

PTHR11937. Actin_like. 1 hit.
PTHR11937:SF31. Arp3. 1 hit.

Pfam

PF00022. Actin. 1 hit.
[Graphical view]

SMART

SM00268. ACTIN. 1 hit.
[Graphical view]

PROSITE

PS01132. ACTINS_ACT_LIKE. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

ARP3_SCHPO

Accession

Primary (citable) accession number: P32390

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	October 1, 1993
Last modified:	November 24, 2009
This is version 73 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)