Skip Header

Contribute Send feedback
Read comments (?) or add your own

P32390 (ARP3_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Actin-related protein 3
Alternative name(s):
Actin-like protein 3
Gene names
Name:act2
ORF Names:SPAC630.03
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length427 AA.
Sequence statusComplete.
Protein existenceEvidence 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 427427Actin-related protein 3
PRO_0000089088

Secondary structure

1 ..................................................... 427
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P32390 [UniParc].

Last modified October 1, 1993. Version 1.
Checksum: C7909FFEE544789B

FASTA42747,373
        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

« Hide

References

« Hide '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. expand/collapse author list , 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: 972 / ATCC 24843.
[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

EMBL
GenBank
DDBJ		M81068 Genomic DNA. No translation available.
CU329670 Genomic DNA. Translation: CAB52725.1.
PIRA41790.
RefSeqNP_592898.1. NM_001018298.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3DWLX-ray3.78A/B1-427[»]
ProteinModelPortalP32390.
SMRP32390. Positions 7-425.
ModBaseSearch...

Protein-protein interaction databases

IntActP32390. 1 interaction.
STRINGP32390.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPAC630.03.1; SPAC630.03.1:pep; SPAC630.03.
GeneID2543233.
GenomeReviewsGene locus act2 in contig CU329670_GR.
KEGGspo:SPAC630.03.
NMPDRfig|4896.1.peg.2868.

Organism-specific databases

GeneDB_SpombeSPAC630.03.

Phylogenomic databases

eggNOGfuNOG07614.
GeneTreeEFGT00050000001097.
HOGENOMHBG559892.
OMADNVIQNC.
OrthoDBEOG45XC4K.

Enzyme and pathway databases

BioCycSPOM-XXX-01:SPOM-XXX-01-000629-MONOMER.

Gene expression databases

ArrayExpressP32390.

Family and domain databases

InterProIPR004000. Actin-like.
IPR020902. Actin/actin-like_CS.
IPR015623. Arp3.
[Graphical view]
PANTHERPTHR11937. Actin_like. 1 hit.
PTHR11937:SF31. Arp3. 1 hit.
PfamPF00022. Actin. 1 hit.
[Graphical view]
SMARTSM00268. ACTIN. 1 hit.
[Graphical view]
PROSITEPS01132. ACTINS_ACT_LIKE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameARP3_SCHPO
AccessionPrimary (citable) accession number: P32390
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: December 14, 2011
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents