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Protein

Actin-related protein 3

Gene

act2

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.By similarity

GO - Molecular functioni

GO - Biological processi

  • actin cortical patch assembly Source: PomBase
  • actin cortical patch localization Source: PomBase
  • actin cortical patch organization Source: PomBase
  • actin filament polymerization Source: PomBase
  • Arp2/3 complex-mediated actin nucleation Source: PomBase
  • endocytosis Source: PomBase
  • mitotic actomyosin contractile ring assembly Source: PomBase
Complete GO annotation...

Keywords - Ligandi

Actin-binding, ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Actin-related protein 3
Alternative name(s):
Actin-like protein 3
Gene namesi
Name:act2
ORF Names:SPAC630.03
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC630.03.
PomBaseiSPAC630.03.

Subcellular locationi

GO - Cellular componenti

  • actin cortical patch Source: PomBase
  • Arp2/3 protein complex Source: PomBase
  • cell cortex of cell tip Source: PomBase
  • cell division site Source: PomBase
  • cytoplasm Source: PomBase
  • cytosol Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 427427Actin-related protein 3PRO_0000089088Add
BLAST

Proteomic databases

MaxQBiP32390.

Interactioni

Subunit structurei

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.1 Publication

Protein-protein interaction databases

BioGridi279661. 14 interactions.
IntActiP32390. 3 interactions.
MINTiMINT-4688385.

Structurei

Secondary structure

1
427
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi8 – 103
Helixi79 – 824
Helixi102 – 11413
Helixi121 – 1233
Beta strandi126 – 1305
Helixi136 – 14611
Turni147 – 1504
Beta strandi156 – 1594
Helixi160 – 1667
Helixi167 – 1704
Beta strandi171 – 1733
Beta strandi183 – 1853
Beta strandi191 – 1944
Beta strandi207 – 2104
Helixi215 – 2228
Helixi235 – 24410
Helixi251 – 2577
Helixi285 – 2884
Helixi290 – 2934
Helixi296 – 2983
Helixi307 – 31610
Helixi320 – 3234
Beta strandi330 – 3334
Helixi347 – 3548
Turni383 – 3875
Helixi392 – 3954
Helixi406 – 4116
Helixi415 – 4173

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3DWLX-ray3.78A/B1-427[»]
ProteinModelPortaliP32390.
SMRiP32390. Positions 7-425.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP32390.

Family & Domainsi

Sequence similaritiesi

Belongs to the actin family. ARP3 subfamily.Curated

Phylogenomic databases

HOGENOMiHOG000233339.
InParanoidiP32390.
KOiK18584.
OMAiKMQRYAV.
OrthoDBiEOG7TJ3T6.
PhylomeDBiP32390.

Family and domain databases

InterProiIPR004000. Actin.
IPR020902. Actin/actin-like_CS.
[Graphical view]
PANTHERiPTHR11937. PTHR11937. 2 hits.
PfamiPF00022. Actin. 1 hit.
[Graphical view]
SMARTiSM00268. ACTIN. 1 hit.
[Graphical view]
PROSITEiPS01132. ACTINS_ACT_LIKE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P32390-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASFNVPIIM DNGTGYSKLG YAGNDAPSYV FPTVIATRSA GASSGPAVSS
60 70 80 90 100
KPSYMASKGS GHLSSKRATE DLDFFIGNDA LKKASAGYSL DYPIRHGQIE
110 120 130 140 150
NWDHMERFWQ QSLFKYLRCE PEDHYFLLTE PPLNPPENRE NTAEIMFESF
160 170 180 190 200
NCAGLYIAVQ AVLALAASWT SSKVTDRSLT GTVVDSGDGV THIIPVAEGY
210 220 230 240 250
VIGSSIKTMP LAGRDVTYFV QSLLRDRNEP DSSLKTAERI KEECCYVCPD
260 270 280 290 300
IVKEFSRFDR EPDRYLKYAS ESITGHSTTI DVGFERFLAP EIFFNPEIAS
310 320 330 340 350
SDFLTPLPEL VDNVVQSSPI DVRKGLYKNI VLSGGSTLFK NFGNRLQRDL
360 370 380 390 400
KRIVDERIHR SEMLSGAKSG GVDVNVISHK RQRNAVWFGG SLLAQTPEFG
410 420
SYCHTKADYE EYGASIARRY QIFGNSL
Length:427
Mass (Da):47,373
Last modified:October 1, 1993 - v1
Checksum:iC7909FFEE544789B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M81068 Genomic DNA. No translation available.
CU329670 Genomic DNA. Translation: CAB52725.1.
PIRiA41790.
RefSeqiNP_592898.1. NM_001018298.2.

Genome annotation databases

EnsemblFungiiSPAC630.03.1; SPAC630.03.1:pep; SPAC630.03.
GeneIDi2543233.
KEGGispo:SPAC630.03.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M81068 Genomic DNA. No translation available.
CU329670 Genomic DNA. Translation: CAB52725.1.
PIRiA41790.
RefSeqiNP_592898.1. NM_001018298.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3DWLX-ray3.78A/B1-427[»]
ProteinModelPortaliP32390.
SMRiP32390. Positions 7-425.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi279661. 14 interactions.
IntActiP32390. 3 interactions.
MINTiMINT-4688385.

Proteomic databases

MaxQBiP32390.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC630.03.1; SPAC630.03.1:pep; SPAC630.03.
GeneIDi2543233.
KEGGispo:SPAC630.03.

Organism-specific databases

EuPathDBiFungiDB:SPAC630.03.
PomBaseiSPAC630.03.

Phylogenomic databases

HOGENOMiHOG000233339.
InParanoidiP32390.
KOiK18584.
OMAiKMQRYAV.
OrthoDBiEOG7TJ3T6.
PhylomeDBiP32390.

Miscellaneous databases

EvolutionaryTraceiP32390.
NextBioi20804255.
PROiP32390.

Family and domain databases

InterProiIPR004000. Actin.
IPR020902. Actin/actin-like_CS.
[Graphical view]
PANTHERiPTHR11937. PTHR11937. 2 hits.
PfamiPF00022. Actin. 1 hit.
[Graphical view]
SMARTiSM00268. ACTIN. 1 hit.
[Graphical view]
PROSITEiPS01132. ACTINS_ACT_LIKE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE ARP2/3 COMPLEX.

Entry informationi

Entry nameiARP3_SCHPO
AccessioniPrimary (citable) accession number: P32390
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: November 11, 2015
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.