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A7MB62 (ARP2_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 46. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Actin-related protein 2
Alternative name(s):
Actin-like protein 2
Gene names
Name:ACTR2
Synonyms:ARP2
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length394 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.

Subunit structure

Component of the Arp2/3 complex composed of ARP2, ARP3, ARPC1B/p41-ARC, ARPC2/p34-ARC, ARPC3/p21-ARC, ARPC4/p20-ARC and ARPC5/p16-ARC.

Subcellular location

Cytoplasm › cytoskeleton By similarity. Cell projection By similarity.

Sequence similarities

Belongs to the actin family. ARP2 subfamily.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

WASLQ951072EBI-6162748,EBI-6162776

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 394394Actin-related protein 2
PRO_0000327246

Regions

Nucleotide binding160 – 1623ATP
Nucleotide binding214 – 2185ATP
Nucleotide binding305 – 3106ATP

Amino acid modifications

Modified residue2991N6-acetyllysine By similarity
Modified residue3221N6-acetyllysine By similarity

Secondary structure

1 ............................................................. 394
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
A7MB62 [UniParc].

Last modified October 2, 2007. Version 1.
Checksum: 1BFA6B442ED1A797

FASTA39444,761
        10         20         30         40         50         60 
MDSQGRKVVV CDNGTGFVKC GYAGSNFPEH IFPALVGRPI IRSTTKVGNI EIKDLMVGDE 

        70         80         90        100        110        120 
ASELRSMLEV NYPMENGIVR NWDDMKHLWD YTFGPEKLNI DTRNCKILLT EPPMNPTKNR 

       130        140        150        160        170        180 
EKIVEVMFET YQFSGVYVAI QAVLTLYAQG LLTGVVVDSG DGVTHICPVY EGFSLPHLTR 

       190        200        210        220        230        240 
RLDIAGRDIT RYLIKLLLLR GYAFNHSADF ETVRMIKEKL CYVGYNIEQE QKLALETTVL 

       250        260        270        280        290        300 
VESYTLPDGR IIKVGGERFE APEALFQPHL INVEGVGVAE LLFNTIQAAD IDTRSEFYKH 

       310        320        330        340        350        360 
IVLSGGSTMY PGLPSRLERE LKQLYLERVL KGDVEKLSKF KIRIEDPPRR KHMVFLGGAV 

       370        380        390 
LADIMKDKDN FWMTRQEYQE KGVRVLEKLG VTVR

« Hide

References

« Hide 'large scale' references
[1]NIH - Mammalian Gene Collection (MGC) project
Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Hereford.
Tissue: Fetal skin.
[2]"Crystal structure of Arp2/3 complex."
Robinson R.C., Turbedsky K., Kaiser D.A., Marchand J.-B., Higgs H.N., Choe S., Pollard T.D.
Science 294:1679-1684(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF ARP2/3 COMPLEX.
[3]"Crystal structures of actin-related protein 2/3 complex with bound ATP or ADP."
Nolen B.J., Littlefield R.S., Pollard T.D.
Proc. Natl. Acad. Sci. U.S.A. 101:15627-15632(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF ARP2/3 COMPLEX WITH BOUND ATP.
[4]"Insights into the influence of nucleotides on actin family proteins from seven structures of Arp2/3 complex."
Nolen B.J., Pollard T.D.
Mol. Cell 26:449-457(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.46 ANGSTROMS) OF ARP2/3 COMPLEX WITH BOUND ATP.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BC151356 mRNA. Translation: AAI51357.1.
IPIIPI00867472.
RefSeqNP_001095683.1. NM_001102213.1.
UniGeneBt.3684.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1K8KX-ray2.00B1-394[»]
1TYQX-ray2.55B1-394[»]
1U2VX-ray2.55B1-394[»]
2P9IX-ray2.46B1-394[»]
2P9KX-ray2.59B1-394[»]
2P9LX-ray2.65B1-394[»]
2P9NX-ray2.85B1-394[»]
2P9PX-ray2.90B1-394[»]
2P9SX-ray2.68B1-394[»]
2P9UX-ray2.75B1-394[»]
3DXKX-ray2.70B1-394[»]
3DXMX-ray2.85B1-394[»]
3RSEX-ray2.65B1-394[»]
3UKRX-ray2.48B1-394[»]
3UKUX-ray2.75B1-394[»]
3ULEX-ray2.50B1-394[»]
ProteinModelPortalA7MB62.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-29789N.
IntActA7MB62. 1 interaction.
STRING9913.ENSBTAP00000012872.

Proteomic databases

PaxDbA7MB62.
PRIDEA7MB62.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID538486.
KEGGbta:538486.

Organism-specific databases

CTD10097.

Phylogenomic databases

eggNOGCOG5277.
HOGENOMHOG000233340.
HOVERGENHBG003771.
InParanoidA7MB62.
OrthoDBEOG4HMJ9D.

Family and domain databases

InterProIPR004000. Actin-related.
IPR020902. Actin/actin-like_CS.
IPR027306. Arp2.
[Graphical view]
PANTHERPTHR11937. PTHR11937. 1 hit.
PTHR11937:SF37. PTHR11937:SF37. 1 hit.
PfamPF00022. Actin. 1 hit.
[Graphical view]
PRINTSPR00190. ACTIN.
SMARTSM00268. ACTIN. 1 hit.
[Graphical view]
PROSITEPS01132. ACTINS_ACT_LIKE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceA7MB62.
NextBio20877389.

Entry information

Entry nameARP2_BOVIN
AccessionPrimary (citable) accession number: A7MB62
Entry history
Integrated into UniProtKB/Swiss-Prot: April 8, 2008
Last sequence update: October 2, 2007
Last modified: May 29, 2013
This is version 46 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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