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Q3MHR7 (ARPC2_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 72. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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

Names and origin

Protein namesRecommended name:
Actin-related protein 2/3 complex subunit 2
Alternative name(s):
Arp2/3 complex 34 kDa subunit
Short name=p34-ARC
Gene names
Name:ARPC2
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length300 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Functions as actin-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 mother actin filament By similarity.

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. Interacts with SHANK3; the interaction probably mediates the association of SHANK3 with the Arp2/3 complex.

Subcellular location

Cytoplasmcytoskeleton By similarity. Cell projection By similarity. Cell junctionsynapsesynaptosome By similarity.

Sequence similarities

Belongs to the ARPC2 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 300300Actin-related protein 2/3 complex subunit 2
PRO_0000246170

Amino acid modifications

Modified residue2751N6-acetyllysine By similarity
Modified residue2951N6-acetyllysine By similarity

Secondary structure

................................................. 300
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q3MHR7 [UniParc].

Last modified October 25, 2005. Version 1.
Checksum: 60801D999BFBF947

FASTA30034,349
        10         20         30         40         50         60 
MILLEVNNRI IEETLALKFE NAAAGNKPEA VEVTFADFDG VLYHISNPNG DKTKVMVSIS 

        70         80         90        100        110        120 
LKFYKELQAH GADELLKRVY GSYLVNPESG YNVSLLYDLE NLPASKDSIV HQAGMLKRNC 

       130        140        150        160        170        180 
FASVFEKYFQ FQEEGKEGEN RAVIHYRDDE TMYVESKKDR VTVVFSTVFK DDDDVVIGKV 

       190        200        210        220        230        240 
FMQEFKEGRR ASHTAPQVLF SHREPPLELK DTDAAVGDNI GYITFVLFPR HTNASARDNT 

       250        260        270        280        290        300 
INLIHTFRDY LHYHIKCSKA YIHTRMRAKT SDFLKVLNRA RPDAEKKEMK TITGKTFSSR 

« Hide

References

« Hide 'large scale' references
[1]NIH - Mammalian Gene Collection (MGC) project
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Crossbred X Angus.
Tissue: Ileum.
[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 THE 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 THE ARP2/3 COMPLEX WITH BOUND ATP.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC105136 mRNA. Translation: AAI05137.1.
RefSeqNP_001029885.1. NM_001034713.2.
UniGeneBt.6846.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1K8KX-ray2.00D1-300[»]
1TYQX-ray2.55D1-300[»]
1U2VX-ray2.55D1-300[»]
2P9IX-ray2.46D1-300[»]
2P9KX-ray2.59D1-300[»]
2P9LX-ray2.65D1-300[»]
2P9NX-ray2.85D1-300[»]
2P9PX-ray2.90D1-300[»]
2P9SX-ray2.68D1-300[»]
2P9UX-ray2.75D1-300[»]
3DXKX-ray2.70D1-300[»]
3DXMX-ray2.85D1-300[»]
3RSEX-ray2.65D1-300[»]
3UKRX-ray2.48D1-300[»]
3UKUX-ray2.75D1-300[»]
3ULEX-ray2.50D1-300[»]
4JD2X-ray3.08D1-300[»]
ProteinModelPortalQ3MHR7.
SMRQ3MHR7. Positions 1-283.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-29792N.
IntActQ3MHR7. 1 interaction.
STRING9913.ENSBTAP00000013707.

Proteomic databases

PaxDbQ3MHR7.
PRIDEQ3MHR7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000013707; ENSBTAP00000013707; ENSBTAG00000010386.
GeneID540838.
KEGGbta:540838.

Organism-specific databases

CTD10109.

Phylogenomic databases

eggNOGNOG327379.
GeneTreeENSGT00390000016794.
HOGENOMHOG000212535.
HOVERGENHBG050580.
InParanoidQ3MHR7.
KOK05758.
OMAYFKFQEE.
OrthoDBEOG73JKVS.
TreeFamTF315006.

Enzyme and pathway databases

ReactomeREACT_227097. Immune System.

Family and domain databases

InterProIPR007188. P34-arc.
[Graphical view]
PANTHERPTHR12058. PTHR12058. 1 hit.
PfamPF04045. P34-Arc. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ3MHR7.
NextBio20878864.

Entry information

Entry nameARPC2_BOVIN
AccessionPrimary (citable) accession number: Q3MHR7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: October 25, 2005
Last modified: May 14, 2014
This is version 72 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references