Summary: ARP2/3 complex 16 kDa subunit (p16-Arc)
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ARP2/3 complex 16 kDa subunit (p16-Arc) Provide feedback
The Arp2/3 protein complex has been implicated in the control of actin polymerisation. The human complex consists of seven subunits which include the actin related proteins Arp2 and Arp3, and five others referred to as p41-Arc, p34-Arc, p21-Arc, p20-Arc, and p16-Arc. The precise function of p16-Arc is currently unknown. Its structure consists of a single domain containing a bundle of seven alpha helices [1,2].
Literature references
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Welch MD, DePace AH, Verma S, Iwamatsu A, Mitchison TJ; , J Cell Biol 1997;138:375-384.: The human Arp2/3 complex is composed of evolutionarily conserved subunits and is localized to cellular regions of dynamic actin filament assembly. PUBMED:9230079 EPMC:9230079
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Robinson RC, Turbedsky K, Kaiser DA, Marchand JB, Higgs HN, Choe S, Pollard TD; , Science 2001;294:1679-1684.: Crystal structure of Arp2/3 complex. PUBMED:11721045 EPMC:11721045
Internal database links
SCOOP: | Utp12 |
This tab holds annotation information from the InterPro database.
InterPro entry IPR006789
Arp2/3 binds to pre-existing actin filaments and nucleates new daughter filaments, and thus becomes incorporated into the dynamic actin network at the leading edge of motile cells and other actin-based protrusive structures [ PUBMED:9600938 ]. In order to nucleate filaments, Arp2/3 must bind to a member of the N-WASp/SCAR family protein [ PUBMED:9889097 ]. Arp2 and Arp3 are thought to be brought together after activation, forming an actin-like nucleus for actin monomers to bind and create a new actin filament. In the absence of an activating protein, Arp2/3 shows very little nucleation activity. Recent research has focused on the binding and hydrolysis of ATP by Arp2 and Arp3 [ PUBMED:11752435 ], and crystal structures of the Arp2/3 complex have been solved [ PUBMED:15505213 ].
The human Arp2/3 complex consists of ARP2, ARP3, ARPC1B/p41-ARC, ARPC2/p34-ARC, ARPC3/p21-ARC, ARPC4/p20-ARC and ARPC5/p16-ARC. This family represents the ARPC5/p16-ARC subunit.
Gene Ontology
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
Cellular component | Arp2/3 protein complex (GO:0005885) |
actin cytoskeleton (GO:0015629) | |
Biological process | regulation of actin filament polymerization (GO:0030833) |
Arp2/3 complex-mediated actin nucleation (GO:0034314) |
Domain organisation
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Alignments
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Seed (119) |
Full (1973) |
Representative proteomes | UniProt (3375) |
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RP15 (346) |
RP35 (861) |
RP55 (1518) |
RP75 (2045) |
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PP/heatmap | 1 |
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
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Seed (119) |
Full (1973) |
Representative proteomes | UniProt (3375) |
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RP15 (346) |
RP35 (861) |
RP55 (1518) |
RP75 (2045) |
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Raw Stockholm | |||||||
Gzipped |
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
HMM logo
HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...
Trees
This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.
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Curation and family details
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Curation
Seed source: | Pfam-B_4180 (release 7.5) |
Previous IDs: | p16_Arc; |
Type: | Domain |
Sequence Ontology: | SO:0000417 |
Author: |
Waterfield DI |
Number in seed: | 119 |
Number in full: | 1973 |
Average length of the domain: | 142 aa |
Average identity of full alignment: | 37 % |
Average coverage of the sequence by the domain: | 84.31 % |
HMM information
HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
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Model details: |
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Model length: | 150 | ||||||||||||
Family (HMM) version: | 17 | ||||||||||||
Download: | download the raw HMM for this family |
Species distribution
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Structures
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the P16-Arc domain has been found. There are 30 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein sequence.
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AlphaFold Structure Predictions
The list of proteins below match this family and have AlphaFold predicted structures. Click on the protein accession to view the predicted structure.