The domain within your query sequence starts at position and ends at position ; the E-value for the VHP domain shown below is < 1e-12.
VHPVillin headpiece domain
|SMART accession number:||SM00153|
|Interpro abstract (IPR003128):|
Villin is an F-actin bundling protein involved in the maintenance of the microvilli of the absorptive epithelia. The villin-type "headpiece" domain is a modular motif found at the extreme C terminus of larger "core" domains in over 25 cytoskeletal proteins in plants and animals, often in assocation with the Gelsolin repeat. Although the headpiece is classified as an F-actin-binding domain, it has been shown that not all headpiece domains are intrinsically F-actin-binding motifs, surface charge distribution may be an important element for F-actin recognition [(PUBMED:11977079)]. An autonomously folding, 35 residue, thermostable subdomain (HP36) of the full-length 76 amino acid residue villin headpiece, is the smallest known example of a cooperatively folded domain of a naturally occurring protein. The structure of HP36, as determined by NMR spectroscopy, consists of three short helices surrounding a tightly packed hydrophobic core [(PUBMED:12095260)].
|GO process:||cytoskeleton organization (GO:0007010)|
|GO function:||actin binding (GO:0003779)|
Click on the following links for more information.
- Evolution (species in which this domain is found)
- Cellular role (predicted cellular role)
- Literature (relevant references for this domain)
- Metabolism (metabolic pathways involving proteins which contain this domain)
- Structure (3D structures containing this domain)
- Links (links to other resources describing this domain)