Villin-1
protein-coding gene in the species Homo sapiens
Villin-1 is a 92.5 kDa tissue-specific actin-binding protein associated with the actin core bundle of the brush border. Villin-1 is encoded by the VIL1 gene. Villin-1 contains multiple gelsolin-like domains capped by a small (8.5 kDa) "headpiece" at the C-terminus consisting of a fast and independently folding three-helix bundle that is stabilized by hydrophobic interactions. The headpiece domain is a commonly studied protein in molecular dynamics due to its small size and fast folding kinetics and short primary sequence.
Expression
Villin-1 is an actin binding protein expressed mainly in the brush border of the epithelium in vertebrates but sometimes it is ubiquitously expressed in protists and plants. Villin is found localized in the microvilli of the brush border of the epithelium lining of the gut and renal tubules in vertebrates.
Structure
Villin-1 consists of seven domains: six homologous domains that form the N-terminal core and a seventh domain that forms the C-terminal headpiece (cap). The core comprises approximately 150 amino acid residues organized into six repeated segments, while the C-terminal headpiece is an 87-residue hydrophobic region. Villin contains three phosphatidylinositol 4,5-bisphosphate (PIP2) binding sites, one in the headpiece and two in the core domain.
The C-terminal headpiece (HP67) is a compact, independently folded 70-amino-acid domain that contains the principal F-actin-binding site.
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Datasets, specimens, observations and peer-reviewed methods provide the appropriate test for the technical claims summarized here. The source revision retrieved here is dated Sep 13, 2026. The linked authority identifier is Q18032328. None of the 0 selected statements returned an explicit reference.
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