Villin-1
| Villin-1 | |||||||
|---|---|---|---|---|---|---|---|
| Identifiers | |||||||
| Symbol | VIL1 | ||||||
| Alt. symbols | VIL | ||||||
| NCBI gene | 7429 | ||||||
| HGNC | 12690 | ||||||
| OMIM | 193040 | ||||||
| RefSeq | NM_007127 | ||||||
| UniProt | P09327 | ||||||
| Other data | |||||||
| Locus | Chr. 2 q35-q36 | ||||||
| 
 | |||||||
| villin 2 (ezrin) | |||||||
|---|---|---|---|---|---|---|---|
| Identifiers | |||||||
| Symbol | VIL2 | ||||||
| NCBI gene | 7430 | ||||||
| HGNC | 12691 | ||||||
| OMIM | 123900 | ||||||
| RefSeq | NM_003379 | ||||||
| UniProt | P15311 | ||||||
| Other data | |||||||
| Locus | Chr. 6 q22-q27 | ||||||
| 
 | |||||||
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.