Villin/Gelsolin (IPR007122)

Short name: Villin/Gelsolin

Overlapping homologous superfamilies


Family relationships


Gelsolin is an actin-modulating protein that severs F-actin, caps the barbed ends of actin filaments preventing monomer exchange, and promotes the nucleation step of actin polymerisation [PMID: 14527663, PMID: 3023087]. It can be regulated by Ca2+ and phosphoinositides [PMID: 3027569]. The interaction between gelsolin and tropomyosin modulates actin dynamics [PMID: 23844991]. Gelsolin also plays a role in ciliogenesis [PMID: 20393563]. The structure of gelsolin has been solved [PMID: 9288746].

Villin is an actin-binding protein that is found in a variety of tissues. It is able to bind to the barbed end of actin filaments with high affinity and can sever filaments [PMID: 3087992]. In addition, villin's activity is important for actin bundling in certain cell types [PMID: 2256904]. It was first isolated as a major component of the core of intestinal microvilli [PMID: 287075].

Villin/gelsolin family includes other actin-binding proteins such as severin and supervillin [PMID: 15526166]. Six large repeating segments occur in gelsolin and villin, and 3 similar segments in severin and fragmin. While the multiple repeats have yet to be related to any known function of the actin-severing proteins, the superfamily appears to have evolved from an ancestral sequence of 120 to 130 amino acid residues [PMID: 2850369].

GO terms

Biological Process

No terms assigned in this category.

Molecular Function

GO:0051015 actin filament binding

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.