LIS - Legume Information System
Information about legume traits for crop improvement
GlycineMine
v5.1.0.3
Glycine data from LIS
v5.1.0.3
Glycine data from LIS
| Type | Family |
| Description | 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 [ , ]. It can be regulated by Ca2+ and phosphoinositides []. The interaction between gelsolin and tropomyosin modulates actin dynamics []. Gelsolin also plays a role in ciliogenesis []. The structure of gelsolin has been solved []. 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 [ ]. In addition, villin's activity is important for actin bundling in certain cell types []. It was first isolated as a major component of the core of intestinal microvilli [].Villin/gelsolin family includes other actin-binding proteins such as severin and supervillin [ ]. 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 []. |
| Short Name | Villin/Gelsolin |
