GELGelsolin homology domain
|SMART accession number:||SM00262|
|Description:||Gelsolin/severin/villin homology domain. Calcium-binding and actin-binding. Both intra- and extracellular domains.|
|Interpro abstract (IPR007122):|
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 [(PUBMED:14527663), (PUBMED:3023087)]. It can be regulated by Ca2+ and phosphoinositides [(PUBMED:3027569)]. The interaction between gelsolin and tropomyosin modulates actin dynamics [(PUBMED:23844991)]. Gelsolin also plays a role in ciliogenesis [(PUBMED:20393563)]. The structure of gelsolin has been solved [(PUBMED: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 [(PUBMED:3087992)]. In addition, villin's activity is important for actin bundling in certain cell types [(PUBMED:2256904)]. It was first isolated as a major component of the core of intestinal microvilli [(PUBMED:287075)].
Villin/gelsolin family includes other actin-binding proteins such as severin and supervillin [(PUBMED: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 [(PUBMED:2850369)].
|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)
- Disease (disease genes where sequence variants are found in 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)