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 a cytoplasmic, calcium-regulated, actin-modulating protein that binds to the barbed ends of actin filaments, preventing monomer exchange (end-blocking or capping) [(PUBMED:3023087)]. It can promote nucleation (the assembly of monomers into filaments), as well as sever existing filaments. In addition, this protein binds with high affinity to fibronectin. Plasma gelsolin and cytoplasmic gelsolin are derived from a single gene by alternate initiation sites and differential splicing.
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)|
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- Evolution (species in which this domain is found)
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