The domain within your query sequence starts at position 14 and ends at position 111; the E-value for the GEL domain shown below is 9.44e-24.



Gelsolin 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 filament binding (GO:0051015)
Family alignment:
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There are 34141 GEL domains in 8112 proteins in SMART's nrdb database.

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