GEL

Gelsolin homology domain
GEL
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)
Family alignment:
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There are 9348 GEL domains in 2451 proteins in SMART's nrdb database.

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