InterPro : IPR007122

Name  Villin/Gelsolin Short Name  Villin/Gelsolin
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 [].
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Sequence Features

GO Displayer

Proteins

InterPro protein domain ID --> Contigs

 

Other

11 Child Features

Id Name Short Name Type
IPR029919 Protein flightless-1 FliI Family
IPR015628 Supervillin SV/p205 Family
IPR030009 Villin-2/3/4/5, plant Villin-2/3/4/5_plant Family
IPR030004 Gelsolin Gelsolin Family
IPR015626 Villin-like protein Villin-like Family
IPR030016 Villin-like protein quail Quail Family
IPR029917 Macrophage-capping protein CapG Family
IPR030007 Villin Villin Family
IPR030010 Villin-1, plant Villin-1_plant Family
IPR030012 Adseverin Adseverin Family
IPR030014 Advillin Advillin Family

1 Contains

Id Name Short Name Type
IPR007123 Gelsolin-like domain Gelsolin-like_dom Domain

0 Found In

0 Parent Features

11 Publications

First Author Title Year Journal Volume Pages
Burtnick LD The crystal structure of plasma gelsolin: implications for actin severing, capping, and nucleation. 1997 Cell 90 661-70
Weeds AG Preparation and characterization of pig plasma and platelet gelsolins. 1986 Eur J Biochem 161 69-76
Way M Nucleotide sequence of pig plasma gelsolin. Comparison of protein sequence with human gelsolin and other actin-severing proteins shows strong homologies and evidence for large internal repeats. 1988 J Mol Biol 203 1127-33
Friederich E From the structure to the function of villin, an actin-binding protein of the brush border. 1990 Bioessays 12 403-8
Silacci P Gelsolin superfamily proteins: key regulators of cellular functions. 2004 Cell Mol Life Sci 61 2614-23
Northrop J Different calcium dependence of the capping and cutting activities of villin. 1986 J Biol Chem 261 9274-81
Bretscher A Villin: the major microfilament-associated protein of the intestinal microvillus. 1979 Proc Natl Acad Sci U S A 76 2321-5
McGough AM The gelsolin family of actin regulatory proteins: modular structures, versatile functions. 2003 FEBS Lett 552 75-81
Khaitlina S The interaction of gelsolin with tropomyosin modulates actin dynamics. 2013 FEBS J 280 4600-11
Kim J Functional genomic screen for modulators of ciliogenesis and cilium length. 2010 Nature 464 1048-51
Janmey PA Modulation of gelsolin function by phosphatidylinositol 4,5-bisphosphate. 1987 Nature 325 362-4



To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)