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Gelsolin (top) was the first member of the group to be sequenced (Kwiatkowski).  Its six domains are a repeat of two sets of three in that G1 (dark blue) is most like G4 (light blue), G2 like G5, and G3, like G6 (Way & Weeds, 1988).  The villin group are characterised by the possesion of the villin head piece (Purple oblong) at the C-terminus. One of the most divergent forms is EhABPH from Entamoeba histolytica (Ebert et al, 2000) which has a coronon-like N-terminal region followed by gelsolin/villin domain but lacking G1.

For extra information look under each particular ABP in the Encyclopaedia of A.B.P.s. 

 

References:-

Ebert, F., Guillen, N., Leippe, M. & Tannich, E. (2000) Molecular cloning and cellular localization of an unusual bipartite Entamoeba histolytica polypeptide with similarity to actin binding proteins., Mol.Biochem.Parasitol. 111, 459-464.

Kwiatkowski, D. J., Stossel, T. P., Orkin, S. H., Mole, J. E., Colten, H. R. & Yin, H. L. (1986) Plasma and cytoplasmic gelsolins are encoded by a single gene and contain a duplicated actin-binding domain, Nature. 323, 455-458.

Way, M. & Weeds, A. G. (1988) 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, J. Mol. Biol. 203, 1127-1133.

 
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