α-actinin is a F-actin cross-linking protein which is thought to anchor
actin to a variety of intracellular structures . The actin-binding domain
of α-actinin seems to reside in the first 250 residues of the protein. A
similar actin-binding domain has been found in the N-terminal region of many
different actin-binding proteins [2,3]:
In the β chain of spectrin (or fodrin).
In dystrophin, the protein defective in Duchenne muscular dystrophy (DMD)
and which may play a role in anchoring the cytoskeleton to the plasma
In the slime mold gelation factor (or ABP-120).
In actin-binding protein ABP-280 (or filamin), a protein that link actin
filaments to membrane glycoproteins.
In fimbrin (or plastin), an actin-bundling protein. Fimbrin differs from
the above proteins in that it contains two tandem copies of the actin-
binding domain and that these copies are located in the C-terminal part of
We selected two conserved regions as signature patterns for this type of
domain. The first of this region is located at the beginning of the domain,
while the second one is located in the central section and has been shown to
be essential for the binding of actin.
April 2006 / Patterns revised.
PROSITE methods (with tools and information) covered by this documentation:
Schleicher M. Andre E. Hartmann H. Noegel A.A.
Actin-binding proteins are conserved from slime molds to man.
PROSITE is copyright. It is produced by the SIB Swiss Institute
Bioinformatics. There are no restrictions on its use by non-profit
institutions as long as its content is in no way modified. Usage by and
for commercial entities requires a license agreement. For information
about the licensing scheme send an email to
or see: prosite_license.html.