SMART accession number:SM00227
Description: The Nebulin repeat is present also in Las1. Tandem arrays of these repeats are known to bind actin.
Interpro abstract (IPR000900): Nebulin is a 600-800kDa protein found in the thin filaments of striated vertebrate muscle. It is presumed to play a role in binding and stabilising F-actin [(PUBMED:8609630)], essentially by providing a template for actin polymerisation (i.e., acting as an "actin zipper"). The amino acid sequence shows a uniform repeating pattern along its length, a repeated 35-residue motif constituting up to 97% of the polypeptide. Analysis of individual repeats reveals a progressive N- to C-terminal divergence, coupled with an increasing alpha-helix propensity. This correlates with a higher binding affinity for F-actin at the C terminus. Thus, it is postulated that once the repeats have formed an initiation complex, the whole length of the nebulin molecule may then associate in a highly co-operative process with the thin filament, in a manner similar to the closing of a zipper [(PUBMED:8609630)].
Family alignment:
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There are 9656 NEBU domains in 269 proteins in SMART's nrdb database.

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