|SMART accession number:||SM00227
||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)].
There are 9656
NEBU domains in 269 proteins in SMART's nrdb database.
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- Evolution (species in which this domain is found)
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