Description

IPR036872 is a CH domain superfamily.

<p>A number of actin-binding proteins, including spectrin, alpha-actinin and fimbrin, contain a 250 amino acid stretch called the actin binding domain (ABD). The ABD has probably arisen from duplication of a domain which is also found in a single copy in a number of other proteins like calponin or the vav proto-oncogene and has been called calponin homology (CH) domain [[cite:PUB00001718], [cite:PUB00018082]].</p> <p>A detailed analysis of The CH domain-containing proteins has shown that they can be divided in three groups [[cite:PUB00001718]]:</p> <ul> <li>The fimbrin family of monomeric actin cross-linking molecules containing two ABDs</li> <li>Dimeric cross-linking proteins (alpha-actinin, beta-spectrin, filamin, etc.) and monomeric F-actin binding proteins (dystrophin, utrophin) each containing one ABD</li> <li>Proteins containing only a single amino terminal CH domain</li> </ul> <p>Each single ABD, comprising two CH domains, is able to bind one actin monomer in the filament. The N-terminal CH domain has the intrinsic ability to bind actin, albeit with lower affinity than the complete ABD, whereas the C-terminal CH bind actin extremely weakly or not at all. Nevertheless both CH domains are required for a fully functional ABD; the C-terminal CH domain contributing to the overall stability of the complete ABD through inter-domain helix-helix interactions [[cite:PUB00001718]]. Some of the proteins containing a single CH domain also bind to actin, although this has not been shown to be via the single CH domain alone [[cite:PUB00018082]]. In addition, the CH domain occurs also in a number of proteins not known to bind actin, a notable example being the vav protooncogene.</p> <p>The resolution of the 3D structure of various CH domains has shown that the conserved core consist of four major α-helices [[cite:PUB00018082]].</p> <p>Proteins containing a calponin domain include:</p> <ul> <li>Calponin, which is involved in the regulation of contractility and organisation of the actin cytoskeleton in smooth muscle cells [[cite:PUB00025538]].</li> <li>Beta-spectrin, a major component of a submembrane cytoskeletal network connecting actin filaments to integral plasma membrane proteins [[cite:PUB00042610]].</li> <li>The actin-cross-linking domain of the fimbrin/plastin family of actin filament bundling or cross-linking proteins [[cite:PUB00036320]].</li> <li>Utrophin,a close homologue of dystrophin [[cite:PUB00018082]].</li> <li>Dystrophin, the protein found to be defective in Duchenne muscular dystrophy; this protein contains a tandem repeat of two CH domains [[cite:PUB00024350]].</li> <li>Actin-binding domain of plectin, a large and widely expressed cytolinker protein [[cite:PUB00031059]].</li> <li>The N-terminal microtubule-binding domain of microtubule-associated protein eb1 (end-binding protein), a member of a conserved family of proteins that localise to the plus-ends of microtubules [[cite:PUB00029793]].</li> <li>Ras GTPase-activating-like protein rng2, an IQGAP protein that is essential for the assembly of an actomyosin ring during cytokinesis [[cite:PUB00029697]].</li> <li>Transgelin, which suppresses androgen receptor transactivation [[cite:PUB00042611]].</li> </ul>

This description is obtained from EB-eye REST.

Associated GO terms

Unable to find any GO terms for the transcript with the identifier.

Associated Lotus transcripts 30

Co-occuring domains 1

A list of co-occurring predicted domains within the L. japonicus gene space: