CTLHC-terminal to LisH motif.
|SMART accession number:||SM00668|
|Description:||Alpha-helical motif of unknown function.|
|Interpro abstract (IPR006595):|
The 33-residue LIS1 homology (LisH) motif (IPR006594) is found in eukaryotic intracellular proteins involved in microtubule dynamics, cell migration, nucleokinesis and chromosome segregation. The LisH motif is likely to possess a conserved protein-binding function and it has been proposed that LisH motifs contribute to the regulation of microtubule dynamics, either by mediating dimerization, or else by binding cytoplasmic dynein heavy chain or microtubules directly. The LisH motif is found associated to other domains, such as WD-40 SPRY, Kelch, AAA ATPase, RasGEF, or HEAT [(PUBMED:11734546), (PUBMED:12384287), (PUBMED:12559565)]. The secondary structure of the LisH domain is predicted to be two alpha- helices [(PUBMED:11734546)].Some proteins known to contain a LisH motif are listed below:
The C-terminal to LisH (CTLH) motif is a predicted alpha-helical sequence of unknown function that is found adjacent to the LisH motif in a number of these proteins but is absent in other (e.g. LIS1) [(PUBMED:11734546), (PUBMED:12384287), (PUBMED:12559565)]. The CTLH domain can also be found in the absence of the LisH motif, like in:
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- Evolution (species in which this domain is found)
- Cellular role (predicted cellular role)
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