FCHFes/CIP4 homology domain
|SMART accession number:||SM00055|
|Description:||Alignment extended from original report. Highly alpha-helical. Also known as the RAEYL motif or the S. pombe Cdc15 N-terminal domain.|
|Interpro abstract (IPR001060):|
FCH domain is a short conserved region of around 60 amino acids first described as a region of homology between FER and CIP4 proteins [(PUBMED:9210375)]. In the CIP4 protein the FCH domain binds to microtubules [(PUBMED:10713100)]. The FCH domain is always found N-terminally and is followed by a coiled-coil region. The FCH and coiled-coil domains are structurally similar to Bin/amphiphysin/RVS (BAR) domains [(PUBMED:18525024)]. They are alpha-helical membrane-binding modules that function in endocytosis, regulation of the actin cytoskeleton and signalling [(PUBMED:18525024)].
Proteins containing an FCH domain can be divided in 3 classes [(PUBMED:11994747)]:
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- Evolution (species in which this domain is found)
- Cellular role (predicted cellular role)
- Literature (relevant references for this domain)
- Metabolism (metabolic pathways involving proteins which contain this domain)
- Structure (3D structures containing this domain)
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