F-BAR domain (IPR001060)
Short name: F-BAR_dom
The F-BAR (also known as FCH) domain is a short conserved region of around 60 amino acids first described as a region of homology between FER and CIP4 proteins [PMID: 9210375]. In the CIP4 protein the FCH domain binds to microtubules [PMID: 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 [PMID: 18525024]. They are alpha-helical membrane-binding modules that function in endocytosis, regulation of the actin cytoskeleton and signalling [PMID: 18525024].
Proteins containing an FCH domain can be divided in 3 classes [PMID: 11994747]:
- A subfamily of protein kinases usually associated with an SH2 domain:
- Fps/fes (Fujimani poultry sarcoma/feline sarcoma) proto-oncogenes. They are non-receptor protein-tyrosine kinases preferentially expressed in myeloid lineage. The viral oncogene has an unregulated kinase activity which abrogates the need for cytokines and influences differentiation of haematopoietic progenitor cells.
- Fes related protein (fer). It is an ubiquitously expressed homologue of Fes.
- Adaptor proteins usually associated with a C-terminal SH3 domain:
- Schizosaccharomyces pombe CDC15 protein. It mediates cytoskeletal rearrangements required for cytokinesis. It is essential for viability.
- CD2 cytoplasmic domain binding protein.
- Mammalian Cdc42-interacting protein 4 (CIP4). It may act as a link between Cdc42 signaling and regulation of the actin cytoskeleton.
- Mammalian PACSIN proteins. A family of cytoplasmic phosphoproteins playing a role in vesicle formation and transport.
- A subfamily of Rho-GAP proteins:
- Mammalian RhoGAP4 proteins. They may down-regulate Rho-like GTPases in hematopoietic cells.
- Yeast hypothetical protein YBR260C.
- Caenorhabditis elegans hypothetical protein ZK669.1.