Protein Domain : F-BAR domain IPR031160

Type	Domain
Description	All eukaryotic cells are surrounded by a plasma membrane, and they also contain multiple membrane-based organelles and structures inside cells. Thusmembrane remodeling is likely to be important for most cellular activities and development. The Bin-Amphiphysin-Rvs (BAR) domain superfamily of proteins hasbeen found to play a major role in remodeling cellular membranes linked with organelle biogenesis, membrane trafficking, cell division, cell morphology andcell migration. The BAR domain superfamily of proteins is evolutionarily conserved with representative members present from yeast to man. Currentlythere are three distinct families of BAR domain proteins: classical BAR, F-BAR (FCH-BAR e.g., Fes/CIP4 homology BAR e.g., Toca-1) and I- BAR (inverse-BAR e.g., IRSp53). The classical BAR, F-BAR, and I-BAR domainsare structurally similar homodimeric modules with antiparallel arrangement of monomers [, ].The F-BAR domain is emerging as an important player in membrane remodeling pathways. F-BAR domain proteins couple membrane remodeling with actin dynamicsassociated with endocytic pathways and filopodium formation. F-BAR domain containing proteins can be categorized into five sub-families based on theirphylogeny which is consistent with the additional protein domains they possess, for example, RhoGAP domains, Cdc42 binding sites,SH2 domains, SH3 domains and tyrosine kinase domains [].The N-terminal part (about one third) of the F-BAR domain was previously characterised as an FCH (FER-CIP4 homology) domain. However, the region ofsequence similarity extends to an adjacent region with a coiled-coil (CC) structure. Hence, the F-BAR domain (FCH+CC, ~300 amino acids) has also beencalled extended FC (EFC) domain. The F-BAR domain plays a role in dimerization and membrane phospholipid binding. It binds specifically to certain kinds oflipids and acts as a a dimeric membrane-binding curvature effector [ , , ].The F-BAR domain is composed of five helices. Its structure is composed of a short N-terminal helix, three long α-helices, and a short C-terminal helixfollowed by an extended peptide of 17 amino acids [ , ].
Short Name	F_BAR