| Primary Identifier | IPR037789 | Type | Family |
| Short Name | FIP_classI |
| description | Rab GTPases recruit various effector proteins to organelles and vesicles. Rab11-family interacting proteins (FIPs) are involved in mediating the role of Rab11. FIPs can be divided into three classes: class I FIPs (Rip11/Rab11-FIP5, RCP/RAB11FIP1, and FIP2) which contain a C2 domain after N terminus of the protein, class II FIPs (FIP3 and FIP4) which contain two EF-hands and a proline rich region, and class III FIPs (FIP1) which exhibits no homology to known protein domains. All FIP proteins contain a highly conserved, 20-amino acid motif at the C terminus of the protein, known as Rab11/25 binding domain (RBD). Class I FIPs are thought to bind to endocytic membranes via their C2 domain, which interacts directly with phospholipids. Class II FIPs do not have any membrane binding domains leaving much to speculate about the mechanism involving FIP3 and FIP4 interactions with endocytic membranes []. Class I FIPs, but not the class II FIPs, also interact with Rab14 [].The exact function of the Rab11 and FIP interaction is unknown, but there is speculation that it involves the role of forming a targeting complex that recruits a group of proteins involved in membrane transport to organelles. Recent studies have identified several Rab11-FIP complex-binding proteins that regulate distinct membrane traffic pathways [].This family consist of class I FIPs. |
