{PDOC51511} {PS51511; FIP_RBD} {BEGIN} ************************** * FIP-RBD domain profile * ************************** The Rab11 GTPase regulates recycling of internalized plasma membrane receptors and is essential for completion of cytokinesis. A family of Rab11 interacting proteins (FIPs) that conserve a C-terminal Rab-binding domain (RBD) selectively recognize the active form of Rab11. FIPs are diverse in sequence length and composition toward their N-termini, presumably a feature that underpins their specific roles in Rab11-mediated vesicle trafficking. They have been divided into three subfamilies (classe I, II, and III)on the basis of domain architecture. Class I FIPs comprises a subfamily of three proteins (Rip11/pp75/FIP5, Rab-coupling protein (RCP), and FIP2) that possess an N- terminal C2 domain (see ), localize to recycling endosomes, and regulate plasma membrane recycling. The class II subfamily consists of two proteins (FIP3/eferin/arfophilin and FIP4) with tandem EF hands (see ) and a proline-rich region. Class II FIPs localize to recycling endosomes, the trans-Golgi network, and have been implicated in the regulation of membrane trafficking during cytokinesis. The class III subfamily consists of a single protein, FIP1, which does not contain obvious homology domains or motifs other than the FIP-RBD [1,2,3,4]. The FIB-RBD domain consists of an N-terminal long alpha-helix, followed by a 90° bend at a conserved proline residue, a 3(10) helix and a C-terminal short beta-strand, adopting an "L" shape (see ). The long alpha-helix forms a parallel coiled-coil homodimer that symmetrically interacts with two Rab11 molecules on both sides, forming a quaternary Rab11-(FIP)2-Rab11 complex. The Rab11-interacting region of FIP-RBD is confined to the C-terminal 24 amino acids, which cover the C-terminal half of the long alpha-helix and the short beta-strand [1,2,3,4]. The profile we developed covers the entire FIP-RBD domain. -Sequences known to belong to this class detected by the profile: ALL. -Other sequence(s) detected in Swiss-Prot: NONE. -Last update: November 2010 / First entry. [ 1] Jagoe W.N., Lindsay A.J., Read R.J., McCoy A.J., McCaffrey M.W., Khan A.R. "Crystal structure of rab11 in complex with rab11 family interacting protein 2." Structure 14:1273-1283(2006). PubMed=16905101; DOI=10.1016/j.str.2006.06.010 [ 2] Eathiraj S., Mishra A., Prekeris R., Lambright D.G. "Structural basis for Rab11-mediated recruitment of FIP3 to recycling endosomes." J. Mol. Biol. 364:121-135(2006). PubMed=17007872; DOI=10.1016/j.jmb.2006.08.064 [ 3] Shiba T., Koga H., Shin H.-W., Kawasaki M., Kato R., Nakayama K., Wakatsuki S. "Structural basis for Rab11-dependent membrane recruitment of a family of Rab11-interacting protein 3 (FIP3)/Arfophilin-1." Proc. Natl. Acad. Sci. U.S.A. 103:15416-15421(2006). PubMed=17030804; DOI=10.1073/pnas.0605357103 [ 4] Wei J., Liu Y., Bose K., Henry G.D., Baleja J.D. "Disorder and structure in the Rab11 binding domain of Rab11 family interacting protein 2." Biochemistry 48:549-557(2009). PubMed=19119858; DOI=10.1021/bi8020197 -------------------------------------------------------------------------------- PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see https://prosite.expasy.org/prosite_license.html -------------------------------------------------------------------------------- {END}