PROSITE documentation PDOC51511
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 <PDOC00380>), 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 <PDOC00018>) 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 α-helix, followed by a 90 bend at a conserved proline residue, a 3(10) helix and a C-terminal short β-strand, adopting an "L" shape (see <PDB:2D7C>). The long α-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 α-helix and the short β-strand [1,2,3,4].

The profile we developed covers the entire FIP-RBD domain.

Last update:

November 2010 / First entry.


Technical section

PROSITE method (with tools and information) covered by this documentation:

FIP_RBD, PS51511; FIP-RBD domain profile  (MATRIX)


1AuthorsJagoe W.N. Lindsay A.J. Read R.J. McCoy A.J. McCaffrey M.W. Khan A.R.
TitleCrystal structure of rab11 in complex with rab11 family interacting protein 2.
SourceStructure 14:1273-1283(2006).
PubMed ID16905101

2AuthorsEathiraj S. Mishra A. Prekeris R. Lambright D.G.
TitleStructural basis for Rab11-mediated recruitment of FIP3 to recycling endosomes.
SourceJ. Mol. Biol. 364:121-135(2006).
PubMed ID17007872

3AuthorsShiba T. Koga H. Shin H.-W. Kawasaki M. Kato R. Nakayama K. Wakatsuki S.
TitleStructural basis for Rab11-dependent membrane recruitment of a family of Rab11-interacting protein 3 (FIP3)/Arfophilin-1.
SourceProc. Natl. Acad. Sci. U.S.A. 103:15416-15421(2006).
PubMed ID17030804

4AuthorsWei J. Liu Y. Bose K. Henry G.D. Baleja J.D.
TitleDisorder and structure in the Rab11 binding domain of Rab11 family interacting protein 2.
SourceBiochemistry 48:549-557(2009).
PubMed ID19119858

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 prosite_license.html.


View entry in original PROSITE document format
View entry in raw text format (no links)