Rab-binding domain (IPR010911)

Short name: Rab_BD

Overlapping homologous superfamilies

Domain relationships



This entry represents the Rab-binding domain.

Rab are small GTPases implicated in vesicle trafficking. Like the other small GTPases, Rab proteins act as molecular switches, with an active GTP-bound form that interacts with its target or effector protein and an inactive GDP-bound form. A subgroup of Rab effectors contain in their N-terminal part a conserved region of around 70 amino acid residues, the Rab-binding domain (RabBD). In some Rab effector domains an atypical FYVE-type zinc finger is inserted in the central part [PMID: 12578829].

The crystal structure of the Rab effector domain of Rabphilin-3A in complex with Rab3A has been solved [PMID: 10025402]. The structure consists of two long helices separated by an atypical FYVE-type zinc finger which adopts a conformation similar to classical ones. The central zinc finger does not directly interact with Rab3A. The amino acids important for this interaction are located around a short C-terminal motif (SGAWFF) and an acidic cluster in the N-terminal area.

GO terms

Biological Process

GO:0006886 intracellular protein transport

Molecular Function

GO:0017137 Rab GTPase binding

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
PROSITE profiles