InterPro : IPR010911

Name  Rab-binding domain Short Name  Rab_BD
Type  Domain Description  This entry represents the Rab-binding domain.Rab are small GTPases implicated in vesicle trafficking. Like the other smallGTPases, Rab proteins act as molecular switches, with an active GTP-bound formthat interacts with its target or effector protein and an inactive GDP-boundform. A subgroup of Rab effectors contain in their N-terminal part a conservedregion of around 70 amino acid residues, the Rab-binding domain (RabBD). Insome Rab effector domains an atypical FYVE-type zinc finger is inserted in thecentral part [].The crystal structure of the Rab effector domain of Rabphilin-3A in complexwith Rab3A has been solved []. The structure consists of twolong helices separated by an atypical FYVE-type zinc finger which adopts aconformation similar to classical ones. The central zincfinger does not directly interact with Rab3A. The amino acids important forthis interaction are located around a short C-terminal motif (SGAWFF) and anacidic cluster in the N-terminal area.

Sequence Features

GO Displayer


InterPro protein domain ID --> Contigs



0 Child Features

0 Contains

0 Found In

1 Parent Features

Id Name Short Name Type
IPR011011 Zinc finger, FYVE/PHD-type Znf_FYVE_PHD Domain

2 Publications

First Author Title Year Journal Volume Pages
Ostermeier C Structural basis of Rab effector specificity: crystal structure of the small G protein Rab3A complexed with the effector domain of rabphilin-3A. 1999 Cell 96 363-74
Fukuda M Distinct Rab binding specificity of Rim1, Rim2, rabphilin, and Noc2. Identification of a critical determinant of Rab3A/Rab27A recognition by Rim2. 2003 J Biol Chem 278 15373-80

To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)