{PDOC51777} {PS51777; RH2} {BEGIN} ********************** * RH2 domain profile * ********************** The RH2 (RILP homology 2) Rab-binding domain is found in the following animal proteins [1,2,3]: - Rab interacting lysosomal proteins (RILP), which interacts with Rab7, Rab34, and Rab36. - RILP-like 1 (RILP-L1), which interacts with Rab12, Rab34, and Rab36. - RILP-like 2 (RILP-L2), which interacts with Rab34 and Rab36. - JNK-interacting protein 3 (JIP3), which interacts with Rab36 alone. - JNK-interacting protein 4 (JIP4), which interacts with Rab36 alone. The RH2 domain is folded into a long helix alpha1 and a short helix alpha2 connected by a very tight loop (see ). The RH2 domain forms a tightly associated four helices homodimer in which both helices alpha1 and alpha2 are involved in dimerization. Such a homodimer binds to two separate Rab-GTP molecules on opposite sides, with both helices involved in the interaction with Rab. In the complex interface, although each Rab-GTP interacts with both helices of the RH2 domain, these two helices are contributed by two different molecules, with helix alpha1 coming from one protomer and helix alpha2 from the other protomer [2]. The profile we developed covers the entire RH2 domain. -Sequences known to belong to this class detected by the profile: ALL. -Other sequence(s) detected in Swiss-Prot: NONE. -Last update: October 2015 / First entry. [ 1] Wang T., Wong K.K., Hong W. "A unique region of RILP distinguishes it from its related proteins in its regulation of lysosomal morphology and interaction with Rab7 and Rab34." Mol. Biol. Cell 15:815-826(2004). PubMed=14668488; DOI=10.1091/mbc.E03-06-0413 [ 2] Wu M., Wang T., Loh E., Hong W., Song H. "Structural basis for recruitment of RILP by small GTPase Rab7." EMBO J. 24:1491-1501(2005). PubMed=15933719; DOI=10.1038/sj.emboj.7600643 [ 3] Matsui T., Ohbayashi N., Fukuda M. "The Rab interacting lysosomal protein (RILP) homology domain functions as a novel effector domain for small GTPase Rab36: Rab36 regulates retrograde melanosome transport in melanocytes." J. Biol. Chem. 287:28619-28631(2012). PubMed=22740695; DOI=10.1074/jbc.M112.370544 -------------------------------------------------------------------------------- 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}