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PROSITE documentation PDOC51777

RH2 domain profile





Description

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 α1 and a short helix α2 connected by a very tight loop (see <PDB:1YHN>). The RH2 domain forms a tightly associated four helices homodimer in which both helices α1 and α2 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 α1 coming from one protomer and helix α2 from the other protomer [2].

The profile we developed covers the entire RH2 domain.

Last update:

October 2015 / First entry.

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Technical section

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

RH2, PS51777; RH2 domain profile  (MATRIX)


References

1AuthorsWang T. Wong K.K. Hong W.
TitleA unique region of RILP distinguishes it from its related proteins in its regulation of lysosomal morphology and interaction with Rab7 and Rab34.
SourceMol. Biol. Cell 15:815-826(2004).
PubMed ID14668488
DOI10.1091/mbc.E03-06-0413

2AuthorsWu M. Wang T. Loh E. Hong W. Song H.
TitleStructural basis for recruitment of RILP by small GTPase Rab7.
SourceEMBO J. 24:1491-1501(2005).
PubMed ID15933719
DOI10.1038/sj.emboj.7600643

3AuthorsMatsui T. Ohbayashi N. Fukuda M.
TitleThe Rab interacting lysosomal protein (RILP) homology domain functions as a novel effector domain for small GTPase Rab36: Rab36 regulates retrograde melanosome transport in melanocytes.
SourceJ. Biol. Chem. 287:28619-28631(2012).
PubMed ID22740695
DOI10.1074/jbc.M112.370544



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