Eukaryotic proteins of the reticulon (RTN) family all share an association
with the endoplasmic reticulum (ER). Whereas amino-terminal regions are not
related to one another, all reticulon proteins share a 200-amino-acid residue
region of sequence similarity at the C-terminus. This region contains two
large hydrophobic regions separated by a 66-residue hydrophilic segment. The
conserved hydrophobic C-terminal portion has been shown to play an essential
role in the association of reticulons with the ER membrane. The hydrophobic
portions are supposed to be membrane-embedded and the hydrophilic 66-residue
localized to the lumenal/extracellular face of the membrane. Most reticulons
have a di-lysine ER retention motif at the C-terminus. Because of their likely
association with the rough as well as the smooth ER, the reticulons might play
some role in transport processes or in regulation of intracellular calcium
levels. It has been suggested that the reticulons may be serving as ER-associated channel-like complexes [1,2,3,4,5].
The profile we developed covers the entire conserved C-terminal reticulon
January 2002 / First entry.
PROSITE method (with tools and information) covered by this documentation:
van de Velde H.J.K. Roebroek A.J.M. Senden N.H.M. Ramaekers F.C.S. Van de Ven W.J.M.
J. Cell Sci. 107:2403-2416(1994).
Roebroek A.J.M. Ayoubi T.A.Y. van de Velde H.J.K. Schoenmakers E.F.P.M. Pauli I.G.L. Van de Ven W.J.M.
Genomic organization of the human NSP gene, prototype of a novel gene family encoding reticulons.
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