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Updated: May 15, 2026

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay
Published on: May 26, 2011
The Remorin C-terminal Anchor was shaped by convergent evolution among membrane binding domains
Sylvain Raffaele1, Artemis Perraki, Sébastien Mongrand
1Laboratoire des Interactions Plantes-Microorganismes (LIPM); UMR441 INRA-CNRS; Castanet-Tolosan, France.
Abstract:
StREM1.3 Remorin is a well-established plant raftophilic protein, predominantly associated with sterol- and sphingolipid-rich membrane rafts. We recently identified a C-terminal domain (RemCA) required and sufficient for StREM1.3 anchoring to the plasma membrane. Here, we report a search for homologs and analogs of RemCA domain in publicly available protein sequence and structure databases. We could not identify RemCA homologous domains outside the Remorin family but we identified domains sharing bias in amino-acid composition and predicted structural fold with RemCA in bacterial, viral and animal proteins. These results suggest that RemCA emerged by convergent evolution among unrelated membrane binding domain.
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