1.G.13.1.1
Membrane fusion protein p14 (fusion-associated small transmembrane (Fast) protein) of 125 aas and 1 TMS of reptilian reovirus has an approximately 38-residue myristoylated N-terminal ectodomain containing a moderately apolar N-proximal region, termed the hydrophobic patch.  The structure of the 38 aa non-myristoylated N-terminal transmembrane/ectodomain has been determined by NMR (2XL0_A) (Corcoran et al. 2004).  Mediates lipid mixing in a liposome fusion assay    The soluble nonmyristoylated p14 ectodomain peptide consists of an N-proximal extended loop flanked by two proline hinges. The remaining two-thirds of the ectodomain is disordered, consistent with predictions based on CD spectra of the myristoylated peptide. The myristoylated p14 ectodomain peptide mediates lipid mixing in a liposome fusion assay. Structural plasticity, environmentally induced conformational changes, and kinked structures predicted for the p14 ectodomain and hydrophobic patch are all features associated with fusion peptides (Corcoran et al. 2004). It lacks a cleavable signal sequence and uses an internal reverse signal-anchor sequence to direct membrane insertion and protein topology. This topology results in the unexpected, cotranslational translocation of the essential myristylated N-terminal domain of p14 across the cell membrane (Corcoran and Duncan 2004).