Fig. 2. Ph50 has three putative sorting signals already described in other proteins. (A) Alignment of the Rh50 protein sequence with diaromatic signals characterized in the cation-dependant mannose 6P receptor (CD-MPR), the human mannose receptor (MR) and the envelope glycoprotein of the human immunodeficiency virus type 1 (HIV-env). Aromatic residues are underlined. (B) Alignment of the two acidic clusters found in Rh50 (Rh50a and Rh50b) with known acidic signals found in furin, HIV-1 Nef and yeast Ent3p. Acidic residues are underlined and the conserved F residue adjacent to acidic clusters is in bold.