Fig. 1
Molecular structures of salmon lice aquaporins. a Multiple sequence alignment of the full-length proteins showing secondary structural features including the N-terminal regions (NT), α-helices (H), transmembrane domains (TMD), loops A-E and C-termini (CT). Unique (white text on black background) and common (boxed residues) putative phosphorylation sites are shown for the N- and C-teminal regions. The two Asn-Pro-Ala (NPA) motifs are highlighted in green and yellow on hemihelices 3 and 7, respectively. Aromatic-arginine (ar/R) residues associated with the selectivity filter in the outer channel vestibule are highlighted in magenta, organge, red and blue, respectively. The position of Ser172, which normally corresponds to the ar/R residue on H2 is highlighted in gray for Bib. Residues predicted to confer glycerol selectivity (P1–P5) are highlighted in gray [50]. b, c and d Extracelluar views of cartoon renders of Bib, PripL and Glp1_v1 with ar/R residues (spacefill) coloured according to highlighted residues in (A). Helices and extracellular loops are annotated