Figure 1.

Amino acid sequence alignment of zebrafish aquaporins. (A) The consensus sequence logo is scaled according to amino acid conservation. Highest residue similarity (blue: 100%, green: 80-100% or sand; 60-80%) is found within the α-helical regions (H1-8). The transmembrane domains (TMD1-6) are annotated for DrAqp0a based upon a molecular sequence wrap to the crystallographically resolved structure of Bos taurus AQP0 (B). The structure wrap consists of the complete peptides (263 amino acids) with a gapless identity/similarity of 70.3/85.9%. The render shows identical residues in red, non-identical in blue. The hemi-helices H3 and H7 (yellow) on loops B and E, respectively, fold such that the opposing NPA motifs (pink in the alignment) interact to present the arginine constriction (DrAqp0a R¹⁸⁷ green ball and stick, and arrow in alignment). The C-terminal domain is shown with a grey α-helix.