Figure 3From: Design and characterization of genetically engineered zebrafish aquaporin-3 mutants highly permeable to the cryoprotectant ethylene glycolAmino acid sequence alignment of zebrafish GLPs, Aqp1a and Aqp0a with mammalian and teleost orthologs. Amino acid sequence alignment of representative GLPs and water-selective aquaporins of teleosts and mammals: Danio rerio Aqp0a (DrAqp0a; FJ666326), -0b (FJ655389), -3a (EU341833), -3b (EU341832), -7 (FJ655385), -9a (FJ655387), -9b (EU341835), -10a (FJ655388), -10b (EU341836), and -1a (AY626937), Fundulus heteroclitus Aqp0a (FhAqp0; AF191906) and -3a (ACI49539), Homo sapiens AQP3 (HsAQP3; BC013566), and Bos taurus AQP0 (BtAQP0; NM_173937). Predicted transmembrane domains (TMD1-6) of DrAqp3b are annotated by blue arrows, and external (out) and internal (in) loops are indicated. The two NPA motifs are shaded in red, whereas the four residues forming the aromatic/arginine (ar/R) constriction in zebrafish GLPs (Phe, Gly/Ser, Tyr/Ala, and Arg) [48] are pointed by red arrowheads. Potential residues involved in pH sensitivity in AQP0 and -3 orthologs are shaded in green, and mutated residues in DrAqp3b are indicated by black arrowheads.Back to article page