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. 2011 Apr 8;11:34. doi: 10.1186/1472-6750-11-34

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Copyright ©2011 Chauvigné et al; licensee BioMed Central Ltd.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Amino 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.