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Figure 7 | BMC Evolutionary Biology

Figure 7

From: Structural and functional divergence of two fish aquaporin-1 water channels following teleost-specific gene duplication

Figure 7

Amino acid sequence alignment of the C termini of human AQP1, and Aqp1a and Aqp1b from representative teleosts. At the bottom, identical residues are indicated by asterisks, whereas conserved amino acid substitutions and substitutions with similar amino acids are indicated by double or single dots, respectively. Residues of teleost Aqp1a and Aqp1b conserved in human AQP1 are in bold, and conserved residues in Aqp1a sequences are boxed. Double underlined residues indicate typical potential sorting and internalization sequences, whereas those single underlined indicate other sorting-like motifs. In each sequence, potential Ser, Thr and Tyr phosphorylation sites (score ≥ 0.9) are indicated by arrowheads. Consensus sites for potential kinases are indicated: grey, candidate Pro-directed kinase and preceding docking domain; arrows, casein kinase I (CK1); circles, CK2. Other candidate phosphorylation sites shown do not match any eukaryotic linear functional motif included in the ELM resource.

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