Figure 1

Multiple sequence alignment of the chicken PTH1R and PTH3R with the mammalian and teleost homologues. The predicted seven transmembrane domains (TM) are annotated and represented by boxes and the signal peptide sequence by an arrow. The six conserved cysteine residues are annotated with “*” and the conserved N-glycosylation consensus motif is dashed boxed. Amino acid residues involved in human with ligand-binding at the N-terminal and TM regions are in italics and underlined [13, 31] and conserved motifs that were found to be determinant for PTH binding are annotated with “:” [11]. Accession numbers: Human1 (PTH1R, AAR1807), Mouse1 (PTH1R, NP_035329); Zebrafish1 (PTH1R, NP_571432); Zebrafish3 (PTH3R, NP_571453); Takifugu1 (PTH1R, CAD79707); Takifugu3 (PTH3R; CAD67555)