Fig. 1. (A) Nucleotide and predicted amino acid sequences of HrFGFR cDNA. The insert of the cDNA encompasses 3,199 bp including 18 adenylyl residues located at the 3' end. The ATG at positions 118-120 represents the putative start codon for the HrFGFR protein. An asterisk indicates the termination codon. The transmembrane domain is indicated by dotted-underline, and the intracellular tyrosine kinase domains are underlined. Bold, italic capitals indicate cysteine residues forming disulfide bridges characteristic of immunogloblin (Ig)-like domains. Bold capitals indicate amino acid residues characteristic of the tyrosine kinase domain. Arrows indicate two regions of amino acid residues that were used in the molecular phylogenetic analysis shown in Fig. 2. (B) Schematic representation of the structural and functional domains of HrFGFR and the mutant dnHrFGFR. The FGF receptor contains two Ig-like domains bounded by cysteine residues that form disulfide bridges (Ig2 and Ig3), a transmembrane domain (TM), and an intracellular tyrosine kinase domain split by 14 amino acids. dnHrFGFR represents a mutant construct in which the entire tyrosine kinase domain starting from amino acid 369 (marked by an arrow on HrFGFR) was deleted.
