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Fig. 1. (A) Domain structure comparison of AmphiTrk, vertebrate Trk receptors (TrkA, TrkB and TrkC) and representative invertebrate Trk-like proteins from Lymnaea stagnalis (LTrk) and Drosophila melanogaster (DTrk). Modules are colour coded: yellow, Cys-rich clusters; green, leucine-rich domains; blue, type C2 IgG domains; grey, transmembrane domain; red, tyrosine-kinase domain; purple, N-terminal extension; turquoise; type V2 IgG domains. (B) AmphiTrk amino acid sequence. Amino acid positions are numbered on the left. The putative signal sequence cleavage site is indicated by an arrowhead. Leucine-rich motifs are in italics and flanking cysteine clusters in bold. Both Ig-like domains are underlined; conserved asparagines with structural roles for ligand binding are indicated by dots. The transmembrane region is underlined by a dotted line. The first phosphorylation site by cAMP/cGMP-dependent kinase proteins, KIS, is shown with a black background, as is the tyrosine responsible for Shc recruitment. Within the tyrosine kinase domain (boxed), the lysine responsible for ATP binding and the second phosphorylation site by cAMP/cGMP-dependent kinase proteins, RKFT, are shown by a black background. The autophosphorylation sequence (DIYSTDYYR) is highlighted in grey and the autophosphorylated tyrosines are shown by a black background. Glutamine located in the same position as the vertebrate docking site for PLC{gamma} is shown by a black background. AmphiTrk sequences have been deposited in the GeneBank under Accession Numbers AY902361-AY902364