The human flg gene has been previously shown to encode a tyrosine kinase whose transcription in endothelial cells is regulated by the fibroblast growth factor (FGF). We report the cloning and sequencing of the murine flg which revealed that the full length transcript encodes a transmembrane receptor-like protein. The extracellular portion is composed of three homologous immunoglobulin-like domains, resembling the organization of the receptor for interleukin-1, and the cytoplasmic domain displays unique organization of tyrosine kinase sequences. An anti-peptide antibody directed to the carboxy-terminus of the flg protein recognized three fibroblast-cell proteins (p150, p130 and p105), that undergo phosphorylation in the immune-complex. Moreover, the antibody specifically immunoprecipitated two proteins (p145 and p120) that were covalently crosslinked to basic FGF, but only one (p155) of the two molecular forms of the receptor for acidic FGF. In situ hybridization analysis of mouse embryos (12.5 days p.c.) indicated that flg is transcribed in the prospective brain, areas of the face and the vertebral column. The latter exhibited progressive cranio-caudal concentration into the intervertebral discs. Taken together, these results strongly suggest that the flg gene encodes a receptor for fibroblast growth factor(s).