We isolated the cDNA encoding a novel member (216 amino acids) of the fibroblast growth factor (FGF) family from rat embryos. As this protein is the 17th documented member of the FGF family, we tentatively termed it FGF-17. We have also determined the structures of mouse and human FGF-17 with high amino acid identity (100 and 98.6%) to rat FGF-17, respectively. Among FGF family members, FGF-17 is most similar (53.7% amino acid identity) to FGF-8. FGF-17 has a typical signal sequence at its amino terminus. As expected, recombinant rat FGF-17 was efficiently secreted by High Five insect cells infected with recombinant baculovirus containing the cDNA indicating that FGF-17 is a secreted protein. FGF-17 mRNA of approximately 2.1 kb was detected in rat embryos at E14.5, but not at E10.5 and E19.5 by Northern analysis. The mRNA was found to be preferentially expressed in the neuroepithelia of the isthmus and septum of the rat embryonic brain at E14.5 by in situ hybridization. The present results indicate that FGF-17 might be a novel secreted signaling molecule in the induction and patterning of the embryonic brain.