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The transforming growth factor beta/bone morphogenetic protein family is composed of a large group of secreted polypeptides with growth-promoting and morphogenic activities. Human F-spondin, an acidic glycoprotein of approximately 50 kDa secreted by human neural retinal pigment epithelial (RPE) cells, was recently identified as a binding protein of transforming growth factor beta. In this study, the human F-spondin gene was isolated and sequenced. A gene-specific intron fragment was used to screen a human YAC library, and the complete gene was isolated from a human genomic library. The nucleotide sequence of the gene spans 5.8 kilobase pairs, is composed of 13 exons and 12 introns, and codes for the entire F-spondin protein. The overall amino acid sequence of F-spondin is identical to human transforming growth factor beta, and the deduced amino acid sequence of F-spondin consists of two identical and hydrophobic N-terminal pentapeptides followed by a single C-terminal cysteine. Northern analysis showed the expression of the F-spondin gene in human fetal brain, prostate, and placenta but not in several other tissues. The human F-spondin
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