We report the identification, structural characterization, and mapping of the human FIGF gene. FIGF is the human homologue of mouse figf (c-fos-induced growth factor), a new member of the platelet-derived growth factor/vascular endothelial growth factor (PDGF/VEGF) family. It codes for a secreted factor with mitogenic and morphogenic activity on fibroblast cells. The predicted amino acid sequence of FIGF is 84% identical to that of the mouse protein, and it is highly conserved (up to 40%) in the dimerization domain with respect to the VEGF members of the family. The 2.5-kb mRNA of FIGF was detected in adult lung and heart tissues. The gene spans about 50 kb and is organized into seven exons and six introns. The FIGF promoter contains an optimal AP-1-binding site and lacks a canonical TATA box. Fluorescence in situ hybridization mapped FIGF to chromosomal region Xp22.1. The subsequent identification of YAC positive clones from this region allowed us to refine the map and localize FIGF centromeric to the phosphatidylinositol glycan complementation class A (PIGA) gene and telomeric to the gastrin-releasing peptide receptor (GRPR) gene. FIGF and PIGA genes lie next to each other in a head-to-tail orientation, with the FIGF polyadenylation signal about 12 kb from the PIGA transcriptional start site.