Bone morphogenetic protein 1 (BMP1) has been proposed as a regulatory molecule involved in the binding or activation of other BMP molecules. It has been described as being identical to the enzyme C-proteinase that processes pro-collagens to fibrillar collagens. A fragment containing an exon of the bovine BMP1 gene was amplified from an adapter-ligated genomic DNA library. The isolated bovine BMP1 fragment was assigned by fluorescence in situ hybridization (FISH) to bovine (BTA) chromosome 8q21, a region containing an evolutionary breakpoint between homology to human (HSA) chromosomes 8 and 9. The assignment to BTA 8 was confirmed by using a hybrid somatic cell panel. The 3’ intron region of the amplified genomic BMP1 fragment showed a SSCP polymorphism, and linkage analysis in the International Bovine Reference Panel (IBRP) of families confirmed the boundary position of this gene. The BMP1 gene presents total linkage (Θ = 0.00, Z = 3.61) with the lipoprotein lipase gene on BTA 8 and HSA 8 and a larger recombination fraction (Θ = 0.11 Z = 5.03) with the marker GGTB2 on BTA 8 and HSA 9. Physical and genetic mapping of the bovine BMP1 gene contribute to narrow the boundary between the HSA 8 and HSA 9 homology segments on BTA 8 and to the comparative mapping between BTA 8, murine chromosome MMU 14, and HSA 8.