Sequence determination of an extremely acidic rat dentin phosphoprotein.

The mineralization process associated with the conversion of predentin to dentin is believed to be initiated and controlled by a set of acidic regulatory noncollagenous proteins (NCPs) which include phosphophoryn, the major NCP in dentin. Phosphophoryn binds tightly to collagen and is believed to initiate the formation of apatite crystals which play a central role in the mineralization process. During the process of analyzing the 3' end of an odontoblast-specific cDNA which codes for dentin sialoprotein (Ritchie, H. H., Hou, H., Veis, A., and Butler, W. T. (1994) J. Biol. Chem. 269, 3698-3702), we discovered a 801-base pair open reading frame. This downstream open reading frame encodes a putative leader sequence and a very acidic mature protein sequence having a deduced amino acid composition containing high percentages of both Ser (43%) and Asp (31%) residues which closely coincides with the amino acid composition of phosphophoryns from human, bovine, rat, and rabbit (i. e. Asp (30-40%) and Ser (38-50%)). This newly identified cDNA therefore encodes a protein with characteristics similar to phosphophoryn. Here we present the cDNA sequence, the deduced amino acid sequence, and the prospective Ser residue-specific casein kinase I and II phosphorylation sites for this putative phosphophoryn.