Journal of Biological Chemistry vol:258 issue:23 pages:14206-11
The complete primary structures of the two main forms, PRP-IV and PRP-V, of a proline-rich polypeptide bound in vivo to rat prostatic binding protein has been determined. Their sequences were established using manual Edman degradation of the native polypeptide and of purified fragments derived from trypsin and thermolysin digestions. Both polypeptides contain 38 amino acid residues (Mr = 4397 and 4339); cysteine, methionine, and serine are missing. In spite of the high proline content (21%), no polyproline stretches were detected. PRP-IV and PRP-V show an extensive structural homology and differ only by three substitutions. These amino acid replacements are located in the NH2-terminal part of the molecule at positions 6 (His leads to Pro), 10 (Pro leads to His), and 11 (Asp leads to Gly). Moreover, each component displays a microheterogeneity at several positions in the sequence which indicates that multiple structural variants exist for PRP-IV and PRP-V. These data not only suggest the existence in rat ventral prostate of a multigene family coding for the proline-rich polypeptides but also the occurrence of a pronounced genetic polymorphism for these components. In addition, a remarkable sequence homology is observed between the PRP components and the region of the B chain in the precursor of mouse renin.