Primary structure of human proacrosin deduced from its cDNA sequence

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Abstract
CDNA clones encoding proacrosin, the zymogen of acrosin, were isolated from a human testis cDNA library by using a fragment of boar acrosin cDNA as a probe. Nucleotide sequencing of the longest cDNA clone has predicted that human proacrosin is synthesized with a 19‐amino‐acid signal peptide at the N‐terminus. The cleavable signal sequence is followed by a 23‐residue segment corresponding to the light chain and then by a 379‐residue stretch that constitutes the heavy chain containing the catalytic site of the mature protease. The C‐terminal portion of the deduced sequence for the heavy chain is very rich in proline residues, most of which are encoded by a unique repeat of CCCCCA. The active‐site residues including histidine, aspartic acid, and serine are also predicted to be located at residues 69, 123, and 221, respectively.

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