Primary structure of human proacrosin deduced from its cDNA sequence.
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.
Baba
T
T
Institute of Applied Biochemistry, University of Tsukuba, Ibaraki, Japan.
Watanabe
K
K
Kashiwabara
S
S
Arai
Y
Y
D000176:Acrosin / Q000235:genetics*; D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D003001:Cloning, Molecular; D004247:DNA / Q000235:genetics*; D004792:Enzyme Precursors / Q000235:genetics*; D006801:Humans; D008297:Male; D008969:Molecular Sequence Data; D015183:Restriction Mapping; D012689:Sequence Homology, Nucleic Acid; D012697:Serine Endopeptidases / Q000235:genetics*; D013552:Swine; D013737:Testis / Q000201:enzymology
D004792:Enzyme Precursors; D004247:DNA; D012697:Serine Endopeptidases; C022438:proacrosin; D000176:Acrosin