Primary structure of human proacrosin deduced from its cDNA sequence

FEBS Letters

Kashiwabara, Shin-ichi¹  Baba, Tadashi¹  Arai, Yuji¹  Watanabe, Ken¹ 

[1] Institute of Applied Biochemistry, University of Tsukuba, Ibaraki 305, Japan

关键词: Acrosin;    Serine protease;    Amino acid sequence;    cDNA;    (Human testis);   

DOI  :  10.1016/0014-5793(89)80549-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown