Complete amino acid sequence of the large subunit of the low‐Ca2+‐requiring form of human Ca2+‐activated neutral protease (μCANP) deduced from its cDNA sequence

FEBS Letters

Koike, Morio¹  Aoki, Kazumasa²  Ohno, Shigeo²  Imajoh, Shinobu²  Emori, Yasufumi²  Kosaki, Goro¹  Suzuki, Koichi² 

[1] Tokyo Metropolitan Komagome Hospital, Bunkyo-ku, Tokyo 113, Japan;Department of Molecular Biology, The Tokyo Metropolitan Institute of Medical Science Tokyo 113, Japan

关键词: Ca2+-activated neutral protease Calpain Thiol protease cDNA cloning Sequence homology Ca2+;   

DOI  :  10.1016/0014-5793(86)80919-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The complete amino acid sequence of the large subunit (catalytic subunit) of human low-Ca²⁺ requiring-calcium-activated neutral protease (μCANP) was deduced from its cDNA base sequence. It is composed of 714 amino acid residues and its sequence is highly homologous to the chicken CANP sequence determined previously. Human μCANP, like chicken CANP, has a clear 4-domain structure, and their fundamental structures are essentially the same, although their Ca²⁺sensitivities are significantly different. The role of each domain in the Ca²⁺sensitivity and protease activity of CANP is discussed on the basis of sequence comparison.

【 授权许可】

Unknown