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Complete amino acid sequence of the large subunit of the low‐Ca 2+ ‐requiring form of human Ca 2+ ‐activated neutral protease (μCANP) deduced from its cDNA sequence
Author(s) -
Aoki Kazumasa,
Imajoh Shinobu,
Ohno Shigeo,
Emori Yasufumi,
Koike Morio,
Kosaki Goro,
Suzuki Koichi
Publication year - 1986
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(86)80919-x
Subject(s) - complementary dna , peptide sequence , protein subunit , protease , sequence (biology) , amino acid , biology , biochemistry , microbiology and biotechnology , enzyme , gene
The complete amino acid sequence of the large subunit (catalytic subunit) of human low‐Ca 2+ 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 Ca 2+ sensitivities are significantly different. The role of each domain in the Ca 2+ sensitivity and protease activity of CANP is discussed on the basis of sequence comparison.