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

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Citation

Aoki K, Imajoh S, Ohno S, Emori Y, Koike M, Kosaki G, Suzuki K

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

FEBS Lett. 1986 Sep 15;205(2):313-7.

PubMed ID
3017764 [ View in PubMed
]
Abstract

The complete amino acid sequence of the large subunit (catalytic subunit) of human low-Ca2+-requiring-calcium-activated neutral protease (muCANP) 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 muCANP, 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.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
Calpain-1 catalytic subunitP07384Details