Structure and function of the small (30K) subunit of calcium-activated neutral protease (CANP).
Calcium-activated neutral protease (CANP), a typical intracellular protease, is composed of a catalytic 80K subunit (80K) and a 30K subunit (30K) of unknown function. The structure of rabbit CANP 30K was examined to clarify its role in the enzyme function. It has a clear two-domain structure composed of 266 amino acid residues. The N-terminal domain presumably determines the location of CANP, whereas the C-terminal domain is a calmodulin-like Ca2+-binding domain and regulates CANP activity.
D000595:Amino Acid Sequence; D000818:Animals; D002118:Calcium / Q000378:metabolism; D002154:Calpain / Q000032:analysis* / Q000378:metabolism; D008970:Molecular Weight; D011817:Rabbits
D002154:Calpain; D002118:Calcium