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enzymatic reaction
Calpain cleaves membrane-bound protein kinase C (group A ==> Ca+2-dependent) to yield constitutively active cytosolic form.
Properties
GENERAL:
catalytic reaction
SPECIFIC:
biochemical ligation
sialylation
active transport
protein phosphorylation
proteolytic cleavage
template-directed reaction
ENZYME:
calpain
COMPARTMENT: cytoplasm
MOTIF: Ca+2-binding site
EFFECTOR-BOUND: Ca+2
STATE: active state
SUBSTRATE:
protein kinase C type-A*
COMPARTMENT: plasma membrane*
CELL: most cell types*
ORGANISM: eukaryote*
STATE: active state
MOTIF: cysteine-rich region
Zinc finger
NAME: Zinc finger (2)
EFFECTOR-BOUND: Zn+2
binding site
EFFECTOR-BOUND: diacylglycerol
C2 domain
MOTIF: allosteric site
EFFECTOR-BOUND: phosphatidylserine
PEST region
EFFECTOR-BOUND: Ca+2
kinase domain
MOTIF: ATP-binding site
NAME: ATP-binding site
PRODUCT:
protein kinase C type-A*
COMPARTMENT: cytoplasm
STATE: active state
MOTIF: cysteine-rich region
Zinc finger
NAME: Zinc finger (2)
EFFECTOR-BOUND: Zn+2
binding site
EFFECTOR-BOUND: diacylglycerol
C2 domain
MOTIF: allosteric site
EFFECTOR-BOUND: phosphatidylserine
PEST region
EFFECTOR-BOUND: Ca+2
kinase domain
MOTIF: ATP-binding site
NAME: ATP-binding site
peptide
COMPARTMENT: plasma membrane
References
- PMID: 90050512
- Wang KK et al
Calmodulin-binding proteins as calpain substrates.
Biochem J 262:693 1989
PMID: 2556106