Calpain 4
Definition:
EC Tree > 3 Hydrolases > 3.4 Acting on peptide bonds (peptidases) > 3.4.22 Cysteine endopeptidases > 3.4.22.B24 calpain 4
Calpain 4 is the small regulatory subunit of the classical calpain heterodimers, found in viruses and cellular organisms. It pairs with the large catalytic subunits calpain-1 and calpain-2 and is required for their stability and membrane association. Although not itself catalytic, it governs broad endopeptidase specificity of the holoenzyme by modulating Ca2+ sensitivity. In cells it supports cytoskeletal remodeling and signal transduction. It features a glycine-rich N-terminal domain and a C-terminal EF-hand Ca2+-binding domain.
Calpain 4 is the small regulatory subunit of the classical calpain heterodimers, found in viruses and cellular organisms. It pairs with the large catalytic subunits calpain-1 and calpain-2 and is required for their stability and membrane association. Although not itself catalytic, it governs broad endopeptidase specificity of the holoenzyme by modulating Ca2+ sensitivity. In cells it supports cytoskeletal remodeling and signal transduction. It features a glycine-rich N-terminal domain and a C-terminal EF-hand Ca2+-binding domain.
References:
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