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Literature summary extracted from

  • Ermolova, N.; Kramerova, I.; Spencer, M.J.
    Autolytic activation of calpain 3 proteinase is facilitated by calmodulin protein (2015), J. Biol. Chem., 290, 996-1004.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.4.22.54 Calmodulin calmodulin binds the calpain 3 non-catalytic domain C2L and promotes enzyme activation Mus musculus

Protein Variants

EC Number Protein Variants Comment Organism
3.4.22.54 C129S inactive Mus musculus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.4.22.54 Ca2+ dependent on Mus musculus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.4.22.54 94000
-
 x * 94000, full-length enzyme, SDS-PAGE Mus musculus

Organism

EC Number Organism UniProt Comment Textmining
3.4.22.54 Mus musculus Q64691
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.4.22.54 skeletal muscle
-
 Mus musculus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.22.54 titin + H2O
-
 Mus musculus ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.4.22.54 ? x * 94000, full-length enzyme, SDS-PAGE Mus musculus

Synonyms

EC Number Synonyms Comment Organism
3.4.22.54 calpain 3
-
 Mus musculus
3.4.22.54 CAPN3
-
 Mus musculus

General Information

EC Number General Information Comment Organism
3.4.22.54 malfunction mutations of calpain 3 cause limb-girdle dystrophy 2A Mus musculus