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Literature summary for 3.4.22.53 extracted from

  • Montgomery, D.S.; Yu, L.; Ghazi, Z.M.; Thai, T.L.; Al-Khalili, O.; Ma, H.P.; Eaton, D.C.; Alli, A.A.
    ENaC activity is regulated by calpain-2 proteolysis of MARCKS proteins (2017), Am. J. Physiol. Cell Physiol., 313, C42-C53 .
    View publication on PubMedView publication on EuropePMC

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ required Sus scrofa

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
MARCKS protein + H2O Sus scrofa MARCKS protein i.e. myristoylated alanine-rich C kinase substrate is a substrate of calpain-2 in the presence of Ca2+. Calpain-2 proteolysis of MARCKS promotes its interaction with lipids and ENaC at the plasma membrane to allow for the phosphatidylinositol 4,5-bisphosphate (PIP2)-dependent regulation of epithelial sodium channel (ENaC) activity in the kidney ?
-
?

Organism

Organism UniProt Comment Textmining
Sus scrofa P43367
-
-

Source Tissue

Source Tissue Comment Organism Textmining
kidney
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Sus scrofa
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
MARCKS protein + H2O MARCKS protein i.e. myristoylated alanine-rich C kinase substrate is a substrate of calpain-2 in the presence of Ca2+. Calpain-2 proteolysis of MARCKS promotes its interaction with lipids and ENaC at the plasma membrane to allow for the phosphatidylinositol 4,5-bisphosphate (PIP2)-dependent regulation of epithelial sodium channel (ENaC) activity in the kidney Sus scrofa ?
-
?
MARCKS protein + H2O MARCKS protein i.e. myristoylated alanine-rich C kinase substrate is a substrate of calpain-2 in the presence of Ca2+ Sus scrofa ?
-
?

General Information

General Information Comment Organism
metabolism MARCKS protein i.e. myristoylated alanine-rich C kinase substrate is a substrate of calpain-2 in the presence of Ca2+. Calpain-2 proteolysis of MARCKS promotes its interaction with lipids and ENaC at the plasma membrane to allow for the phosphatidylinositol 4,5-bisphosphate (PIP2)-dependent regulation of epithelial sodium channel (ENaC) activity in the kidney Sus scrofa