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CALM

Domain

The N-terminal and C-terminal lobes of CALM bind to the C-terminus of KCNQ1 in a clamp-like conformation. Binding of CALM C-terminus to KCNQ1 is calcium-independent but is essential for assembly of the structure. Binding of CALM N-terminus to KCNQ1 is calcium-dependent and regulates electrophysiological activity of the channel. The C-lobe interacts with KCNN4 channels in a calcium-independent manner, whereas the N-lobe interacts with the S4-S5 linker of KCNN4 in a calcium-dependent manner playing a role as calcium sensor and gating the channel.

Function

Calmodulin acts as part of a calcium signal transduction pathway by mediating the control of a large number of enzymes, ion channels, aquaporins and other proteins through calcium-binding. Calcium-binding is required for the activation of calmodulin. Among the enzymes to be stimulated by the calmodulin-calcium complex are a number of protein kinases, such as myosin light-chain kinases and calmodulin-dependent protein kinase type II (CaMK2), and phosphatases. Together with CCP110 and centrin, is involved in a genetic pathway that regulates the centrosome cycle and progression through cytokinesis. Is a regulator of voltage-dependent L-type calcium channels. Mediates calcium-dependent inactivation of CACNA1C. Positively regulates calcium-activated potassium channel activity of KCNN2. Forms a potassium channel complex with KCNQ1 and regulates electrophysiological activity of the channel via calcium-binding. Acts as a sensor to modulate the endoplasmic reticulum contacts with other organelles mediated by VMP1:ATP2A2.

Post-translational modifications

Ubiquitination results in a strongly decreased activity.

Phosphorylation results in a decreased activity.

Sequence Similarities

Belongs to the calmodulin family.

Cellular localization

Alternative names

CAM, CALM, Calmodulin, CaM

swissprot:P62157 entrezGene:520277 entrezGene:326597