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For Research Use Only. Not For Clinical Use.
Disease related genes, FDA approved drug targets, Human disease related genes, Transporters, Voltage-gated ion channels
Intracellular, Membrane (different isoforms)
Group enriched (Excitatory neurons, Inhibitory neurons, Horizontal cells, Oligodendrocyte precursor cells)
Not detected in immune cells
Cell line enriched (HDLM-2)
Component of a calcium channel complex consisting of a pore-forming alpha subunit (CACNA1C) and ancillary beta, gamma and delta subunits (PubMed:12181424, PubMed:12176756, PubMed:29742403, PubMed:29078335, PubMed:15141227, PubMed:16299511, PubMed:20953164). The channel complex contains alpha, beta, gamma and delta subunits in a 1:1:1:1 ratio, i.e. it contains only one of each type of subunit (Probable). CACNA1C channel activity is modulated by ancillary subunits, such as CACNB1, CACNB2, CACNB3, CACNA2D1 and CACNA2D4 (PubMed:11741969, PubMed:12181424, PubMed:29742403, PubMed:17224476). Interacts with the gamma subunits CACNG4, CACNG6, CACNG7 and CACNG8 (By similarity). Interacts with CACNB1 (By similarity). Interacts with CACNB2 (PubMed:12176756, PubMed:11741969, PubMed:29742403, PubMed:15141227, PubMed:20953164, PubMed:15863612, PubMed:17224476, PubMed:24728418). Identified in a complex with CACNA2D4 and CACNB3 (PubMed:12181424). Interacts with CACNB3 (PubMed:12181424, PubMed:29742403). Interacts with CACNA2D1 (PubMed:29742403, PubMed:20953164, PubMed:15863612, PubMed:24728418). Interacts with CACNA2D4 (PubMed:12181424). Interacts with CALM1 (PubMed:29742403, PubMed:16299511, PubMed:16338416, PubMed:19279214, PubMed:20953164, PubMed:22518098). Interacts (via the N-terminus and the C-terminal C and IQ motifs) with CABP1; this inhibits Ca(2+)-dependent channel inactivation (PubMed:15140941, PubMed:15980432). The binding via the C motif is calcium independent whereas the binding via IQ requires the presence of calcium and is mutually exclusive with calmodulin binding (PubMed:15140941). The binding to the cytoplasmic N-terminal domain is calcium independent but is essential for the channel modulation. Interacts (via C-terminal CDB motif) with CABP5; in a calcium-dependent manner (By similarity). Interacts with CIB1; the interaction increases upon cardiomyocytes hypertrophy (By similarity). Interacts with STAC2 and STAC3; this inhibits channel inactivation (PubMed:29078335). (Microbial infection) Interacts with influenzavirus H1 hemagglutinin.
Calcium channel, Calmodulin-binding, Ion channel, Voltage-gated channel