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Trpc6 forms a receptor-activated calcium channel in the cell membrane. The Trpc6 channel is activated by diacylglycerol and is thought to be under the control of a phosphatidylinositol second messenger system. Activation of the Trpc6 channel occurs independently of protein kinase C and is not triggered by low levels of intracellular calcium. Defects in the Trpc6 gene are a cause of focal segmental glomerulosclerosis 2 (FSGS2). Further, Trpc6 is a member of the mammalian transient receptor potential (TRP) superfamily can be divided into three major families including the “canonical TRP” (TRPC) family. The seven members of this family share the activation through PLC-coupled receptors and have been suggested to be components of receptor-regulated cation channels in different cell types. Furthermore, the members of the TRPC6/6/7 subfamily can be activated by diacylglycerol (DAG) analogs, suggesting a possible mechanism of activation of these channels by PLC-coupled receptors. When expressed in transfected cells, Trpc6 acts as a non-selective store-independent receptor-activated cation channel. Trpc6 is activated by DAG in a PKC-independent manner and is insensitive to IP3 activation. There is increasing evidence that Trpc6 encodes endogenous DAG-activated receptor-operated cation channels in vivo. Diseases associated with TRPC6 include Glomerulosclerosis, Focal Segmental, 2 and Focal Segmental Glomerulosclerosis.
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Protein Aliases: FLJ11098; FLJ14863; focal segmental glomerulosclerosis 2; HGNC:12338; Short transient receptor potential channel 6; transient receptor potential cation channel, subfamily C, member 6; Transient receptor protein 6; TRP-6; trp6A; TrpC6
Gene Aliases: FSGS2; TRP6; TRPC6
UniProt ID: (Human) Q9Y210
Entrez Gene ID: (Human) 7225
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