Aliases for TRPC4 Gene
External Ids for TRPC4 Gene
Previous GeneCards Identifiers for TRPC4 Gene
This gene encodes a member of the canonical subfamily of transient receptor potential cation channels. The encoded protein forms a non-selective calcium-permeable cation channel that is activated by Gq-coupled receptors and tyrosine kinases, and plays a role in multiple processes including endothelial permeability, vasodilation, neurotransmitter release and cell proliferation. Single nucleotide polymorphisms in this gene may be associated with generalized epilepsy with photosensitivity. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene. [provided by RefSeq, Aug 2011]
GeneCards Summary for TRPC4 Gene
TRPC4 (Transient Receptor Potential Cation Channel, Subfamily C, Member 4) is a Protein Coding gene. Among its related pathways are L1CAM interactions and CREB Pathway. GO annotations related to this gene include beta-catenin binding and store-operated calcium channel activity. An important paralog of this gene is TRPC6.
UniProtKB/Swiss-Prot for TRPC4 Gene
Form a receptor-activated non-selective calcium permeant cation channel. Acts as a cell-cell contact-dependent endothelial calcium entry channel. Probably operated by a phosphatidylinositol second messenger system activated by receptor tyrosine kinases or G-protein coupled receptors. Mediates cation entry, with an enhanced permeability to barium over calcium. May also be activated by intracellular calcium store depletion.
The classical or canonical transient receptor potential (TRPC) channels are the subfamily most closely related to the founding member of the TRP family, the Drosophila TRP channel. TRPC channels have seven TRPC genes that encode the channel protein; these are named TRPC1-7 (TRPC2 is a pseudogene in humans). They are non-selective, calcium permeable cation channels; however their permeability ratio of calcium/sodium ions varies between different members of the family. Generally, TRPC channels can be activated by phospholipase C, with some members (TRPC3, -6 and -7) being activated directly by diacylglycerol (DAG)