Trpc6

Enables several functions, including ATPase binding activity; clathrin binding activity; and cytoskeletal protein binding activity. Involved in several processes, including cellular response to hydrogen peroxide; negative regulation of dendrite morphogenesis; and positive regulation of peptidyl-threonine phosphorylation. Predicted to be located in cytoplasm; plasma membrane; and slit diaphragm. Used to study focal segmental glomerulosclerosis; kidney disease; and transient cerebral ischemia. Biomarker of proteinuria and type 2 diabetes mellitus. Human ortholog(s) of this gene implicated in chronic fatigue syndrome; focal segmental glomerulosclerosis; focal segmental glomerulosclerosis 2; and nephrotic syndrome type 2. Orthologous to human TRPC6 (transient receptor potential cation channel subfamily C member 6). [provided by Alliance of Genome Resources, Jul 2025]

A protein domain is a distinct structural or functional region within a protein that can evolve, function, and exist independently of the rest of the protein chain. These domains in rat Trpc6 often fold into stable, three-dimensional structures and are associated with specific biological functions, such as binding to DNA, other proteins, or small molecules.

Biological processes and signaling networks where the Trpc6 gene in rat plays a role, providing insight into its function and relevance in health or disease.

The most significant associations for this gene, including commonly observed domains, pathway involvement, and functional highlights based on current data.

Locations within the cell where the protein is known or predicted to be active, providing insight into its function and cellular context.

Describes the biological processes, cellular components, and molecular functions associated with the rat Trpc6 gene, providing context for its role in the cell.