Carmil3

Predicted to be involved in cell migration; regulation of Arp2/3 complex-mediated actin nucleation; and regulation of postsynapse assembly. Predicted to be located in cytoplasm. Predicted to be active in several cellular components, including glutamatergic synapse; lamellipodium; and postsynapse. Orthologous to human CARMIL3 (capping protein regulator and myosin 1 linker 3). [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 Carmil3 often fold into stable, three-dimensional structures and are associated with specific biological functions, such as binding to DNA, other proteins, or small molecules.

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 Carmil3 gene, providing context for its role in the cell.