Dclk1

This gene encodes a member of the protein kinase superfamily and the doublecortin family. The typical protein encoded by this gene contains two N-terminal doublecortin domains, which bind microtubules and regulate microtubule polymerization, a C-terminal serine/threonine protein kinase domain, which shows substantial homology to Ca2+/calmodulin-dependent protein kinase, and a serine/proline-rich domain in between the doublecortin and the protein kinase domains, which mediates multiple protein-protein interactions. The microtubule-polymerizing activity of the protein is independent of its protein kinase activity. This gene is involved in several different cellular processes, including neuronal migration, retrograde transport, neuronal apoptosis and neurogenesis. Multiple transcript variants generated by two alternative promoter usage and alternative splicing have been found, but the full-length nature of the variant produced from the 5' promoter has not been determined. Current reference sequence data represents two alternatively spliced transcript variants produced from the 3' promoter and their protein products lack the doublecortin domain.[provided by RefSeq, Sep 2010]

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 Dclk1 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 Dclk1 gene, providing context for its role in the cell.