Ache

Enables acetylcholinesterase activity; identical protein binding activity; and laminin binding activity. Involved in positive regulation of cold-induced thermogenesis. Acts upstream of or within several processes, including acetylcholine catabolic process; acetylcholine receptor signaling pathway; and regulation of receptor recycling. Located in several cellular components, including basement membrane; cell surface; and neuromuscular junction. Is expressed in several structures, including alimentary system; genitourinary system; musculature; nervous system; and sensory organ. Human ortholog(s) of this gene implicated in Alzheimer's disease; drug dependence (multiple); epilepsy; myasthenia gravis; and subacute delirium. Orthologous to human ACHE (acetylcholinesterase (Yt blood group)). [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 mouse Ache 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 Ache gene in mouse 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 mouse Ache gene, providing context for its role in the cell.