Napepld

Enables N-acylphosphatidylethanolamine-specific phospholipase D activity. Involved in several processes, including N-acylphosphatidylethanolamine metabolic process; host-mediated regulation of intestinal microbiota composition; and positive regulation of brown fat cell differentiation. Acts upstream of or within N-acylethanolamine metabolic process. Is active in hippocampal mossy fiber to CA3 synapse; smooth endoplasmic reticulum membrane; and synaptic membrane. Is expressed in cerebral cortex. Orthologous to human NAPEPLD (N-acyl phosphatidylethanolamine phospholipase D). [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 Napepld 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 Napepld 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 Napepld gene, providing context for its role in the cell.