Lpl

Enables lipoprotein lipase activity and triglyceride binding activity. Involved in several processes, including lipid catabolic process; negative regulation of cellular response to insulin stimulus; and triglyceride biosynthetic process. Located in extracellular space. Used to study abdominal obesity-metabolic syndrome 1; familial hyperlipidemia; metabolic dysfunction-associated steatotic liver disease; and obesity. Biomarker of end stage renal disease; focal segmental glomerulosclerosis; metabolic dysfunction-associated steatotic liver disease; obesity; and type 2 diabetes mellitus. Human ortholog(s) of this gene implicated in Alzheimer's disease; artery disease (multiple); familial hyperlipidemia (multiple); muscular disease; and type 2 diabetes mellitus. Orthologous to human LPL (lipoprotein lipase). [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 Lpl 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 Lpl 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 Lpl gene, providing context for its role in the cell.