Mboat2

Predicted to enable 1-acylglycerophosphocholine O-acyltransferase activity; 1-acylglycerophosphoethanolamine O-acyltransferase activity; and 1-acylglycerophosphoserine O-acyltransferase activity. Predicted to be involved in glycerophospholipid metabolic process; lipid modification; and regulation of chondrocyte differentiation. Predicted to be located in endoplasmic reticulum membrane. Predicted to be active in membrane. Orthologous to human MBOAT2 (membrane bound O-acyltransferase domain containing 2). [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 Mboat2 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 Mboat2 gene, providing context for its role in the cell.