Pla2g4e

Predicted to enable several functions, including calcium-dependent phospholipase A2 activity; phosphatidylinositol-3,4-bisphosphate binding activity; and phospholipid binding activity. Predicted to be involved in N-acylphosphatidylethanolamine metabolic process; glycerophospholipid catabolic process; and positive regulation of endocytic recycling. Predicted to be located in early endosome membrane; lysosomal membrane; and plasma membrane. Predicted to be active in cytosol. Orthologous to human PLA2G4E (phospholipase A2 group IVE). [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 Pla2g4e 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 Pla2g4e 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 Pla2g4e gene, providing context for its role in the cell.