Serpinb9

Predicted to enable cysteine-type endopeptidase inhibitor activity involved in apoptotic process; protease binding activity; and serine-type endopeptidase inhibitor activity. Predicted to be involved in several processes, including cellular response to estrogen stimulus; negative regulation of endopeptidase activity; and protection from natural killer cell mediated cytotoxicity. Predicted to act upstream of or within several processes, including T cell mediated cytotoxicity; acute inflammatory response to antigenic stimulus; and negative regulation of T cell apoptotic process. Predicted to be located in Golgi apparatus; cytosol; and nucleoplasm. Predicted to be active in cytoplasm and extracellular space. Orthologous to human SERPINB9 (serpin family B member 9). [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 Serpinb9 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 Serpinb9 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.