Ace

Enables heterocyclic compound binding activity; metallopeptidase activity; and peptidyl-dipeptidase activity. Involved in several processes, including blood vessel diameter maintenance; negative regulation of transport; and response to corticosteroid. Located in several cellular components, including basal plasma membrane; brush border membrane; and sperm midpiece. Used to study several diseases, including artery disease (multiple); glomerulonephritis (multiple); kidney failure (multiple); lung disease (multiple); and proteinuria (multiple). Biomarker of several diseases, including artery disease (multiple); congenital diaphragmatic hernia; endomyocardial fibrosis; liver cirrhosis (multiple); and lung disease (multiple). Human ortholog(s) of this gene implicated in several diseases, including artery disease (multiple); autoimmune disease (multiple); gastrointestinal system cancer (multiple); heart valve disease (multiple); and lung disease (multiple). Orthologous to human ACE (angiotensin I converting enzyme). [provided by Alliance of Genome Resources, Apr 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 Ace 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 Ace 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.