Vwf

Predicted to enable several functions, including identical protein binding activity; integrin binding activity; and protein-folding chaperone binding activity. Involved in several processes, including cellular response to cold; cellular response to lipopolysaccharide; and liver regeneration. Located in collagen-containing extracellular matrix and extracellular space. Used to study transient cerebral ischemia. Biomarker of hypertension; mesangial proliferative glomerulonephritis; myocardial infarction; pulmonary fibrosis; and type 1 diabetes mellitus. Human ortholog(s) of this gene implicated in several diseases, including Behcet's disease; Bernard-Soulier syndrome; end stage renal disease; essential thrombocythemia; and von Willebrand's disease (multiple). Orthologous to human VWF (von Willebrand factor). [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 Vwf 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 Vwf 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 Vwf gene, providing context for its role in the cell.