Sod1

Enables copper ion binding activity; protein phosphatase 2B binding activity; and superoxide dismutase activity. Involved in several processes, including hydrogen peroxide biosynthetic process; removal of superoxide radicals; and response to antipsychotic drug. Located in several cellular components, including dense core granule; neuronal cell body; and peroxisome. Part of protein-containing complex. Used to study hyperthyroidism; hypothyroidism; middle cerebral artery infarction; and sciatic neuropathy. Biomarker of several diseases, including alcohol use disorder; artery disease (multiple); congenital diaphragmatic hernia; metabolic dysfunction-associated steatohepatitis; and middle cerebral artery infarction. Human ortholog(s) of this gene implicated in several diseases, including Down syndrome; artery disease (multiple); eye disease (multiple); glucose metabolism disease (multiple); and neurodegenerative disease (multiple). Orthologous to human SOD1 (superoxide dismutase 1). [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 Sod1 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 Sod1 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 Sod1 gene, providing context for its role in the cell.