Rhoa

Enables several functions, including GTPase activity; Rho GDP-dissociation inhibitor binding activity; and guanyl ribonucleotide binding activity. Involved in several processes, including negative regulation of canonical NF-kappaB signal transduction; positive regulation of actin filament polymerization; and regulation of neuron projection development. Acts upstream of or within Rho protein signal transduction; negative regulation of vascular associated smooth muscle cell migration; and negative regulation of vascular associated smooth muscle cell proliferation. Located in several cellular components, including axon; dendritic spine; and neuronal cell body. Used to study membranous glomerulonephritis. Biomarker of artery disease (multiple); asthma; fetal alcohol syndrome; obesity; and primary biliary cholangitis. Human ortholog(s) of this gene implicated in breast carcinoma. Orthologous to human RHOA (ras homolog family member A). [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 Rhoa 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 Rhoa 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 Rhoa gene, providing context for its role in the cell.