RORa Protein, Human (sf9, His)

RORa Protein, a nuclear receptor, functions as a key regulator in diverse physiological processes, including embryonic development, cellular differentiation, immunity, circadian rhythm, and metabolism of lipids, steroids, xenobiotics, and glucose. Operating as a monomer, RORa binds DNA to ROR response elements (RORE) and exhibits intrinsic transcriptional activity. Natural ligands like oxysterols act as agonists or inverse agonists, modulating its transcriptional activity. RORa recruits distinct cofactor combinations to target gene regulatory regions, modulating their expression depending on tissue, time, and promoter contexts. Its regulatory influence extends to genes involved in photoreceptor and skeletal muscle development, cerebellum development, granule cell proliferation, calcium-mediated signal transduction, and circadian expression of clock genes. In the liver, RORa, along with RORC, acts as a positive or negative modulator of lipid, steroid, and xenobiotic metabolism genes. It also plays a role in hepatic glucose metabolism and adipocyte differentiation regulation. Moreover, RORa is implicated in CD4(+) T-helper cell lineage specification into T(H)17 cells, inhibits NF-kappa-B signaling, and interacts with HIF1A in hypoxia signaling. The multifaceted interactions of RORa with various cofactors and regulatory elements underscore its versatile role in orchestrating complex biological processes.