Uveal autoantigen with coiled-coil domains and ankyrin repeats (UACA)

Uveal autoantigen with coiled-coil domains and ankyrin repeats (UACA) is a human protein coded by the UACA gene and characterized by a structure containing ankyrin repeats and coiled-coil domains[1][9]. It acts primarily as a regulatory adaptor/scaffold protein influencing apoptotic pathways—specifically promoting apoptosis through upregulation of the apoptosome, inhibition of galectin-3, and inactivation of NF-κB, as well as modulating the localization and function of APAF1[4][1]. UACA has been implicated in regulation of cell growth, motility, and cell structure via actin dynamics[8]. UACA expression is upregulated in several human cancers, notably hepatocellular carcinoma, where it may promote tumor growth and invasion; silencing or knockdown reduces proliferation, invasiveness, and induces senescence in cancer cells[2]. UACA is regulated by hypoxia, possibly mediated by HIF1α, and is associated with cancer progression under hypoxic conditions[2]. UACA is also recognized as an autoantigen in human diseases such as panuveitis and Graves' disease, where autoantibodies against UACA have diagnostic utility[1][3][5]. No targeted drugs or inhibitors to UACA are in clinical use or advanced development, but UACA is considered a potential therapeutic target in oncology research, particularly for tumors with high UACA expression[2][1].

Other names

KIAA1561FLJ10128Nuclingnuclear membrane binding proteinUACA

No clinically proven drugs or mechanistic drug interventions directly target UACA.