Domain:The 2 CARD domains are responsible for interaction with and signaling through MAVS.,Domain:The helicase domain is responsible for dsRNA recognition.,Domain:The repressor domain controls homomultimerization and interaction with MAVS.,Function:Involved in innate immune defense against viruses. Upon interaction with intracellular dsRNA produced during viral replication, triggers a transduction cascade involving MAVS/IPS1, which results in the activation of NF-kappa-B, IRF3 and IRF7 and the induction of the expression of antiviral cytokines such as IFN-beta and RANTES (CCL5). Essential for the production of interferons in response to RNA viruses including paramyxoviruses, influenza viruses, Japanese encephalitis virus and HCV.,induction:By bacterial lipopolysaccharide (LPS) in endothelial cells. By IFN-alpha, -beta and -gamma.,PTM:Isgylated. Conjugated to ubiquitin-like protein ISG15 upon IFN-beta stimulation.,similarity:Belongs to the helicase family.,similarity:Contains 1 helicase ATP-binding domain.,similarity:Contains 1 helicase C-terminal domain.,similarity:Contains 2 CARD domains.,subunit:Monomer; maintained as a monomer in an autoinhibited state. Upon viral dsRNA binding and conformation shift, homomultimerizes and interacts with MAVS. Interacts with DHX58/LGP2, IKBKE, TBK1 and TMEM173/STING.,tissue specificity:Present in vascular smooth cells (at protein level).,
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