Converts multiple adenosines to inosines and creates I/U mismatched base pairs in double-helical RNA substrates without apparent sequence specificity. Has been found to modify more frequently adenosines in AU-rich regions, probably due to the relative ease of melting A/U base pairs as compared to G/C pairs. Functions to modify viral RNA genomes and may be responsible for hypermutation of certain negative-stranded viruses. Edits the messenger RNAs for glutamate receptor (GLUR) subunits by site- selective adenosine deamination. Produces low-level editing at the GLUR-B Q/R site, but edits efficiently at the R/G site and HOTSPOT1. Binds to short interfering RNAs (siRNA) without editing them and suppresses siRNA-mediated RNA interference. Binds to ILF3/NF90 and up-regulates ILF3-mediated gene expression. Isoform 1 is induced by interferon alpha. Isoform 5 is constitutively expressed. Homodimer. Isoform 1 interacts with ILF2/NF45 and ILF3/NF90. 5 isoforms of the human protein are produced by alternative promoter. Note: This description may include information from UniProtKB.
Protein type: EC 3.5.4.-; Hydrolase; RNA processing
Molecular Function: double-stranded RNA adenosine deaminase activity; protein binding; DNA binding; metal ion binding; double-stranded RNA binding
Biological Process: base conversion or substitution editing; positive regulation of viral genome replication; cytokine and chemokine mediated signaling pathway; response to virus; adenosine to inosine editing; protein import into nucleus; mRNA modification; innate immune response; gene expression; RNA-mediated gene silencing; protein export from nucleus; mRNA processing; negative regulation of apoptosis
SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.