Function: Catalyzes the hydrolytic deamination of adenosine to inosine in double-stranded RNA (dsRNA) referred to as A-to-I RNA editing. This may affect gene expression and function in a number of ways that include mRNA translation by changing codons and hence the amino acid sequence of proteins; pre-mRNA splicing by altering splice site recognition sequences; RNA stability by changing sequences involved in nuclease recognition; genetic stability in the case of RNA virus genomes by changing sequences during viral RNA replication; and RNA structure-dependent activities such as microRNA production or targeting or protein-RNA interactions. Can edit both viral and cellular RNAs and can edit RNAs at multiple sites (hyper-editing) or at specific sites (site-specific editing). Its cellular RNA substrates include: bladder cancer-associated protein (BLCAP), neurotransmitter receptors for glutamate (GRIA2 and GRIK2) and serotonin (HTR2C), GABA receptor (GABRA3) and potassium voltage-gated channel (KCNA1). Site-specific RNA editing of transcripts encoding these proteins results in amino acid substitutions which consequently alter their functional activities. Edits GRIA2 at both the Q/R and R/G sites efficiently but converts the adenosine in hotspot1 much less efficiently
By similarity. Can inhibit cell proliferation and migration and can stimulate exocytosis. Ref.2 Ref.3 Ref.4
Cofactor: Binds 1 inositol hexakisphosphate (IP6) per subunit
By similarity.
Subunit structure: Homodimer. Homodimerization is essential for its catalytic activity
By similarity.
Subcellular location: Nucleus
By similarity. Nucleus › nucleolus
By similarity. Note: Shuttles between nucleoli and the nucleoplasm
By similarity.
Tissue specificity: Brain and peripheral tissues.
Sequence similarities: Contains 1 A to I editase domain.Contains 2 DRBM (double-stranded RNA-binding) domains.
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