UniProt functional annotation for Q91ZS8



	UniProt functional annotation for Q91ZS8

UniProt code: Q91ZS8.

Organism: Mus musculus (Mouse).

Taxonomy: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus.

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. Can inhibit cell proliferation and migration and can stimulate exocytosis. {ECO:0000269|PubMed:17369310}.

Catalytic activity: Reaction=adenosine in double-stranded RNA + H(+) + H2O = inosine in double-stranded RNA + NH4(+); Xref=Rhea:RHEA:10120, Rhea:RHEA- COMP:13885, Rhea:RHEA-COMP:13886, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:74411, ChEBI:CHEBI:82852; EC=3.5.4.37;

Cofactor: Name=1D-myo-inositol hexakisphosphate; Xref=ChEBI:CHEBI:58130; Evidence={ECO:0000250}; Note=Binds 1 myo-inositol hexakisphosphate (IP6) per subunit. {ECO:0000250};

Subunit: Homodimer. Homodimerization is essential for its catalytic activity. Can form heterodimers with isoform 5 of ADAR/ADAR1 (By similarity). {ECO:0000250}.

Subcellular location: Nucleus {ECO:0000250}. Nucleus, nucleolus {ECO:0000250}. Note=Shuttles between nucleoli and the nucleoplasm. {ECO:0000250}.

Miscellaneous: [Isoform 6]: Likely expressed from an alternative promoter. Contains a region highly similar to the so-called ssRNA- binding R-domain of ADARB2. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Mus musculus (Mouse).
Taxonomy:		Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus.



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. Can inhibit cell proliferation and migration and can stimulate exocytosis. {ECO:0000269\|PubMed:17369310}.


Catalytic activity:		Reaction=adenosine in double-stranded RNA + H(+) + H2O = inosine in double-stranded RNA + NH4(+); Xref=Rhea:RHEA:10120, Rhea:RHEA- COMP:13885, Rhea:RHEA-COMP:13886, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:74411, ChEBI:CHEBI:82852; EC=3.5.4.37;
Cofactor:		Name=1D-myo-inositol hexakisphosphate; Xref=ChEBI:CHEBI:58130; Evidence={ECO:0000250}; Note=Binds 1 myo-inositol hexakisphosphate (IP6) per subunit. {ECO:0000250};
Subunit:		Homodimer. Homodimerization is essential for its catalytic activity. Can form heterodimers with isoform 5 of ADAR/ADAR1 (By similarity). {ECO:0000250}.
Subcellular location:		Nucleus {ECO:0000250}. Nucleus, nucleolus {ECO:0000250}. Note=Shuttles between nucleoli and the nucleoplasm. {ECO:0000250}.
Miscellaneous:		[Isoform 6]: Likely expressed from an alternative promoter. Contains a region highly similar to the so-called ssRNA- binding R-domain of ADARB2. {ECO:0000305}.