Rat Predicted to work with:
Fusion protein: SFRARRDLLQLSYGEAKKAARDYDLAKNYFKKSLRDMGYGNWISKPQEEK NFYLCPVPND, corresponding to amino acids 1116-1176 of Rat ADAR1.
The fusion protein was constructed in the pGEX-KG vector by inserting a fragment corresponding to nucleotides +3346 through +3525 of ADAR1 at the XbaI and XhoI sites in the vector.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
1/1000. Predicted molecular weight: 136 kDa.
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.
Ubiquitously expressed, highest levels were found in brain and lung.
Involvement in disease
Defects in ADAR are a cause of dyschromatosis symmetrical hereditaria (DSH) [MIM:127400]; also known as reticulate acropigmentation of Dohi. DSH is a pigmentary genodermatosis of autosomal dominant inheritance characterized by a mixture of hyperpigmented and hypopigmented macules distributed on the dorsal parts of the hands and feet.
Contains 1 A to I editase domain. Contains 2 DRADA repeats. Contains 3 DRBM (double-stranded RNA-binding) domains.
Sumoylation reduces RNA-editing activity.
Cytoplasm. Nucleus > nucleolus. Isoform 1 is found predominantly in cytoplasm but appears to shuttle between the cytoplasm and nucleus. Isoform 5 is found exclusively in the nucleolus.