ADAR

Adenosine deaminase, RNA-specific

PDB rendering based on 1qbj.

Available structures
PDB	1QBJ, 1QGP, 1XMK, 2ACJ, 2GXB, 3F21, 3F22, 3F23, 3IRQ, 3IRR

Identifiers

Symbols

ADAR; ADAR1; DRADA; DSH; DSRAD; G1P1; IFI-4; IFI4; K88DSRBP; P136

External IDs

OMIM: 146920 MGI: 1889575 HomoloGene: 9281 GeneCards: ADAR Gene

EC number

3.5.4.-

Gene Ontology
Molecular function	• DNA binding • double-stranded RNA binding • double-stranded RNA adenosine deaminase activity • double-stranded RNA adenosine deaminase activity • double-stranded RNA adenosine deaminase activity • hydrolase activity • metal ion binding
Cellular component	• intracellular • nucleus • nucleus • nucleoplasm • nucleolus • cytoplasm
Biological process	• adenosine to inosine editing • mRNA processing • base conversion or substitution editing • mRNA modification • cytokine-mediated signaling pathway • gene silencing by RNA • negative regulation of apoptosis • type I interferon-mediated signaling pathway
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 1:
154.55 – 154.6 Mb

Chr 3:
89.52 – 89.56 Mb

PubMed search

[1]

[2]

Double-stranded RNA-specific adenosine deaminase is an enzyme that in humans is encoded by the ADAR gene.^[1]^[2]

This gene encodes the enzyme responsible for RNA editing by site-specific deamination of adenosines. This enzyme destabilizes double stranded RNA through conversion of adenosine to inosine. Mutations in this gene have been associated with dyschromatosis symmetrica hereditaria. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.^[2]

References

^ Kim U, Wang Y, Sanford T, Zeng Y, Nishikura K (Dec 1994). "Molecular cloning of cDNA for double-stranded RNA adenosine deaminase, a candidate enzyme for nuclear RNA editing". Proc Natl Acad Sci USA 91 (24): 11457–61. doi:10.1073/pnas.91.24.11457. PMC 45250. PMID 7972084. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=45250.
^ ^a ^b "Entrez Gene: ADAR Adenosine Deaminase Acting on RNA". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=103.

Valenzuela A, Blanco J, Callebaut C, et al. (1997). "HIV-1 envelope gp120 and viral particles block adenosine deaminase binding to human CD26". Adv. Exp. Med. Biol. 421: 185–92. PMID 9330696.
Wathelet MG, Szpirer J, Nols CB, et al. (1988). "Cloning and chromosomal location of human genes inducible by type I interferon". Somat. Cell Mol. Genet. 14 (5): 415–26. doi:10.1007/BF01534709. PMID 3175763.
Wang Y, Zeng Y, Murray JM, Nishikura K (1996). "Genomic organization and chromosomal location of the human dsRNA adenosine deaminase gene: the enzyme for glutamate-activated ion channel RNA editing". J. Mol. Biol. 254 (2): 184–95. doi:10.1006/jmbi.1995.0610. PMID 7490742.
Patterson JB, Samuel CE (1995). "Expression and regulation by interferon of a double-stranded-RNA-specific adenosine deaminase from human cells: evidence for two forms of the deaminase". Mol. Cell. Biol. 15 (10): 5376–88. PMC 230787. PMID 7565688. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=230787.
Patterson JB, Thomis DC, Hans SL, Samuel CE (1995). "Mechanism of interferon action: double-stranded RNA-specific adenosine deaminase from human cells is inducible by alpha and gamma interferons". Virology 210 (2): 508–11. doi:10.1006/viro.1995.1370. PMID 7618288.
O'Connell MA, Krause S, Higuchi M, et al. (1995). "Cloning of cDNAs encoding mammalian double-stranded RNA-specific adenosine deaminase". Mol. Cell. Biol. 15 (3): 1389–97. PMC 230363. PMID 7862132. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=230363.
Weier HU, George CX, Greulich KM, Samuel CE (1996). "The interferon-inducible, double-stranded RNA-specific adenosine deaminase gene (DSRAD) maps to human chromosome 1q21.1-21.2". Genomics 30 (2): 372–5. doi:10.1006/geno.1995.0034. PMID 8586444.
Liu Y, George CX, Patterson JB, Samuel CE (1997). "Functionally distinct double-stranded RNA-binding domains associated with alternative splice site variants of the interferon-inducible double-stranded RNA-specific adenosine deaminase". J. Biol. Chem. 272 (7): 4419–28. doi:10.1074/jbc.272.7.4419. PMID 9020165.
Valenzuela A, Blanco J, Callebaut C, et al. (1997). "Adenosine deaminase binding to human CD26 is inhibited by HIV-1 envelope glycoprotein gp120 and viral particles". J. Immunol. 158 (8): 3721–9. PMID 9103436.
Herbert A, Alfken J, Kim YG, et al. (1997). "A Z-DNA binding domain present in the human editing enzyme, double-stranded RNA adenosine deaminase". Proc. Natl. Acad. Sci. U.S.A. 94 (16): 8421–6. doi:10.1073/pnas.94.16.8421. PMC 22942. PMID 9237992. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=22942.
Liu Y, Herbert A, Rich A, Samuel CE (1998). "Double-stranded RNA-specific adenosine deaminase: nucleic acid binding properties". Methods 15 (3): 199–205. doi:10.1006/meth.1998.0624. PMID 9735305.
George CX, Samuel CE (1999). "Human RNA-specific adenosine deaminase ADAR1 transcripts possess alternative exon 1 structures that initiate from different promoters, one constitutively active and the other interferon inducible". Proc. Natl. Acad. Sci. U.S.A. 96 (8): 4621–6. doi:10.1073/pnas.96.8.4621. PMC 16382. PMID 10200312. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=16382.
Schwartz T, Rould MA, Lowenhaupt K, et al. (1999). "Crystal structure of the Zalpha domain of the human editing enzyme ADAR1 bound to left-handed Z-DNA". Science 284 (5421): 1841–5. doi:10.1126/science.284.5421.1841. PMID 10364558.
Schade M, Turner CJ, Kühne R, et al. (1999). "The solution structure of the Zα domain of the human RNA editing enzyme ADAR1 reveals a prepositioned binding surface for Z-DNA". Proc. Natl. Acad. Sci. U.S.A. 96 (22): 12465–70. doi:10.1073/pnas.96.22.12465. PMC 22950. PMID 10535945. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=22950.
Blanco J, Valenzuela A, Herrera C, et al. (2000). "The HIV-1 gp120 inhibits the binding of adenosine deaminase to CD26 by a mechanism modulated by CD4 and CXCR4 expression". FEBS Lett. 477 (1–2): 123–8. doi:10.1016/S0014-5793(00)01751-8. PMID 10899322.
Herrera C, Morimoto C, Blanco J, et al. (2001). "Comodulation of CXCR4 and CD26 in human lymphocytes". J. Biol. Chem. 276 (22): 19532–9. doi:10.1074/jbc.M004586200. PMID 11278278.
Wong SK, Sato S, Lazinski DW (2001). "Substrate recognition by ADAR1 and ADAR2". RNA 7 (6): 846–58. doi:10.1017/S135583820101007X. PMC 1370134. PMID 11421361. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1370134.
Eckmann CR, Neunteufl A, Pfaffstetter L, Jantsch MF (2001). "The Human But Not the Xenopus RNA-editing Enzyme ADAR1 Has an Atypical Nuclear Localization Signal and Displays the Characteristics of a Shuttling Protein". Mol. Biol. Cell 12 (7): 1911–24. PMC 55639. PMID 11451992. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=55639.

PDB gallery

1qbj: CRYSTAL STRUCTURE OF THE ZALPHA Z-DNA COMPLEX

1qgp: NMR STRUCTURE OF THE Z-ALPHA DOMAIN OF ADAR1, 15 STRUCTURES

1xmk: The Crystal structure of the Zb domain from the RNA editing enzyme ADAR1

2acj: Crystal structure of the B/Z junction containing DNA bound to Z-DNA binding proteins

2gxb: Crystal Structure of The Za Domain bound to Z-RNA

ADAR

See also

References

Further reading