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Information on EC 3.5.4.37 - double-stranded RNA adenine deaminase and Organism(s) Mus musculus and UniProt Accession Q99MU3
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3.5.4.37 double-stranded RNA adenine deaminaseIUBMB Comments
This eukaryotic enzyme is involved in RNA editing. It destabilizes double-stranded RNA through conversion of adenosine to inosine. Inositol hexakisphosphate is required for activity .
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Word Map
- 3.5.4.37
- inosine
-
a-to-i
- deaminases
-
deamination
-
adenosine-to-inosine
-
hereditaria
-
rna-editing
- pre-mrnas
-
dyschromatosis
-
symmetrica
- z-dna
- duplex
- ampa
-
left-handed
-
unedited
-
glur-b
-
recoding
-
site-selective
-
macules
-
interferon-inducible
- mda5
-
hypopigmented
-
ifn-inducible
-
dsrbds
-
interferon-stimulated
-
ca2+-permeable
-
5-ht2cr
- dicer
- samhd1
-
genodermatosis
- rig-i
-
hypermutation
-
ifn-stimulated
-
pigmentary
-
interferonopathy
-
autoinflammatory
- medicine
-
inosine-containing
-
dsrna-binding
- drug development
-
protein-rna
-
antigenome
The taxonomic range for the selected organisms is: Mus musculus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
adenine in double-stranded RNA
+
=
hypoxanthine in double-stranded RNA
+
Synonyms
adar1, adar2, dsrad, dadar, adenosine deaminase acting on rna 1, double-stranded rna adenosine deaminase, double-stranded rna-specific adenosine deaminase, ciadar1, dsrna adenosine deaminase, adar2 deaminase, 
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topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ADAR1
ADAR1
-
two major isoforms of ADAR1, P150 and P110, named following their molecular weights, are yielded by different RNA splicings. The 150 kDa isoform, translated from exon 1a, is the full length protein that is mainly distributed in the cytosol. The 110 kDa isoform, coded by other alternative first exons and lacking the Z-DNA binding domains, is mainly located in the cell nucleus
SYSTEMATIC NAME
IUBMB Comments
double-stranded RNA(adenine) aminohydrolase
This eukaryotic enzyme is involved in RNA editing. It destabilizes double-stranded RNA through conversion of adenosine to inosine. Inositol hexakisphosphate is required for activity [4].
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
adenine in double-stranded RNA + H2O
hypoxanthine in double-stranded RNA + NH3
-
-
-
-
?
adenine in double-stranded RNA + H2O
hypoxanthine in double-stranded RNA + NH3
-
editing of Blcap, FlnA, and some sites within B1 and B2 SINEs clearly depends on ADAR1
-
-
?
adenine in double-stranded RNA + H2O
hypoxanthine in double-stranded RNA + NH3
-
ADAR1 specifically or preferentially edits 5HT2CR A and B sites
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
adenine in double-stranded RNA + H2O
hypoxanthine in double-stranded RNA + NH3
-
-
-
-
?
adenine in double-stranded RNA + H2O
hypoxanthine in double-stranded RNA + NH3
-
editing of Blcap, FlnA, and some sites within B1 and B2 SINEs clearly depends on ADAR1
-
-
?
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
spatiotemporal expression patterns for ADAR1 and ADAR2 in mouse forebrain. ADAR1 and ADAR2 are broadly distributed in most regions of the mouse forebrain, including the cerebral cortex, hippocampus, and diencephalon. High expression levels are maintained into adulthood. ADAR1 and ADAR2 are expressed in neurons but not astrocytes. ADAR1 mRNA has its lowest expression in the choroid plexus, cortex and hippocampus, while ADAR2 mRNA is least expressed in the cortex and hippocampus, with increased expression in the thalamus
spatiotemporal expression patterns for ADAR1 and ADAR2 in mouse forebrain. ADAR1 and ADAR2 are broadly distributed in most regions of the mouse forebrain, including the cerebral cortex, hippocampus, and diencephalon. High expression levels are maintained into adulthood. ADAR1 and ADAR2 are expressed in neurons but not astrocytes. ADAR1 mRNA has its lowest expression in the choroid plexus, cortex and hippocampus, while ADAR2 mRNA is least expressed in the cortex and hippocampus, with increased expression in the thalamus
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
two major isoforms of ADAR1, P150 and P110, named following their molecular weights, are yielded by different RNA splicings. The 150 kDa isoform, translated from exon 1a, is the full length protein that is mainly distributed in the cytosol. The 110 kDa isoform, coded by other alternative first exons and lacking the Z-DNA binding domains, is mainly located in the cell nucleus
-
two major isoforms of ADAR1, P150 and P110, named following their molecular weights, are yielded by different RNA splicings. The 150 kDa isoform, translated from exon 1a, is the full length protein that is mainly distributed in the cytosol. The 110 kDa isoform, coded by other alternative first exons and lacking the Z-DNA binding domains, is mainly located in the cell nucleus
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
malfunction
physiological function
-
ADAR1 is essential for intestinal homeostasis and stem cell maintenance by suppressing endoplasmic reticulum stress and interferon signaling
malfunction
ADAR1-/- homozygous embryos die at E11.0 to E12.5. Widespread apoptosis is detected in many tissues of ADAR1-/- embryos collected live at E10.5 to E11.5, despite their normal gross appearance
malfunction
homozygosity for two different null alleles of ADAR1 causes a consistent embryonic phenotype appearing early at embryonic day 11 and leading to death between embryonic days 11.5 and 12.5. This phenotype manifests a rapidly disintegrating liver structure, along with severe defects in definitive hematopoiesis, encompassing both erythroid and myeloid/granuloid progenitors as well as spleen colonyforming activity from the aorta-gonad-mesonephros region and fetal liver
malfunction
interferon treatment of Adar1-/-x02cells lacking both the p110 constitutive and p150 interferon-inducible ADAR1 proteins induces formation of stress granules, whereas neither wild-type nor Adar2x02-/-x02 cells display a comparable stress granule response following interferon treatment. Phosphorylation of protein synthesis initiation factor eIF2alpha at Ser51 is increased in interferon-treated Adar1x02-/-x02cells but not in either wild-type or Adar2x02-/- cells following interferon treatment
physiological function
ADAR1 is required for cell survival and embryo development by protecting against stress-induced apoptosis
physiological function
ADAR1 plays an essential role in adult hematopoiesis through its RNA editing activity in hematopoietic progenitor cells
physiological function
A-to-I editing of endogenous dsRNA is the essential function of ADAR1, preventing the activation of the cytosolic dsRNA response by endogenous transcripts
physiological function
the majority of editing in mouse embryo fibroblasts is carried out by ADAR1. ADAR1 p150 as the major A-to-I editor in mouse embryo fibroblasts, acts as a feedback suppressor of innate immune responses otherwise triggered by self-RNAs possessing regions of double-stranded character
malfunction
-
ADAR1 knockout embryos die at day 11.5 to 12. ADAR1 is not completely necessary for cell survival because some cells survive without ADAR1. ADAR1 is dispensable in pluripotent cells for their survival and proliferation
malfunction
-
the ADAR2 knockout phenotype can be attributed to the lack of editing of the GluR-B receptor. ADAR1 deficiency results in an embryonic lethal phenotype
malfunction
-
loss of ADAR1 induces endoplasmic reticulum stress and activation of interferon signaling, and alters expression in WNT targets, followed by intestinal inflammation and crypt apoptosis
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). DSRAD_MOUSE
1178
0
130447
Swiss-Prot
other Location (Reliability: 4)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E861A
editing-deficient knock-in mutation. Adar1(E861A/E861A) embryos die at embryonic day 13.5, with activated interferon and double-stranded RNA-sensing pathways
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
ADAR1 and ADAR2 are expressed at low levels in the fetal brain, and increase gradually over time. High expression levels were maintained into adulthood
isoform P110 is constitutively expressed in cells. In early mouse embryos, isoform P110 is expressed on day 10.5, but P150 was not expressed until day 15
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wang, Q.
RNA editing catalyzed by ADAR1 and its function in mammalian cells
Biochemistry (Moscow)
76
900-911
2011
Mus musculus
Jacobs, M.M.; Fogg, R.L.; Emeson, R.B.; Stanwood, G.D.
ADAR1 and ADAR2 expression and editing activity during forebrain development
Dev. Neurosci.
31
223-237
2009
Mus musculus (Q99MU3), Mus musculus
Cho, D.S.; Yang, W.; Lee, J.T.; Shiekhattar, R.; Murray, J.M.; Nishikura, K.
Requirement of dimerization for RNA editing activity of adenosine deaminases acting on RNA
J. Biol. Chem.
278
17093-17102
2003
Homo sapiens, Homo sapiens (P55265), Mus musculus (Q99MU3), Mus musculus
Hartner, J.C.; Schmittwolf, C.; Kispert, A.; Mller, A.M.,; Higuchi, M.; Seeburg, P.H.
Liver disintegration in the mouse embryo caused by deficiency in the RNA-editing enzyme ADAR1
J. Biol. Chem.
279
4894-4902
2004
Mus musculus (Q99MU3), Mus musculus
Wang, Q.; Miyakoda, M.; Yang, W.; Khillan, J.; Stachura, D.L.; Weiss, M.J.; Nishikura, K.
Stress-induced apoptosis associated with null mutation of ADAR1 RNA editing deaminase gene
J. Biol. Chem.
279
4952-4961
2003
Mus musculus (Q99MU3)
XuFeng, R.; Boyer, M.J.; Shen, H.; Li, Y.; Yu, H.; Gao, Y.; Yang, Q.; Wang, Q.; Cheng, T.
ADAR1 is required for hematopoietic progenitor cell survival via RNA editing
Proc. Natl. Acad. Sci. USA
106
17763-17768
2009
Mus musculus (Q99MU3)
Riedmann, E.M.; Schopoff, S.; Hartner, J.C.; Jantsch, M.F.
Specificity of ADAR-mediated RNA editing in newly identified targets
RNA
14
1110-1118
2008
Mus musculus
Qiu, W.; Wang, X.; Buchanan, M.; He, K.; Sharma, R.; Zhang, L.; Wang, Q.; Yu, J.
ADAR1 is essential for intestinal homeostasis and stem cell maintenance
Cell Death Dis.
4
e599
2013
Mus musculus
George, C.X.; Ramaswami, G.; Li, J.B.; Samuel, C.E.
Editing of cellular self-RNAs by adenosine deaminase ADAR1 suppresses innate immune stress responses
J. Biol. Chem.
291
6158-6168
2016
Mus musculus (Q99MU3), Mus musculus
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