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Protein

Double-stranded RNA-specific editase 1

Gene

Adarb1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

Adenine in double-stranded RNA + H2O = hypoxanthine in double-stranded RNA + NH3.

Cofactori

1D-myo-inositol hexakisphosphateBy similarityNote: Binds 1 myo-inositol hexakisphosphate (IP6) per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi394 – 3941ZincPROSITE-ProRule annotation
Active sitei396 – 3961Proton donorPROSITE-ProRule annotation
Binding sitei400 – 4001Inositol hexakisphosphateBy similarity
Binding sitei401 – 4011Inositol hexakisphosphateBy similarity
Metal bindingi451 – 4511ZincPROSITE-ProRule annotation
Metal bindingi526 – 5261ZincPROSITE-ProRule annotation
Binding sitei529 – 5291Inositol hexakisphosphateBy similarity
Binding sitei532 – 5321Inositol hexakisphosphateBy similarity
Binding sitei639 – 6391Inositol hexakisphosphateBy similarity
Binding sitei672 – 6721Inositol hexakisphosphateBy similarity
Binding sitei682 – 6821Inositol hexakisphosphateBy similarity
Binding sitei700 – 7001Inositol hexakisphosphateBy similarity

GO - Molecular functioni

  • double-stranded RNA adenosine deaminase activity Source: HGNC
  • double-stranded RNA binding Source: HGNC
  • metal ion binding Source: UniProtKB-KW
  • poly(A) RNA binding Source: MGI
  • RNA binding Source: HGNC

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

mRNA processing

Keywords - Ligandi

Metal-binding, RNA-binding, Zinc

Enzyme and pathway databases

ReactomeiR-MMU-75102. C6 deamination of adenosine.
R-MMU-77042. Formation of editosomes by ADAR proteins.

Names & Taxonomyi

Protein namesi
Recommended name:
Double-stranded RNA-specific editase 1 (EC:3.5.4.37)
Alternative name(s):
RNA-editing deaminase 1
RNA-editing enzyme 1
dsRNA adenosine deaminase
Gene namesi
Name:Adarb1
Synonyms:Adar2, Red1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 10

Organism-specific databases

MGIiMGI:891999. Adarb1.

Subcellular locationi

  • Nucleus By similarity
  • Nucleusnucleolus By similarity

  • Note: Shuttles between nucleoli and the nucleoplasm.By similarity

GO - Cellular componenti

  • cytoplasm Source: MGI
  • nucleolus Source: UniProtKB
  • nucleoplasm Source: MGI
  • nucleus Source: HGNC
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 711711Double-stranded RNA-specific editase 1PRO_0000171780Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei149 – 1491PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ91ZS8.
PaxDbiQ91ZS8.
PeptideAtlasiQ91ZS8.
PRIDEiQ91ZS8.

PTM databases

iPTMnetiQ91ZS8.
PhosphoSiteiQ91ZS8.

Expressioni

Gene expression databases

BgeeiENSMUSG00000020262.
CleanExiMM_ADARB1.
ExpressionAtlasiQ91ZS8. baseline and differential.
GenevisibleiQ91ZS8. MM.

Interactioni

Subunit structurei

Homodimer. Homodimerization is essential for its catalytic activity. Can form heterodimers with isoform 5 of ADAR/ADAR1 (By similarity).By similarity

Protein-protein interaction databases

IntActiQ91ZS8. 1 interaction.
MINTiMINT-4122233.
STRINGi10090.ENSMUSP00000095976.

Structurei

Secondary structure

1
711
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi236 – 2438Combined sources
Beta strandi248 – 2569Combined sources
Beta strandi262 – 2698Combined sources
Beta strandi272 – 2809Combined sources
Helixi281 – 29616Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2L2KNMR-B231-301[»]
ProteinModelPortaliQ91ZS8.
SMRiQ91ZS8. Positions 74-298, 306-710.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ91ZS8.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini78 – 14467DRBM 1PROSITE-ProRule annotationAdd
BLAST
Domaini231 – 29868DRBM 2PROSITE-ProRule annotationAdd
BLAST
Domaini370 – 707338A to I editasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni83 – 886Interaction with substrate RNABy similarity
Regioni104 – 1052Interaction with substrate RNABy similarity
Regioni237 – 2426Interaction with substrate RNABy similarity
Regioni259 – 2591Interaction with substrate RNABy similarity

Sequence similaritiesi

Contains 1 A to I editase domain.PROSITE-ProRule annotation
Contains 2 DRBM (double-stranded RNA-binding) domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG2777. Eukaryota.
ENOG410XT0Z. LUCA.
GeneTreeiENSGT00550000074412.
HOVERGENiHBG003836.
InParanoidiQ91ZS8.
KOiK13194.
OMAiFKMTVTI.
OrthoDBiEOG091G0MZP.
PhylomeDBiQ91ZS8.
TreeFamiTF315806.

Family and domain databases

Gene3Di3.30.160.20. 2 hits.
InterProiIPR002466. A_deamin.
IPR014720. dsRBD_dom.
[Graphical view]
PfamiPF02137. A_deamin. 1 hit.
PF00035. dsrm. 2 hits.
[Graphical view]
SMARTiSM00552. ADEAMc. 1 hit.
SM00358. DSRM. 2 hits.
[Graphical view]
PROSITEiPS50141. A_DEAMIN_EDITASE. 1 hit.
PS50137. DS_RBD. 2 hits.
[Graphical view]

Sequences (6)i

Sequence statusi: Complete.

This entry describes 6 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q91ZS8-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MDIEDEENMS SSSTDIKENR NLDNMPPKDS STPGPGEGIP LSNGGGGSTS
60 70 80 90 100
RKRPLEEGSN GHSKYRLKKR RKTPGPVLPK NALMQLNEIK PGLQYMLLSQ
110 120 130 140 150
TGPVHAPLFV MSVEVNGQVF EGSGPTKKKA KLHAAEKALR SFVQFPNASE
160 170 180 190 200
AHLAMGRTLS VNTDFTSDQA DFPDTLFNGF ETPDKSEPPF YVGSNGDDSF
210 220 230 240 250
SSSGDVSLSA SPVPASLTQP PLPIPPPFPP PSGKNPVMIL NELRPGLKYD
260 270 280 290 300
FLSESGESHA KSFVMSVVVD GQFFEGSGRN KKLAKARAAQ SALATVFNLH
310 320 330 340 350
LDQTPSRQPV LSEGLQLHLP QVLADAVSRL VLGKFSDLTD NFSSPHARRK
360 370 380 390 400
VLSGVVMTTG TDVKDAKVIS VSTGTKCING EYMSDRGLAL NDCHAEIISR
410 420 430 440 450
RSLLRFLYAQ LELYLNNKED QKKSIFQKSE RGGFRLKDTV QFHLYISTSP
460 470 480 490 500
CGDARIFSPH EPVLEGMTPD SHQLTEPADR HPNRKARGQL RTKIESGEGT
510 520 530 540 550
IPVRSNASIQ TWDGVLQGER LLTMSCSDKI ARWNVVGIQG SLLSIFVEPI
560 570 580 590 600
YFSSIILGSL YHGDHLSRAM YQRISNIEDL PPLYTLNKPL LSGISNAEAR
610 620 630 640 650
QPGKAPNFSV NWTVGDATIE VINATTGKDE LGRPSRLCKH ALYCRWMRVH
660 670 680 690 700
GKVPPHLLRT KITKPTTYHE SKLAAREYQA AKARLFTAFI KAGLGAWVEK
710
PTEQDQFSFT P
Length:711
Mass (Da):78,001
Last modified:December 1, 2001 - v1
Checksum:iA5C87E894C867DE1
GO
Isoform 2 (identifier: Q91ZS8-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     466-475: Missing.

Show »
Length:701
Mass (Da):76,932
Checksum:i9DC35AB940ECDC1B
GO
Isoform 3 (identifier: Q91ZS8-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-10: MDIEDEENMS → MPLG
     466-475: Missing.

Show »
Length:695
Mass (Da):76,137
Checksum:iF88ED2F95BBC3A98
GO
Isoform 4 (identifier: Q91ZS8-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-24: Missing.

Show »
Length:687
Mass (Da):75,232
Checksum:iAE6B8C4AAAD81726
GO
Isoform 5 (identifier: Q91ZS8-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-24: Missing.
     466-475: Missing.

Show »
Length:677
Mass (Da):74,164
Checksum:iCB889950207BC99B
GO
Isoform 6 (identifier: Q91ZS8-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MASLGLGTLTVGAFFSFVGRRYKRRRKKRSERKDKRGLRQSRSPQKCFTM

Note: Likely expressed from an alternative promoter. Contains a region highly similar to the so-called ssRNA-binding R-domain of ADARB2.
Show »
Length:760
Mass (Da):83,732
Checksum:i0EDD0CC438EE2393
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti65 – 651Y → C in AAK17102 (PubMed:12709013).Curated
Sequence conflicti559 – 5591S → G in AAK17102 (PubMed:12709013).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2424Missing in isoform 4 and isoform 5. 1 PublicationVSP_013709Add
BLAST
Alternative sequencei1 – 1010MDIEDEENMS → MPLG in isoform 3. 1 PublicationVSP_013710
Alternative sequencei1 – 11M → MASLGLGTLTVGAFFSFVGR RYKRRRKKRSERKDKRGLRQ SRSPQKCFTM in isoform 6. 1 PublicationVSP_041423
Alternative sequencei466 – 47510Missing in isoform 2, isoform 3 and isoform 5. 2 PublicationsVSP_013711

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF403106 mRNA. Translation: AAL01301.1.
AF403107 mRNA. Translation: AAL01302.1.
AF403108 mRNA. Translation: AAL01303.1.
AF403109 mRNA. Translation: AAL01304.1.
AF525421 mRNA. Translation: AAM83099.1.
AY162454 mRNA. Translation: AAN86546.1.
AF291049 mRNA. Translation: AAK17102.1.
FJ169505 mRNA. Translation: ACN49026.1.
AK141777 mRNA. Translation: BAE24831.1.
AK147298 mRNA. Translation: BAE27830.1.
CH466553 Genomic DNA. Translation: EDL31813.1.
CCDSiCCDS35948.1. [Q91ZS8-1]
CCDS35949.1. [Q91ZS8-2]
RefSeqiNP_001020008.1. NM_001024837.2. [Q91ZS8-1]
NP_570965.2. NM_130895.3. [Q91ZS8-2]
XP_006513128.1. XM_006513065.1. [Q91ZS8-3]
XP_011241567.1. XM_011243265.1. [Q91ZS8-1]
UniGeneiMm.276815.

Genome annotation databases

EnsembliENSMUST00000020496; ENSMUSP00000020496; ENSMUSG00000020262. [Q91ZS8-2]
ENSMUST00000098374; ENSMUSP00000095976; ENSMUSG00000020262. [Q91ZS8-1]
ENSMUST00000105406; ENSMUSP00000101046; ENSMUSG00000020262. [Q91ZS8-1]
GeneIDi110532.
KEGGimmu:110532.
UCSCiuc007fvl.2. mouse. [Q91ZS8-3]
uc007fvm.2. mouse. [Q91ZS8-1]
uc007fvn.2. mouse. [Q91ZS8-5]
uc007fvp.2. mouse. [Q91ZS8-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF403106 mRNA. Translation: AAL01301.1.
AF403107 mRNA. Translation: AAL01302.1.
AF403108 mRNA. Translation: AAL01303.1.
AF403109 mRNA. Translation: AAL01304.1.
AF525421 mRNA. Translation: AAM83099.1.
AY162454 mRNA. Translation: AAN86546.1.
AF291049 mRNA. Translation: AAK17102.1.
FJ169505 mRNA. Translation: ACN49026.1.
AK141777 mRNA. Translation: BAE24831.1.
AK147298 mRNA. Translation: BAE27830.1.
CH466553 Genomic DNA. Translation: EDL31813.1.
CCDSiCCDS35948.1. [Q91ZS8-1]
CCDS35949.1. [Q91ZS8-2]
RefSeqiNP_001020008.1. NM_001024837.2. [Q91ZS8-1]
NP_570965.2. NM_130895.3. [Q91ZS8-2]
XP_006513128.1. XM_006513065.1. [Q91ZS8-3]
XP_011241567.1. XM_011243265.1. [Q91ZS8-1]
UniGeneiMm.276815.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2L2KNMR-B231-301[»]
ProteinModelPortaliQ91ZS8.
SMRiQ91ZS8. Positions 74-298, 306-710.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ91ZS8. 1 interaction.
MINTiMINT-4122233.
STRINGi10090.ENSMUSP00000095976.

PTM databases

iPTMnetiQ91ZS8.
PhosphoSiteiQ91ZS8.

Proteomic databases

MaxQBiQ91ZS8.
PaxDbiQ91ZS8.
PeptideAtlasiQ91ZS8.
PRIDEiQ91ZS8.

Protocols and materials databases

DNASUi110532.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000020496; ENSMUSP00000020496; ENSMUSG00000020262. [Q91ZS8-2]
ENSMUST00000098374; ENSMUSP00000095976; ENSMUSG00000020262. [Q91ZS8-1]
ENSMUST00000105406; ENSMUSP00000101046; ENSMUSG00000020262. [Q91ZS8-1]
GeneIDi110532.
KEGGimmu:110532.
UCSCiuc007fvl.2. mouse. [Q91ZS8-3]
uc007fvm.2. mouse. [Q91ZS8-1]
uc007fvn.2. mouse. [Q91ZS8-5]
uc007fvp.2. mouse. [Q91ZS8-2]

Organism-specific databases

CTDi104.
MGIiMGI:891999. Adarb1.

Phylogenomic databases

eggNOGiKOG2777. Eukaryota.
ENOG410XT0Z. LUCA.
GeneTreeiENSGT00550000074412.
HOVERGENiHBG003836.
InParanoidiQ91ZS8.
KOiK13194.
OMAiFKMTVTI.
OrthoDBiEOG091G0MZP.
PhylomeDBiQ91ZS8.
TreeFamiTF315806.

Enzyme and pathway databases

ReactomeiR-MMU-75102. C6 deamination of adenosine.
R-MMU-77042. Formation of editosomes by ADAR proteins.

Miscellaneous databases

EvolutionaryTraceiQ91ZS8.
PROiQ91ZS8.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000020262.
CleanExiMM_ADARB1.
ExpressionAtlasiQ91ZS8. baseline and differential.
GenevisibleiQ91ZS8. MM.

Family and domain databases

Gene3Di3.30.160.20. 2 hits.
InterProiIPR002466. A_deamin.
IPR014720. dsRBD_dom.
[Graphical view]
PfamiPF02137. A_deamin. 1 hit.
PF00035. dsrm. 2 hits.
[Graphical view]
SMARTiSM00552. ADEAMc. 1 hit.
SM00358. DSRM. 2 hits.
[Graphical view]
PROSITEiPS50141. A_DEAMIN_EDITASE. 1 hit.
PS50137. DS_RBD. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRED1_MOUSE
AccessioniPrimary (citable) accession number: Q91ZS8
Secondary accession number(s): C3TTQ1
, Q3UHM7, Q8K3X1, Q91ZS6, Q91ZS7, Q91ZS9, Q99MU8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2005
Last sequence update: December 1, 2001
Last modified: September 7, 2016
This is version 114 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.