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Protein

Double-stranded RNA-specific editase 1

Gene

Adarb1

Organism
Rattus norvegicus (Rat)
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 (By similarity). Can inhibit cell proliferation and migration and can stimulate exocytosis.By similarity3 Publications

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)DescriptionActionsGraphical viewLength
Metal bindingi394ZincPROSITE-ProRule annotation1
Active sitei396Proton donorPROSITE-ProRule annotation1
Binding sitei400Inositol hexakisphosphateBy similarity1
Binding sitei401Inositol hexakisphosphateBy similarity1
Metal bindingi451ZincPROSITE-ProRule annotation1
Metal bindingi526ZincPROSITE-ProRule annotation1
Binding sitei529Inositol hexakisphosphateBy similarity1
Binding sitei532Inositol hexakisphosphateBy similarity1
Binding sitei639Inositol hexakisphosphateBy similarity1
Binding sitei672Inositol hexakisphosphateBy similarity1
Binding sitei682Inositol hexakisphosphateBy similarity1
Binding sitei700Inositol hexakisphosphateBy similarity1

GO - Molecular functioni

  • double-stranded RNA adenosine deaminase activity Source: HGNC
  • double-stranded RNA binding Source: HGNC
  • metal ion binding Source: UniProtKB-KW
  • protein homodimerization activity Source: RGD
  • 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

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:Red1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2033. Adarb1.

Subcellular locationi

  • Nucleus By similarity
  • Nucleusnucleolus By similarity

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

GO - Cellular componenti

  • nucleolus Source: RGD
  • nucleoplasm Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi84M → A: Strongly reduced RNA editing activity. 1 Publication1
Mutagenesisi104 – 105VH → AA: Strongly reduced RNA editing activity. 1 Publication2
Mutagenesisi128K → A: Reduced RNA editing activity; when associated with A-281. 1 Publication1
Mutagenesisi238M → A: Strongly reduced RNA editing activity. 1 Publication1
Mutagenesisi258 – 259SH → AA: Abolishes RNA editing activity. 1 Publication2
Mutagenesisi281K → A: Reduced RNA editing activity; when associated with A-128. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001717811 – 711Double-stranded RNA-specific editase 1Add BLAST711

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei149PhosphoserineBy similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP51400.
PRIDEiP51400.

Expressioni

Tissue specificityi

Brain and peripheral tissues.

Interactioni

Subunit structurei

Homodimer. Homodimerization is essential for its catalytic activity (By similarity).By similarity

GO - Molecular functioni

  • protein homodimerization activity Source: RGD

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000001642.

Structurei

Secondary structure

1711
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi76 – 79Combined sources4
Helixi80 – 89Combined sources10
Beta strandi94 – 101Combined sources8
Beta strandi103 – 106Combined sources4
Beta strandi108 – 126Combined sources19
Helixi127 – 143Combined sources17
Beta strandi183 – 186Combined sources4
Beta strandi193 – 195Combined sources3
Beta strandi197 – 201Combined sources5
Beta strandi217 – 219Combined sources3
Beta strandi221 – 224Combined sources4
Helixi236 – 243Combined sources8
Beta strandi248 – 253Combined sources6
Turni258 – 260Combined sources3
Beta strandi263 – 268Combined sources6
Beta strandi273 – 280Combined sources8
Helixi281 – 299Combined sources19

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2B7TNMR-A74-146[»]
2B7VNMR-A231-301[»]
2L3CNMR-A74-147[»]
2L3JNMR-A74-301[»]
ProteinModelPortaliP51400.
SMRiP51400.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP51400.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini78 – 144DRBM 1PROSITE-ProRule annotationAdd BLAST67
Domaini231 – 298DRBM 2PROSITE-ProRule annotationAdd BLAST68
Domaini370 – 707A to I editasePROSITE-ProRule annotationAdd BLAST338

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni83 – 88Interaction with substrate RNA6
Regioni104 – 105Interaction with substrate RNA2
Regioni237 – 242Interaction with substrate RNA6
Regioni259Interaction with substrate RNA1

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.
HOGENOMiHOG000290164.
HOVERGENiHBG003836.
InParanoidiP51400.
KOiK13194.
PhylomeDBiP51400.

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]

Sequencei

Sequence statusi: Complete.

P51400-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDIEDEENMS SSSIDVKENR 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 EPVLEGMAPD SHQLTEPADR HPNRKARGQL RTKIESGEGT
510 520 530 540 550
IPVRSNASIQ TWDGVLQGER LLTMSCSDKI ARWNVVGIQG ALLSIFVEPI
560 570 580 590 600
YFSSIILGSL YHGDHLSRAM YQRISNIEDL PPLYTLNKPL LSGISNAEAR
610 620 630 640 650
QPGKAPNFSV NWTVGDTAIE VINATTGKDE LGRPSRLCKH ALYCRWMRVH
660 670 680 690 700
GKVPPHLLRT KITKPTTYHE SKLAAKEYQA AKARLFTAFI KAGLGAWVEK
710
PTEQDQFSFT P
Length:711
Mass (Da):77,925
Last modified:October 1, 1996 - v1
Checksum:i5A25C4B202530C54
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U43534 mRNA. Translation: AAA96755.1.
PIRiS68443.
RefSeqiNP_001104525.1. NM_001111055.1.
NP_001104526.1. NM_001111056.1.
NP_001104527.1. NM_001111057.1.
NP_037026.2. NM_012894.2.
UniGeneiRn.172406.
Rn.89675.

Genome annotation databases

GeneIDi25367.
KEGGirno:25367.
UCSCiRGD:2033. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U43534 mRNA. Translation: AAA96755.1.
PIRiS68443.
RefSeqiNP_001104525.1. NM_001111055.1.
NP_001104526.1. NM_001111056.1.
NP_001104527.1. NM_001111057.1.
NP_037026.2. NM_012894.2.
UniGeneiRn.172406.
Rn.89675.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2B7TNMR-A74-146[»]
2B7VNMR-A231-301[»]
2L3CNMR-A74-147[»]
2L3JNMR-A74-301[»]
ProteinModelPortaliP51400.
SMRiP51400.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000001642.

Proteomic databases

PaxDbiP51400.
PRIDEiP51400.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi25367.
KEGGirno:25367.
UCSCiRGD:2033. rat.

Organism-specific databases

CTDi104.
RGDi2033. Adarb1.

Phylogenomic databases

eggNOGiKOG2777. Eukaryota.
ENOG410XT0Z. LUCA.
HOGENOMiHOG000290164.
HOVERGENiHBG003836.
InParanoidiP51400.
KOiK13194.
PhylomeDBiP51400.

Miscellaneous databases

EvolutionaryTraceiP51400.
PROiP51400.

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_RAT
AccessioniPrimary (citable) accession number: P51400
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: November 2, 2016
This is version 117 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.