UniProtKB - P51400 (RED1_RAT)
Protein
Double-stranded RNA-specific editase 1
Gene
Adarb1
Organism
Rattus norvegicus (Rat)
Status
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
- EC:3.5.4.37
Cofactori
1D-myo-inositol hexakisphosphateBy similarityNote: Binds 1 myo-inositol hexakisphosphate (IP6) per subunit.By similarity
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 394 | ZincPROSITE-ProRule annotation | 1 | |
Active sitei | 396 | Proton donorPROSITE-ProRule annotation | 1 | |
Binding sitei | 400 | Inositol hexakisphosphateBy similarity | 1 | |
Binding sitei | 401 | Inositol hexakisphosphateBy similarity | 1 | |
Metal bindingi | 451 | ZincPROSITE-ProRule annotation | 1 | |
Metal bindingi | 526 | ZincPROSITE-ProRule annotation | 1 | |
Binding sitei | 529 | Inositol hexakisphosphateBy similarity | 1 | |
Binding sitei | 532 | Inositol hexakisphosphateBy similarity | 1 | |
Binding sitei | 639 | Inositol hexakisphosphateBy similarity | 1 | |
Binding sitei | 672 | Inositol hexakisphosphateBy similarity | 1 | |
Binding sitei | 682 | Inositol hexakisphosphateBy similarity | 1 | |
Binding sitei | 700 | Inositol hexakisphosphateBy similarity | 1 |
GO - Molecular functioni
- double-stranded RNA adenosine deaminase activity Source: RGD
- double-stranded RNA binding Source: RGD
- identical protein binding Source: RGD
- metal ion binding Source: UniProtKB-KW
- RNA binding Source: RGD
- tRNA-specific adenosine deaminase activity Source: GO_Central
GO - Biological processi
- adenosine to inosine editing Source: RGD
- base conversion or substitution editing Source: RGD
- brain development Source: RGD
- facial nerve morphogenesis Source: RGD
- hypoglossal nerve morphogenesis Source: RGD
- innervation Source: RGD
- motor behavior Source: RGD
- motor neuron apoptotic process Source: RGD
- mRNA modification Source: RGD
- mRNA processing Source: UniProtKB-KW
- multicellular organism growth Source: RGD
- muscle tissue morphogenesis Source: RGD
- negative regulation of cell migration Source: UniProtKB
- negative regulation of cell population proliferation Source: UniProtKB
- negative regulation of protein kinase activity by regulation of protein phosphorylation Source: UniProtKB
- neuromuscular process controlling posture Source: RGD
- neuromuscular synaptic transmission Source: RGD
- positive regulation of mRNA processing Source: RGD
- positive regulation of viral genome replication Source: UniProtKB
- regulation of cell cycle Source: UniProtKB
- RNA processing Source: HGNC-UCL
- spinal cord ventral commissure morphogenesis Source: RGD
Keywordsi
Molecular function | Hydrolase, RNA-binding |
Biological process | mRNA processing |
Ligand | Metal-binding, Zinc |
Enzyme and pathway databases
Reactomei | R-RNO-75102, C6 deamination of adenosine R-RNO-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:Red1 |
Organismi | Rattus norvegicus (Rat) |
Taxonomic identifieri | 10116 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus |
Proteomesi |
|
Organism-specific databases
RGDi | 2033, Adarb1 |
Subcellular locationi
Nucleus
- nucleolus Source: RGD
- nucleoplasm Source: RGD
- nucleus Source: RGD
Other locations
Keywords - Cellular componenti
NucleusPathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 84 | M → A: Strongly reduced RNA editing activity. 1 Publication | 1 | |
Mutagenesisi | 104 – 105 | VH → AA: Strongly reduced RNA editing activity. 1 Publication | 2 | |
Mutagenesisi | 128 | K → A: Reduced RNA editing activity; when associated with A-281. 1 Publication | 1 | |
Mutagenesisi | 238 | M → A: Strongly reduced RNA editing activity. 1 Publication | 1 | |
Mutagenesisi | 258 – 259 | SH → AA: Abolishes RNA editing activity. 1 Publication | 2 | |
Mutagenesisi | 281 | K → A: Reduced RNA editing activity; when associated with A-128. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000171781 | 1 – 711 | Double-stranded RNA-specific editase 1Add BLAST | 711 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 149 | PhosphoserineBy similarity | 1 |
Keywords - PTMi
PhosphoproteinProteomic databases
PaxDbi | P51400 |
PRIDEi | P51400 |
Expressioni
Tissue specificityi
Brain and peripheral tissues.
Interactioni
Subunit structurei
Homodimer. Homodimerization is essential for its catalytic activity (By similarity).
By similarityGO - Molecular functioni
- identical protein binding Source: RGD
Protein-protein interaction databases
STRINGi | 10116.ENSRNOP00000001642 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
BMRBi | P51400 |
SMRi | P51400 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P51400 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 78 – 144 | DRBM 1PROSITE-ProRule annotationAdd BLAST | 67 | |
Domaini | 231 – 298 | DRBM 2PROSITE-ProRule annotationAdd BLAST | 68 | |
Domaini | 370 – 707 | A to I editasePROSITE-ProRule annotationAdd BLAST | 338 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 83 – 88 | Interaction with substrate RNA | 6 | |
Regioni | 104 – 105 | Interaction with substrate RNA | 2 | |
Regioni | 237 – 242 | Interaction with substrate RNA | 6 | |
Regioni | 259 | Interaction with substrate RNA | 1 |
Keywords - Domaini
RepeatPhylogenomic databases
eggNOGi | KOG2777, Eukaryota |
InParanoidi | P51400 |
OrthoDBi | 947117at2759 |
PhylomeDBi | P51400 |
Family and domain databases
CDDi | cd00048, DSRM, 2 hits |
InterProi | View protein in InterPro IPR002466, A_deamin IPR014720, dsRBD_dom |
Pfami | View protein in Pfam PF02137, A_deamin, 1 hit PF00035, dsrm, 2 hits |
SMARTi | View protein in SMART SM00552, ADEAMc, 1 hit SM00358, DSRM, 2 hits |
PROSITEi | View protein in PROSITE PS50141, A_DEAMIN_EDITASE, 1 hit PS50137, DS_RBD, 2 hits |
(1+)i Sequence
Sequence statusi: Complete.
This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All
P51400-1 [UniParc]FASTAAdd to basket
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
Computationally mapped potential isoform sequencesi
There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basketA0A0G2JUX0 | A0A0G2JUX0_RAT | Double-stranded RNA-specific editas... | Adarb1 | 726 | Annotation score: | ||
G3V649 | G3V649_RAT | Adenosine deaminase, RNA-specific, ... | Adarb1 rCG_60571 | 687 | Annotation score: |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | U43534 mRNA Translation: AAA96755.1 |
PIRi | S68443 |
RefSeqi | NP_001104525.1, NM_001111055.1 NP_001104526.1, NM_001111056.1 NP_001104527.1, NM_001111057.1 NP_037026.2, NM_012894.2 |
Genome annotation databases
GeneIDi | 25367 |
KEGGi | rno:25367 |
UCSCi | RGD:2033, rat |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | U43534 mRNA Translation: AAA96755.1 |
PIRi | S68443 |
RefSeqi | NP_001104525.1, NM_001111055.1 NP_001104526.1, NM_001111056.1 NP_001104527.1, NM_001111057.1 NP_037026.2, NM_012894.2 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
2B7T | NMR | - | A | 74-146 | [»] | |
2B7V | NMR | - | A | 231-301 | [»] | |
2L3C | NMR | - | A | 74-147 | [»] | |
2L3J | NMR | - | A | 74-301 | [»] | |
BMRBi | P51400 | |||||
SMRi | P51400 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
STRINGi | 10116.ENSRNOP00000001642 |
Proteomic databases
PaxDbi | P51400 |
PRIDEi | P51400 |
Genome annotation databases
GeneIDi | 25367 |
KEGGi | rno:25367 |
UCSCi | RGD:2033, rat |
Organism-specific databases
CTDi | 104 |
RGDi | 2033, Adarb1 |
Phylogenomic databases
eggNOGi | KOG2777, Eukaryota |
InParanoidi | P51400 |
OrthoDBi | 947117at2759 |
PhylomeDBi | P51400 |
Enzyme and pathway databases
Reactomei | R-RNO-75102, C6 deamination of adenosine R-RNO-77042, Formation of editosomes by ADAR proteins |
Miscellaneous databases
EvolutionaryTracei | P51400 |
PROi | PR:P51400 |
Family and domain databases
CDDi | cd00048, DSRM, 2 hits |
InterProi | View protein in InterPro IPR002466, A_deamin IPR014720, dsRBD_dom |
Pfami | View protein in Pfam PF02137, A_deamin, 1 hit PF00035, dsrm, 2 hits |
SMARTi | View protein in SMART SM00552, ADEAMc, 1 hit SM00358, DSRM, 2 hits |
PROSITEi | View protein in PROSITE PS50141, A_DEAMIN_EDITASE, 1 hit PS50137, DS_RBD, 2 hits |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | RED1_RAT | |
Accessioni | P51400Primary (citable) accession number: P51400 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | October 1, 1996 |
Last sequence update: | October 1, 1996 | |
Last modified: | December 2, 2020 | |
This is version 134 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references