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Protein

Double-stranded RNA-specific adenosine deaminase

Gene

Adar

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 serotonin (HTR2C) and GABA receptor (GABRA3). Site-specific RNA editing of transcripts encoding these proteins results in amino acid substitutions which consequently alters their functional activities. Exhibits low-level editing at the GRIA2 Q/R site, but edits efficiently at the R/G site and HOTSPOT1. Does not affect polyomavirus replication but provides protection against virus-induced cytopathic effects. Essential for embryonic development and cell survival and plays a critical role in the maintenance of hematopoietic stem cells (By similarity).By similarity

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi856 – 8561ZincPROSITE-ProRule annotation
Active sitei858 – 8581Proton donorPROSITE-ProRule annotation
Metal bindingi912 – 9121ZincPROSITE-ProRule annotation
Metal bindingi982 – 9821ZincPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi171 – 19727By similarityAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Antiviral defense, Immunity, Innate immunity, mRNA processing, RNA-mediated gene silencing, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, RNA-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Double-stranded RNA-specific adenosine deaminase (EC:3.5.4.37)
Short name:
DRADA
Gene namesi
Name:Adar
Synonyms:Dsrad
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi71099. Adar.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB-SubCell
  • nuclear speck Source: RGD
  • nucleolus Source: RGD
  • supraspliceosomal complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11751175Double-stranded RNA-specific adenosine deaminasePRO_0000171776Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei228 – 2281PhosphoserineCombined sources
Modified residuei235 – 2351PhosphoserineCombined sources
Cross-linki368 – 368Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternateBy similarity
Cross-linki368 – 368Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateBy similarity
Cross-linki368 – 368Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei431 – 4311PhosphoserineBy similarity
Modified residuei564 – 5641PhosphoserineBy similarity
Modified residuei579 – 5791PhosphoserineBy similarity
Modified residuei586 – 5861PhosphoserineBy similarity
Modified residuei754 – 7541PhosphothreonineBy similarity
Modified residuei760 – 7601PhosphoserineBy similarity
Modified residuei769 – 7691PhosphoserineBy similarity
Modified residuei771 – 7711PhosphoserineBy similarity

Post-translational modificationi

Sumoylation reduces RNA-editing activity.By similarity

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP55266.
PRIDEiP55266.

PTM databases

iPTMnetiP55266.
PhosphoSiteiP55266.

Interactioni

Subunit structurei

Homodimer. Homodimerization is essential for its catalytic activity. Interacts with ILF2/NF45 and ILF3/NF90. Binding to ILF3/NF90 up-regulates ILF3-mediated gene expression. Interacts with UPF1 and EIF2AK2/PKR (By similarity).By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000028181.

Structurei

3D structure databases

ProteinModelPortaliP55266.
SMRiP55266. Positions 128-199, 244-316.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati135 – 20470DRADA 1Add
BLAST
Repeati243 – 31068DRADA 2Add
BLAST
Domaini453 – 52169DRBM 1PROSITE-ProRule annotationAdd
BLAST
Domaini564 – 63269DRBM 2PROSITE-ProRule annotationAdd
BLAST
Domaini672 – 74069DRBM 3PROSITE-ProRule annotationAdd
BLAST
Domaini832 – 1167336A to I editasePROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi70 – 12152Pro-richAdd
BLAST

Sequence similaritiesi

Contains 1 A to I editase domain.PROSITE-ProRule annotation
Contains 2 DRADA repeats.PROSITE-ProRule annotation
Contains 3 DRBM (double-stranded RNA-binding) domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG2777. Eukaryota.
ENOG410XT0Z. LUCA.
HOGENOMiHOG000049121.
HOVERGENiHBG067087.
InParanoidiP55266.
KOiK12968.
PhylomeDBiP55266.

Family and domain databases

Gene3Di1.10.10.10. 2 hits.
3.30.160.20. 3 hits.
InterProiIPR002466. A_deamin.
IPR014720. dsRBD_dom.
IPR000607. dsRNA_A_deaminase.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF02137. A_deamin. 1 hit.
PF00035. dsrm. 3 hits.
PF02295. z-alpha. 2 hits.
[Graphical view]
SMARTiSM00552. ADEAMc. 1 hit.
SM00358. DSRM. 3 hits.
SM00550. Zalpha. 2 hits.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 2 hits.
PROSITEiPS50141. A_DEAMIN_EDITASE. 1 hit.
PS50139. DRADA_REPEAT. 2 hits.
PS50137. DS_RBD. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P55266-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQGFRGPTG VFPHQTQPCL DPSYEHSKWR YLQPRGSESY LRSFQLQQIE
60 70 80 90 100
FLKGRLPEAP LIGAQTQSLP PFLPGHWPRF PGPPAQGKQP EIWGFPRSVT
110 120 130 140 150
LRNQGFHIGP PLPPPHSRGP PWRGAEGLCS HFQELSISQN PEQKVLNRLE
160 170 180 190 200
ELGEGKATTA YALARELRTP KKDINRILYS LERKGKLHRG VGKPPLWSLV
210 220 230 240 250
PLSQACTQPP RAVNSDKEVP RGEPDLDSED GDPASDLEGP SELLDMAEIK
260 270 280 290 300
EKICDYLFNV SKSSALNLAK NIGLAKARDV NAVLIDLERQ GDVYREGATP
310 320 330 340 350
PIWYLTDKKR ERLQMKRSTH SGPAATPAAV SEATQSTSFP TCHPPQSGGS
360 370 380 390 400
SSMATSKRVE NGQEPVTKYE SRHEARPGPV RLRPHAYHNG PSRAGYVASE
410 420 430 440 450
NGPWATDDIP DNLNSIHTAP GEFRAIMEMP SFYSPTLPRC SPYKKLTECQ
460 470 480 490 500
LKNPVSGLLE YAQFTSQTCD FNLIEQSGPS HEPRFKFQVV INGREFPPAE
510 520 530 540 550
AGSKKVAKQD AAVKAMAILL REAKAKDSGQ PEELSNCPME EDPEKPAESQ
560 570 580 590 600
PPSSSATSLF SGKSPVTTLL ECMHKLGNSC EFRLLSKEGP AHDPKFQYCV
610 620 630 640 650
AVGAQTFPSV SAPSKKVAKQ MAAEEAMKAL QEEAANSADD QSGGANTDSL
660 670 680 690 700
DESVAPNKIR RIGELVRYLN TNPVGGLLEY ARSHGFAAEF KLIDQSGPPH
710 720 730 740 750
EPKFVYQAKV GGRWFPAVCA HSKKQGKQDA ADAALRVLIG ESEKAEQLGF
760 770 780 790 800
AEVTPVTGAS LRRTMLLLSR SPDAHPKTLP LTGSTFHDQI AMLSHRCFNA
810 820 830 840 850
LTNSFQPSLL GRKILAAIIM KRDPEDMGVV VSLGTGNRCV KGDSLSLKGE
860 870 880 890 900
TVNDCHAEII SRRGFIRFLY SELMKYNHHT AKNSIFELAR GGEKLQIKKT
910 920 930 940 950
VSFHLYISTA PCGDGAHFDK SCSDRAVEST ESRHYPVFEN PKQGKLRTKV
960 970 980 990 1000
ENGEGTIPVE SSDIVPTWDG IRLGERLRTM SCSDKILRWN VLGLQGALLT
1010 1020 1030 1040 1050
HFLQPVYLKS VTLGYLFSQG HLTRAICCRV TRDGNAFEDG LRYPFIVNHP
1060 1070 1080 1090 1100
KVGRVSVYDS KRQSGKTKET SVNWCLADGY DLEILDGTRG TVDGPGKELS
1110 1120 1130 1140 1150
RVSKKNIFLQ FKKLCSFRAR RDLLQLSYGE AKKAARDYDL AKNYFKKSLR
1160 1170
DMGYGNWISK PQEEKNFYLC PVPND
Length:1,175
Mass (Da):129,911
Last modified:October 1, 1996 - v1
Checksum:iF5C7B5FFB771168C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U18942 mRNA. Translation: AAA65039.1.
PIRiI57549.
RefSeqiNP_112268.1. NM_031006.1.
UniGeneiRn.10056.

Genome annotation databases

GeneIDi81635.
KEGGirno:81635.
UCSCiRGD:71099. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U18942 mRNA. Translation: AAA65039.1.
PIRiI57549.
RefSeqiNP_112268.1. NM_031006.1.
UniGeneiRn.10056.

3D structure databases

ProteinModelPortaliP55266.
SMRiP55266. Positions 128-199, 244-316.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000028181.

PTM databases

iPTMnetiP55266.
PhosphoSiteiP55266.

Proteomic databases

PaxDbiP55266.
PRIDEiP55266.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi81635.
KEGGirno:81635.
UCSCiRGD:71099. rat.

Organism-specific databases

CTDi103.
RGDi71099. Adar.

Phylogenomic databases

eggNOGiKOG2777. Eukaryota.
ENOG410XT0Z. LUCA.
HOGENOMiHOG000049121.
HOVERGENiHBG067087.
InParanoidiP55266.
KOiK12968.
PhylomeDBiP55266.

Miscellaneous databases

PROiP55266.

Family and domain databases

Gene3Di1.10.10.10. 2 hits.
3.30.160.20. 3 hits.
InterProiIPR002466. A_deamin.
IPR014720. dsRBD_dom.
IPR000607. dsRNA_A_deaminase.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF02137. A_deamin. 1 hit.
PF00035. dsrm. 3 hits.
PF02295. z-alpha. 2 hits.
[Graphical view]
SMARTiSM00552. ADEAMc. 1 hit.
SM00358. DSRM. 3 hits.
SM00550. Zalpha. 2 hits.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 2 hits.
PROSITEiPS50141. A_DEAMIN_EDITASE. 1 hit.
PS50139. DRADA_REPEAT. 2 hits.
PS50137. DS_RBD. 3 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiDSRAD_RAT
AccessioniPrimary (citable) accession number: P55266
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: July 6, 2016
This is version 119 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

Complete proteome, Reference proteome

Documents

  1. 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.