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Protein

Double-stranded RNA-specific editase Adar

Gene

Adar

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Has A-to-I RNA editing activity on extended dsRNA: edits RNA-binding protein Rnp4F. A-to-I editing of pre-mRNAs acts predominantly through nervous system targets to affect adult nervous system integrity, function and behavior. Essential for adaptation to environmental stresses, such as oxygen deprivation, and for the prevention of premature neuronal degeneration, through the editing of ion channels as targets.4 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi372 – 3721ZincPROSITE-ProRule annotationBy similarity
Active sitei374 – 3741Proton donorPROSITE-ProRule annotation
Metal bindingi430 – 4301ZincPROSITE-ProRule annotationBy similarity
Metal bindingi493 – 4931ZincPROSITE-ProRule annotationBy similarity

GO - Molecular functioni

  • double-stranded RNA adenosine deaminase activity Source: FlyBase
  • double-stranded RNA binding Source: FlyBase
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • adenosine to inosine editing Source: UniProtKB
  • adult behavior Source: FlyBase
  • adult locomotory behavior Source: FlyBase
  • locomotor rhythm Source: FlyBase
  • locomotory behavior Source: FlyBase
  • male courtship behavior Source: FlyBase
  • mRNA modification Source: FlyBase
  • mRNA processing Source: UniProtKB-KW
  • regulation of circadian rhythm Source: FlyBase
  • regulation of gene silencing by miRNA Source: FlyBase
  • regulation of glucose metabolic process Source: FlyBase
  • regulation of membrane potential Source: FlyBase
  • response to heat Source: FlyBase
  • response to hypoxia Source: FlyBase
  • response to oxidative stress Source: UniProtKB
  • RNA modification Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

mRNA processing

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi3.5.4.37. 1994.
ReactomeiR-DME-75102. C6 deamination of adenosine.
R-DME-77042. Formation of editosomes by ADAR proteins.

Names & Taxonomyi

Protein namesi
Recommended name:
Double-stranded RNA-specific editase Adar (EC:3.5.-.-)
Alternative name(s):
Adenosine deaminase that act on RNA
Pre-mRNA adenosine deaminase
RNA-editing deaminase 1
RNA-editing enzyme 1
dADAR
dsRNA adenosine deaminase
Gene namesi
Name:AdarImported
Synonyms:hypnos-21 Publication
ORF Names:CG12598
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome X

Organism-specific databases

FlyBaseiFBgn0026086. Adar.

Subcellular locationi

GO - Cellular componenti

  • intracellular Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Disruption phenotypei

Adult flies are morphologically wild-type but exhibit extreme behavioral defects including temperature-sensitive paralysis, locomotor uncoordination, and tremors which increase in severity with age.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 676676Double-stranded RNA-specific editase AdarPRO_0000004790Add
BLAST

Proteomic databases

PaxDbiQ9NII1.
PRIDEiQ9NII1.

Expressioni

Tissue specificityi

Expressed in embryonic nervous system; late stage 13 sees ventral nerve cord expression which spreads to brain by stage 16. Expression is maintained through to adulthood.1 Publication2 Publications

Developmental stagei

Expressed throughout development, highest expression is during pupal stage. Isoforms A, C and D have lowest expression levels.1 Publication

Gene expression databases

BgeeiQ9NII1.
ExpressionAtlasiQ9NII1. differential.
GenevisibleiQ9NII1. DM.

Interactioni

Protein-protein interaction databases

BioGridi57679. 1 interaction.
IntActiQ9NII1. 1 interaction.
STRINGi7227.FBpp0300329.

Structurei

Secondary structure

1
676
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi65 – 728Combined sources
Beta strandi77 – 848Combined sources
Beta strandi87 – 893Combined sources
Beta strandi91 – 988Combined sources
Beta strandi101 – 1099Combined sources
Helixi110 – 12516Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2LJHNMR-A48-140[»]
ProteinModelPortaliQ9NII1.
SMRiQ9NII1. Positions 48-272, 288-674.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini61 – 12767DRBM 1PROSITE-ProRule annotationAdd
BLAST
Domaini197 – 27276DRBM 2PROSITE-ProRule annotationAdd
BLAST
Domaini348 – 672325A to I editasePROSITE-ProRule annotationAdd
BLAST

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.
InParanoidiQ9NII1.
OrthoDBiEOG7VHSX4.
PhylomeDBiQ9NII1.

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 (7)i

Sequence statusi: Complete.

This entry describes 7 isoformsi produced by alternative splicing and alternative initiation. AlignAdd to basket

Isoform C1 Publication (identifier: Q9NII1-1) [UniParc]FASTAAdd to basket

Also known as: b1 Publication

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
MKFDSRVMLN SANNNSPQHP VSAPSDINMN GYNRKLPQKR GYEMPKYSDP
60 70 80 90 100
KKKMCKERIP QPKNTVAMLN ELRHGLIYKL ESQTGPVHAP LFTISVEVDG
110 120 130 140 150
QKYLGQGRSK KVARIEAAAT ALRSFIQFKD GAVLSPLKPA GNLDFTSDEH
160 170 180 190 200
LENGIENLSS SKMFEIIQTM LTEKLSNPTS LEQPTFCMSQ NVSKSAITVD
210 220 230 240 250
GQKKVPDKGP VMLLYELFND VNFECINIDG AQNNCRFKMT VTINEKKFDG
260 270 280 290 300
TGPSKKTAKN AAAKAALASL CNISYSPMVV PQKNVPLPID DKSSSMELPQ
310 320 330 340 350
IHADTIGRLV LEKFMEVIKG QEAYSRRKVL AGIVMTENMN FCEAKVISVS
360 370 380 390 400
TGTKCVSGEH MSVNGAVLND SHAEIVSRRC LLKYLYAQLD LQCNQATAYQ
410 420 430 440 450
SIFVRNTDGQ YPYKLKSGVH FHLYINTAPC GDARIFSPHE NDTGVDKHPN
460 470 480 490 500
RKARGQLRTK IESGEGTIPV KSSDGIQTWD GVLQGQRLLT MSCSDKIARW
510 520 530 540 550
NIVGIQGSLL SSIIEPVYLH SIVLGSLLHP EHMYRAVCGR IEKSIQGLPP
560 570 580 590 600
PYHLNKPRLA LVTSAEPRNQ AKAPNFGINW TIGDTELEVV NSLTGRTIGG
610 620 630 640 650
QVSRITKQAF FVKYGFLMAN LPGILVRKVT TDYGQTKANV KDYQIAKLEL
660 670
FSAFKREDLG SWLKKPIEQD EFGLAE
Length:676
Mass (Da):74,978
Last modified:February 1, 2005 - v2
Checksum:i6570D16D25D1C9F4
GO
Isoform A1 Publication (identifier: Q9NII1-2) [UniParc]FASTAAdd to basket

Also known as: a1 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     154-191: GIENLSSSKMFEIIQTMLTEKLSNPTSLEQPTFCMSQN → D

Show »
Length:639
Mass (Da):70,832
Checksum:iB1FD5629F6836008
GO
Isoform B1 Publication (identifier: Q9NII1-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-19: MKFDSRVMLNSANNNSPQH → MTLCRYSE
     154-191: GIENLSSSKMFEIIQTMLTEKLSNPTSLEQPTFCMSQN → D

Show »
Length:628
Mass (Da):69,644
Checksum:iCAC6899EB4812A5E
GO
Isoform D1 Publication (identifier: Q9NII1-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-19: MKFDSRVMLNSANNNSPQH → MKFECFSLYCTVLK

Show »
Length:671
Mass (Da):74,500
Checksum:i747B60F654D2DF83
GO
Isoform F1 Publication (identifier: Q9NII1-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-28: Missing.

Show »
Length:648
Mass (Da):71,925
Checksum:iBDD164B681DEFD22
GO
Isoform G1 Publication (identifier: Q9NII1-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-28: Missing.
     154-191: GIENLSSSKMFEIIQTMLTEKLSNPTSLEQPTFCMSQN → D

Show »
Length:611
Mass (Da):67,779
Checksum:i02201A647CD817BC
GO
Isoform E (identifier: Q9NII1-7) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-7: Missing.

Note: Produced by alternative initiation at Met-8 of isoform C.
Show »
Length:669
Mass (Da):74,114
Checksum:i0D601A34987E3508
GO

Sequence cautioni

The sequence AAM50022.1 differs from that shown.Intron retention.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti346 – 3461V → VSPQPAKHCETNYNAKPILD QV in CAA22774 (PubMed:10731137).Curated

RNA editingi

Edited at position 437.1 Publication
Partially edited. Editing is low in embryos and pupae and increases dramatically upon eclosion.1 Publication

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti437 – 4371S → G in RNA edited version. 1 Publication

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2828Missing in isoform F and isoform G. 1 PublicationVSP_051650Add
BLAST
Alternative sequencei1 – 1919MKFDS…NSPQH → MTLCRYSE in isoform B. 1 PublicationVSP_051649Add
BLAST
Alternative sequencei1 – 1919MKFDS…NSPQH → MKFECFSLYCTVLK in isoform D. 1 PublicationVSP_051648Add
BLAST
Alternative sequencei1 – 77Missing in isoform E. CuratedVSP_018700
Alternative sequencei154 – 19138GIENL…CMSQN → D in isoform A, isoform B and isoform G. 3 PublicationsVSP_051651Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF208535 Genomic DNA. Translation: AAF63702.1.
AF208535 Genomic DNA. Translation: AAF63703.1.
AF343579 mRNA. Translation: AAK26850.1.
AE014298 Genomic DNA. Translation: AAF45665.2.
AE014298 Genomic DNA. Translation: AAN09057.2.
AL035207 Genomic DNA. Translation: CAA22774.1.
AY118653 mRNA. Translation: AAM50022.1. Sequence problems.
RefSeqiNP_001245469.1. NM_001258540.1.
NP_569940.2. NM_130584.4.
NP_726761.2. NM_166903.3. [Q9NII1-3]
UniGeneiDm.19.

Genome annotation databases

GeneIDi31130.
KEGGidme:Dmel_CG12598.

Keywords - Coding sequence diversityi

Alternative initiation, Alternative splicing, RNA editing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF208535 Genomic DNA. Translation: AAF63702.1.
AF208535 Genomic DNA. Translation: AAF63703.1.
AF343579 mRNA. Translation: AAK26850.1.
AE014298 Genomic DNA. Translation: AAF45665.2.
AE014298 Genomic DNA. Translation: AAN09057.2.
AL035207 Genomic DNA. Translation: CAA22774.1.
AY118653 mRNA. Translation: AAM50022.1. Sequence problems.
RefSeqiNP_001245469.1. NM_001258540.1.
NP_569940.2. NM_130584.4.
NP_726761.2. NM_166903.3. [Q9NII1-3]
UniGeneiDm.19.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2LJHNMR-A48-140[»]
ProteinModelPortaliQ9NII1.
SMRiQ9NII1. Positions 48-272, 288-674.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi57679. 1 interaction.
IntActiQ9NII1. 1 interaction.
STRINGi7227.FBpp0300329.

Proteomic databases

PaxDbiQ9NII1.
PRIDEiQ9NII1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi31130.
KEGGidme:Dmel_CG12598.

Organism-specific databases

CTDi103.
FlyBaseiFBgn0026086. Adar.

Phylogenomic databases

eggNOGiKOG2777. Eukaryota.
ENOG410XT0Z. LUCA.
InParanoidiQ9NII1.
OrthoDBiEOG7VHSX4.
PhylomeDBiQ9NII1.

Enzyme and pathway databases

BRENDAi3.5.4.37. 1994.
ReactomeiR-DME-75102. C6 deamination of adenosine.
R-DME-77042. Formation of editosomes by ADAR proteins.

Miscellaneous databases

GenomeRNAii31130.
PROiQ9NII1.

Gene expression databases

BgeeiQ9NII1.
ExpressionAtlasiQ9NII1. differential.
GenevisibleiQ9NII1. DM.

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...

Publicationsi

« Hide 'large scale' publications
  1. "dADAR, a Drosophila double-stranded RNA-specific adenosine deaminase is highly developmentally regulated and is itself a target for RNA editing."
    Palladino M.J., Keegan L.P., O'Connell M.A., Reenan R.A.
    RNA 6:1004-1018(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS A; C; D; E; F AND G), FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, RNA EDITING OF POSITION 437.
    Strain: Canton-SImported.
  2. "Mutation in pre-mRNA adenosine deaminase markedly attenuates neuronal tolerance to O(2) deprivation in Drosophila melanogaster."
    Ma E., Gu X.-Q., Wu X., Xu T., Haddad G.G.
    J. Clin. Invest. 107:685-693(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, TISSUE SPECIFICITY.
  3. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley1 Publication.
  4. Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
    Strain: Berkeley.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Oregon-R1 Publication.
  6. "A Drosophila full-length cDNA resource."
    Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
    Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley1 Publication.
    Tissue: Embryo1 Publication.
  7. "A-to-I pre-mRNA editing in Drosophila is primarily involved in adult nervous system function and integrity."
    Palladino M.J., Keegan L.P., O'Connell M.A., Reenan R.A.
    Cell 102:437-449(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
  8. "RNA editing and regulation of Drosophila 4f-rnp expression by sas-10 antisense readthrough mRNA transcripts."
    Peters N.T., Rohrbach J.A., Zalewski B.A., Byrkett C.M., Vaughn J.C.
    RNA 9:698-710(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiADAR_DROME
AccessioniPrimary (citable) accession number: Q9NII1
Secondary accession number(s): O96834
, Q8IRX2, Q8MSQ9, Q9BJ37, Q9NII2, Q9W562
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: February 1, 2005
Last modified: June 8, 2016
This is version 104 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  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.