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Q9NII1 (ADAR_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Adar
Synonyms:hypnos-2
ORF Names:CG12598
OrganismDrosophila melanogaster (Fruit fly)
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length676 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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. Ref.1 Ref.2 Ref.7 Ref.8

Tissue specificity

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. Ref.1 Ref.2 Ref.7

Developmental stage

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

Disruption phenotype

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. Ref.7

Sequence similarities

Contains 1 A to I editase domain.

Contains 2 DRBM (double-stranded RNA-binding) domains.

RNA editing

Edited at position 437.
Partially edited. Editing is low in embryos and pupae and increases dramatically upon eclosion. Ref.1

Sequence caution

The sequence AAM50022.1 differs from that shown. Reason: Intron retention.

Alternative products

This entry describes 7 isoforms produced by alternative splicing and alternative initiation. [Align] [Select]
Isoform C Ref.1 (identifier: Q9NII1-1)

Also known as: b;

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.
Isoform A Ref.1 (identifier: Q9NII1-2)

Also known as: a;

The sequence of this isoform differs from the canonical sequence as follows:
     154-191: GIENLSSSKMFEIIQTMLTEKLSNPTSLEQPTFCMSQN → D
Isoform B Ref.3 (identifier: Q9NII1-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-19: MKFDSRVMLNSANNNSPQH → MTLCRYSE
     154-191: GIENLSSSKMFEIIQTMLTEKLSNPTSLEQPTFCMSQN → D
Isoform D Ref.1 (identifier: Q9NII1-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-19: MKFDSRVMLNSANNNSPQH → MKFECFSLYCTVLK
Isoform F Ref.1 (identifier: Q9NII1-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-28: Missing.
Isoform G Ref.1 (identifier: Q9NII1-6)

The sequence of this isoform differs from the canonical sequence as follows:
     1-28: Missing.
     154-191: GIENLSSSKMFEIIQTMLTEKLSNPTSLEQPTFCMSQN → D
Isoform E (identifier: Q9NII1-7)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 676676Double-stranded RNA-specific editase Adar Ref.1
PRO_0000004790

Regions

Domain61 – 12767DRBM 1
Domain197 – 27276DRBM 2
Domain348 – 672325A to I editase

Sites

Active site3741Proton donor By similarity UniProtKB P78563
Metal binding3721Zinc By similarity UniProtKB P78563
Metal binding4301Zinc By similarity UniProtKB P78563
Metal binding4931Zinc By similarity UniProtKB P78563

Natural variations

Alternative sequence1 – 2828Missing in isoform F and isoform G. Ref.1
VSP_051650
Alternative sequence1 – 1919MKFDS…NSPQH → MTLCRYSE in isoform B. Ref.3
VSP_051649
Alternative sequence1 – 1919MKFDS…NSPQH → MKFECFSLYCTVLK in isoform D. Ref.1
VSP_051648
Alternative sequence1 – 77Missing in isoform E.
VSP_018700
Alternative sequence154 – 19138GIENL…CMSQN → D in isoform A, isoform B and isoform G. Ref.1 Ref.3
VSP_051651
Natural variant4371S → G in RNA edited version. Ref.1

Experimental info

Sequence conflict3461V → VSPQPAKHCETNYNAKPILD QV in CAA22774. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Isoform C (b) [UniParc].

Last modified February 1, 2005. Version 2.
Checksum: 6570D16D25D1C9F4

FASTA67674,978
        10         20         30         40         50         60 
MKFDSRVMLN SANNNSPQHP VSAPSDINMN GYNRKLPQKR GYEMPKYSDP KKKMCKERIP 

        70         80         90        100        110        120 
QPKNTVAMLN ELRHGLIYKL ESQTGPVHAP LFTISVEVDG QKYLGQGRSK KVARIEAAAT 

       130        140        150        160        170        180 
ALRSFIQFKD GAVLSPLKPA GNLDFTSDEH LENGIENLSS SKMFEIIQTM LTEKLSNPTS 

       190        200        210        220        230        240 
LEQPTFCMSQ NVSKSAITVD GQKKVPDKGP VMLLYELFND VNFECINIDG AQNNCRFKMT 

       250        260        270        280        290        300 
VTINEKKFDG TGPSKKTAKN AAAKAALASL CNISYSPMVV PQKNVPLPID DKSSSMELPQ 

       310        320        330        340        350        360 
IHADTIGRLV LEKFMEVIKG QEAYSRRKVL AGIVMTENMN FCEAKVISVS TGTKCVSGEH 

       370        380        390        400        410        420 
MSVNGAVLND SHAEIVSRRC LLKYLYAQLD LQCNQATAYQ SIFVRNTDGQ YPYKLKSGVH 

       430        440        450        460        470        480 
FHLYINTAPC GDARIFSPHE NDTGVDKHPN RKARGQLRTK IESGEGTIPV KSSDGIQTWD 

       490        500        510        520        530        540 
GVLQGQRLLT MSCSDKIARW NIVGIQGSLL SSIIEPVYLH SIVLGSLLHP EHMYRAVCGR 

       550        560        570        580        590        600 
IEKSIQGLPP PYHLNKPRLA LVTSAEPRNQ AKAPNFGINW TIGDTELEVV NSLTGRTIGG 

       610        620        630        640        650        660 
QVSRITKQAF FVKYGFLMAN LPGILVRKVT TDYGQTKANV KDYQIAKLEL FSAFKREDLG 

       670 
SWLKKPIEQD EFGLAE 

« Hide

Isoform A (a) [UniParc].

Checksum: B1FD5629F6836008
Show »

FASTA63970,832
Isoform B [UniParc].

Checksum: CAC6899EB4812A5E
Show »

FASTA62869,644
Isoform D [UniParc].

Checksum: 747B60F654D2DF83
Show »

FASTA67174,500
Isoform F [UniParc].

Checksum: BDD164B681DEFD22
Show »

FASTA64871,925
Isoform G [UniParc].

Checksum: 02201A647CD817BC
Show »

FASTA61167,779
Isoform E [UniParc].

Checksum: 0D601A34987E3508
Show »

FASTA66974,114

References

« Hide 'large scale' references
[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: 10917596] [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-S.
[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: 11254668] [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. expand/collapse author list , 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: 10731132] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[4]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract]
Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
Strain: Berkeley.
[5]"From sequence to chromosome: the tip of the X chromosome of D. melanogaster."
Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., Barrell B.G., Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Borkova D., Minana B. expand/collapse author list , Kafatos F.C., Louis C., Siden-Kiamos I., Bolshakov S., Papagiannakis G., Spanos L., Cox S., Madueno E., de Pablos B., Modolell J., Peter A., Schoettler P., Werner M., Mourkioti F., Beinert N., Dowe G., Schaefer U., Jaeckle H., Bucheton A., Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S., McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C., Glover D.M.
Science 287:2220-2222(2000) [PubMed: 10731137] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Oregon-R.
[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: 12537569] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
Tissue: Embryo.
[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: 10966106] [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: 12756328] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_569940.2. NM_130584.2.
NP_726761.2. NM_166903.1.
UniGeneDm.5410.

3D structure databases

ProteinModelPortalQ9NII1.
SMRQ9NII1. Positions 23-277, 287-675.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ9NII1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID31130.
KEGGdme:Dmel_CG12598.

Organism-specific databases

CTD103.
FlyBaseFBgn0026086. Adar.

Phylogenomic databases

InParanoidQ9NII1.
OrthoDBEOG4VQ84C.
PhylomeDBQ9NII1.

Gene expression databases

BgeeQ9NII1.

Family and domain databases

InterProIPR002466. A_deamin.
IPR001159. Ds-RNA-bd.
IPR014720. dsRNA-bd-like.
[Graphical view]
Gene3DG3DSA:3.30.160.20. dsRNA-bd-like. 2 hits.
PfamPF02137. A_deamin. 1 hit.
PF00035. dsrm. 2 hits.
[Graphical view]
SMARTSM00552. ADEAMc. 1 hit.
SM00358. DSRM. 2 hits.
[Graphical view]
PROSITEPS50141. A_DEAMIN_EDITASE. 1 hit.
PS50137. DS_RBD. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio772061.

Entry information

Entry nameADAR_DROME
AccessionPrimary (citable) accession number: Q9NII1
Secondary accession number(s): O96834 expand/collapse secondary AC list , Q8IRX2, Q8MSQ9, Q9BJ37, Q9NII2, Q9W562
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: February 1, 2005
Last modified: January 25, 2012
This is version 69 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

Drosophila

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

SIMILARITY comments

Index of protein domains and families