DSRAD_MOUSE
ID DSRAD_MOUSE Reviewed; 1178 AA.
AC Q99MU3; O70375; Q80UZ6; Q8C222; Q99MU2; Q99MU4; Q99MU7;
DT 14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2003, sequence version 2.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Double-stranded RNA-specific adenosine deaminase;
DE Short=DRADA;
DE EC=3.5.4.37;
DE AltName: Full=RNA adenosine deaminase 1;
GN Name=Adar;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4 AND 5), SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
RC STRAIN=C57BL/6J; TISSUE=Spleen;
RX PubMed=12954622; DOI=10.1074/jbc.m308612200;
RA Yang J.-H., Nie Y., Zhao Q., Su Y., Pypaert M., Su H., Rabinovici R.;
RT "Intracellular localization of differentially regulated RNA-specific
RT adenosine deaminase isoforms in inflammation.";
RL J. Biol. Chem. 278:45833-45842(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE SPLICING, AND
RP INDUCTION.
RX PubMed=12709013; DOI=10.1046/j.1365-2567.2003.01598.x;
RA Yang J.-H., Luo X., Nie Y., Su Y., Zhao Q., Kabir K., Zhang D.-X.,
RA Rabinovici R.;
RT "Widespread inosine-containing mRNA in lymphocytes regulated by ADAR1 in
RT response to inflammation.";
RL Immunology 109:15-23(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Fibroblast;
RA Young S.B., Carmichael G.G.;
RT "cDNA for mouse double-stranded RNA-specific adenosine deaminase (ADAR1).";
RL Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANTS SER-20;
RP LEU-32 AND LEU-330.
RC STRAIN=Czech II; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1173 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Dendritic cell;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [6]
RP HOMODIMERIZATION, AND SUBUNIT.
RX PubMed=12618436; DOI=10.1074/jbc.m213127200;
RA Cho D.-S.C., Yang W., Lee J.T., Shiekhattar R., Murray J.M., Nishikura K.;
RT "Requirement of dimerization for RNA editing activity of adenosine
RT deaminases acting on RNA.";
RL J. Biol. Chem. 278:17093-17102(2003).
RN [7]
RP DISRUPTION PHENOTYPE.
RX PubMed=14615479; DOI=10.1074/jbc.m311347200;
RA Hartner J.C., Schmittwolf C., Kispert A., Mueller A.M., Higuchi M.,
RA Seeburg P.H.;
RT "Liver disintegration in the mouse embryo caused by deficiency in the RNA-
RT editing enzyme ADAR1.";
RL J. Biol. Chem. 279:4894-4902(2004).
RN [8]
RP DISRUPTION PHENOTYPE.
RX PubMed=14613934; DOI=10.1074/jbc.m310162200;
RA Wang Q., Miyakoda M., Yang W., Khillan J., Stachura D.L., Weiss M.J.,
RA Nishikura K.;
RT "Stress-induced apoptosis associated with null mutation of ADAR1 RNA
RT editing deaminase gene.";
RL J. Biol. Chem. 279:4952-4961(2004).
RN [9]
RP FUNCTION.
RX PubMed=15556947; DOI=10.1074/jbc.m407876200;
RA Yang W., Wang Q., Howell K.L., Lee J.T., Cho D.-S.C., Murray J.M.,
RA Nishikura K.;
RT "ADAR1 RNA deaminase limits short interfering RNA efficacy in mammalian
RT cells.";
RL J. Biol. Chem. 280:3946-3953(2005).
RN [10]
RP INTERACTION WITH ILF2 AND ILF3.
RX PubMed=16055709; DOI=10.1128/mcb.25.16.6956-6963.2005;
RA Nie Y., Ding L., Kao P.N., Braun R., Yang J.-H.;
RT "ADAR1 interacts with NF90 through double-stranded RNA and regulates NF90-
RT mediated gene expression independently of RNA editing.";
RL Mol. Cell. Biol. 25:6956-6963(2005).
RN [11]
RP FUNCTION, AND INTERACTION WITH EIF2AK2.
RX PubMed=17079286; DOI=10.1128/jvi.01527-06;
RA Nie Y., Hammond G.L., Yang J.H.;
RT "Double-stranded RNA deaminase ADAR1 increases host susceptibility to virus
RT infection.";
RL J. Virol. 81:917-923(2007).
RN [12]
RP FUNCTION.
RX PubMed=17369310; DOI=10.1261/rna.349107;
RA Ohlson J., Pedersen J.S., Haussler D., Ohman M.;
RT "Editing modifies the GABA(A) receptor subunit alpha3.";
RL RNA 13:698-703(2007).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-582, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [14]
RP REVIEW.
RX PubMed=21182352; DOI=10.1089/jir.2010.0097;
RA George C.X., Gan Z., Liu Y., Samuel C.E.;
RT "Adenosine deaminases acting on RNA, RNA editing, and interferon action.";
RL J. Interferon Cytokine Res. 31:99-117(2011).
RN [15]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-30 AND ARG-42, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Catalyzes the hydrolytic deamination of adenosine to inosine
CC in double-stranded RNA (dsRNA) referred to as A-to-I RNA editing. This
CC may affect gene expression and function in a number of ways that
CC include mRNA translation by changing codons and hence the amino acid
CC sequence of proteins since the translational machinery read the inosine
CC as a guanosine; pre-mRNA splicing by altering splice site recognition
CC sequences; RNA stability by changing sequences involved in nuclease
CC recognition; genetic stability in the case of RNA virus genomes by
CC changing sequences during viral RNA replication; and RNA structure-
CC dependent activities such as microRNA production or targeting or
CC protein-RNA interactions. Can edit both viral and cellular RNAs and can
CC edit RNAs at multiple sites (hyper-editing) or at specific sites (site-
CC specific editing). Its cellular RNA substrates include: bladder cancer-
CC associated protein (BLCAP), neurotransmitter receptors for glutamate
CC (GRIA2) and serotonin (HTR2C) and GABA receptor (GABRA3). Site-specific
CC RNA editing of transcripts encoding these proteins results in amino
CC acid substitutions which consequently alters their functional
CC activities. Exhibits low-level editing at the GRIA2 Q/R site, but edits
CC efficiently at the R/G site and HOTSPOT1. Does not affect polyomavirus
CC replication but provides protection against virus-induced cytopathic
CC effects. Essential for embryonic development and cell survival and
CC plays a critical role in the maintenance of hematopoietic stem cells.
CC {ECO:0000269|PubMed:15556947, ECO:0000269|PubMed:17079286,
CC ECO:0000269|PubMed:17369310}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine in double-stranded RNA + H(+) + H2O = inosine in
CC double-stranded RNA + NH4(+); Xref=Rhea:RHEA:10120, Rhea:RHEA-
CC COMP:13885, Rhea:RHEA-COMP:13886, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:74411,
CC ChEBI:CHEBI:82852; EC=3.5.4.37;
CC -!- SUBUNIT: Homodimer. Homodimerization is essential for its catalytic
CC activity (PubMed:12618436). Isoform 5 can form heterodimers with
CC ADARB1/ADAR2. Isoform 1 and isoform 5 (via DRBM 3 domain) interact with
CC TNPO1. Isoform 5 (via DRBM domains) interacts with XPO5. Isoform 1 and
CC isoform 5 can interact with UPF1 (By similarity). Isoform 1 interacts
CC with ILF2/NF45 and ILF3/NF90 (PubMed:16055709). Binding to ILF3/NF90
CC up-regulates ILF3-mediated gene expression. Isoform 1 and isoform 5
CC interact with EIF2AK2/PKR (PubMed:17079286).
CC {ECO:0000250|UniProtKB:P55265, ECO:0000269|PubMed:12618436,
CC ECO:0000269|PubMed:16055709, ECO:0000269|PubMed:17079286}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm. Nucleus, nucleolus.
CC Note=Long forms starting at Met-1 are found predominantly in cytoplasm.
CC Shuttles between the cytoplasm and nucleus.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm. Nucleus, nucleolus.
CC Note=Long forms starting at Met-1 are found predominantly in cytoplasm.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Nucleus, nucleolus. Note=Short forms
CC starting at Met-519 are found exclusively in the nucleolus.
CC -!- SUBCELLULAR LOCATION: [Isoform 4]: Nucleus, nucleolus. Note=Short forms
CC starting at Met-519 are found exclusively in the nucleolus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1; Synonyms=ADAR1Lb, p150;
CC IsoId=Q99MU3-1; Sequence=Displayed;
CC Name=2; Synonyms=ADAR1La;
CC IsoId=Q99MU3-2; Sequence=VSP_008875;
CC Name=3; Synonyms=ADAR1Sa;
CC IsoId=Q99MU3-3; Sequence=VSP_019236, VSP_008875;
CC Name=4; Synonyms=ADAR1Sb, p80;
CC IsoId=Q99MU3-4; Sequence=VSP_019236;
CC Name=5; Synonyms=p110;
CC IsoId=Q99MU3-5; Sequence=VSP_019237;
CC -!- TISSUE SPECIFICITY: Highest levels in brain and spleen. Lowest levels
CC in liver. {ECO:0000269|PubMed:12954622}.
CC -!- INDUCTION: By inflammation. Under normal conditions, long forms
CC starting at Met-1 are dominant. Inflammation causes selective induction
CC of short forms starting at Met-519. {ECO:0000269|PubMed:12709013,
CC ECO:0000269|PubMed:12954622}.
CC -!- DOMAIN: The third dsRNA-binding domain (DRBM 3) contains an additional
CC N-terminal alpha-helix that is part of a bi-partite nuclear
CC localization signal, together with the sequence immediately C-terminal
CC to DRBM 3. The presence of DRBM 3 is important to bring together the N-
CC terminal and the C-terminal part of the bi-partite nuclear localization
CC signal for import mediated by TNPO1. RNA binding interferes with
CC nuclear import. {ECO:0000250|UniProtKB:P55265}.
CC -!- DOMAIN: The first Z-binding domain binds Z-DNA. {ECO:0000255|PROSITE-
CC ProRule:PRU00073}.
CC -!- PTM: Sumoylation reduces RNA-editing activity.
CC {ECO:0000250|UniProtKB:P55265}.
CC -!- DISRUPTION PHENOTYPE: Mice do not survive past 11.0-12.5 dpc, and
CC embryos display widespread apoptosis, a rapidly disintegrating liver
CC structure and severe defects in hematopoiesis.
CC {ECO:0000269|PubMed:14613934, ECO:0000269|PubMed:14615479}.
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DR EMBL; AF291875; AAK16101.1; -; mRNA.
DR EMBL; AF291876; AAK16102.1; -; mRNA.
DR EMBL; AF291877; AAK16103.1; -; mRNA.
DR EMBL; AF291050; AAK17103.1; -; mRNA.
DR EMBL; AF052506; AAC06233.1; -; mRNA.
DR EMBL; BC042505; AAH42505.1; -; mRNA.
DR EMBL; AK089451; BAC40888.2; -; mRNA.
DR CCDS; CCDS17513.1; -. [Q99MU3-2]
DR CCDS; CCDS17514.1; -. [Q99MU3-5]
DR CCDS; CCDS50963.1; -. [Q99MU3-1]
DR RefSeq; NP_001139768.1; NM_001146296.1. [Q99MU3-1]
DR RefSeq; NP_062629.3; NM_019655.3. [Q99MU3-2]
DR RefSeq; XP_006501817.1; XM_006501754.2. [Q99MU3-5]
DR AlphaFoldDB; Q99MU3; -.
DR SMR; Q99MU3; -.
DR BioGRID; 207963; 13.
DR STRING; 10090.ENSMUSP00000103028; -.
DR iPTMnet; Q99MU3; -.
DR PhosphoSitePlus; Q99MU3; -.
DR SwissPalm; Q99MU3; -.
DR EPD; Q99MU3; -.
DR MaxQB; Q99MU3; -.
DR PaxDb; Q99MU3; -.
DR PeptideAtlas; Q99MU3; -.
DR PRIDE; Q99MU3; -.
DR ProteomicsDB; 277508; -. [Q99MU3-1]
DR ProteomicsDB; 277509; -. [Q99MU3-2]
DR ProteomicsDB; 277510; -. [Q99MU3-3]
DR ProteomicsDB; 277511; -. [Q99MU3-4]
DR ProteomicsDB; 277512; -. [Q99MU3-5]
DR Antibodypedia; 1280; 285 antibodies from 32 providers.
DR DNASU; 56417; -.
DR Ensembl; ENSMUST00000029563; ENSMUSP00000029563; ENSMUSG00000027951. [Q99MU3-2]
DR Ensembl; ENSMUST00000098924; ENSMUSP00000096525; ENSMUSG00000027951. [Q99MU3-5]
DR Ensembl; ENSMUST00000107405; ENSMUSP00000103028; ENSMUSG00000027951. [Q99MU3-1]
DR Ensembl; ENSMUST00000118341; ENSMUSP00000113453; ENSMUSG00000027951. [Q99MU3-4]
DR Ensembl; ENSMUST00000121094; ENSMUSP00000112969; ENSMUSG00000027951. [Q99MU3-3]
DR GeneID; 56417; -.
DR KEGG; mmu:56417; -.
DR UCSC; uc008pzv.2; mouse. [Q99MU3-1]
DR UCSC; uc008pzw.2; mouse. [Q99MU3-2]
DR UCSC; uc008pzy.2; mouse. [Q99MU3-3]
DR CTD; 103; -.
DR MGI; MGI:1889575; Adar.
DR VEuPathDB; HostDB:ENSMUSG00000027951; -.
DR eggNOG; KOG2777; Eukaryota.
DR GeneTree; ENSGT00940000157243; -.
DR HOGENOM; CLU_005382_0_0_1; -.
DR InParanoid; Q99MU3; -.
DR OMA; MQMRLKA; -.
DR OrthoDB; 947117at2759; -.
DR PhylomeDB; Q99MU3; -.
DR TreeFam; TF315806; -.
DR BRENDA; 3.5.4.37; 3474.
DR Reactome; R-MMU-75102; C6 deamination of adenosine.
DR Reactome; R-MMU-77042; Formation of editosomes by ADAR proteins.
DR BioGRID-ORCS; 56417; 19 hits in 77 CRISPR screens.
DR ChiTaRS; Adar; mouse.
DR PRO; PR:Q99MU3; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q99MU3; protein.
DR Bgee; ENSMUSG00000027951; Expressed in dorsal tegmental nucleus and 253 other tissues.
DR Genevisible; Q99MU3; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0044530; C:supraspliceosomal complex; ISS:UniProtKB.
DR GO; GO:0003726; F:double-stranded RNA adenosine deaminase activity; ISO:MGI.
DR GO; GO:0003725; F:double-stranded RNA binding; IBA:GO_Central.
DR GO; GO:0003692; F:left-handed Z-DNA binding; TAS:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008251; F:tRNA-specific adenosine deaminase activity; IBA:GO_Central.
DR GO; GO:0006382; P:adenosine to inosine editing; IDA:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IMP:MGI.
DR GO; GO:0016553; P:base conversion or substitution editing; ISO:MGI.
DR GO; GO:0098586; P:cellular response to virus; IDA:UniProtKB.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR GO; GO:0060216; P:definitive hemopoiesis; IMP:MGI.
DR GO; GO:0030218; P:erythrocyte differentiation; IMP:MGI.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IMP:MGI.
DR GO; GO:0061484; P:hematopoietic stem cell homeostasis; IMP:MGI.
DR GO; GO:0097284; P:hepatocyte apoptotic process; IMP:MGI.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0035196; P:miRNA processing; IMP:MGI.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:1903944; P:negative regulation of hepatocyte apoptotic process; IMP:MGI.
DR GO; GO:1900369; P:negative regulation of post-transcriptional gene silencing by RNA; IMP:MGI.
DR GO; GO:0044387; P:negative regulation of protein kinase activity by regulation of protein phosphorylation; IMP:UniProtKB.
DR GO; GO:0060339; P:negative regulation of type I interferon-mediated signaling pathway; IMP:MGI.
DR GO; GO:0001649; P:osteoblast differentiation; IMP:MGI.
DR GO; GO:0045070; P:positive regulation of viral genome replication; IMP:UniProtKB.
DR GO; GO:0031054; P:pre-miRNA processing; ISO:MGI.
DR GO; GO:0006611; P:protein export from nucleus; ISO:MGI.
DR GO; GO:0006606; P:protein import into nucleus; ISO:MGI.
DR GO; GO:0035455; P:response to interferon-alpha; ISS:UniProtKB.
DR GO; GO:0009615; P:response to virus; ISS:UniProtKB.
DR GO; GO:0070922; P:RISC complex assembly; ISO:MGI.
DR GO; GO:0006396; P:RNA processing; IBA:GO_Central.
DR GO; GO:0002566; P:somatic diversification of immune receptors via somatic mutation; IDA:MGI.
DR CDD; cd19913; DSRM_DRADA_rpt1; 1.
DR CDD; cd19915; DSRM_DRADA_rpt3; 1.
DR Gene3D; 1.10.10.10; -; 2.
DR InterPro; IPR002466; A_deamin.
DR InterPro; IPR044456; ADAR1_DSRM_1.
DR InterPro; IPR044457; ADAR1_DSRM_3.
DR InterPro; IPR014720; dsRBD_dom.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR InterPro; IPR042371; Z_dom.
DR Pfam; PF02137; A_deamin; 1.
DR Pfam; PF00035; dsrm; 3.
DR Pfam; PF02295; z-alpha; 2.
DR SMART; SM00552; ADEAMc; 1.
DR SMART; SM00358; DSRM; 3.
DR SMART; SM00550; Zalpha; 2.
DR SUPFAM; SSF46785; SSF46785; 2.
DR PROSITE; PS50141; A_DEAMIN_EDITASE; 1.
DR PROSITE; PS50137; DS_RBD; 3.
DR PROSITE; PS50139; Z_BINDING; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Antiviral defense; Cytoplasm; DNA-binding; Hydrolase;
KW Immunity; Innate immunity; Isopeptide bond; Metal-binding; Methylation;
KW mRNA processing; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW RNA-binding; RNA-mediated gene silencing; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc.
FT CHAIN 1..1178
FT /note="Double-stranded RNA-specific adenosine deaminase"
FT /id="PRO_0000171775"
FT DOMAIN 135..201
FT /note="Z-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00073"
FT DOMAIN 246..310
FT /note="Z-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00073"
FT DOMAIN 456..524
FT /note="DRBM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00266"
FT DOMAIN 567..635
FT /note="DRBM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00266"
FT DOMAIN 675..743
FT /note="DRBM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00266"
FT DOMAIN 835..1170
FT /note="A to I editase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00240"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 135..204
FT /note="Interaction with Z-DNA"
FT /evidence="ECO:0000250|UniProtKB:P55265"
FT REGION 221..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 316..383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 527..564
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 631..657
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 665..674
FT /note="N-terminal extension of DRBM 3 and constituent of a
FT bi-partite nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:P55265"
FT REGION 744..750
FT /note="C-terminal extension of DRBM 3 and constituent of a
FT bi-partite nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:P55265"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 365..383
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 528..550
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 638..656
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 861
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00240"
FT BINDING 859
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00240"
FT BINDING 915
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00240"
FT BINDING 985
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00240"
FT MOD_RES 30
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 42
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 231
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55266"
FT MOD_RES 238
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55266"
FT MOD_RES 434
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55265"
FT MOD_RES 567
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55265"
FT MOD_RES 582
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 589
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55265"
FT MOD_RES 757
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P55265"
FT MOD_RES 763
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55265"
FT MOD_RES 772
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55265"
FT MOD_RES 774
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55265"
FT CROSSLNK 371
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT /evidence="ECO:0000250"
FT CROSSLNK 371
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P55265"
FT CROSSLNK 371
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P55265"
FT CROSSLNK 824
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P55265"
FT VAR_SEQ 1..518
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:12954622"
FT /id="VSP_019236"
FT VAR_SEQ 1..248
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:12954622"
FT /id="VSP_019237"
FT VAR_SEQ 756..781
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:12709013,
FT ECO:0000303|PubMed:12954622, ECO:0000303|PubMed:15489334,
FT ECO:0000303|Ref.3"
FT /id="VSP_008875"
FT VARIANT 20
FT /note="L -> S (in strain: Czech II)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT VARIANT 32
FT /note="P -> L (in strain: Czech II)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT VARIANT 120
FT /note="T -> P (in strain: Czech II)"
FT VARIANT 330
FT /note="P -> L (in strain: Czech II)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT CONFLICT 415
FT /note="N -> D (in Ref. 1; AAK16102)"
FT /evidence="ECO:0000305"
FT CONFLICT 644
FT /note="Q -> K (in Ref. 3; AAC06233)"
FT /evidence="ECO:0000305"
FT CONFLICT 730
FT /note="K -> R (in Ref. 3; AAC06233)"
FT /evidence="ECO:0000305"
FT CONFLICT 920
FT /note="L -> H (in Ref. 3; AAC06233)"
FT /evidence="ECO:0000305"
FT CONFLICT 1003
FT /note="T -> A (in Ref. 5; BAC40888)"
FT /evidence="ECO:0000305"
FT CONFLICT 1098
FT /note="P -> S (in Ref. 1; AAK16102)"
FT /evidence="ECO:0000305"
FT CONFLICT 1149
FT /note="K -> R (in Ref. 1; AAK16102)"
FT /evidence="ECO:0000305"
FT CONFLICT 1173
FT /note="C -> R (in Ref. 5; BAC40888)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1178 AA; 130447 MW; 8C28B71F00744724 CRC64;
MSQGFRGPTG VFPHQTQSYL DPSHEHSKWR YPQPQGPESY PRSFQLQQIE FLKGRLPEAP
LIGIQTQSLP PFLPGHWPRF PGPPAQDRQL EIWEFPRSVT LRNQGFHIGP PLPPPHSRGT
PWRGADGLCS HFRELSISQS PEQKVLNRLE ELGEGKATTA HVLARELRIP KRDINRILYS
LEKKGKLHRG RGKPPLWSLV PLSQAWTQPP GVVNPDSCIQ EFPRGEPGLD SEDGDPASDL
EGPSEPLDMA EIKEKICDYL FNVSNSSALN LAKNIGLTKA RDVTSVLIDL ERQGDVYRQG
ATPPIWYLTD KKRERLQMKR STHSAPAPTP TAVPEATRSP SFPACHPPPA GASSSVAASK
RVENGQEPAI KHESRHEARP GPMRLRPHAY HNGPSRAGYV ASENGQWATD DIPDNLNSIH
TAPGEFRAIM EMPSFYSPTL PRCSPYKKLT ECQLKNPVSG LLEYAQFTSQ TCDFNLIEQS
GPSHEPRFKF QVVINGREFP PAEAGSKKVA KQDAAVKAMA ILLREAKAKD SGQPEDLSHC
PMEEDSEKPA EAQAPSSSAT SLFSGKSPVT TLLECMHKLG NSCEFRLLSK EGPAHDPKFQ
YCVAVGAQTF PPVSAPSKKV AKQMAAEEAM KALQEEAASS ADDQSGGANT DSLDESMAPN
KIRRIGELVR YLNTNPVGGL LEYARSHGFA AEFKLIDQSG PPHEPKFVYQ AKVGGRWFPA
VCAHSKKQGK QDAADAALRV LIGESEKAEQ LGFAEVTPVT GASLRRTMLL LSRSPDAHPK
TLPLSGSTFH DQIAMLSHRC FNALTNSFQP SLLGRKILAA IIMKRDPEDM GVVVSLGTGN
RCVKGDSLSL KGETVNDCHA EIISRRGFIR FLYSELMKYN HHTAKNSIFE LARGGEKLQI
KKTVSFHLYI STAPCGDGAL FDKSCSDRAV ESTESRHYPV FENPKQGKLR TKVENGEGTI
PVESSDIVPT WDGIRLGERL RTMSCSDKIL RWNVLGLQGA LLTHFLQPVY LKSVTLGYLF
SQGHLTRAIC CRVTRDGKAF EDGLRYPFIV NHPKVGRVSV YDSKRQSGKT KETSVNWCMA
DGYDLEILDG TRGTVDGPGK ELSRVSKKNI FLQFKKLCSF RARRDLLQLS YGEAKKAARD
YDLAKNYFKK SLRDMGYGNW ISKPQEEKNF YLCPVPND
