ID RED2_MOUSE Reviewed; 745 AA.
AC Q9JI20; Q3UTP1; Q8CC51; Q9JIE5;
DT 19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2003, sequence version 2.
DT 27-MAR-2024, entry version 145.
DE RecName: Full=Double-stranded RNA-specific editase B2;
DE EC=3.5.-.-;
DE AltName: Full=RNA-dependent adenosine deaminase 3;
DE AltName: Full=RNA-editing deaminase 2;
DE AltName: Full=RNA-editing enzyme 2;
DE AltName: Full=dsRNA adenosine deaminase B2;
GN Name=Adarb2; Synonyms=Adar3, Red2;
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].
RC STRAIN=C57BL/6J;
RA Chen M.-H., Kabir K., Yang J.-H.;
RT "Editing activity of mouse RED2 (ADAR3) in vitro.";
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, and Diencephalon;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 11-741.
RC TISSUE=Brain;
RX PubMed=10854777; DOI=10.1016/s0378-1119(00)00174-8;
RA Slavov D., Clark M., Gardiner K.;
RT "Comparative analysis of the RED1 and RED2 A-to-I RNA editing genes from
RT mammals, pufferfish and zebrafish.";
RL Gene 250:41-51(2000).
CC -!- FUNCTION: Lacks editing activity. It prevents the binding of other ADAR
CC enzymes to targets in vitro, and decreases the efficiency of these
CC enzymes. Capable of binding to dsRNA but also to ssRNA (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Brain specific.
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DR EMBL; AF270495; AAF76894.1; -; mRNA.
DR EMBL; AK033916; BAC28513.1; -; mRNA.
DR EMBL; AK139079; BAE23882.1; -; mRNA.
DR EMBL; AK139273; BAE23939.1; -; mRNA.
DR EMBL; BC052426; AAH52426.1; -; mRNA.
DR EMBL; AF232942; AAF78580.1; -; mRNA.
DR CCDS; CCDS26231.1; -.
DR RefSeq; NP_443209.2; NM_052977.5.
DR AlphaFoldDB; Q9JI20; -.
DR SMR; Q9JI20; -.
DR STRING; 10090.ENSMUSP00000064775; -.
DR iPTMnet; Q9JI20; -.
DR PhosphoSitePlus; Q9JI20; -.
DR EPD; Q9JI20; -.
DR PaxDb; 10090-ENSMUSP00000064775; -.
DR ProteomicsDB; 255281; -.
DR Antibodypedia; 23825; 41 antibodies from 18 providers.
DR DNASU; 94191; -.
DR Ensembl; ENSMUST00000064473.13; ENSMUSP00000064775.7; ENSMUSG00000052551.17.
DR Ensembl; ENSMUST00000135574.8; ENSMUSP00000115148.2; ENSMUSG00000052551.17.
DR GeneID; 94191; -.
DR KEGG; mmu:94191; -.
DR UCSC; uc007pkf.2; mouse.
DR AGR; MGI:2151118; -.
DR CTD; 105; -.
DR MGI; MGI:2151118; Adarb2.
DR VEuPathDB; HostDB:ENSMUSG00000052551; -.
DR eggNOG; KOG2777; Eukaryota.
DR GeneTree; ENSGT00940000157252; -.
DR HOGENOM; CLU_005382_3_1_1; -.
DR InParanoid; Q9JI20; -.
DR OMA; VMSHRTE; -.
DR OrthoDB; 118472at2759; -.
DR PhylomeDB; Q9JI20; -.
DR TreeFam; TF315806; -.
DR BioGRID-ORCS; 94191; 1 hit in 77 CRISPR screens.
DR ChiTaRS; Adarb2; mouse.
DR PRO; PR:Q9JI20; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q9JI20; Protein.
DR Bgee; ENSMUSG00000052551; Expressed in lateral geniculate body and 122 other cell types or tissues.
DR ExpressionAtlas; Q9JI20; baseline and differential.
DR Genevisible; Q9JI20; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR GO; GO:0003726; F:double-stranded RNA adenosine deaminase activity; IBA:GO_Central.
DR GO; GO:0003725; F:double-stranded RNA binding; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0006396; P:RNA processing; IBA:GO_Central.
DR CDD; cd19896; DSRM_RED2_rpt1; 1.
DR Gene3D; 3.30.160.20; -; 2.
DR InterPro; IPR002466; A_deamin.
DR InterPro; IPR044460; ADAR3_DSRM_1.
DR InterPro; IPR014720; dsRBD_dom.
DR PANTHER; PTHR10910:SF17; DOUBLE-STRANDED RNA-SPECIFIC EDITASE B2; 1.
DR PANTHER; PTHR10910; EUKARYOTE SPECIFIC DSRNA BINDING PROTEIN; 1.
DR Pfam; PF02137; A_deamin; 1.
DR Pfam; PF00035; dsrm; 2.
DR SMART; SM00552; ADEAMc; 1.
DR SMART; SM00358; DSRM; 2.
DR SUPFAM; SSF54768; dsRNA-binding domain-like; 2.
DR PROSITE; PS50141; A_DEAMIN_EDITASE; 1.
DR PROSITE; PS50137; DS_RBD; 2.
PE 2: Evidence at transcript level;
KW Hydrolase; Metal-binding; mRNA processing; Nucleus; Reference proteome;
KW Repeat; RNA-binding; Zinc.
FT CHAIN 1..745
FT /note="Double-stranded RNA-specific editase B2"
FT /id="PRO_0000171783"
FT DOMAIN 125..191
FT /note="DRBM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00266"
FT DOMAIN 283..347
FT /note="DRBM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00266"
FT DOMAIN 414..741
FT /note="A to I editase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00240"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 23..35
FT /note="R-domain (ssRNA-binding)"
FT /evidence="ECO:0000250"
FT REGION 50..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..34
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..79
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 440
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00240"
FT BINDING 438
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00240"
FT BINDING 496
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00240"
FT BINDING 561
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00240"
FT CONFLICT 25
FT /note="R -> G (in Ref. 1; AAF76894)"
FT /evidence="ECO:0000305"
FT CONFLICT 65
FT /note="S -> N (in Ref. 4; AAF78580)"
FT /evidence="ECO:0000305"
FT CONFLICT 310
FT /note="K -> R (in Ref. 1; AAF76894)"
FT /evidence="ECO:0000305"
FT CONFLICT 410
FT /note="A -> G (in Ref. 4; AAF78580)"
FT /evidence="ECO:0000305"
FT CONFLICT 731
FT /note="W -> R (in Ref. 1; AAF76894)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 745 AA; 82187 MW; A336473C760902F7 CRC64;
MASVLGSGRG SGGLSSQLKC KSKRRRRRRS KRKDKVSILS TFLAPFKYLS PGTTNTEDED
NLSTSSAEVK ENRNVSNLGT RPLPPGDWAR GSTPSVKRKR PLEEGNGGHF CKLQLIWKKL
SWSVTPKNAL VQLHELKPGL QYRMVSQTGP VHAPVFAVAV EVNGLTFEGT GPTKKKAKMR
AAEMALKSFV QFPNAFQAHL AMGSSTSPCT DFTSDQADFP DTLFKEFEPS SKNEDFPGCH
PVDTEFLSSA YRRGRLLYHT LDLMGQALPD RSRLAPGALG ERNPVVVLNE LRSGLRYVCL
SETAEKPRVK SFVMAVCVDG RTFEGSGRSK KLAKGQAAQA ALQALFDIRL PGHIPSRSKS
NLLPQDFADS VSQLVTQKFR ELTVGLTSVY ARHKTLAGIV MTKGLDTKQA QVIVLSSGTK
CISGEHISDQ GLVVNDCHAE IVARRAFLHF LYSQLELHLS KHQEDPERSI FIRLKEGGYR
LRENILFHLY VSTSPCGDAR VNSPYEITTD LNSSKHIVRK FRGHLRTKIE SGEGTVPVRG
PSAVQTWDGI LLGEQLITMS CTDKIASWNV LGLQGALLCH FIEPVYLHSI IVGSLHHTGH
LARVMSHRME GIGQLPASYR QNRPLLSGVS HAEARQPGKS PHFSANWVVG SADLEIINAT
TGKRSCGGSS RLCKHVFSAW WARLHGRLST RIPSHGDTPS MYCEAKQGAH TYQSVKQQLF
KAFQKAGLGT WVRKPPEQDQ FLLSL
//
