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RED2_MOUSE
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   03-AUG-2022, entry version 137.
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; Q9JI20; -.
DR   PRIDE; Q9JI20; -.
DR   ProteomicsDB; 255281; -.
DR   Antibodypedia; 23825; 37 antibodies from 17 providers.
DR   DNASU; 94191; -.
DR   Ensembl; ENSMUST00000064473; ENSMUSP00000064775; ENSMUSG00000052551.
DR   Ensembl; ENSMUST00000135574; ENSMUSP00000115148; ENSMUSG00000052551.
DR   GeneID; 94191; -.
DR   KEGG; mmu:94191; -.
DR   UCSC; uc007pkf.2; mouse.
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; MYLHSII; -.
DR   OrthoDB; 947117at2759; -.
DR   PhylomeDB; Q9JI20; -.
DR   TreeFam; TF315806; -.
DR   BioGRID-ORCS; 94191; 1 hit in 72 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 119 other 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   InterPro; IPR002466; A_deamin.
DR   InterPro; IPR044460; ADAR3_DSRM_1.
DR   InterPro; IPR014720; dsRBD_dom.
DR   Pfam; PF02137; A_deamin; 1.
DR   Pfam; PF00035; dsrm; 2.
DR   SMART; SM00552; ADEAMc; 1.
DR   SMART; SM00358; DSRM; 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
 
 
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