RED2_RAT
ID RED2_RAT Reviewed; 746 AA.
AC P97616;
DT 19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 113.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=8943218; DOI=10.1074/jbc.271.50.31795;
RA Melcher T., Maas S., Herb A., Sprengel R., Higuchi M., Seeburg P.H.;
RT "RED2, a brain-specific member of the RNA-specific adenosine deaminase
RT family.";
RL J. Biol. Chem. 271:31795-31798(1996).
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. {ECO:0000269|PubMed:8943218}.
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DR EMBL; U74586; AAB41862.1; -; mRNA.
DR RefSeq; NP_579836.1; NM_133302.2.
DR AlphaFoldDB; P97616; -.
DR SMR; P97616; -.
DR STRING; 10116.ENSRNOP00000047468; -.
DR jPOST; P97616; -.
DR PaxDb; P97616; -.
DR PRIDE; P97616; -.
DR GeneID; 117088; -.
DR KEGG; rno:117088; -.
DR UCSC; RGD:621519; rat.
DR CTD; 105; -.
DR RGD; 621519; Adarb2.
DR eggNOG; KOG2777; Eukaryota.
DR InParanoid; P97616; -.
DR OrthoDB; 947117at2759; -.
DR PhylomeDB; P97616; -.
DR PRO; PR:P97616; -.
DR Proteomes; UP000002494; Unplaced.
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..746
FT /note="Double-stranded RNA-specific editase B2"
FT /id="PRO_0000171784"
FT DOMAIN 126..192
FT /note="DRBM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00266"
FT DOMAIN 284..348
FT /note="DRBM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00266"
FT DOMAIN 415..742
FT /note="A to I editase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00240"
FT REGION 1..36
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..105
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 441
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00240"
FT BINDING 439
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00240"
FT BINDING 497
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00240"
FT BINDING 562
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00240"
SQ SEQUENCE 746 AA; 82227 MW; 6741BA5FDA699077 CRC64;
MASVLGSGRG SGGLSSQLKC KSKRRRRRRS KRKDKVSILS TFLAPFKYLS PGTTNTEDED
NLSTSSAEVK ENRNVSNLGT RPLPPGDWAR GGSTPSVKRK RPLEEGNGGH FCKLQLIWKK
LSWSMTPKNA LVQLHELKPG LQYRMVSQTG PVHAPVFAVA VEVNGLTFEG TGPTKKKAKM
RAAEMALKSF VQFPNAFQAH LAMGSSTSPC TDFTSDQADF PDTLFKEFEP SSRNEDFPGC
CPVDTEFLSS AYRRGRLLYH TLDLMGQALP DRSRLAPGAL GERNPVVVLN ELRSGLRYVC
LSETAEKPRV KSFVMAVCVD GRTFEGSGRS KKLAKGQAAQ AALQALFDIR LPGHIPSRSK
SNLLPQDFAD SVSQLVTQKF RELTVGLTSV YARHKTLAGI VMTKGLDTKQ AQVIVLSSGT
KCISGEHISD QGLVVNDCHA EIVARRAFLH FLYTQLELHL SKHQEDPERS IFIRVKEGGY
RLRENILFHL YVSTSPCGDA RLNSPYEITI DLNSSKHIVR KFRGHLRTKI ESGEGTVPVR
GPSAVQTWDG ILLGEQLVTM SCTDKIASWN VLGLQGALLC HFIEPVYLHS IIVGSLHHTG
HLARVMSHRM EGIGQLPASY RQNRPLLSGV SNAEARQPGK SPHFSANWVV GSADLEIINA
TTGKRSCGGS SRLCKHVFSA RWARLHGRLS TRIPGHGDTP SMYCEAKRGA HTYQSVKQQL
FKAFQKAGLG TWVRKPPEQD QFLLSL
