CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-019973
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Double-stranded RNA-specific adenosine deaminase 
Protein Synonyms/Alias
 DRADA; RNA adenosine deaminase 1 
Gene Name
 Adar 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
53LQQIEFLKGRLPEAPubiquitination[1]
511AGSKKVAKQDAAVKAubiquitination[1]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023] 
Functional Description
 Catalyzes the hydrolytic deamination of adenosine to inosine in double-stranded RNA (dsRNA) referred to as A-to-I RNA editing. This may affect gene expression and function in a number of ways that include mRNA translation by changing codons and hence the amino acid sequence of proteins; pre-mRNA splicing by altering splice site recognition sequences; RNA stability by changing sequences involved in nuclease recognition; genetic stability in the case of RNA virus genomes by changing sequences during viral RNA replication; and RNA structure-dependent activities such as microRNA production or targeting or protein-RNA interactions. Can edit both viral and cellular RNAs and can edit RNAs at multiple sites (hyper-editing) or at specific sites (site-specific editing). Its cellular RNA substrates include: bladder cancer- associated protein (BLCAP), neurotransmitter receptors for glutamate (GRIA2) and serotonin (HTR2C) and GABA receptor (GABRA3). Site-specific RNA editing of transcripts encoding these proteins results in amino acid substitutions which consequently alters their functional activities. Exhibits low-level editing at the GRIA2 Q/R site, but edits efficiently at the R/G site and HOTSPOT1. Does not affect polyomavirus replication but provides protection against virus-induced cytopathic effects. Essential for embryonic development and cell survival and plays a critical role in the maintenance of hematopoietic stem cells. 
Sequence Annotation
 REPEAT 135 204 DRADA 1.
 REPEAT 246 313 DRADA 2.
 DOMAIN 456 524 DRBM 1.
 DOMAIN 567 635 DRBM 2.
 DOMAIN 675 743 DRBM 3.
 DOMAIN 835 1170 A to I editase.
 DNA_BIND 171 197 By similarity.
 ACT_SITE 861 861 Proton donor (By similarity).
 METAL 859 859 Zinc (By similarity).
 METAL 915 915 Zinc (By similarity).
 METAL 985 985 Zinc (By similarity).
 MOD_RES 567 567 Phosphoserine (By similarity).
 MOD_RES 757 757 Phosphothreonine (By similarity).
 MOD_RES 772 772 Phosphoserine (By similarity).
 MOD_RES 774 774 Phosphoserine (By similarity).
 CROSSLNK 371 371 Glycyl lysine isopeptide (Lys-Gly)  
Keyword
 Alternative splicing; Antiviral defense; Complete proteome; Cytoplasm; DNA-binding; Hydrolase; Immunity; Innate immunity; Isopeptide bond; Metal-binding; mRNA processing; Nucleus; Phosphoprotein; Reference proteome; Repeat; RNA-binding; RNA-mediated gene silencing; Transcription; Transcription regulation; Ubl conjugation; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1178 AA 
Protein Sequence
MSQGFRGPTG VFPHQTQSYL DPSHEHSKWR YPQPQGPESY PRSFQLQQIE FLKGRLPEAP 60
LIGIQTQSLP PFLPGHWPRF PGPPAQDRQL EIWEFPRSVT LRNQGFHIGP PLPPPHSRGT 120
PWRGADGLCS HFRELSISQS PEQKVLNRLE ELGEGKATTA HVLARELRIP KRDINRILYS 180
LEKKGKLHRG RGKPPLWSLV PLSQAWTQPP GVVNPDSCIQ EFPRGEPGLD SEDGDPASDL 240
EGPSEPLDMA EIKEKICDYL FNVSNSSALN LAKNIGLTKA RDVTSVLIDL ERQGDVYRQG 300
ATPPIWYLTD KKRERLQMKR STHSAPAPTP TAVPEATRSP SFPACHPPPA GASSSVAASK 360
RVENGQEPAI KHESRHEARP GPMRLRPHAY HNGPSRAGYV ASENGQWATD DIPDNLNSIH 420
TAPGEFRAIM EMPSFYSPTL PRCSPYKKLT ECQLKNPVSG LLEYAQFTSQ TCDFNLIEQS 480
GPSHEPRFKF QVVINGREFP PAEAGSKKVA KQDAAVKAMA ILLREAKAKD SGQPEDLSHC 540
PMEEDSEKPA EAQAPSSSAT SLFSGKSPVT TLLECMHKLG NSCEFRLLSK EGPAHDPKFQ 600
YCVAVGAQTF PPVSAPSKKV AKQMAAEEAM KALQEEAASS ADDQSGGANT DSLDESMAPN 660
KIRRIGELVR YLNTNPVGGL LEYARSHGFA AEFKLIDQSG PPHEPKFVYQ AKVGGRWFPA 720
VCAHSKKQGK QDAADAALRV LIGESEKAEQ LGFAEVTPVT GASLRRTMLL LSRSPDAHPK 780
TLPLSGSTFH DQIAMLSHRC FNALTNSFQP SLLGRKILAA IIMKRDPEDM GVVVSLGTGN 840
RCVKGDSLSL KGETVNDCHA EIISRRGFIR FLYSELMKYN HHTAKNSIFE LARGGEKLQI 900
KKTVSFHLYI STAPCGDGAL FDKSCSDRAV ESTESRHYPV FENPKQGKLR TKVENGEGTI 960
PVESSDIVPT WDGIRLGERL RTMSCSDKIL RWNVLGLQGA LLTHFLQPVY LKSVTLGYLF 1020
SQGHLTRAIC CRVTRDGKAF EDGLRYPFIV NHPKVGRVSV YDSKRQSGKT KETSVNWCMA 1080
DGYDLEILDG TRGTVDGPGK ELSRVSKKNI FLQFKKLCSF RARRDLLQLS YGEAKKAARD 1140
YDLAKNYFKK SLRDMGYGNW ISKPQEEKNF YLCPVPND 1178 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:MGI.
 GO:0005730; C:nucleolus; IDA:MGI.
 GO:0044530; C:supraspliceosomal complex; ISS:UniProtKB.
 GO:0003726; F:double-stranded RNA adenosine deaminase activity; IEA:InterPro.
 GO:0003725; F:double-stranded RNA binding; IEA:InterPro.
 GO:0003692; F:left-handed Z-DNA binding; TAS:MGI.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0006382; P:adenosine to inosine editing; IDA:UniProtKB.
 GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
 GO:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW.
 GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
 GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
 GO:0043066; P:negative regulation of apoptotic process; IMP:MGI.
 GO:0044387; P:negative regulation of protein kinase activity by regulation of protein phosphorylation; IMP:UniProtKB.
 GO:0045070; P:positive regulation of viral genome replication; IMP:UniProtKB.
 GO:0006611; P:protein export from nucleus; IEA:Compara.
 GO:0006606; P:protein import into nucleus; IEA:Compara.
 GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
 GO:0035455; P:response to interferon-alpha; ISS:UniProtKB.
 GO:0009615; P:response to virus; ISS:UniProtKB.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 IPR002466; A_deamin.
 IPR001159; Ds-RNA-bd.
 IPR014720; dsRNA-bd-like_dom.
 IPR000607; dsRNA_A_deaminase.
 IPR011991; WHTH_DNA-bd_dom. 
Pfam
 PF02137; A_deamin
 PF00035; dsrm
 PF02295; z-alpha 
SMART
 SM00552; ADEAMc
 SM00358; DSRM
 SM00550; Zalpha 
PROSITE
 PS50141; A_DEAMIN_EDITASE
 PS50139; DRADA_REPEAT
 PS50137; DS_RBD 
PRINTS