ADR1_CAEEL
ID ADR1_CAEEL Reviewed; 964 AA.
AC Q9U3D6; G5EF17; G5EG30; Q86GC2; Q86GC3; Q8I8G9; Q8I8H0; Q8I8H1;
DT 31-JAN-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=A-to-I RNA editing regulator adr-1 {ECO:0000305};
GN Name=adr-1 {ECO:0000312|WormBase:H15N14.1c};
GN ORFNames=H15N14.1 {ECO:0000312|WormBase:H15N14.1c};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|EMBL:AAN61049.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS C; D; E; F AND G), FUNCTION, AND
RP TISSUE SPECIFICITY.
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:AAN61049.1};
RX PubMed=12426375; DOI=10.1093/emboj/cdf607;
RA Tonkin L.A., Saccomanno L., Morse D.P., Brodigan T., Krause M., Bass B.L.;
RT "RNA editing by ADARs is important for normal behavior in Caenorhabditis
RT elegans.";
RL EMBO J. 21:6025-6035(2002).
RN [2] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3] {ECO:0000305}
RP FUNCTION, AND ROLE IN TRANSGENE SILENCING.
RX PubMed=12419225; DOI=10.1016/s1097-2765(02)00649-4;
RA Knight S.W., Bass B.L.;
RT "The role of RNA editing by ADARs in RNAi.";
RL Mol. Cell 10:809-817(2002).
RN [4] {ECO:0000305}
RP FUNCTION.
RX PubMed=14657490; DOI=10.1126/science.1091340;
RA Tonkin L.A., Bass B.L.;
RT "Mutations in RNAi rescue aberrant chemotaxis of ADAR mutants.";
RL Science 302:1725-1725(2003).
RN [5] {ECO:0000305}
RP SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=18719245; DOI=10.1261/rna.1165008;
RA Hundley H.A., Krauchuk A.A., Bass B.L.;
RT "C. elegans and H. sapiens mRNAs with edited 3' UTRs are present on
RT polysomes.";
RL RNA 14:2050-2060(2008).
RN [6] {ECO:0000305}
RP FUNCTION.
RX PubMed=20011587; DOI=10.1371/journal.pone.0008210;
RA Sebastiani P., Montano M., Puca A., Solovieff N., Kojima T., Wang M.C.,
RA Melista E., Meltzer M., Fischer S.E., Andersen S., Hartley S.H.,
RA Sedgewick A., Arai Y., Bergman A., Barzilai N., Terry D.F., Riva A.,
RA Anselmi C.V., Malovini A., Kitamoto A., Sawabe M., Arai T., Gondo Y.,
RA Steinberg M.H., Hirose N., Atzmon G., Ruvkun G., Baldwin C.T., Perls T.T.;
RT "RNA editing genes associated with extreme old age in humans and with
RT lifespan in C. elegans.";
RL PLoS ONE 4:E8210-E8210(2009).
RN [7] {ECO:0000305}
RP FUNCTION, INTERACTION WITH ADR-2, AND MUTAGENESIS OF 223-LYS--LYS-227 AND
RP 584-LYS--LYS-588.
RX PubMed=24508457; DOI=10.1016/j.celrep.2014.01.011;
RA Washburn M.C., Kakaradov B., Sundararaman B., Wheeler E., Hoon S.,
RA Yeo G.W., Hundley H.A.;
RT "The dsRBP and inactive editor ADR-1 utilizes dsRNA binding to regulate A-
RT to-I RNA editing across the C. elegans transcriptome.";
RL Cell Rep. 6:599-607(2014).
RN [8] {ECO:0000305}
RP FUNCTION.
RX PubMed=25373143; DOI=10.1101/gr.176107.114;
RA Zhao H.Q., Zhang P., Gao H., He X., Dou Y., Huang A.Y., Liu X.M., Ye A.Y.,
RA Dong M.Q., Wei L.;
RT "Profiling the RNA editomes of wild-type C. elegans and ADAR mutants.";
RL Genome Res. 25:66-75(2015).
RN [9] {ECO:0000305}
RP FUNCTION.
RX PubMed=26917557; DOI=10.1261/rna.055079.115;
RA Washburn M.C., Hundley H.A.;
RT "Trans and cis factors affecting A-to-I RNA editing efficiency of a
RT noncoding editing target in C. elegans.";
RL RNA 22:722-728(2016).
RN [10] {ECO:0000305}
RP FUNCTION.
RX PubMed=28925356; DOI=10.7554/elife.28625;
RA Deffit S.N., Yee B.A., Manning A.C., Rajendren S., Vadlamani P.,
RA Wheeler E.C., Domissy A., Washburn M.C., Yeo G.W., Hundley H.A.;
RT "The C. elegans neural editome reveals an ADAR target mRNA required for
RT proper chemotaxis.";
RL Elife 6:0-0(2017).
CC -!- FUNCTION: Required for the hydrolytic deamination of adenosine to
CC inosine in double-stranded RNA (dsRNA) referred to as A-to-I RNA
CC editing (PubMed:12426375). Does not have deaminase activity but binds
CC to dsRNA and regulates A-to-I RNA editing, possibly by modulating the
CC accessibility of the double-stranded RNA-specific adenosine deaminase
CC adr-2 for target adenosines (PubMed:24508457, PubMed:25373143).
CC Regulates editing efficiency of specific adenosines in 3' untranslated
CC regions of target mRNAs (PubMed:24508457). Represses editing efficiency
CC of the Y75B8A.8 3' UTR in neurons (PubMed:26917557). Required for
CC correct expression and A-to-I editing of clec-41 (PubMed:28925356).
CC Required for normal chemotaxis (PubMed:12426375, PubMed:14657490). Also
CC required for normal vulva development (PubMed:12426375). Plays a role
CC in determining lifespan (PubMed:20011587, PubMed:25373143). Not
CC required for RNA interference (PubMed:12419225). Likely to play a role
CC in determining whether a dsRNA enters the RNAi pathway
CC (PubMed:14657490). {ECO:0000269|PubMed:12419225,
CC ECO:0000269|PubMed:12426375, ECO:0000269|PubMed:14657490,
CC ECO:0000269|PubMed:20011587, ECO:0000269|PubMed:24508457,
CC ECO:0000269|PubMed:25373143, ECO:0000269|PubMed:26917557,
CC ECO:0000269|PubMed:28925356}.
CC -!- SUBUNIT: Interacts with double-stranded RNA-specific adenosine
CC deaminase adr-2. {ECO:0000269|PubMed:24508457}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18719245}. Cytoplasm
CC {ECO:0000269|PubMed:18719245}. Note=Detected both in the nuclear
CC fraction and in the ribosome-containing pellet of the cytoplasm.
CC {ECO:0000269|PubMed:18719245}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=c {ECO:0000303|PubMed:12426375};
CC IsoId=Q9U3D6-1; Sequence=Displayed;
CC Name=d {ECO:0000303|PubMed:12426375};
CC IsoId=Q9U3D6-2; Sequence=VSP_059300, VSP_059305, VSP_059306,
CC VSP_059307;
CC Name=e {ECO:0000303|PubMed:12426375};
CC IsoId=Q9U3D6-3; Sequence=VSP_059300, VSP_059305, VSP_059306;
CC Name=f {ECO:0000303|PubMed:12426375};
CC IsoId=Q9U3D6-4; Sequence=VSP_059301, VSP_059302;
CC Name=g {ECO:0000303|PubMed:12426375};
CC IsoId=Q9U3D6-5; Sequence=VSP_059303, VSP_059304;
CC -!- TISSUE SPECIFICITY: Expression begins early in embryogenesis where it
CC is detected in late gastrula and comma stage embryos. By the comma
CC stage, expression is highest in developing neuronal tissue in the head,
CC tail and ventral side. Neuronal expression continues through
CC embryogenesis and, by the L1 larval stage, is the prominent pattern.
CC Expressed in most, if not all, cells of the nervous system at all
CC larval stages and in adult animals. Also expressed in the developing
CC vulva but not expressed in the adult vulva.
CC {ECO:0000269|PubMed:12426375}.
CC -!- DEVELOPMENTAL STAGE: Highest expression observed in the embryo. Levels
CC decrease dramatically after embryogenesis, remain relatively constant
CC during larval stages and increase again at the onset of adulthood.
CC {ECO:0000269|PubMed:18719245}.
CC -!- MISCELLANEOUS: Can prevent somatic transgenes from inducing gene
CC silencing via the RNA interference pathway. This may occur due to A-to-
CC I editing of transgene-derived dsRNA, preventing transgene RNAi.
CC {ECO:0000269|PubMed:12419225}.
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DR EMBL; AY150815; AAN61049.1; -; mRNA.
DR EMBL; AY150816; AAN61050.1; -; mRNA.
DR EMBL; AY150817; AAN61051.1; -; mRNA.
DR EMBL; AY150818; AAN61052.1; -; mRNA.
DR EMBL; AY150819; AAN61053.1; -; mRNA.
DR EMBL; BX284601; CAB09530.2; -; Genomic_DNA.
DR EMBL; BX284601; CAD60417.1; -; Genomic_DNA.
DR EMBL; BX284601; CAD60418.1; -; Genomic_DNA.
DR EMBL; BX284601; CAD60419.1; -; Genomic_DNA.
DR EMBL; BX284601; CAD60420.1; -; Genomic_DNA.
DR PIR; T23095; T23095.
DR RefSeq; NP_492153.2; NM_059752.5. [Q9U3D6-1]
DR RefSeq; NP_492154.2; NM_059753.5. [Q9U3D6-2]
DR RefSeq; NP_871801.1; NM_182001.3. [Q9U3D6-3]
DR RefSeq; NP_871802.1; NM_182002.3.
DR RefSeq; NP_871803.1; NM_182003.3. [Q9U3D6-5]
DR AlphaFoldDB; Q9U3D6; -.
DR SMR; Q9U3D6; -.
DR STRING; 6239.H15N14.1c; -.
DR EPD; Q9U3D6; -.
DR PaxDb; Q9U3D6; -.
DR PeptideAtlas; Q9U3D6; -.
DR EnsemblMetazoa; H15N14.1c.1; H15N14.1c.1; WBGene00000079. [Q9U3D6-1]
DR EnsemblMetazoa; H15N14.1d.1; H15N14.1d.1; WBGene00000079. [Q9U3D6-2]
DR EnsemblMetazoa; H15N14.1e.1; H15N14.1e.1; WBGene00000079. [Q9U3D6-3]
DR EnsemblMetazoa; H15N14.1f.1; H15N14.1f.1; WBGene00000079. [Q9U3D6-4]
DR EnsemblMetazoa; H15N14.1g.1; H15N14.1g.1; WBGene00000079. [Q9U3D6-5]
DR GeneID; 172542; -.
DR KEGG; cel:CELE_H15N14.1; -.
DR UCSC; H15N14.1c; c. elegans.
DR CTD; 172542; -.
DR WormBase; H15N14.1c; CE32459; WBGene00000079; adr-1. [Q9U3D6-1]
DR WormBase; H15N14.1d; CE33125; WBGene00000079; adr-1. [Q9U3D6-2]
DR WormBase; H15N14.1e; CE33126; WBGene00000079; adr-1. [Q9U3D6-3]
DR WormBase; H15N14.1f; CE33127; WBGene00000079; adr-1. [Q9U3D6-4]
DR WormBase; H15N14.1g; CE33128; WBGene00000079; adr-1. [Q9U3D6-5]
DR eggNOG; KOG2777; Eukaryota.
DR GeneTree; ENSGT00940000157942; -.
DR InParanoid; Q9U3D6; -.
DR OMA; YALHQLM; -.
DR OrthoDB; 578137at2759; -.
DR PRO; PR:Q9U3D6; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00000079; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0022626; C:cytosolic ribosome; IDA:WormBase.
DR GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0003725; F:double-stranded RNA binding; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IDA:UniProtKB.
DR GO; GO:0008251; F:tRNA-specific adenosine deaminase activity; IBA:GO_Central.
DR GO; GO:0006382; P:adenosine to inosine editing; IMP:UniProtKB.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0050921; P:positive regulation of chemotaxis; IMP:UniProtKB.
DR GO; GO:0040028; P:regulation of vulval development; IMP:UniProtKB.
DR GO; GO:0006396; P:RNA processing; IBA:GO_Central.
DR InterPro; IPR002466; A_deamin.
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 1: Evidence at protein level;
KW Alternative splicing; Chemotaxis; Cytoplasm; mRNA processing; Nucleus;
KW Reference proteome; RNA-binding.
FT CHAIN 1..964
FT /note="A-to-I RNA editing regulator adr-1"
FT /id="PRO_0000442984"
FT DOMAIN 179..240
FT /note="DRBM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00266"
FT DOMAIN 527..601
FT /note="DRBM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00266"
FT DOMAIN 670..953
FT /note="A to I editase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00240"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 86..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 149..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 95..160
FT /note="Missing (in isoform d and isoform e)"
FT /evidence="ECO:0000269|PubMed:12426375"
FT /id="VSP_059300"
FT VAR_SEQ 95..100
FT /note="KYGQQG -> VYLFLI (in isoform f)"
FT /evidence="ECO:0000269|PubMed:12426375"
FT /id="VSP_059301"
FT VAR_SEQ 101..964
FT /note="Missing (in isoform f)"
FT /evidence="ECO:0000269|PubMed:12426375"
FT /id="VSP_059302"
FT VAR_SEQ 114..115
FT /note="GA -> AK (in isoform g)"
FT /evidence="ECO:0000269|PubMed:12426375"
FT /id="VSP_059303"
FT VAR_SEQ 116..964
FT /note="Missing (in isoform g)"
FT /evidence="ECO:0000269|PubMed:12426375"
FT /id="VSP_059304"
FT VAR_SEQ 277..279
FT /note="Missing (in isoform d and isoform e)"
FT /evidence="ECO:0000269|PubMed:12426375"
FT /id="VSP_059305"
FT VAR_SEQ 300..301
FT /note="Missing (in isoform d and isoform e)"
FT /evidence="ECO:0000269|PubMed:12426375"
FT /id="VSP_059306"
FT VAR_SEQ 938
FT /note="K -> KVGVLFSSFLRLLLHNINFQ (in isoform d)"
FT /evidence="ECO:0000269|PubMed:12426375"
FT /id="VSP_059307"
FT MUTAGEN 223..227
FT /note="KKAAK->EAAAA: Defective mRNA binding, A-to-I editing
FT and interaction with adr-2; when associated with 584-E--A-
FT 588."
FT /evidence="ECO:0000269|PubMed:24508457"
FT MUTAGEN 584..588
FT /note="KKLAK->EAAAA: Defective mRNA binding, A-to-I editing
FT and interaction with adr-2; when associated with 223-E--A-
FT 227."
FT /evidence="ECO:0000269|PubMed:24508457"
FT CONFLICT 152
FT /note="F -> L (in Ref. 1; AAN61049)"
FT /evidence="ECO:0000305"
FT CONFLICT 285
FT /note="N -> H (in Ref. 1; AAN61049)"
FT /evidence="ECO:0000305"
FT CONFLICT 387
FT /note="T -> A (in Ref. 1; AAN61050)"
FT /evidence="ECO:0000305"
FT CONFLICT 472
FT /note="C -> Y (in Ref. 1; AAN61049)"
FT /evidence="ECO:0000305"
FT CONFLICT 635
FT /note="C -> R (in Ref. 1; AAN61049)"
FT /evidence="ECO:0000305"
FT CONFLICT 671
FT /note="M -> V (in Ref. 1; AAN61051)"
FT /evidence="ECO:0000305"
FT CONFLICT 749
FT /note="C -> R (in Ref. 1; AAN61049)"
FT /evidence="ECO:0000305"
FT CONFLICT 756
FT /note="A -> V (in Ref. 1; AAN61050)"
FT /evidence="ECO:0000305"
FT CONFLICT 803
FT /note="L -> M (in Ref. 1; AAN61049)"
FT /evidence="ECO:0000305"
FT CONFLICT 809
FT /note="L -> P (in Ref. 1; AAN61050)"
FT /evidence="ECO:0000305"
FT CONFLICT 834
FT /note="S -> P (in Ref. 1; AAN61050)"
FT /evidence="ECO:0000305"
FT CONFLICT 834
FT /note="S -> T (in Ref. 1; AAN61051)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 964 AA; 107427 MW; 2CE3A400BBE7AAB8 CRC64;
MDQNPNYNFG YGQAYGSGTD HTSDSTNNYN WASQWSQPES AASLATHTFP QYVSQQQQQQ
QQQAQQQAQN TYAAMNPIST FMQQQQRAQT FPQKKYGQQG GAPKPSAIRN NNFGAFGGGH
ALSQEWVQPM SQNQMGGPQG NRFFNNQKGG PFNQNKPNWR QNKPKGPAAP KKFDSTGKSP
AMLLHELFKD VSEEYTEVEG VPKKYCCTLK VNGRTFQMES VNKKAAKQKC SELVVRDLRP
DVHVTPFEEG VAAKAAAPVK KEIDAASGNG QNNKRNLLQA DAISNQPTPK KVSAVKKAKL
QLTPVESALS LLDLMQKIIA ESAEKYSPVF EASEVPKDPE IPEVEVKKEE VDTNGENVAN
EKKSGWRKNE TMHNVTLKFV EQNKQYTKMG PSRGVLKDMV IREALRDLFN VSHADITTVA
RRHASNRLGH DTTILQCLNT ICSILNCTLT IECEPAEDRP LGIGRAYFMA KCTIIDHNEN
DLKFEVKSSS LASKAMAKDW VAQETLKNYF AIDPSSCVKT DAVSSQGPCA LLHAMLNKQT
KQKCKIAYEF KDNVPPVAGQ ATTTFYCECV IDETDRYIGV GRSKKLAKSE AAMQALKKLF
KIDYDPAGNY PLALTSRAMT ESKVSPLCRH IAEFCKREYH QMTEYYQIPP SNLFAAFLLV
NAQEEKRVLA MGSSIQYIVE PDTLSGANGT SLLHLDAIIL ARRAMLKAFI HELSTVDSEC
SIFEKKEEGK AALKPNLRLV LYSNYSPPCI HAVDDAATKK LSYVTPTNLT CVPDDVLTYE
QIKETKSLRV HCTADKLFKW NTLGIQGALL SNVLHPIFID NIFFGSEAPV SDESLSYALQ
GRLGPNENER EIIVESMPVQ MRMHMGISHL WHRGVDSVET LDYNTGRTSK GSPSRVCKAE
IFEAYRKLNG VDQAVVNYAK AKEMASEYQY EKKVFYEKLE AAGLGKWQTK PAELVDSFTL
AAFD
