NRDE2_CAEEL
ID NRDE2_CAEEL Reviewed; 1270 AA.
AC G5EG51;
DT 06-FEB-2013, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=Nuclear exosome regulator NRDE2 {ECO:0000305};
DE AltName: Full=Nuclear RNAi defective-2 protein;
GN Name=nrde-2; ORFNames=T01E8.5;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
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 [2]
RP SUBCELLULAR LOCATION, INTERACTION WITH NRDE-3, AND FUNCTION.
RX PubMed=20543824; DOI=10.1038/nature09095;
RA Guang S., Bochner A.F., Burkhart K.B., Burton N., Pavelec D.M., Kennedy S.;
RT "Small regulatory RNAs inhibit RNA polymerase II during the elongation
RT phase of transcription.";
RL Nature 465:1097-1101(2010).
RN [3]
RP FUNCTION.
RX PubMed=26365259; DOI=10.1016/j.cub.2015.07.051;
RA Mao H., Zhu C., Zong D., Weng C., Yang X., Huang H., Liu D., Feng X.,
RA Guang S.;
RT "The Nrde pathway mediates small-RNA-directed histone H3 lysine 27
RT trimethylation in Caenorhabditis elegans.";
RL Curr. Biol. 25:2398-2403(2015).
CC -!- FUNCTION: Protein of the nuclear speckles that regulates RNA exosomal
CC degradation (By similarity). Involved in short interfering RNAs-
CC mediated silencing in nuclei (PubMed:20543824). Functions with nrde-3
CC in the nuclear RNA-mediated gene silencing (RNAi) pathway to regulate
CC gene expression via inhibition of RNA polymerase II during the
CC elongation phase of transcription (PubMed:20543824). Required for
CC exogenous RNAi-induced H3K27 methylation (PubMed:26365259).
CC {ECO:0000250|UniProtKB:Q9H7Z3, ECO:0000269|PubMed:20543824,
CC ECO:0000269|PubMed:26365259}.
CC -!- SUBUNIT: Interacts with nrde-3. {ECO:0000269|PubMed:20543824}.
CC -!- INTERACTION:
CC G5EG51; Q21691: nrde-3; NbExp=2; IntAct=EBI-16359048, EBI-2419607;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20543824}. Nucleus
CC speckle {ECO:0000250|UniProtKB:Q9H7Z3}.
CC -!- SIMILARITY: Belongs to the NRDE2 family. {ECO:0000305}.
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DR EMBL; Z48809; CAA88749.1; -; Genomic_DNA.
DR EMBL; Z48583; CAA88749.1; JOINED; Genomic_DNA.
DR PIR; T22615; T22615.
DR RefSeq; NP_496209.1; NM_063808.4.
DR AlphaFoldDB; G5EG51; -.
DR BioGRID; 39908; 3.
DR IntAct; G5EG51; 1.
DR STRING; 6239.T01E8.5; -.
DR EPD; G5EG51; -.
DR PaxDb; G5EG51; -.
DR PeptideAtlas; G5EG51; -.
DR PRIDE; G5EG51; -.
DR EnsemblMetazoa; T01E8.5.1; T01E8.5.1; WBGene00011333.
DR GeneID; 174589; -.
DR KEGG; cel:CELE_T01E8.5; -.
DR CTD; 174589; -.
DR WormBase; T01E8.5; CE18165; WBGene00011333; nrde-2.
DR eggNOG; KOG1972; Eukaryota.
DR GeneTree; ENSGT00390000005524; -.
DR HOGENOM; CLU_264027_0_0_1; -.
DR InParanoid; G5EG51; -.
DR OMA; KEIAKCR; -.
DR OrthoDB; 1205288at2759; -.
DR PRO; PR:G5EG51; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00011333; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0031047; P:gene silencing by RNA; IMP:UniProtKB.
DR GO; GO:0031048; P:heterochromatin assembly by small RNA; IMP:WormBase.
DR GO; GO:1902369; P:negative regulation of RNA catabolic process; ISS:UniProtKB.
DR GO; GO:0035194; P:post-transcriptional gene silencing by RNA; IMP:WormBase.
DR InterPro; IPR013633; NRDE-2.
DR PANTHER; PTHR13471; PTHR13471; 1.
DR Pfam; PF08424; NRDE-2; 1.
PE 1: Evidence at protein level;
KW Nucleus; Reference proteome; RNA-mediated gene silencing.
FT CHAIN 1..1270
FT /note="Nuclear exosome regulator NRDE2"
FT /id="PRO_0000420972"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 119..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..150
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..165
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..187
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..203
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1270 AA; 147636 MW; DCB661227D75F541 CRC64;
MFRAYGNNGL KNPERISGEN PDLYTQTRAA VQQRATTTLK RNEKQKLAVQ NDSVFQQVGI
GESDSDDDNG GVRIRMSPHR YIDPDDVFTL PEVKKQNALR DAKIAARAAQ ATAYNTFPSV
KSLNGCQDPP ETSQQSTSRK RSASNSRSPS RSHSRRYDRD NGRQRSRSRE KKRRKKERRR
KRSSSRSSSS SRSRDRSSRA RDTSSHTLMK MNKPAKYAFL TDEEYRTCDA YISSAFITQT
KSDCENYTQG VPKKEIAKCR LSVKFIVGLE HNNILFNNIY GAEYARDKEN RPFWEQLDRY
LKDVPKETFF RYVPPVGGYW KIRDRVDLLN LDHIDDDVLA NDSDNRKDAF TFELEQAKKT
FSENVHNIDA LIKVISMEEE MCRRNVGSFS SSNPAALAER HQEMVKKAIK ADGRNAKLRL
MKIELLIKMD PNSPTIIDDF KNLTITFPHE PMVWIKYLDY IQYDSNVYNY KKLKNAFEDC
IRQVTGLTNG TLLSHLNAVN DRPLLRMFHL WIYIRYLKWM ISCAHTPVVL ANIQATFEYN
FGLADVEKRT STNSKEREVR LEEFWESGLP RIGDEGAVGA EKMLKQSEEL SDEDIQKLEN
DDFDILISRT EETIATCLQA QRDVQISWIE VEREMMNIDA RVKRTKLKDC ELYEDHVDDL
ETCELWDIIP FDRIRYYEAP GDCANFDFVQ PFLELLGVKF LNSTNCFTTT EQIISDWISN
DSTVNFYKTP TYTEKKCFEV GNNILKFMLY NRLKLTENNP EYLDKTMVKY LLAMLVTEAS
EQEKKLNFHS FKLNLKNLVG TFITKHPDIF KRAMLSKITG IVYMEKFVSW WERALKEQEK
VVEADERRKN YKEIKMEEGV VDDVKFDVIL LKKDKERVQT IRDKIRDMID IAIPKSTEKL
IQSADSSLPT LQLHLYANVL RGRLSILNQN ALEETRDVFC KEILGIHTSE FESDEALLLA
LDQGLNELLE HCKEKDNLES VDSIPELPRA EALCEALKVV AVFVFLDKMA FSRRAVDCLI
ANAITKFEQF EAKKNDFNRG TYEKYCDQID LKFITDTLIT FFSHKKHRFI YNENFKKLIF
QASQAFPCDS KYAKMLGELH SSGRLQVMKL QGFTDSRNSI LNAKRDQQFD PELETRLLMN
SLTIMFSWMN AANRIGDAGN QILYKNWKRE AANTRDPAIW RQVIRVASKL SQKILKDDAY
TRARGQCTWA LNLHFDYIEA KTVRKNGDLM EMIYLILEQS MGQEHSLFVT DEEYMKTQQE
IGLQYSESGR