NRDE2_MOUSE
ID NRDE2_MOUSE Reviewed; 1172 AA.
AC Q80XC6; E9QKV8; Q8R3D7; Q99LT9;
DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Nuclear exosome regulator NRDE2 {ECO:0000305};
DE AltName: Full=Protein NRDE2 homolog {ECO:0000305};
GN Name=Nrde2;
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 [LARGE SCALE MRNA].
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 21-1172.
RC TISSUE=Mammary tumor, and Olfactory epithelium;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Protein of the nuclear speckles that regulates RNA
CC degradation and export from the nucleus through its interaction with
CC MTREX an essential factor directing various RNAs to exosomal
CC degradation. Changes the conformation of MTREX, precluding its
CC association with the nuclear exosome and interaction with proteins
CC required for its function in RNA exosomal degradation. Negatively
CC regulates, for instance, the degradation of mRNAs and lncRNAs by
CC inhibiting their MTREX-mediated recruitment to nuclear exosome. By
CC preventing the degradation of RNAs in the nucleus, it promotes their
CC export to the cytoplasm (By similarity). U5 snRNP-associated RNA
CC splicing factor which is required for efficient splicing of CEP131 pre-
CC mRNA and plays an important role in centrosome maturation, integrity
CC and function during mitosis (By similarity). Suppresses intron
CC retention in a subset of pre-mRNAs containing short, GC-rich introns
CC with relatively weak 5' and 3' splice sites (By similarity). Plays a
CC role in DNA damage response (By similarity).
CC {ECO:0000250|UniProtKB:Q9H7Z3}.
CC -!- SUBUNIT: Interacts with MTREX; the interaction is direct and stabilizes
CC NRDE2 (By similarity). Interacts with EXOSC10, EFTUD2 and EIF4A3 (By
CC similarity). {ECO:0000250|UniProtKB:Q9H7Z3}.
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250|UniProtKB:Q9H7Z3}.
CC Nucleus, nucleolus {ECO:0000250|UniProtKB:Q9H7Z3}. Nucleus, nucleoplasm
CC {ECO:0000250|UniProtKB:Q9H7Z3}. Nucleus {ECO:0000250|UniProtKB:Q9H7Z3}.
CC -!- DOMAIN: The MID/MTR4-interacting domain is necessary and sufficient to
CC mediate interaction with MTREX. {ECO:0000250|UniProtKB:Q9H7Z3}.
CC -!- SIMILARITY: Belongs to the NRDE2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH25577.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH51175.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=BY182441; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; BY182441; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC166349; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC002230; AAH02230.1; -; mRNA.
DR EMBL; BC025577; AAH25577.1; ALT_INIT; mRNA.
DR EMBL; BC051175; AAH51175.1; ALT_SEQ; mRNA.
DR CCDS; CCDS70414.1; -.
DR RefSeq; NP_001277232.1; NM_001290303.1.
DR AlphaFoldDB; Q80XC6; -.
DR BioGRID; 229964; 2.
DR IntAct; Q80XC6; 1.
DR MINT; Q80XC6; -.
DR STRING; 10090.ENSMUSP00000021596; -.
DR iPTMnet; Q80XC6; -.
DR PhosphoSitePlus; Q80XC6; -.
DR EPD; Q80XC6; -.
DR jPOST; Q80XC6; -.
DR MaxQB; Q80XC6; -.
DR PaxDb; Q80XC6; -.
DR PeptideAtlas; Q80XC6; -.
DR PRIDE; Q80XC6; -.
DR ProteomicsDB; 253013; -.
DR Antibodypedia; 26518; 28 antibodies from 12 providers.
DR Ensembl; ENSMUST00000021596; ENSMUSP00000021596; ENSMUSG00000021179.
DR GeneID; 217827; -.
DR KEGG; mmu:217827; -.
DR UCSC; uc007oso.2; mouse.
DR CTD; 55051; -.
DR MGI; MGI:2670969; Nrde2.
DR VEuPathDB; HostDB:ENSMUSG00000021179; -.
DR eggNOG; KOG1972; Eukaryota.
DR GeneTree; ENSGT00390000005524; -.
DR HOGENOM; CLU_007550_1_0_1; -.
DR InParanoid; Q80XC6; -.
DR OMA; VQVEFFE; -.
DR OrthoDB; 833360at2759; -.
DR PhylomeDB; Q80XC6; -.
DR TreeFam; TF323791; -.
DR BioGRID-ORCS; 217827; 9 hits in 67 CRISPR screens.
DR PRO; PR:Q80XC6; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q80XC6; protein.
DR Bgee; ENSMUSG00000021179; Expressed in humerus cartilage element and 252 other tissues.
DR ExpressionAtlas; Q80XC6; baseline and differential.
DR Genevisible; Q80XC6; MM.
DR GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0000278; P:mitotic cell cycle; ISS:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:1902369; P:negative regulation of RNA catabolic process; ISS:UniProtKB.
DR GO; GO:0046833; P:positive regulation of RNA export from nucleus; ISS:UniProtKB.
DR GO; GO:0035194; P:post-transcriptional gene silencing by RNA; IBA:GO_Central.
DR GO; GO:0008380; P:RNA splicing; ISS:UniProtKB.
DR Gene3D; 1.25.40.10; -; 3.
DR InterPro; IPR003107; HAT.
DR InterPro; IPR013633; NRDE-2.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR13471; PTHR13471; 1.
DR Pfam; PF08424; NRDE-2; 1.
DR SMART; SM00386; HAT; 5.
DR SUPFAM; SSF48452; SSF48452; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell cycle; Cell division; Coiled coil; DNA damage; Mitosis;
KW mRNA processing; mRNA splicing; Nucleus; Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9H7Z3"
FT CHAIN 2..1172
FT /note="Nuclear exosome regulator NRDE2"
FT /id="PRO_0000089908"
FT REPEAT 314..346
FT /note="HAT 1"
FT REPEAT 404..436
FT /note="HAT 2"
FT REPEAT 766..800
FT /note="HAT 3"
FT REPEAT 986..1018
FT /note="HAT 4"
FT REPEAT 1075..1109
FT /note="HAT 5"
FT REGION 46..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 171..275
FT /note="MID/MTR4-interacting domain"
FT /evidence="ECO:0000250|UniProtKB:Q9H7Z3"
FT REGION 292..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 78..330
FT /evidence="ECO:0000255"
FT COMPBIAS 85..107
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..139
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9H7Z3"
FT CONFLICT 21..28
FT /note="KELDWLSN -> VKVRLAEH (in Ref. 3; AAH51175)"
FT /evidence="ECO:0000305"
FT CONFLICT 707
FT /note="R -> H (in Ref. 1; AAH25577)"
FT /evidence="ECO:0000305"
FT CONFLICT 741..742
FT /note="LS -> VC (in Ref. 1; AAH25577)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1172 AA; 133467 MW; 060E2A1A0CE5739D CRC64;
MALFPAFADV SEASGDGAFR KELDWLSNPS FRVGNLTSLS RQTEEVTALA SEGSPPPRYS
FIRSPLKSEL SGESNTSEKL AQTSRKKKKE KKKRRKHQHH RKTKRRHEQL SSSGSESDTE
AGKDRASRSI RDDQKEAEKP CQGSNAAAAV AAAAGHRSIW LEDIHDLTDV FRTDKKPDPA
NWEYKSLYRG DIARYKRKGD SCLGINPKKQ CISWEGASAA KKHSHRHLER YFTKKNVGLM
RTEGIAVCSN PEPASSEPVT FIPVKDSAEA ATPVTSWLNP LGIYDQSTTQ WLQGQGPAEQ
ESKQPDSQQD RENAALKARV EEFNRRVREN PWDTQLWMAF VAFQDEVMRS PGIYALGEGE
QEKHRKSLKL LLEKKLAVLE RAIESNPGSV ELKLAKLQLC SEFWEPSALA KEWQKLLFLH
PNNTSLWQRY LSFCQSQFGT FSVSKLHSLY GKCLSTLSAV KDGSMLSHPV LPGTEEAMFG
LFLQQCHFLR QAGHSEKVIS LFQAMVDFTF FKPDSVKELP TKVQVEFFEP FWDSGEPRVG
EKGARGWRAW MHQQERGGWV LITPDEDDEE PEEEDQEIKD KTLPRWQIWL AVERSRDQRH
WRPWRPDKTK KQTEEDCEDP ERQVLFDDIG QSLIRLSSPD LQFQLIQAFL QFLGVPSGFL
PPASCLYLAM DESSIFESEL YDEKPLTYFN PSFSGISCVG SMEQLGRPRW TKGHNREGEE
FVRNVFHLVL PLLAGKQKSQ LSLSWLRYEI AKVIWCLHTK KKRLKSQGKS CKKLAKNLLK
EPENRNNFCL WKQYAHLEWL LGNTEDARKV FDTALSMAGS SELKDRELCE LSLLYAELEM
ELSPDSRGAT TGRAVHILTR LTESSPYGPY TGQVSSTQVL KARKAYELAL QDCLGQSCAS
SPAPAEALDC LGSLVRCFML FQYLTVGIDA AVQIYGRVFA KLKGSARLED PGPEDSTSSQ
SLTNVLEAVS MMHTSLLRFH MNVCVYPLAP LRETLSDALK LYPGNQVLWR AYVQIQNKSH
SANKTRRFFD TVTRSAKHLE PWLFAIEAEK LRKKLVESVQ RVGGREVHAT IPETGLTHRI
RALFENAIRS DKGNQCPLLW RMYLNFLVSL GNKERSKGVF YKALQSCPWA KVLYMDAMEY
FPDELQEILD VMTEKELRVR LPLEELELLL ED
