RRP44_MOUSE
ID RRP44_MOUSE Reviewed; 958 AA.
AC Q9CSH3; Q6ZQ07; Q8C074;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 4.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Exosome complex exonuclease RRP44;
DE EC=3.1.13.-;
DE EC=3.1.26.-;
DE AltName: Full=Protein DIS3 homolog;
DE AltName: Full=Ribosomal RNA-processing protein 44;
GN Name=Dis3; Synonyms=Kiaa1008, Rrp44;
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] OF 1-267 AND 272-958.
RC STRAIN=C57BL/6J; TISSUE=Medulla oblongata;
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 MRNA] OF 131-588.
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-215, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen,
RC 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: Putative catalytic component of the RNA exosome complex which
CC has 3'->5' exoribonuclease activity and participates in a multitude of
CC cellular RNA processing and degradation events. In the nucleus, the RNA
CC exosome complex is involved in proper maturation of stable RNA species
CC such as rRNA, snRNA and snoRNA, in the elimination of RNA processing
CC by-products and non-coding 'pervasive' transcripts, such as antisense
CC RNA species and promoter-upstream transcripts (PROMPTs), and of mRNAs
CC with processing defects, thereby limiting or excluding their export to
CC the cytoplasm. The RNA exosome may be involved in Ig class switch
CC recombination (CSR) and/or Ig variable region somatic hypermutation
CC (SHM) by targeting AICDA deamination activity to transcribed dsDNA
CC substrates. In the cytoplasm, the RNA exosome complex is involved in
CC general mRNA turnover and specifically degrades inherently unstable
CC mRNAs containing AU-rich elements (AREs) within their 3' untranslated
CC regions, and in RNA surveillance pathways, preventing translation of
CC aberrant mRNAs. It seems to be involved in degradation of histone mRNA.
CC DIS3 has both 3'-5' exonuclease and endonuclease activities.
CC {ECO:0000250|UniProtKB:Q9Y2L1}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q9Y2L1};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q9Y2L1};
CC -!- SUBUNIT: Component of the RNA exosome complex (By similarity). The
CC catalytically inactive RNA exosome core (Exo-9) complex is believed to
CC associate with catalytic subunits EXOSC10, and DIS3 or DIS3L in
CC cytoplasmic- and nuclear-specific RNA exosome complex forms (By
CC similarity). Interacts with DHX34; the interaction is RNA-independent
CC (By similarity). {ECO:0000250|UniProtKB:Q9Y2L1}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9Y2L1}.
CC Nucleus, nucleolus {ECO:0000250|UniProtKB:Q9Y2L1}. Nucleus, nucleoplasm
CC {ECO:0000250|UniProtKB:Q9Y2L1}. Nucleus {ECO:0000250|UniProtKB:Q9Y2L1}.
CC Note=Predominantly located in the nucleus. According to, found in the
CC nucleolus. According to, excluded from nucleolus supporting the
CC existence of a nucleolar RNA exosome complex devoid of DIS3.
CC {ECO:0000250|UniProtKB:Q9Y2L1}.
CC -!- SIMILARITY: Belongs to the RNR ribonuclease family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC98069.1; Type=Miscellaneous discrepancy; Note=Incompletely spliced mRNA.; Evidence={ECO:0000305};
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DR EMBL; AK012840; BAB28503.3; -; mRNA.
DR EMBL; AK032091; BAC27692.1; -; mRNA.
DR EMBL; AK129259; BAC98069.1; ALT_SEQ; Transcribed_RNA.
DR CCDS; CCDS49555.1; -.
DR RefSeq; NP_082591.2; NM_028315.2.
DR AlphaFoldDB; Q9CSH3; -.
DR SMR; Q9CSH3; -.
DR BioGRID; 215499; 16.
DR ComplexPortal; CPX-594; Nuclear exosome complex, Dis3-Exosc10 variant.
DR ComplexPortal; CPX-598; Exosome complex, Dis3 variant.
DR IntAct; Q9CSH3; 2.
DR MINT; Q9CSH3; -.
DR STRING; 10090.ENSMUSP00000041906; -.
DR iPTMnet; Q9CSH3; -.
DR PhosphoSitePlus; Q9CSH3; -.
DR SwissPalm; Q9CSH3; -.
DR EPD; Q9CSH3; -.
DR MaxQB; Q9CSH3; -.
DR PaxDb; Q9CSH3; -.
DR PeptideAtlas; Q9CSH3; -.
DR PRIDE; Q9CSH3; -.
DR ProteomicsDB; 260843; -.
DR Antibodypedia; 24401; 229 antibodies from 30 providers.
DR DNASU; 72662; -.
DR Ensembl; ENSMUST00000042471; ENSMUSP00000041906; ENSMUSG00000033166.
DR GeneID; 72662; -.
DR KEGG; mmu:72662; -.
DR UCSC; uc007uuw.1; mouse.
DR CTD; 22894; -.
DR MGI; MGI:1919912; Dis3.
DR VEuPathDB; HostDB:ENSMUSG00000033166; -.
DR eggNOG; KOG2102; Eukaryota.
DR GeneTree; ENSGT00530000063106; -.
DR HOGENOM; CLU_002333_5_0_1; -.
DR InParanoid; Q9CSH3; -.
DR OMA; VVKRNWR; -.
DR OrthoDB; 1104619at2759; -.
DR PhylomeDB; Q9CSH3; -.
DR TreeFam; TF105755; -.
DR Reactome; R-MMU-429958; mRNA decay by 3' to 5' exoribonuclease.
DR Reactome; R-MMU-450385; Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA.
DR Reactome; R-MMU-450513; Tristetraprolin (TTP, ZFP36) binds and destabilizes mRNA.
DR Reactome; R-MMU-450604; KSRP (KHSRP) binds and destabilizes mRNA.
DR Reactome; R-MMU-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR BioGRID-ORCS; 72662; 26 hits in 76 CRISPR screens.
DR ChiTaRS; Dis3; mouse.
DR PRO; PR:Q9CSH3; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q9CSH3; protein.
DR Bgee; ENSMUSG00000033166; Expressed in primitive streak and 233 other tissues.
DR ExpressionAtlas; Q9CSH3; baseline and differential.
DR Genevisible; Q9CSH3; MM.
DR GO; GO:0000177; C:cytoplasmic exosome (RNase complex); IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0000178; C:exosome (RNase complex); IBA:GO_Central.
DR GO; GO:0000176; C:nuclear exosome (RNase complex); ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0000175; F:3'-5'-exoribonuclease activity; ISS:UniProtKB.
DR GO; GO:0004519; F:endonuclease activity; ISS:UniProtKB.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0071034; P:CUT catabolic process; ISO:MGI.
DR GO; GO:0006401; P:RNA catabolic process; ISO:MGI.
DR GO; GO:0006396; P:RNA processing; ISO:MGI.
DR GO; GO:0016075; P:rRNA catabolic process; ISO:MGI.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR Gene3D; 2.40.50.140; -; 1.
DR InterPro; IPR041505; Dis3_CSD2.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR029060; PIN-like_dom_sf.
DR InterPro; IPR002716; PIN_dom.
DR InterPro; IPR001900; RNase_II/R.
DR InterPro; IPR022966; RNase_II/R_CS.
DR InterPro; IPR033771; Rrp44_CSD1.
DR InterPro; IPR033770; RRP44_S1.
DR Pfam; PF17849; OB_Dis3; 1.
DR Pfam; PF13638; PIN_4; 1.
DR Pfam; PF00773; RNB; 1.
DR Pfam; PF17216; Rrp44_CSD1; 1.
DR Pfam; PF17215; Rrp44_S1; 1.
DR SMART; SM00670; PINc; 1.
DR SMART; SM00955; RNB; 1.
DR SUPFAM; SSF50249; SSF50249; 3.
DR SUPFAM; SSF88723; SSF88723; 1.
DR PROSITE; PS01175; RIBONUCLEASE_II; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Endonuclease; Exonuclease; Exosome; Hydrolase;
KW Magnesium; Manganese; Nuclease; Nucleus; Phosphoprotein;
KW Reference proteome; RNA-binding; rRNA processing.
FT CHAIN 1..958
FT /note="Exosome complex exonuclease RRP44"
FT /id="PRO_0000314757"
FT DOMAIN 64..182
FT /note="PINc"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2L1"
FT MOD_RES 18
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2L1"
FT MOD_RES 215
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 586..588
FT /note="ASL -> VSV (in Ref. 2; BAC98069)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 958 AA; 108838 MW; 31045737557AB4AE CRC64;
MLRSKTFLKK TRAGGVVKIV REHYLRDDIG CGAPACSACG GAHAGPALEL QPRDQASSLC
PWPHYLLPDT NVLLHQIDVL EHPAIRNVIV LQTVMQEVRN RSAPIYKRIR DVTNNQEKHF
YTFTNEHHKE TYIEQEQGEN ANDRNDRAIR VAAKWYNEHL KRVAADSQLQ VILITNDRKN
KEKAVQEGIP AFTCEEYVKS LTANPELIDR LAYLSDEMNE IESGKIIFSE HLPLSKLQQG
IKSGSYLQGT FRASRENYLE ATVWIHGDKE EEKEILIQGI KHLNRAVHED IVAVELLPRS
QWVAPSSVVL DDEGQNEDDV EKDEERELLL KTAVSEKMLR PTGRVVGIIK RNWRPYCGML
SKSDIKESRR HLFTPADKRI PRIRIETRQA SALEGRRIIV AIDGWPRNSR YPNGHFVKNL
GDVGEKETET EVLLLEHDVP HQPFSQAVLS FLPRMPWSIT EEDMKNREDL RHLCVCSVDP
PGCTDIDDAL HCRELSNGNL EVGVHIADVS HFIRPGNALD QESARRGTTV YLCEKRIDMV
PELLSSNLCS LRSNVDRLAF SCIWEMNHNA EILKTRFTKS VINSKASLTY AEAQMRIDSA
AMNDDITTSL RGLNQLAKIL KKGRIEKGAL TLSSPEIRFH MDSETHDPID LQTKELRETN
SMVEEFMLLA NISVAKKIHE EFSEHALLRK HPAPPPSNYD ILVKAAKSKN LQIKTDTAKS
LADSLDRAES PDFPYLNTLL RILATRCMMQ AVYFCSGMDN DFHHYGLASP IYTHFTSPIR
RYADIIVHRL LAVAIGADCT YPELTDKHKL SDICKNLNFR HKMAQYAQRA SVAFHTQLFF
KSKGIVSEEA YILFVRKNAI VVLIPKYGLE GTVFFEEKDK PKPRLAYDDE IPSLRIEGTV
FHVFDKVKVK ITLDSSNLQH QKIRMALVEP QIPGINIPPN VADKALTAPG GKKRKLEK
