ID EXOS6_MOUSE Reviewed; 273 AA. AC Q8BTW3; Q9CSR7; DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 27-NOV-2024, entry version 143. DE RecName: Full=Exosome complex component MTR3; DE AltName: Full=Exosome component 6; DE AltName: Full=mRNA transport regulator 3 homolog; GN Name=Exosc6; Synonyms=Mtr3; 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]. RC STRAIN=C57BL/6J, and NOD; TISSUE=Thymus; 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]. RC TISSUE=Brain; 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 [3] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, 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). RN [4] RP FUNCTION IN IG CLASS-SWITCH RECOMBINATION. RX PubMed=21255825; DOI=10.1016/j.cell.2011.01.001; RA Basu U., Meng F.L., Keim C., Grinstein V., Pefanis E., Eccleston J., RA Zhang T., Myers D., Wasserman C.R., Wesemann D.R., Januszyk K., RA Gregory R.I., Deng H., Lima C.D., Alt F.W.; RT "The RNA exosome targets the AID cytidine deaminase to both strands of RT transcribed duplex DNA substrates."; RL Cell 144:353-363(2011). CC -!- FUNCTION: Non-catalytic component of the RNA exosome complex which has CC 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 The catalytic inactive RNA exosome core complex of 9 subunits (Exo-9) CC is proposed to play a pivotal role in the binding and presentation of CC RNA for ribonucleolysis, and to serve as a scaffold for the association CC with catalytic subunits and accessory proteins or complexes (By CC similarity). {ECO:0000250|UniProtKB:Q5RKV6, CC ECO:0000269|PubMed:21255825}. CC -!- SUBUNIT: Component of the RNA exosome core complex (Exo-9), composed of CC EXOSC1, EXOSC2, EXOSC3, EXOSC4, EXOSC5, EXOSC6, EXOSC7, EXOSC8 and CC EXOSC9; within the complex interacts with EXOSC1, EXOSC7 and EXOSC8 (By CC similarity). The catalytically inactive RNA exosome core complex (Exo- CC 9) associates with the catalytic subunit EXOSC10/RRP6 (By similarity). CC Exo-9 may associate with DIS3 to form the nucleolar exosome complex, or CC DIS3L to form the cytoplasmic exosome complex (By similarity). Exo-9 is CC formed by a hexameric base ring consisting of the heterodimers EXOSC4- CC EXOSC9, EXOSC5-EXOSC8 and EXOSC6-EXOSC7, and a cap ring consisting of CC EXOSC1, EXOSC2 and EXOSC3 (By similarity). The RNA exosome complex CC associates with cofactors EXOSC10/RRP6, C1D/RRP47, MPHOSPH6/MPP6 and CC MTREX/MTR4 (By similarity). {ECO:0000250|UniProtKB:Q5RKV6}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus, nucleolus CC {ECO:0000250}. Nucleus {ECO:0000250}. CC -!- SIMILARITY: Belongs to the RNase PH family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAB28033.1; Type=Frameshift; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AK012102; BAB28033.1; ALT_FRAME; mRNA. DR EMBL; AK088532; BAC40407.1; -; mRNA. DR EMBL; BC116985; AAI16986.1; -; mRNA. DR EMBL; BC119082; AAI19083.1; -; mRNA. DR CCDS; CCDS85611.1; -. DR RefSeq; NP_082550.1; NM_028274.4. DR AlphaFoldDB; Q8BTW3; -. DR SMR; Q8BTW3; -. DR BioGRID; 215428; 5. DR ComplexPortal; CPX-594; Nuclear exosome complex, Dis3-Exosc10 variant. DR ComplexPortal; CPX-595; Nucleolar exosome complex, Exosc10 variant. DR ComplexPortal; CPX-596; Cytoplasmic exosome complex, Dis3l variant. DR ComplexPortal; CPX-598; Exosome complex, Dis3 variant. DR ComplexPortal; CPX-601; Cytoplasmic exosome complex, Dis3l-Exosc10 variant. DR IntAct; Q8BTW3; 4. DR MINT; Q8BTW3; -. DR STRING; 10090.ENSMUSP00000147696; -. DR PhosphoSitePlus; Q8BTW3; -. DR SwissPalm; Q8BTW3; -. DR PeptideAtlas; Q8BTW3; -. DR ProteomicsDB; 275792; -. DR Pumba; Q8BTW3; -. DR Antibodypedia; 29956; 90 antibodies from 15 providers. DR DNASU; 72544; -. DR Ensembl; ENSMUST00000210390.2; ENSMUSP00000147696.2; ENSMUSG00000109941.2. DR GeneID; 72544; -. DR KEGG; mmu:72544; -. DR UCSC; uc009nlp.2; mouse. DR AGR; MGI:1919794; -. DR CTD; 118460; -. DR MGI; MGI:1919794; Exosc6. DR VEuPathDB; HostDB:ENSMUSG00000109941; -. DR GeneTree; ENSGT00940000153348; -. DR InParanoid; Q8BTW3; -. DR OMA; KLMCCVY; -. DR OrthoDB; 4642487at2759; -. DR PhylomeDB; Q8BTW3; -. DR BRENDA; 1.8.1.9; 3474. 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; 72544; 8 hits in 54 CRISPR screens. DR ChiTaRS; Exosc6; mouse. DR PRO; PR:Q8BTW3; -. DR Proteomes; UP000000589; Chromosome 8. DR RNAct; Q8BTW3; protein. DR Bgee; ENSMUSG00000109941; Expressed in mesodermal cell in embryo and 50 other cell types or tissues. DR GO; GO:0000177; C:cytoplasmic exosome (RNase complex); NAS:ComplexPortal. DR GO; GO:0005829; C:cytosol; ISO:ComplexPortal. DR GO; GO:0000178; C:exosome (RNase complex); ISS:UniProtKB. DR GO; GO:0000176; C:nuclear exosome (RNase complex); NAS:ComplexPortal. DR GO; GO:0101019; C:nucleolar exosome (RNase complex); NAS:ComplexPortal. DR GO; GO:0005730; C:nucleolus; ISO:ComplexPortal. DR GO; GO:0005634; C:nucleus; ISO:ComplexPortal. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. DR GO; GO:0045006; P:DNA deamination; IEA:Ensembl. DR GO; GO:0045190; P:isotype switching; IMP:UniProtKB. DR GO; GO:0045830; P:positive regulation of isotype switching; IMP:MGI. DR GO; GO:0006401; P:RNA catabolic process; ISO:ComplexPortal. DR GO; GO:0006396; P:RNA processing; ISO:ComplexPortal. DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW. DR CDD; cd11371; RNase_PH_MTR3; 1. DR FunFam; 3.30.230.70:FF:000023; exosome complex component MTR3; 1. DR Gene3D; 3.30.230.70; GHMP Kinase, N-terminal domain; 1. DR InterPro; IPR001247; ExoRNase_PH_dom1. DR InterPro; IPR036345; ExoRNase_PH_dom2_sf. DR InterPro; IPR027408; PNPase/RNase_PH_dom_sf. DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF. DR InterPro; IPR050080; RNase_PH. DR PANTHER; PTHR11953; EXOSOME COMPLEX COMPONENT; 1. DR PANTHER; PTHR11953:SF2; EXOSOME COMPLEX COMPONENT MTR3; 1. DR Pfam; PF01138; RNase_PH; 1. DR SUPFAM; SSF55666; Ribonuclease PH domain 2-like; 1. DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1. PE 1: Evidence at protein level; KW Cytoplasm; Exosome; Nucleus; Reference proteome; RNA-binding; KW rRNA processing. FT CHAIN 1..273 FT /note="Exosome complex component MTR3" FT /id="PRO_0000287479" FT REGION 1..36 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 273 AA; 28370 MW; 6AC4310F46742B10 CRC64; MPGDHRRIRG PEESQPPQLY AAEDDETPAA RDPTRLRPVY ARAGLLSQAK GSAYLEAGGT KVLCAVSGPR QAEGGERGSG PAGAGGEAPA ALRGRLLCDF RRAPFSGRRR RAPQGGGGED RELGLALQEA LEPAVRLGRY PRAQLEVSAL LLEDGGCALA AALTAAALAL ADAGVEMYDL VVGCGLSLTP GPSPTWLLDP TRLEEEHSAA GLTVALMPVL NQVAGLLGSG EGGQTESWTD AVRLGLEGCQ RLYPVLQQCL VRAARRRGAA APP //