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 29-OCT-2014, entry version 85. 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; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; 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., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA 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., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] 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 CC has 3'->5' exoribonuclease activity and participates in a CC multitude of cellular RNA processing and degradation events. In CC the nucleus, the RNA exosome complex is involved in proper CC maturation of stable RNA species such as rRNA, snRNA and snoRNA, CC in the elimination of RNA processing by-products and non-coding CC 'pervasive' transcripts, such as antisense RNA species and CC promoter-upstream transcripts (PROMPTs), and of mRNAs with CC 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 CC hypermutation (SHM) by targeting AICDA deamination activity to CC transcribed dsDNA substrates. In the cytoplasm, the RNA exosome CC complex is involved in general mRNA turnover and specifically CC degrades inherently unstable mRNAs containing AU-rich elements CC (AREs) within their 3' untranslated regions, and in RNA CC surveillance pathways, preventing translation of aberrant mRNAs. CC It seems to be involved in degradation of histone mRNA. The CC catalytic inactive RNA exosome core complex of 9 subunits (Exo-9) CC is proposed to play a pivotal role in the binding and presentation CC of RNA for ribonucleolysis, and to serve as a scaffold for the CC association with catalytic subunits and accessory proteins or CC complexes (By similarity). {ECO:0000250}. CC -!- SUBUNIT: Component of the RNA exosome complex. Specifically part CC of the catalytically inactive RNA exosome core (Exo-9) complex CC which is believed to associate with catalytic subunits EXOSC10, CC and DIS3 or DIS3L in cytoplasmic- and nuclear-specific RNA exosome CC complex forms. Exo-9 is formed by a hexameric ring of RNase PH CC domain-containing subunits specifically containing the CC heterodimers EXOSC4-EXOSC9, EXOSC5-EXOSC8 and EXOSC6-EXOSC7, and CC peripheral S1 domain-containing components EXOSC1, EXOSC2 and CC EXOSC3 located on the top of the ring structure (By similarity). CC {ECO:0000250}. 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; Positions=79; 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 RefSeq; NP_082550.1; NM_028274.4. DR UniGene; Mm.24174; -. DR UniGene; Mm.334810; -. DR ProteinModelPortal; Q8BTW3; -. DR SMR; Q8BTW3; 29-261. DR BioGrid; 215428; 1. DR IntAct; Q8BTW3; 3. DR STRING; 10090.ENSMUSP00000111863; -. DR PhosphoSite; Q8BTW3; -. DR MaxQB; Q8BTW3; -. DR PaxDb; Q8BTW3; -. DR PRIDE; Q8BTW3; -. DR GeneID; 72544; -. DR KEGG; mmu:72544; -. DR UCSC; uc009nlp.1; mouse. DR CTD; 118460; -. DR MGI; MGI:1919794; Exosc6. DR eggNOG; COG0689; -. DR HOGENOM; HOG000229515; -. DR HOVERGEN; HBG057826; -. DR InParanoid; Q8BTW3; -. DR KO; K12587; -. DR PhylomeDB; Q8BTW3; -. DR NextBio; 336459; -. DR PRO; PR:Q8BTW3; -. DR CleanEx; MM_EXOSC6; -. DR Genevestigator; Q8BTW3; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW. DR GO; GO:0000178; C:exosome (RNase complex); ISS:UniProtKB. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. DR GO; GO:0045190; P:isotype switching; IMP:UniProtKB. DR GO; GO:0045830; P:positive regulation of isotype switching; IMP:MGI. DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW. DR Gene3D; 3.30.230.70; -; 1. DR InterPro; IPR001247; ExoRNase_PH_dom1. DR InterPro; IPR015847; ExoRNase_PH_dom2. DR InterPro; IPR027408; PNPase/RNase_PH_dom. DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold. DR Pfam; PF01138; RNase_PH; 1. DR SUPFAM; SSF54211; SSF54211; 1. DR SUPFAM; SSF55666; SSF55666; 1. PE 1: Evidence at protein level; KW Complete proteome; Cytoplasm; Exosome; Nucleus; Reference proteome; KW RNA-binding; rRNA processing. FT CHAIN 1 273 Exosome complex component MTR3. FT /FTId=PRO_0000287479. 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 //