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   15-FEB-2017, entry version 102.
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   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, Spleen, and
RC   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
RT   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
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       ECO:0000269|PubMed:21255825}.
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};
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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   UniGene; Mm.24174; -.
DR   UniGene; Mm.334810; -.
DR   ProteinModelPortal; Q8BTW3; -.
DR   SMR; Q8BTW3; -.
DR   BioGrid; 215428; 1.
DR   IntAct; Q8BTW3; 3.
DR   PhosphoSitePlus; Q8BTW3; -.
DR   EPD; Q8BTW3; -.
DR   MaxQB; Q8BTW3; -.
DR   PeptideAtlas; Q8BTW3; -.
DR   PRIDE; Q8BTW3; -.
DR   Ensembl; ENSMUST00000210390; ENSMUSP00000147696; ENSMUSG00000109941.
DR   GeneID; 72544; -.
DR   KEGG; mmu:72544; -.
DR   UCSC; uc009nlp.2; mouse.
DR   CTD; 118460; -.
DR   MGI; MGI:1919794; Exosc6.
DR   GeneTree; ENSGT00550000074804; -.
DR   HOGENOM; HOG000229515; -.
DR   HOVERGEN; HBG057826; -.
DR   InParanoid; Q8BTW3; -.
DR   KO; K12587; -.
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-450604; KSRP (KHSRP) binds and destabilizes mRNA.
DR   Reactome; R-MMU-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR   PRO; PR:Q8BTW3; -.
DR   Proteomes; UP000000589; Chromosome 8.
DR   CleanEx; MM_EXOSC6; -.
DR   GO; GO:0000177; C:cytoplasmic exosome (RNase complex); IBA:GO_Central.
DR   GO; GO:0000178; C:exosome (RNase complex); ISS:UniProtKB.
DR   GO; GO:0000176; C:nuclear exosome (RNase complex); IBA:GO_Central.
DR   GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR   GO; GO:0044822; F:poly(A) RNA binding; ISO:MGI.
DR   GO; GO:0045006; P:DNA deamination; ISO:MGI.
DR   GO; GO:0045190; P:isotype switching; IMP:UniProtKB.
DR   GO; GO:0071028; P:nuclear mRNA surveillance; IBA:GO_Central.
DR   GO; GO:0034427; P:nuclear-transcribed mRNA catabolic process, exonucleolytic, 3'-5'; IBA:GO_Central.
DR   GO; GO:0071051; P:polyadenylation-dependent snoRNA 3'-end processing; IBA:GO_Central.
DR   GO; GO:0045830; P:positive regulation of isotype switching; IMP:MGI.
DR   GO; GO:0031125; P:rRNA 3'-end processing; IBA:GO_Central.
DR   GO; GO:0016075; P:rRNA catabolic process; IBA:GO_Central.
DR   GO; GO:0034475; P:U4 snRNA 3'-end processing; IBA:GO_Central.
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
//