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-MAR-2024, entry version 139.
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
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 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, ECO:0000269|PubMed:21255825}.
CC   -!- SUBUNIT: Component of the RNA exosome complex. Specifically part of the
CC       catalytically inactive RNA exosome core (Exo-9) complex which is
CC       believed to associate with catalytic subunits EXOSC10, and DIS3 or
CC       DIS3L in cytoplasmic- and nuclear-specific RNA exosome complex forms.
CC       Exo-9 is formed by a hexameric ring of RNase PH domain-containing
CC       subunits specifically containing the heterodimers EXOSC4-EXOSC9,
CC       EXOSC5-EXOSC8 and EXOSC6-EXOSC7, and peripheral S1 domain-containing
CC       components EXOSC1, EXOSC2 and EXOSC3 located on the top of the ring
CC       structure (By similarity). {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; 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   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   EPD; Q8BTW3; -.
DR   MaxQB; Q8BTW3; -.
DR   PeptideAtlas; Q8BTW3; -.
DR   ProteomicsDB; 275792; -.
DR   Pumba; Q8BTW3; -.
DR   Antibodypedia; 29956; 112 antibodies from 16 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); IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
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:0101019; C:nucleolar exosome (RNase complex); NAS:ComplexPortal.
DR   GO; GO:0005730; C:nucleolus; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
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:0006401; P:RNA catabolic process; ISO:MGI.
DR   GO; GO:0006396; P:RNA processing; ISO:MGI.
DR   GO; GO:0016075; P:rRNA catabolic process; IBA:GO_Central.
DR   GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0034475; P:U4 snRNA 3'-end processing; IBA:GO_Central.
DR   CDD; cd11371; RNase_PH_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   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
//