ID   EXOS8_MOUSE             Reviewed;         276 AA.
AC   Q9D753;
DT   11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   27-MAR-2024, entry version 155.
DE   RecName: Full=Exosome complex component RRP43;
DE   AltName: Full=Exosome component 8;
DE   AltName: Full=Ribosomal RNA-processing protein 43;
GN   Name=Exosc8; Synonyms=Rrp43;
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; TISSUE=Tongue;
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   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Kidney, Liver, 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).
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. EXOSC8
CC       binds to ARE-containing RNAs (By similarity). {ECO:0000250}.
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   -!- INTERACTION:
CC       Q9D753; Q8K4E0: Alms1; NbExp=3; IntAct=EBI-8387079, EBI-6272972;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus, nucleolus
CC       {ECO:0000250}. Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the RNase PH family. {ECO:0000305}.
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DR   EMBL; AK009584; -; NOT_ANNOTATED_CDS; mRNA.
DR   CCDS; CCDS17352.1; -.
DR   RefSeq; NP_081424.3; NM_027148.3.
DR   AlphaFoldDB; Q9D753; -.
DR   SMR; Q9D753; -.
DR   BioGRID; 213583; 7.
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; Q9D753; 1.
DR   MINT; Q9D753; -.
DR   STRING; 10090.ENSMUSP00000029316; -.
DR   PhosphoSitePlus; Q9D753; -.
DR   EPD; Q9D753; -.
DR   MaxQB; Q9D753; -.
DR   PaxDb; 10090-ENSMUSP00000029316; -.
DR   ProteomicsDB; 267676; -.
DR   Pumba; Q9D753; -.
DR   Antibodypedia; 23142; 169 antibodies from 27 providers.
DR   DNASU; 69639; -.
DR   Ensembl; ENSMUST00000029316.16; ENSMUSP00000029316.10; ENSMUSG00000027752.16.
DR   GeneID; 69639; -.
DR   KEGG; mmu:69639; -.
DR   UCSC; uc008pfq.2; mouse.
DR   AGR; MGI:1916889; -.
DR   CTD; 11340; -.
DR   MGI; MGI:1916889; Exosc8.
DR   VEuPathDB; HostDB:ENSMUSG00000027752; -.
DR   eggNOG; KOG1613; Eukaryota.
DR   GeneTree; ENSGT00950000183130; -.
DR   HOGENOM; CLU_038194_3_1_1; -.
DR   InParanoid; Q9D753; -.
DR   OMA; RIWYQPP; -.
DR   OrthoDB; 21598at2759; -.
DR   PhylomeDB; Q9D753; -.
DR   TreeFam; TF320415; -.
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; 69639; 27 hits in 79 CRISPR screens.
DR   ChiTaRS; Exosc8; mouse.
DR   PRO; PR:Q9D753; -.
DR   Proteomes; UP000000589; Chromosome 3.
DR   RNAct; Q9D753; Protein.
DR   Bgee; ENSMUSG00000027752; Expressed in yolk sac and 246 other cell types or tissues.
DR   ExpressionAtlas; Q9D753; baseline and differential.
DR   GO; GO:0005694; C:chromosome; ISO:MGI.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
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:0001650; C:fibrillar center; ISO:MGI.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
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:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0035925; F:mRNA 3'-UTR AU-rich region binding; ISO:MGI.
DR   GO; GO:0043928; P:exonucleolytic catabolism of deadenylated mRNA; IBA:GO_Central.
DR   GO; GO:0000467; P:exonucleolytic trimming to generate mature 3'-end of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR   GO; GO:0071028; P:nuclear mRNA surveillance; IBA:GO_Central.
DR   GO; GO:0071042; P:nuclear polyadenylation-dependent mRNA catabolic process; IBA:GO_Central.
DR   GO; GO:0071035; P:nuclear polyadenylation-dependent rRNA catabolic process; IBA:GO_Central.
DR   GO; GO:0071038; P:nuclear polyadenylation-dependent tRNA catabolic process; IBA:GO_Central.
DR   GO; GO:0034427; P:nuclear-transcribed mRNA catabolic process, exonucleolytic, 3'-5'; IBA:GO_Central.
DR   GO; GO:0006401; P:RNA catabolic process; ISO:MGI.
DR   GO; GO:0006396; P:RNA processing; ISO:MGI.
DR   GO; GO:0034473; P:U1 snRNA 3'-end processing; IBA:GO_Central.
DR   GO; GO:0034475; P:U4 snRNA 3'-end processing; IBA:GO_Central.
DR   GO; GO:0034476; P:U5 snRNA 3'-end processing; IBA:GO_Central.
DR   CDD; cd11369; RNase_PH_RRP43; 1.
DR   Gene3D; 3.30.230.70; GHMP Kinase, N-terminal domain; 1.
DR   InterPro; IPR001247; ExoRNase_PH_dom1.
DR   InterPro; IPR015847; ExoRNase_PH_dom2.
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; IPR033196; Rrp43.
DR   PANTHER; PTHR11097:SF9; EXOSOME COMPLEX COMPONENT RRP43; 1.
DR   PANTHER; PTHR11097; EXOSOME COMPLEX EXONUCLEASE RIBOSOMAL RNA PROCESSING PROTEIN; 1.
DR   Pfam; PF01138; RNase_PH; 1.
DR   Pfam; PF03725; RNase_PH_C; 1.
DR   SUPFAM; SSF55666; Ribonuclease PH domain 2-like; 1.
DR   SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR   Genevisible; Q9D753; MM.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Exosome; Nucleus; Reference proteome; RNA-binding;
KW   rRNA processing.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q96B26"
FT   CHAIN           2..276
FT                   /note="Exosome complex component RRP43"
FT                   /id="PRO_0000139968"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96B26"
SQ   SEQUENCE   276 AA;  29949 MW;  297E1E45F5C0F794 CRC64;
     MAAGFKTVEP LEYYRRFLKE NCRPDGRELG EFRATTVNIG SISTADGSAL VKLGNTTVIC
     GVKAEFAAPP VDAPDRGYVV PNVDLPPLCS SRFRTGPPGE EAQVTSQFIA DVVDNSQVIK
     KEDLCISPGK LAWVLYCDLI CLDYDGNILD ACTFALLAAL KNVQLPEVTI NEETALAEVN
     LKKKSYLNVR TNPVATSFAV FDDTLLIVDP TGEEEHLSTG TLTVVTDEDG KLCCLHKPGG
     SGLTGAKLQD CMSRAVTRHK EVSKLLDEVI QSMRHK
//