EXOS9_MOUSE
ID EXOS9_MOUSE Reviewed; 438 AA.
AC Q9JHI7; Q9CSZ2;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Exosome complex component RRP45;
DE AltName: Full=Autoantigen PM/Scl 1;
DE AltName: Full=Exosome component 9;
DE AltName: Full=P75 polymyositis-scleroderma overlap syndrome-associated autoantigen;
DE AltName: Full=Polymyositis/scleroderma autoantigen 1;
DE AltName: Full=Polymyositis/scleroderma autoantigen 75 kDa;
DE Short=PM/Scl-75;
GN Name=Exosc9; Synonyms=Pmscl1;
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 [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Brain, and Spleen;
RX PubMed=10708524; DOI=10.1006/geno.2000.6118;
RA Bliskovski V., Liddell R., Ramsay E.S., Miller M.J., Mock B.A.;
RT "Structure and localization of mouse Pmscl1 and Pmscl2 genes.";
RL Genomics 64:106-110(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo, and Mammary gland;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-395.
RC STRAIN=C57BL/6J; TISSUE=Embryo;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-393 AND SER-395, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, 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. EXOSC9
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. Interacts (via C-terminus region) with SETX (via N-terminus
CC domain); the interaction enhances SETX sumoylation (By similarity).
CC {ECO:0000250|UniProtKB:Q06265}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:Q06265}. Nucleus {ECO:0000250|UniProtKB:Q06265}.
CC Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q06265}. Note=Colocalizes
CC with SETX in nuclear foci upon induction of transcription-related DNA
CC damage at the S phase (By similarity). {ECO:0000250|UniProtKB:Q06265}.
CC -!- SIMILARITY: Belongs to the RNase PH family. {ECO:0000305}.
CC -!- CAUTION: The six exosome core subunits containing a RNase PH-domain are
CC not phosphorolytically active. {ECO:0000305}.
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DR EMBL; AF152841; AAF73218.1; -; mRNA.
DR EMBL; AF152842; AAF73219.1; -; mRNA.
DR EMBL; BC005622; AAH05622.1; -; mRNA.
DR EMBL; BC052156; AAH52156.1; -; mRNA.
DR EMBL; AK011636; BAB27749.1; -; mRNA.
DR CCDS; CCDS17312.1; -.
DR RefSeq; NP_062266.1; NM_019393.2.
DR AlphaFoldDB; Q9JHI7; -.
DR SMR; Q9JHI7; -.
DR BioGRID; 206150; 13.
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; Q9JHI7; 1.
DR STRING; 10090.ENSMUSP00000029269; -.
DR iPTMnet; Q9JHI7; -.
DR PhosphoSitePlus; Q9JHI7; -.
DR EPD; Q9JHI7; -.
DR MaxQB; Q9JHI7; -.
DR PaxDb; Q9JHI7; -.
DR PeptideAtlas; Q9JHI7; -.
DR PRIDE; Q9JHI7; -.
DR ProteomicsDB; 275793; -.
DR Antibodypedia; 26749; 150 antibodies from 28 providers.
DR DNASU; 50911; -.
DR Ensembl; ENSMUST00000029269; ENSMUSP00000029269; ENSMUSG00000027714.
DR GeneID; 50911; -.
DR KEGG; mmu:50911; -.
DR UCSC; uc008ozm.1; mouse.
DR CTD; 5393; -.
DR MGI; MGI:1355319; Exosc9.
DR VEuPathDB; HostDB:ENSMUSG00000027714; -.
DR eggNOG; KOG1614; Eukaryota.
DR GeneTree; ENSGT00950000183130; -.
DR HOGENOM; CLU_038194_7_0_1; -.
DR InParanoid; Q9JHI7; -.
DR OMA; CQIAKYG; -.
DR OrthoDB; 996662at2759; -.
DR PhylomeDB; Q9JHI7; -.
DR TreeFam; TF300092; -.
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; 50911; 25 hits in 71 CRISPR screens.
DR ChiTaRS; Exosc9; mouse.
DR PRO; PR:Q9JHI7; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q9JHI7; protein.
DR Bgee; ENSMUSG00000027714; Expressed in ear vesicle and 239 other tissues.
DR ExpressionAtlas; Q9JHI7; baseline and differential.
DR Genevisible; Q9JHI7; MM.
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:0000228; C:nuclear chromosome; ISS:UniProtKB.
DR GO; GO:0000176; C:nuclear exosome (RNase complex); ISO:MGI.
DR GO; GO:0101019; C:nucleolar exosome (RNase complex); IC:ComplexPortal.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0035925; F:mRNA 3'-UTR AU-rich region binding; ISO:MGI.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0043928; P:exonucleolytic catabolism of deadenylated mRNA; ISO:MGI.
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; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0071038; P:nuclear polyadenylation-dependent tRNA catabolic process; IBA:GO_Central.
DR GO; GO:0000956; P:nuclear-transcribed mRNA catabolic process; ISO:MGI.
DR GO; GO:0034427; P:nuclear-transcribed mRNA catabolic process, exonucleolytic, 3'-5'; IBA:GO_Central.
DR GO; GO:0030307; P:positive regulation of cell growth; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO: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: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; cd11368; RNase_PH_RRP45; 1.
DR Gene3D; 3.30.230.70; -; 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_S5_D2-typ_fold.
DR InterPro; IPR033100; Rrp45.
DR Pfam; PF01138; RNase_PH; 1.
DR Pfam; PF03725; RNase_PH_C; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF55666; SSF55666; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Exosome; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; RNA-binding; rRNA processing; Ubl conjugation.
FT CHAIN 1..438
FT /note="Exosome complex component RRP45"
FT /id="PRO_0000139972"
FT REGION 337..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 377..438
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..365
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 65
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q06265"
FT MOD_RES 297
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q06265"
FT MOD_RES 306
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q06265"
FT MOD_RES 346
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q06265"
FT MOD_RES 393
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 395
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CROSSLNK 297
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q06265"
FT CROSSLNK 297
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q06265"
SQ SEQUENCE 438 AA; 48937 MW; 7AAE63DBF12F5149 CRC64;
MKETPLSNCE RRFLLRAIEE KKRLDGRQTY DYRNIRISFG TDYGCCIVEL GKTRVLGQVS
CELVSPKLNR ATEGILFFNL ELSQMAAPAF EPGRQSDLLV KLNRLLERCL RNSKCIDTES
LCVVAGEKVW QIRVDLHLLN HDGNIIDAAS IAAIVALCHF RRPDVSVQGE EVTLYTPEER
DPVPLSIHHM PICVSFAFFQ QGTYLLVDPN EREERVMDGL LVIAMNKHRE ICTIQSSGGI
MLLKDQVFRC SKIAGVKVAE ITELIQKALE NDQRVRKEGG KFGFAESIAN QRITAFKMET
APIDTSNIEE RAEEIIAEAE PPPEVVSQPV LWTPGTAQIG DGIENSWGDL EDSEKEEEEE
EGGIDEAVIL DDTKMDTGEV SDIGSQGAPI VLSDSEEEEM IILEPEKNPK KIRAQTSANQ
KAPSKGQGKR KKKKRTAN
