EXOSX_MOUSE
ID EXOSX_MOUSE Reviewed; 887 AA.
AC P56960; B1ARY9; Q9QYS8; Q9R0B1;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Exosome component 10;
DE EC=3.1.13.-;
DE AltName: Full=Autoantigen PM/Scl 2 homolog;
DE AltName: Full=Polymyositis/scleroderma autoantigen 2 homolog;
GN Name=Exosc10; Synonyms=Pmscl2;
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 [GENOMIC DNA / MRNA].
RC STRAIN=129/SvJ, and BALB/cJ;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP PROTEIN SEQUENCE OF 395-400, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, 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: Putative catalytic component of the RNA exosome complex which
CC has 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 EXOSC10 has 3'-5' exonuclease activity (By similarity). EXOSC10 is
CC required for nucleolar localization of C1D and probably mediates the
CC association of MTREX, C1D and MPHOSPH6 with the RNA exosome involved in
CC the maturation of 5.8S rRNA (By similarity).
CC {ECO:0000250|UniProtKB:Q01780}.
CC -!- SUBUNIT: Component of the RNA exosome complex. The catalytically
CC inactive RNA exosome core (Exo-9) complex is believed to associate with
CC catalytic subunits EXOSC10, and DIS3 or DIS3L in cytoplasmic- and
CC nuclear-specific RNA exosome complex forms. Interacts with C1D and
CC MPHOSPH6 (By similarity). Interacts with ALYREF/THOC4 (By similarity).
CC Interacts with MTREX; the interaction mediates the association of MTREX
CC with nuclear RNA exosomes (By similarity). Interacts with DHX36; this
CC interaction occurs in a RNase-insensitive manner (By similarity).
CC Interacts with NRDE2 (By similarity). {ECO:0000250|UniProtKB:Q01780}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q01780}.
CC Nucleus, nucleolus {ECO:0000250|UniProtKB:Q01780}. Nucleus
CC {ECO:0000250|UniProtKB:Q01780}.
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DR EMBL; AF091392; AAF01779.1; -; mRNA.
DR EMBL; AF091505; AAF01781.1; -; Genomic_DNA.
DR EMBL; AF091506; AAF01781.1; JOINED; Genomic_DNA.
DR EMBL; AF092074; AAF01781.1; JOINED; Genomic_DNA.
DR EMBL; AF092075; AAF01781.1; JOINED; Genomic_DNA.
DR EMBL; AF092076; AAF01781.1; JOINED; Genomic_DNA.
DR EMBL; AF092077; AAF01781.1; JOINED; Genomic_DNA.
DR EMBL; AF092078; AAF01781.1; JOINED; Genomic_DNA.
DR EMBL; AF092079; AAF01781.1; JOINED; Genomic_DNA.
DR EMBL; AF092080; AAF01781.1; JOINED; Genomic_DNA.
DR EMBL; AF092081; AAF01781.1; JOINED; Genomic_DNA.
DR EMBL; AF092082; AAF01781.1; JOINED; Genomic_DNA.
DR EMBL; AF092083; AAF01781.1; JOINED; Genomic_DNA.
DR EMBL; AL606969; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL713995; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS18939.1; -.
DR RefSeq; NP_057908.2; NM_016699.2.
DR AlphaFoldDB; P56960; -.
DR SMR; P56960; -.
DR BioGRID; 206151; 2.
DR ComplexPortal; CPX-594; Nuclear exosome complex, Dis3-Exosc10 variant.
DR ComplexPortal; CPX-595; Nucleolar exosome complex, Exosc10 variant.
DR ComplexPortal; CPX-601; Cytoplasmic exosome complex, Dis3l-Exosc10 variant.
DR CORUM; P56960; -.
DR IntAct; P56960; 2.
DR MINT; P56960; -.
DR STRING; 10090.ENSMUSP00000017408; -.
DR iPTMnet; P56960; -.
DR PhosphoSitePlus; P56960; -.
DR EPD; P56960; -.
DR MaxQB; P56960; -.
DR PaxDb; P56960; -.
DR PeptideAtlas; P56960; -.
DR PRIDE; P56960; -.
DR ProteomicsDB; 275706; -.
DR Antibodypedia; 13683; 200 antibodies from 29 providers.
DR DNASU; 50912; -.
DR Ensembl; ENSMUST00000017408; ENSMUSP00000017408; ENSMUSG00000017264.
DR GeneID; 50912; -.
DR KEGG; mmu:50912; -.
DR UCSC; uc008vut.2; mouse.
DR CTD; 5394; -.
DR MGI; MGI:1355322; Exosc10.
DR VEuPathDB; HostDB:ENSMUSG00000017264; -.
DR eggNOG; KOG2206; Eukaryota.
DR GeneTree; ENSGT00390000015408; -.
DR HOGENOM; CLU_010129_1_1_1; -.
DR InParanoid; P56960; -.
DR OMA; NIMRPQM; -.
DR OrthoDB; 677201at2759; -.
DR PhylomeDB; P56960; -.
DR TreeFam; TF105991; -.
DR Reactome; R-MMU-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR BioGRID-ORCS; 50912; 21 hits in 107 CRISPR screens.
DR ChiTaRS; Exosc10; mouse.
DR PRO; PR:P56960; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; P56960; protein.
DR Bgee; ENSMUSG00000017264; Expressed in undifferentiated genital tubercle and 254 other tissues.
DR ExpressionAtlas; P56960; baseline and differential.
DR Genevisible; P56960; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0000177; C:cytoplasmic exosome (RNase complex); IC:ComplexPortal.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0000791; C:euchromatin; ISO:MGI.
DR GO; GO:0000178; C:exosome (RNase complex); ISS:UniProtKB.
DR GO; GO:0000176; C:nuclear exosome (RNase complex); ISS:UniProtKB.
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; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0000175; F:3'-5'-exoribonuclease activity; ISO:MGI.
DR GO; GO:0004532; F:exoribonuclease activity; ISO:MGI.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0003727; F:single-stranded RNA binding; IBA:GO_Central.
DR GO; GO:0071034; P:CUT catabolic process; ISO:MGI.
DR GO; GO:0009048; P:dosage compensation by inactivation of X chromosome; IMP: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:0071044; P:histone mRNA catabolic process; ISS:UniProtKB.
DR GO; GO:0000460; P:maturation of 5.8S rRNA; ISO:MGI.
DR GO; GO:0032211; P:negative regulation of telomere maintenance via telomerase; ISO:MGI.
DR GO; GO:0071028; P:nuclear mRNA surveillance; ISO:MGI.
DR GO; GO:0071040; P:nuclear polyadenylation-dependent antisense transcript catabolic process; IBA:GO_Central.
DR GO; GO:0071039; P:nuclear polyadenylation-dependent CUT catabolic process; IBA:GO_Central.
DR GO; GO:0071035; P:nuclear polyadenylation-dependent rRNA catabolic process; ISO:MGI.
DR GO; GO:0071036; P:nuclear polyadenylation-dependent snoRNA catabolic process; IBA:GO_Central.
DR GO; GO:0071037; P:nuclear polyadenylation-dependent snRNA catabolic process; IBA:GO_Central.
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:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IEA:UniProtKB-KW.
DR GO; GO:0071051; P:polyadenylation-dependent snoRNA 3'-end processing; IBA:GO_Central.
DR GO; GO:1904872; P:regulation of telomerase RNA localization to Cajal body; ISO:MGI.
DR GO; GO:0006401; P:RNA catabolic process; ISO:MGI.
DR GO; GO:0006396; P:RNA processing; ISO:MGI.
DR Gene3D; 1.10.150.80; -; 1.
DR Gene3D; 3.30.420.10; -; 1.
DR InterPro; IPR002562; 3'-5'_exonuclease_dom.
DR InterPro; IPR012588; Exosome-assoc_fac_Rrp6_N.
DR InterPro; IPR010997; HRDC-like_sf.
DR InterPro; IPR002121; HRDC_dom.
DR InterPro; IPR044876; HRDC_dom_sf.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR045092; Rrp6-like.
DR PANTHER; PTHR12124; PTHR12124; 1.
DR Pfam; PF01612; DNA_pol_A_exo1; 1.
DR Pfam; PF00570; HRDC; 1.
DR Pfam; PF08066; PMC2NT; 1.
DR SMART; SM00474; 35EXOc; 1.
DR SMART; SM00341; HRDC; 1.
DR SUPFAM; SSF47819; SSF47819; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR PROSITE; PS50967; HRDC; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Exonuclease; Exosome; Hydrolase;
KW Isopeptide bond; Nonsense-mediated mRNA decay; Nuclease; Nucleus;
KW Phosphoprotein; Reference proteome; RNA-binding; rRNA processing;
KW Ubl conjugation.
FT CHAIN 1..887
FT /note="Exosome component 10"
FT /id="PRO_0000087134"
FT DOMAIN 503..583
FT /note="HRDC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00328"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 734..757
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 777..887
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 735..757
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 777..815
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 823
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q01780"
FT CROSSLNK 19
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q01780"
FT CROSSLNK 583
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q01780"
FT CROSSLNK 583
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q01780"
FT CROSSLNK 710
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q01780"
FT CROSSLNK 835
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q01780"
FT CROSSLNK 861
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q01780"
FT CROSSLNK 875
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q01780"
FT CONFLICT 792
FT /note="I -> V (in Ref. 1; AAF01779/AAF01781)"
FT /evidence="ECO:0000305"
FT CONFLICT 860
FT /note="C -> F (in Ref. 1; AAF01779)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 887 AA; 100942 MW; 173164944163620C CRC64;
MAPPSPREHQ SAPATSATKP DAEMVLPGFP DADSFVKFAL GSVVAVTKAS GGLPQFGDEY
DFYRSFPAFQ AFCETQGDRL LQCMSRVMQY HGCRSNIKDR SKVTELEDKF DLLVDTNDVI
LERVGMLLDE ASGVNKHQQP VLPAGLQVPK TIVSSWNRKA GEYGKKAKSE TFRLLHAKNI
VRPQLRFREK IDNSNTPFLP KIFVKPNARK PLPLALSKER RERPQDRPED LDVPPALADF
IHQQRTQQVE QDMFAHPYQY ELDHFTPPQS VLQRPKPQLY RAVGETPCHL VSSLDELVEL
NEKLLGCQEF AVDLEHHSYR SFLGLTCLMQ ISTRTEDFIV DTLELRSDMY ILNESLTDPA
IVKVFHGADS DIEWLQKDFG LYVVNMFDTH QAARLLNLAR HSLDHLLRLY CGVESNKQYQ
LADWRIRPLP EEMLSYARDD THYLLYIYDR MRLELWERGN HQPVQLQVVW QRSRDICLKK
FVKPIFTDES YLELYRKQKK HLNSQQLTAF QLLFAWRDKT ARREDESYGY VLPNHMMLKI
AEELPKEPQG IIACCNPVPP LVRQQINEMH LLIQQAREMP LLKSENAAGV RKSGPLPSAE
RLENDLFGPH DCSHAPPDNY QNTSTDGTLP LQKQPSLFTE GKEETSVDAG CLLATAVITL
FSEPNTEEGG KTPLTVAQKK AQNIMQSFEN PFRMFLPSLE HKAHISQAAK FDPSSKIYEI
SNRWKLASQV QVQKEPKEAT KKKVAEQTAA REEAKEEAAA GVLEQAIPVR QQAALENATK
KRERATSDLR TIEQKQEKKR LKSSKKAKDP DPPGKDFSPY DYSQSDFRAF AGDSKSKPSS
QFDPNKLAPS GKKGVGAKKC KQSVGNKSMS FAVGKSDRGF RHNWPKR
