EXOS2_MOUSE
ID EXOS2_MOUSE Reviewed; 293 AA.
AC Q8VBV3;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Exosome complex component RRP4;
DE AltName: Full=Exosome component 2;
DE AltName: Full=Ribosomal RNA-processing protein 4;
GN Name=Exosc2; Synonyms=Rrp4;
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=FVB/N; TISSUE=Mammary tumor;
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 [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, 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. EXOSC2 as
CC peripheral part of the Exo-9 complex stabilizes the hexameric ring of
CC RNase PH-domain subunits through contacts with EXOSC4 and EXOSC7 (By
CC 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 with DIS3. Interacts with GTPBP1. Interacts with
CC ZFP36L1 (via N-terminus). {ECO:0000250|UniProtKB:Q13868}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus, nucleolus
CC {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the RRP4 family. {ECO:0000305}.
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DR EMBL; BC021485; AAH21485.1; -; mRNA.
DR EMBL; BC021807; AAH21807.1; -; mRNA.
DR CCDS; CCDS15900.1; -.
DR RefSeq; NP_659135.1; NM_144886.3.
DR AlphaFoldDB; Q8VBV3; -.
DR SMR; Q8VBV3; -.
DR BioGRID; 230671; 3.
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; Q8VBV3; 1.
DR STRING; 10090.ENSMUSP00000043519; -.
DR iPTMnet; Q8VBV3; -.
DR PhosphoSitePlus; Q8VBV3; -.
DR EPD; Q8VBV3; -.
DR MaxQB; Q8VBV3; -.
DR PaxDb; Q8VBV3; -.
DR PRIDE; Q8VBV3; -.
DR ProteomicsDB; 267673; -.
DR Antibodypedia; 17999; 186 antibodies from 28 providers.
DR DNASU; 227715; -.
DR Ensembl; ENSMUST00000038474; ENSMUSP00000043519; ENSMUSG00000039356.
DR GeneID; 227715; -.
DR KEGG; mmu:227715; -.
DR UCSC; uc008jdy.1; mouse.
DR CTD; 23404; -.
DR MGI; MGI:2385133; Exosc2.
DR VEuPathDB; HostDB:ENSMUSG00000039356; -.
DR eggNOG; KOG3013; Eukaryota.
DR GeneTree; ENSGT00940000153596; -.
DR HOGENOM; CLU_034114_3_1_1; -.
DR InParanoid; Q8VBV3; -.
DR OMA; GVNGFIW; -.
DR OrthoDB; 1121868at2759; -.
DR PhylomeDB; Q8VBV3; -.
DR TreeFam; TF105623; -.
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; 227715; 29 hits in 66 CRISPR screens.
DR ChiTaRS; Exosc2; mouse.
DR PRO; PR:Q8VBV3; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q8VBV3; protein.
DR Bgee; ENSMUSG00000039356; Expressed in molar tooth and 199 other tissues.
DR ExpressionAtlas; Q8VBV3; baseline and differential.
DR Genevisible; Q8VBV3; 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: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; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0071034; P:CUT catabolic process; IBA:GO_Central.
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: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:0071051; P:polyadenylation-dependent snoRNA 3'-end processing; IBA:GO_Central.
DR GO; GO:0030307; P:positive regulation of cell growth; ISO:MGI.
DR GO; GO:0006401; P:RNA catabolic process; ISO:MGI.
DR GO; GO:0006396; P:RNA processing; ISO:MGI.
DR GO; GO:0034475; P:U4 snRNA 3'-end processing; IBA:GO_Central.
DR Gene3D; 2.40.50.140; -; 1.
DR InterPro; IPR025721; Exosome_cplx_N_dom.
DR InterPro; IPR026699; Exosome_RNA_bind1/RRP40/RRP4.
DR InterPro; IPR004088; KH_dom_type_1.
DR InterPro; IPR036612; KH_dom_type_1_sf.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR PANTHER; PTHR21321; PTHR21321; 1.
DR Pfam; PF14382; ECR1_N; 1.
DR Pfam; PF15985; KH_6; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR SUPFAM; SSF54791; SSF54791; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Exosome; Nucleus; Phosphoprotein; Reference proteome;
KW RNA-binding; rRNA processing.
FT CHAIN 1..293
FT /note="Exosome complex component RRP4"
FT /id="PRO_0000087130"
FT DOMAIN 79..159
FT /note="S1 motif"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 124
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13868"
SQ SEQUENCE 293 AA; 32632 MW; 832C75F57980DDF8 CRC64;
MALEMRLPKA RKPLSESLGR DSKKHLVVPG DTITTDTGFM RGHGTYMGEE KLIASVAGSV
ERVNKLICVK ALKTRYNGEV GDIVVGRITE VQQKRWKVET NSRLDSVLLL SSMNLPGGEL
RRRSAEDELA MRGFLQEGDL ISAEVQAVFS DGAVSLHTRS LKYGKLGQGV LVQVSPSLVK
RQKTHFHDLP CGASVILGNN GFIWIYPTPE HKDEDAGGFI ANLEPVALSD REVISRLRNC
VVLLVTQRMM LFDTSILYCY EASLAHQIKD ILKPEVMEEI MLETRQRLLD QEG
