EXOS4_MOUSE
ID EXOS4_MOUSE Reviewed; 245 AA.
AC Q921I9;
DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Exosome complex component RRP41;
DE AltName: Full=Exosome component 4;
DE AltName: Full=Ribosomal RNA-processing protein 41;
GN Name=Exosc4; Synonyms=Rrp41;
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].
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=Kidney, 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: 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. EXOSC4
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). Interacts with DDX60 (By similarity).
CC {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}.
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DR EMBL; BC012277; AAH12277.1; -; mRNA.
DR CCDS; CCDS37119.1; -.
DR RefSeq; NP_780608.1; NM_175399.4.
DR AlphaFoldDB; Q921I9; -.
DR SMR; Q921I9; -.
DR BioGRID; 224543; 10.
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; Q921I9; 1.
DR STRING; 10090.ENSMUSP00000050940; -.
DR PhosphoSitePlus; Q921I9; -.
DR EPD; Q921I9; -.
DR MaxQB; Q921I9; -.
DR PaxDb; Q921I9; -.
DR PRIDE; Q921I9; -.
DR ProteomicsDB; 267674; -.
DR Antibodypedia; 14755; 180 antibodies from 27 providers.
DR DNASU; 109075; -.
DR Ensembl; ENSMUST00000059045; ENSMUSP00000050940; ENSMUSG00000034259.
DR GeneID; 109075; -.
DR KEGG; mmu:109075; -.
DR UCSC; uc007wjp.1; mouse.
DR CTD; 54512; -.
DR MGI; MGI:1923576; Exosc4.
DR VEuPathDB; HostDB:ENSMUSG00000034259; -.
DR eggNOG; KOG1068; Eukaryota.
DR GeneTree; ENSGT00940000153348; -.
DR HOGENOM; CLU_063514_0_0_1; -.
DR InParanoid; Q921I9; -.
DR OMA; GIAMYDY; -.
DR OrthoDB; 1394468at2759; -.
DR PhylomeDB; Q921I9; -.
DR TreeFam; TF313915; -.
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; 109075; 26 hits in 74 CRISPR screens.
DR ChiTaRS; Exosc4; mouse.
DR PRO; PR:Q921I9; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q921I9; protein.
DR Bgee; ENSMUSG00000034259; Expressed in floor plate of midbrain and 245 other tissues.
DR ExpressionAtlas; Q921I9; baseline and differential.
DR Genevisible; Q921I9; 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:0000791; C:euchromatin; ISO:MGI.
DR GO; GO:0000178; C:exosome (RNase complex); ISS:UniProtKB.
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); 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:0035925; F:mRNA 3'-UTR AU-rich region binding; ISO:MGI.
DR GO; GO:0051607; P:defense response to virus; ISO:MGI.
DR GO; GO:0045006; P:DNA deamination; ISO:MGI.
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:0071028; P:nuclear mRNA surveillance; ISO:MGI.
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: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:0016075; P:rRNA catabolic process; IBA:GO_Central.
DR GO; GO:0034475; P:U4 snRNA 3'-end processing; IBA:GO_Central.
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 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; Nucleus; Reference proteome; RNA-binding;
KW rRNA processing.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9NPD3"
FT CHAIN 2..245
FT /note="Exosome complex component RRP41"
FT /id="PRO_0000139959"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9NPD3"
SQ SEQUENCE 245 AA; 26250 MW; E06C1CA2CA1FBF57 CRC64;
MAGLELLSDQ GYRIDGRRAG ELRKIQARMG VFAQADGSAY IEQGNTKALA VVYGPHEIRG
SRSRALPDRA LVNCQYSSAT FSTGERKRRP HGDRKSCEMG LQLRQTFEAA ILTQLHPRSQ
IDIYVQVLQA DGGTYAACVN AATLAVMDAG IPMRDFVCAC SAGFVDGTAL ADLSHVEEAA
GGPQLALALL PASGQIALLE MDSRLHEDHL EQVLEAAAQA ARGVHTLLDL VVRQHVQEAS
VSLGD
