EXOS9_BOVIN
ID EXOS9_BOVIN Reviewed; 440 AA.
AC Q3SWZ4;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 25-MAY-2022, entry version 86.
DE RecName: Full=Exosome complex component RRP45;
DE AltName: Full=Exosome component 9;
GN Name=EXOSC9;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Uterus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; BC104587; AAI04588.1; -; mRNA.
DR RefSeq; NP_001030225.1; NM_001035053.1.
DR AlphaFoldDB; Q3SWZ4; -.
DR SMR; Q3SWZ4; -.
DR STRING; 9913.ENSBTAP00000006502; -.
DR PaxDb; Q3SWZ4; -.
DR GeneID; 508005; -.
DR KEGG; bta:508005; -.
DR CTD; 5393; -.
DR eggNOG; KOG1614; Eukaryota.
DR InParanoid; Q3SWZ4; -.
DR OrthoDB; 996662at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000178; C:exosome (RNase complex); ISS:UniProtKB.
DR GO; GO:0000228; C:nuclear chromosome; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; Exosome; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; RNA-binding; rRNA processing; Ubl conjugation.
FT CHAIN 1..440
FT /note="Exosome complex component RRP45"
FT /id="PRO_0000287542"
FT REGION 341..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 404..440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 426..440
FT /note="Basic 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:0000250|UniProtKB:Q06265"
FT MOD_RES 395
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q06265"
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 440 AA; 49150 MW; AE2F7605F56613C8 CRC64;
MKETPLSNCE RRFLLRAIEE KKRLDGRQTY DYRNIKISFG TDYGCCIVEL GKTRVLGQVS
CELVSPKLNR ATEGILFFNL ELSQMAAPAF EPGRQSDLLV KLNRLLERCL RNSKCIDTES
LCVVAGEKVW QIRVDLHLLN HDGNIIDAAS IAAIVALCHF RRPDVSVQGD EVTLYTLEER
DPVPLSIHHM PICVSFAFFQ QGTYLLVDPS EREERVMDGL LVIAMNKHRE ICTIQSSGGI
MLLKDQVLRC SKIAGVKVVE ITELIQKALE NDQKVRKEGG KFGFVESMAN QRITAFKMEK
APIDTSDVEE KAEEIISEAE PPSEVVSKPV LWTPGTAQIG EGIENSWGHL EDSEKEDEDE
GGSDEAIILD GMKMDTGVEV SNIGSQDAPI VLSDSEEEEM IILEPDKNPK KIRTQTISAT
QVKAPSKKPV KKRKKKRAAN
