EXOS1_MOUSE
ID EXOS1_MOUSE Reviewed; 195 AA.
AC Q9DAA6; Q9DCB9;
DT 12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Exosome complex component CSL4;
DE AltName: Full=Exosome component 1;
GN Name=Exosc1; Synonyms=Csl4;
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 {ECO:0000312|EMBL:BAB24368.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Testis;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Liver, Lung, Pancreas, 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. EXOSC1 as
CC peripheral part of the Exo-9 complex stabilizes the hexameric ring of
CC RNase PH-domain subunits through contacts with EXOSC6 and EXOSC8 (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 EXOSC5, EXOSC7 and EXOSC10 (By similarity).
CC Interacts with DDX60 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus. Nucleus {ECO:0000250}.
CC Cytoplasm {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9DAA6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9DAA6-2; Sequence=VSP_004176;
CC -!- SIMILARITY: Belongs to the CSL4 family. {ECO:0000305}.
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DR EMBL; AK002930; BAB22465.1; -; mRNA.
DR EMBL; AK006018; BAB24368.1; -; mRNA.
DR EMBL; BC024423; AAH24423.1; -; mRNA.
DR CCDS; CCDS29816.1; -. [Q9DAA6-1]
DR CCDS; CCDS50436.1; -. [Q9DAA6-2]
DR RefSeq; NP_001158033.1; NM_001164561.1. [Q9DAA6-2]
DR RefSeq; NP_001307160.1; NM_001320231.1.
DR RefSeq; NP_001307161.1; NM_001320232.1.
DR RefSeq; NP_001307162.1; NM_001320233.1.
DR RefSeq; NP_079920.1; NM_025644.4. [Q9DAA6-1]
DR AlphaFoldDB; Q9DAA6; -.
DR SMR; Q9DAA6; -.
DR BioGRID; 211569; 19.
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; Q9DAA6; 16.
DR STRING; 10090.ENSMUSP00000074756; -.
DR iPTMnet; Q9DAA6; -.
DR PhosphoSitePlus; Q9DAA6; -.
DR EPD; Q9DAA6; -.
DR MaxQB; Q9DAA6; -.
DR PaxDb; Q9DAA6; -.
DR PeptideAtlas; Q9DAA6; -.
DR PRIDE; Q9DAA6; -.
DR ProteomicsDB; 267671; -. [Q9DAA6-1]
DR ProteomicsDB; 267672; -. [Q9DAA6-2]
DR Antibodypedia; 30884; 242 antibodies from 25 providers.
DR DNASU; 66583; -.
DR Ensembl; ENSMUST00000075280; ENSMUSP00000074756; ENSMUSG00000034321. [Q9DAA6-1]
DR Ensembl; ENSMUST00000112123; ENSMUSP00000107751; ENSMUSG00000034321. [Q9DAA6-2]
DR GeneID; 66583; -.
DR KEGG; mmu:66583; -.
DR UCSC; uc008hmm.2; mouse. [Q9DAA6-1]
DR UCSC; uc008hmn.2; mouse. [Q9DAA6-2]
DR CTD; 51013; -.
DR MGI; MGI:1913833; Exosc1.
DR VEuPathDB; HostDB:ENSMUSG00000034321; -.
DR eggNOG; KOG3409; Eukaryota.
DR GeneTree; ENSGT00390000015287; -.
DR HOGENOM; CLU_067135_3_0_1; -.
DR InParanoid; Q9DAA6; -.
DR OMA; MDEMFRV; -.
DR OrthoDB; 1200489at2759; -.
DR PhylomeDB; Q9DAA6; -.
DR TreeFam; TF316607; -.
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; 66583; 23 hits in 74 CRISPR screens.
DR ChiTaRS; Exosc1; mouse.
DR PRO; PR:Q9DAA6; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q9DAA6; protein.
DR Bgee; ENSMUSG00000034321; Expressed in dorsal pancreas and 223 other tissues.
DR Genevisible; Q9DAA6; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0000177; C:cytoplasmic exosome (RNase complex); IC:ComplexPortal.
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); IBA:GO_Central.
DR GO; GO:0101019; C:nucleolar exosome (RNase complex); IC:ComplexPortal.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006401; P:RNA catabolic process; ISO:MGI.
DR GO; GO:0006396; P:RNA processing; ISO:MGI.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR Gene3D; 2.40.50.140; -; 1.
DR InterPro; IPR039771; Csl4.
DR InterPro; IPR019495; EXOSC1_C.
DR InterPro; IPR025721; Exosome_cplx_N_dom.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR022967; S1_dom.
DR PANTHER; PTHR12686; PTHR12686; 1.
DR Pfam; PF14382; ECR1_N; 1.
DR Pfam; PF10447; EXOSC1; 1.
DR SMART; SM00316; S1; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Exosome; Nucleus; Phosphoprotein;
KW Reference proteome; RNA-binding; rRNA processing.
FT CHAIN 1..195
FT /note="Exosome complex component CSL4"
FT /id="PRO_0000087128"
FT DOMAIN 66..147
FT /note="S1 motif"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3B2"
FT VAR_SEQ 76..116
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_004176"
SQ SEQUENCE 195 AA; 21424 MW; 2F8D214B2B6A2953 CRC64;
MAPPVRYCIP GERLCNLEEG SPGSGTYTRH GYIFSSLAGC LMKTSENGAV PVVSVMRETE
SQLLPDVGAV VTCKVSSINS RFAKVHILYV GSTPLKNAFR GTIRKEDIRA TEKDKVEIYK
SFRPGDIVLA KVISLGDAQS NYLLTTAENE LGVVVAHSES GVQMVPISWC EMQCPKTHTK
EFRKVARVQP EFLQT
