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Exosome complex component CSL4 (Exosome component 1)

 EXOS1_MOUSE             Reviewed;         195 AA.
Q9DAA6; Q9DCB9;
12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 1.
12-SEP-2018, entry version 128.
RecName: Full=Exosome complex component CSL4;
AltName: Full=Exosome component 1;
Name=Exosc1; Synonyms=Csl4;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090 {ECO:0000312|EMBL:BAB24368.1};
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
STRAIN=C57BL/6J; TISSUE=Testis;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Non-catalytic component of the RNA exosome complex which
has 3'->5' exoribonuclease activity and participates in a
multitude of cellular RNA processing and degradation events. In
the nucleus, the RNA exosome complex is involved in proper
maturation of stable RNA species such as rRNA, snRNA and snoRNA,
in the elimination of RNA processing by-products and non-coding
'pervasive' transcripts, such as antisense RNA species and
promoter-upstream transcripts (PROMPTs), and of mRNAs with
processing defects, thereby limiting or excluding their export to
the cytoplasm. The RNA exosome may be involved in Ig class switch
recombination (CSR) and/or Ig variable region somatic
hypermutation (SHM) by targeting AICDA deamination activity to
transcribed dsDNA substrates. In the cytoplasm, the RNA exosome
complex is involved in general mRNA turnover and specifically
degrades inherently unstable mRNAs containing AU-rich elements
(AREs) within their 3' untranslated regions, and in RNA
surveillance pathways, preventing translation of aberrant mRNAs.
It seems to be involved in degradation of histone mRNA. The
catalytic inactive RNA exosome core complex of 9 subunits (Exo-9)
is proposed to play a pivotal role in the binding and presentation
of RNA for ribonucleolysis, and to serve as a scaffold for the
association with catalytic subunits and accessory proteins or
complexes. EXOSC1 as peripheral part of the Exo-9 complex
stabilizes the hexameric ring of RNase PH-domain subunits through
contacts with EXOSC6 and EXOSC8 (By similarity). {ECO:0000250}.
-!- SUBUNIT: Component of the RNA exosome complex. Specifically part
of the catalytically inactive RNA exosome core (Exo-9) complex
which is believed to associate with catalytic subunits EXOSC10,
and DIS3 or DIS3L in cytoplasmic- and nuclear-specific RNA exosome
complex forms. Exo-9 is formed by a hexameric ring of RNase PH
domain-containing subunits specifically containing the
heterodimers EXOSC4-EXOSC9, EXOSC5-EXOSC8 and EXOSC6-EXOSC7, and
peripheral S1 domain-containing components EXOSC1, EXOSC2 and
EXOSC3 located on the top of the ring structure. Interacts with
EXOSC5, EXOSC7 and EXOSC10 (By similarity). Interacts with DDX60
(By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Nucleus, nucleolus. Nucleus {ECO:0000250}.
Cytoplasm {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9DAA6-1; Sequence=Displayed;
Name=2;
IsoId=Q9DAA6-2; Sequence=VSP_004176;
Note=No experimental confirmation available.;
-!- SIMILARITY: Belongs to the CSL4 family. {ECO:0000305}.
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EMBL; AK002930; BAB22465.1; -; mRNA.
EMBL; AK006018; BAB24368.1; -; mRNA.
EMBL; BC024423; AAH24423.1; -; mRNA.
CCDS; CCDS29816.1; -. [Q9DAA6-1]
CCDS; CCDS50436.1; -. [Q9DAA6-2]
RefSeq; NP_001158033.1; NM_001164561.1. [Q9DAA6-2]
RefSeq; NP_001307160.1; NM_001320231.1.
RefSeq; NP_001307161.1; NM_001320232.1.
RefSeq; NP_001307162.1; NM_001320233.1.
RefSeq; NP_079920.1; NM_025644.4. [Q9DAA6-1]
UniGene; Mm.289086; -.
ProteinModelPortal; Q9DAA6; -.
SMR; Q9DAA6; -.
BioGrid; 211569; 18.
ComplexPortal; CPX-594; Nuclear exosome complex, Dis3-Exosc10 variant.
ComplexPortal; CPX-595; Nucleolar exosome complex, Exosc10 variant.
ComplexPortal; CPX-596; Cytoplasmic exosome complex, Dis3l variant.
ComplexPortal; CPX-598; Exosome complex, Dis3 variant.
ComplexPortal; CPX-601; Cytoplasmic exosome complex, Dis3l-Exosc10 variant.
IntAct; Q9DAA6; 16.
STRING; 10090.ENSMUSP00000074756; -.
iPTMnet; Q9DAA6; -.
PhosphoSitePlus; Q9DAA6; -.
EPD; Q9DAA6; -.
PaxDb; Q9DAA6; -.
PeptideAtlas; Q9DAA6; -.
PRIDE; Q9DAA6; -.
DNASU; 66583; -.
Ensembl; ENSMUST00000075280; ENSMUSP00000074756; ENSMUSG00000034321. [Q9DAA6-1]
Ensembl; ENSMUST00000112123; ENSMUSP00000107751; ENSMUSG00000034321. [Q9DAA6-2]
GeneID; 66583; -.
KEGG; mmu:66583; -.
UCSC; uc008hmm.2; mouse. [Q9DAA6-1]
UCSC; uc008hmn.2; mouse. [Q9DAA6-2]
CTD; 51013; -.
MGI; MGI:1913833; Exosc1.
eggNOG; KOG3409; Eukaryota.
eggNOG; COG1096; LUCA.
GeneTree; ENSGT00390000015287; -.
HOGENOM; HOG000177330; -.
HOVERGEN; HBG051516; -.
InParanoid; Q9DAA6; -.
KO; K07573; -.
OMA; KPGFHLT; -.
OrthoDB; EOG091G0NLQ; -.
PhylomeDB; Q9DAA6; -.
TreeFam; TF316607; -.
Reactome; R-MMU-429958; mRNA decay by 3' to 5' exoribonuclease.
Reactome; R-MMU-450385; Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA.
Reactome; R-MMU-450604; KSRP (KHSRP) binds and destabilizes mRNA.
Reactome; R-MMU-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
ChiTaRS; Exosc1; mouse.
PRO; PR:Q9DAA6; -.
Proteomes; UP000000589; Chromosome 19.
Bgee; ENSMUSG00000034321; Expressed in 243 organ(s), highest expression level in dorsal pancreas.
CleanEx; MM_EXOSC1; -.
Genevisible; Q9DAA6; MM.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0000178; C:exosome (RNase complex); ISS:UniProtKB.
GO; GO:0000176; C:nuclear exosome (RNase complex); IBA:GO_Central.
GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
GO; GO:0006396; P:RNA processing; ISO:MGI.
GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
InterPro; IPR019495; EXOSC1.
InterPro; IPR025721; Exosome_cplx_N_dom.
InterPro; IPR012340; NA-bd_OB-fold.
InterPro; IPR022967; S1_dom.
Pfam; PF14382; ECR1_N; 1.
Pfam; PF10447; EXOSC1; 1.
SMART; SM00316; S1; 1.
SUPFAM; SSF50249; SSF50249; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Cytoplasm; Exosome; Nucleus;
Phosphoprotein; Reference proteome; RNA-binding; rRNA processing.
CHAIN 1 195 Exosome complex component CSL4.
/FTId=PRO_0000087128.
DOMAIN 66 147 S1 motif.
MOD_RES 21 21 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Y3B2}.
VAR_SEQ 76 116 Missing (in isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_004176.
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


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