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Exosome complex component csl4

 CSL4_SCHPO              Reviewed;         181 AA.
O59821;
12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
01-MAY-1999, sequence version 2.
25-OCT-2017, entry version 114.
RecName: Full=Exosome complex component csl4;
Name=csl4; ORFNames=SPCC1840.11, SPCC965.01;
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
Schizosaccharomycetes; Schizosaccharomycetales;
Schizosaccharomycetaceae; Schizosaccharomyces.
NCBI_TaxID=284812;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=972 / ATCC 24843;
PubMed=11859360; DOI=10.1038/nature724;
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M.,
Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A.,
Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G.,
Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K.,
James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J.,
Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C.,
Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E.,
Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S.,
Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K.,
Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S.,
Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B.,
Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S.,
Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D.,
Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R.,
Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B.,
Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S.,
Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M.,
Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G.,
Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J.,
Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L.,
Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J.,
Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
"The genome sequence of Schizosaccharomyces pombe.";
Nature 415:871-880(2002).
[2]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=16823372; DOI=10.1038/nbt1222;
Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
Yoshida M.;
"ORFeome cloning and global analysis of protein localization in the
fission yeast Schizosaccharomyces pombe.";
Nat. Biotechnol. 24:841-847(2006).
-!- 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 cryptic
unstable transcripts (CUTs), and of mRNAs with processing defects,
thereby limiting or excluding their export to the cytoplasm. In
the cytoplasm, the RNA exosome complex is involved in general mRNA
turnover and in RNA surveillance pathways, preventing translation
of aberrant mRNAs. 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 (By similarity). {ECO:0000250}.
-!- SUBUNIT: Component of the RNA exosome complex. Specifically part
of the catalytically inactive RNA exosome core (Exo-9) complex
which associates with catalytic subunits dis3 and rrp6 in
cytoplasmic- and nuclear-specific RNA exosome complex forms. Exo-9
is formed by a hexameric ring of RNase PH domain-containing
subunits and peripheral S1 domain-containing components csl4, rrp4
and rrp40 located on the top of the ring structure (By
similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Nucleus, nucleolus
{ECO:0000269|PubMed:16823372}. Cytoplasm
{ECO:0000269|PubMed:16823372}.
-!- SIMILARITY: Belongs to the CSL4 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; CU329672; CAA20134.1; -; Genomic_DNA.
PIR; T41179; T41179.
PIR; T41654; T41654.
RefSeq; NP_588510.1; NM_001023500.2.
ProteinModelPortal; O59821; -.
SMR; O59821; -.
BioGrid; 275917; 9.
MINT; MINT-4676431; -.
STRING; 4896.SPCC1840.11.1; -.
iPTMnet; O59821; -.
MaxQB; O59821; -.
PRIDE; O59821; -.
EnsemblFungi; SPCC1840.11.1; SPCC1840.11.1:pep; SPCC1840.11.
GeneID; 2539351; -.
KEGG; spo:SPCC1840.11; -.
EuPathDB; FungiDB:SPCC1840.11; -.
PomBase; SPCC1840.11; csl4.
HOGENOM; HOG000177330; -.
InParanoid; O59821; -.
KO; K07573; -.
OMA; KPGFHLT; -.
OrthoDB; EOG092C53BP; -.
PhylomeDB; O59821; -.
Reactome; R-SPO-429958; mRNA decay by 3' to 5' exoribonuclease.
Reactome; R-SPO-450385; Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA.
Reactome; R-SPO-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
PRO; PR:O59821; -.
Proteomes; UP000002485; Chromosome III.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0000177; C:cytoplasmic exosome (RNase complex); ISO:PomBase.
GO; GO:0005829; C:cytosol; IDA:PomBase.
GO; GO:0000178; C:exosome (RNase complex); IDA:PomBase.
GO; GO:0000176; C:nuclear exosome (RNase complex); ISO:PomBase.
GO; GO:0005730; C:nucleolus; ISO:PomBase.
GO; GO:0005634; C:nucleus; IDA:PomBase.
GO; GO:0000175; F:3'-5'-exoribonuclease activity; ISO:PomBase.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
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); ISO:PomBase.
GO; GO:0034661; P:ncRNA catabolic process; ISO:PomBase.
GO; GO:0070651; P:nonfunctional rRNA decay; ISO:PomBase.
GO; GO:0071042; P:nuclear polyadenylation-dependent mRNA catabolic process; ISO:PomBase.
GO; GO:0071035; P:nuclear polyadenylation-dependent rRNA catabolic process; ISO:PomBase.
GO; GO:0071038; P:nuclear polyadenylation-dependent tRNA catabolic process; ISO:PomBase.
GO; GO:0070478; P:nuclear-transcribed mRNA catabolic process, 3'-5' exonucleolytic nonsense-mediated decay; ISO:PomBase.
GO; GO:0070481; P:nuclear-transcribed mRNA catabolic process, non-stop decay; ISO:PomBase.
InterPro; IPR019495; EXOSC1.
InterPro; IPR012340; NA-bd_OB-fold.
InterPro; IPR022967; S1_dom.
InterPro; IPR003029; S1_domain.
Pfam; PF10447; EXOSC1; 2.
SMART; SM00316; S1; 1.
SUPFAM; SSF50249; SSF50249; 1.
PROSITE; PS50126; S1; 1.
3: Inferred from homology;
Complete proteome; Cytoplasm; Exosome; Nucleus; Reference proteome;
RNA-binding; rRNA processing.
CHAIN 1 181 Exosome complex component csl4.
/FTId=PRO_0000079402.
DOMAIN 58 137 S1 motif. {ECO:0000255|PROSITE-
ProRule:PRU00180}.
SEQUENCE 181 AA; 19890 MW; 71D8FB400B79A155 CRC64;
MNLVLPGQVV ARGAPNGEGT VKRGDYIIST RTGIFDPEKN SVTYPRKVEE TAVLPNVGSI
VLARVSRINA RQATVNISVV DDVCTKDEFQ GVIHVQDIRA TEKNKVKVQN SFRPGDIVRA
LVISLGDGSS YFLTTARNDL GVIFAQSSET GEQMFPVDYQ HMQTKSGYTE MRKCAKPILD
E


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