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Q9DAA6 (EXOS1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Exosome complex component CSL4
Alternative name(s):
Exosome component 1
Gene names
Name:Exosc1
Synonyms:Csl4
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length195 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

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.

Subunit structure

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.

Subcellular location

Nucleusnucleolus. Nucleus By similarity. Cytoplasm By similarity.

Sequence similarities

Belongs to the CSL4 family.

Contains 1 S1 motif domain.

Ontologies

Keywords
   Biological processrRNA processing
   Cellular componentCytoplasm
Exosome
Nucleus
   Coding sequence diversityAlternative splicing
   LigandRNA-binding
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processrRNA processing

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

exosome (RNase complex)

Inferred from sequence or structural similarity. Source: UniProtKB

nucleolus

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionRNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9DAA6-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9DAA6-2)

The sequence of this isoform differs from the canonical sequence as follows:
     76-116: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 195195Exosome complex component CSL4
PRO_0000087128

Regions

Domain66 – 14782S1 motif

Amino acid modifications

Modified residue211Phosphoserine By similarity

Natural variations

Alternative sequence76 – 11641Missing in isoform 2.
VSP_004176

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 2F8D214B2B6A2953

FASTA19521,424
        10         20         30         40         50         60 
MAPPVRYCIP GERLCNLEEG SPGSGTYTRH GYIFSSLAGC LMKTSENGAV PVVSVMRETE 

        70         80         90        100        110        120 
SQLLPDVGAV VTCKVSSINS RFAKVHILYV GSTPLKNAFR GTIRKEDIRA TEKDKVEIYK 

       130        140        150        160        170        180 
SFRPGDIVLA KVISLGDAQS NYLLTTAENE LGVVVAHSES GVQMVPISWC EMQCPKTHTK 

       190 
EFRKVARVQP EFLQT 

« Hide

Isoform 2 [UniParc].

Checksum: 7FA6B8509060F16C
Show »

FASTA15416,794

References

[1]"The transcriptional landscape of the mammalian genome."
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. expand/collapse author list , 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.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Strain: C57BL/6J.
Tissue: Testis.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK002930 mRNA. Translation: BAB22465.1.
AK006018 mRNA. Translation: BAB24368.1.
BC024423 mRNA. Translation: AAH24423.1.
RefSeqNP_001158033.1. NM_001164561.1.
NP_079920.1. NM_025644.4.
UniGeneMm.289086.

3D structure databases

ProteinModelPortalQ9DAA6.
SMRQ9DAA6. Positions 6-185.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid211569. 2 interactions.
STRING10090.ENSMUSP00000074756.

PTM databases

PhosphoSiteQ9DAA6.

Proteomic databases

PaxDbQ9DAA6.
PRIDEQ9DAA6.

Protocols and materials databases

DNASU66583.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000075280; ENSMUSP00000074756; ENSMUSG00000034321. [Q9DAA6-1]
ENSMUST00000112123; ENSMUSP00000107751; ENSMUSG00000034321. [Q9DAA6-2]
GeneID66583.
KEGGmmu:66583.
UCSCuc008hmm.2. mouse. [Q9DAA6-1]
uc008hmn.2. mouse. [Q9DAA6-2]

Organism-specific databases

CTD51013.
MGIMGI:1913833. Exosc1.

Phylogenomic databases

eggNOGCOG1096.
GeneTreeENSGT00390000015287.
HOGENOMHOG000177330.
HOVERGENHBG051516.
InParanoidQ9DAA6.
KOK07573.
OMAVTSINPR.
OrthoDBEOG7V4B0J.
PhylomeDBQ9DAA6.
TreeFamTF316607.

Gene expression databases

BgeeQ9DAA6.
CleanExMM_EXOSC1.
GenevestigatorQ9DAA6.

Family and domain databases

InterProIPR019495. EXOSC1.
IPR025721. Exosome_cplx_N_dom.
IPR012340. NA-bd_OB-fold.
IPR022967. RNA-binding_domain_S1.
[Graphical view]
PfamPF14382. ECR1_N. 1 hit.
PF10447. EXOSC1. 1 hit.
[Graphical view]
SMARTSM00316. S1. 1 hit.
[Graphical view]
SUPFAMSSF50249. SSF50249. 1 hit.
ProtoNetSearch...

Other

NextBio322064.
PROQ9DAA6.
SOURCESearch...

Entry information

Entry nameEXOS1_MOUSE
AccessionPrimary (citable) accession number: Q9DAA6
Secondary accession number(s): Q9DCB9
Entry history
Integrated into UniProtKB/Swiss-Prot: February 12, 2003
Last sequence update: June 1, 2001
Last modified: April 16, 2014
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot