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Q7TQK4 (EXOS3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 87. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Exosome complex component RRP40

EC=3.1.13.-
Alternative name(s):
Exosome component 3
Ribosomal RNA-processing protein 40
Gene names
Name:Exosc3
Synonyms:Rrp40
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length274 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein 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. EXOSC3 as peripheral part of the Exo-9 complex stabilizes the hexameric ring of RNase PH-domain subunits through contacts with EXOSC9 and EXOSC5 By similarity. Ref.3

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 GTPBP1 By similarity. Interacts with ZC3HAV1 By similarity. Interacts with DDX17 only in the presence of ZC3HAV1 in an RNA-independent manner By similarity.

Subcellular location

Cytoplasm By similarity. Nucleusnucleolus By similarity. Nucleus By similarity.

Sequence similarities

Belongs to the RRP40 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 274273Exosome complex component RRP40
PRO_0000087132

Amino acid modifications

Modified residue21N-acetylalanine By similarity

Experimental info

Sequence conflict321E → P in BAB24501. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q7TQK4 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 0932E5B03DD708D4

FASTA27429,546
        10         20         30         40         50         60 
MAEVLSAGPE SVAGCRARAV HKVLNQVVLP GEELVLPDHE DVDGLGGAGE QPLRLNAGAR 

        70         80         90        100        110        120 
PRLRVVCGPG LRRCGDRLLV TKCGRLRHKE PSGGGGGVYW VDSQQKRYVP VKGDHVIGIV 

       130        140        150        160        170        180 
IAKSGDIFKV DVGGSEPASL SYLAFEGATK RNRPNVQVGD LIYGQCVVAN KDMEPEMVCI 

       190        200        210        220        230        240 
DSCGRANGMG VIGQDGLLFK VTLGLIRKLL APDCEIVQEL GKLYPLEIVF GMNGRIWVKA 

       250        260        270 
KTIQQTLILA NVLEACEHMT TEQRKQIFAR LAES 

« Hide

References

« Hide 'large scale' references
[1]"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].
Tissue: Mammary gland.
[2]"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] OF 32-274.
Strain: C57BL/6J.
Tissue: Testis and Tongue.
[3]"The RNA exosome targets the AID cytidine deaminase to both strands of transcribed duplex DNA substrates."
Basu U., Meng F.L., Keim C., Grinstein V., Pefanis E., Eccleston J., Zhang T., Myers D., Wasserman C.R., Wesemann D.R., Januszyk K., Gregory R.I., Deng H., Lima C.D., Alt F.W.
Cell 144:353-363(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN IG CLASS-SWITCH.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC023669 mRNA. Translation: AAH23669.1.
BC054085 mRNA. Translation: AAH54085.1.
AK006281 mRNA. Translation: BAB24501.1.
AK009165 mRNA. Translation: BAB26116.1.
CCDSCCDS18136.1.
RefSeqNP_079789.1. NM_025513.3.
UniGeneMm.275788.

3D structure databases

ProteinModelPortalQ7TQK4.
SMRQ7TQK4. Positions 17-274.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ7TQK4. 2 interactions.
MINTMINT-4094772.

PTM databases

PhosphoSiteQ7TQK4.

Proteomic databases

MaxQBQ7TQK4.
PaxDbQ7TQK4.
PRIDEQ7TQK4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000030003; ENSMUSP00000030003; ENSMUSG00000028322.
GeneID66362.
KEGGmmu:66362.
UCSCuc008ssk.1. mouse.

Organism-specific databases

CTD51010.
MGIMGI:1913612. Exosc3.

Phylogenomic databases

eggNOGCOG1097.
GeneTreeENSGT00390000012042.
HOGENOMHOG000184644.
HOVERGENHBG051518.
InParanoidQ7TQK4.
KOK03681.
OMAVNGRVWI.
OrthoDBEOG76HQ2F.
PhylomeDBQ7TQK4.
TreeFamTF314927.

Gene expression databases

BgeeQ7TQK4.
CleanExMM_EXOSC3.
GenevestigatorQ7TQK4.

Family and domain databases

InterProIPR026699. Exosome_RNA_bind1/RRP40/RRP4.
IPR004088. KH_dom_type_1.
IPR012340. NA-bd_OB-fold.
[Graphical view]
PANTHERPTHR21321. PTHR21321. 1 hit.
SUPFAMSSF50249. SSF50249. 1 hit.
SSF54791. SSF54791. 1 hit.
ProtoNetSearch...

Other

ChiTaRSEXOSC3. mouse.
NextBio321447.
PROQ7TQK4.
SOURCESearch...

Entry information

Entry nameEXOS3_MOUSE
AccessionPrimary (citable) accession number: Q7TQK4
Secondary accession number(s): Q9CV81, Q9CVW2
Entry history
Integrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 87 of the entry and version 3 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