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Q921I9 (EXOS4_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 97. 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 RRP41
Alternative name(s):
Exosome component 4
Ribosomal RNA-processing protein 41
Gene names
Name:Exosc4
Synonyms:Rrp41
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length245 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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. EXOSC4 binds to ARE-containing RNAs 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 By similarity. Interacts with DDX60 By similarity.

Subcellular location

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

Sequence similarities

Belongs to the RNase PH family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 245244Exosome complex component RRP41
PRO_0000139959

Amino acid modifications

Modified residue21N-acetylalanine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q921I9 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: E06C1CA2CA1FBF57

FASTA24526,250
        10         20         30         40         50         60 
MAGLELLSDQ GYRIDGRRAG ELRKIQARMG VFAQADGSAY IEQGNTKALA VVYGPHEIRG 

        70         80         90        100        110        120 
SRSRALPDRA LVNCQYSSAT FSTGERKRRP HGDRKSCEMG LQLRQTFEAA ILTQLHPRSQ 

       130        140        150        160        170        180 
IDIYVQVLQA DGGTYAACVN AATLAVMDAG IPMRDFVCAC SAGFVDGTAL ADLSHVEEAA 

       190        200        210        220        230        240 
GGPQLALALL PASGQIALLE MDSRLHEDHL EQVLEAAAQA ARGVHTLLDL VVRQHVQEAS 


VSLGD 

« Hide

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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC012277 mRNA. Translation: AAH12277.1.
RefSeqNP_780608.1. NM_175399.4.
UniGeneMm.322752.

3D structure databases

ProteinModelPortalQ921I9.
SMRQ921I9. Positions 7-241.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid224543. 1 interaction.
IntActQ921I9. 1 interaction.
MINTMINT-4094786.

PTM databases

PhosphoSiteQ921I9.

Proteomic databases

PaxDbQ921I9.
PRIDEQ921I9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000059045; ENSMUSP00000050940; ENSMUSG00000034259.
GeneID109075.
KEGGmmu:109075.
UCSCuc007wjp.1. mouse.

Organism-specific databases

CTD54512.
MGIMGI:1923576. Exosc4.

Phylogenomic databases

eggNOGCOG0689.
GeneTreeENSGT00550000074804.
HOGENOMHOG000229515.
HOVERGENHBG051519.
InParanoidQ921I9.
KOK11600.
OMADITLLQM.
OrthoDBEOG74J98C.
PhylomeDBQ921I9.
TreeFamTF313915.

Gene expression databases

ArrayExpressQ921I9.
BgeeQ921I9.
CleanExMM_EXOSC4.
GenevestigatorQ921I9.

Family and domain databases

Gene3D3.30.230.70. 1 hit.
InterProIPR001247. ExoRNase_PH_dom1.
IPR015847. ExoRNase_PH_dom2.
IPR027408. PNPase/RNase_PH_dom.
IPR020568. Ribosomal_S5_D2-typ_fold.
[Graphical view]
PfamPF01138. RNase_PH. 1 hit.
PF03725. RNase_PH_C. 1 hit.
[Graphical view]
SUPFAMSSF54211. SSF54211. 1 hit.
SSF55666. SSF55666. 1 hit.
ProtoNetSearch...

Other

ChiTaRSEXOSC4. mouse.
NextBio361620.
PROQ921I9.
SOURCESearch...

Entry information

Entry nameEXOS4_MOUSE
AccessionPrimary (citable) accession number: Q921I9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 11, 2002
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 97 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