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Protein

Exosome complex component RRP43

Gene

Exosc8

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

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. EXOSC8 binds to ARE-containing RNAs (By similarity).By similarity

GO - Molecular functioni

  1. AU-rich element binding Source: MGI

GO - Biological processi

  1. rRNA processing Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

rRNA processing

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiREACT_291652. mRNA decay by 3' to 5' exoribonuclease.
REACT_300665. KSRP destabilizes mRNA.

Names & Taxonomyi

Protein namesi
Recommended name:
Exosome complex component RRP43
Alternative name(s):
Exosome component 8
Ribosomal RNA-processing protein 43
Gene namesi
Name:Exosc8
Synonyms:Rrp43
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:1916889. Exosc8.

Subcellular locationi

  1. Cytoplasm By similarity
  2. Nucleusnucleolus By similarity
  3. Nucleus By similarity

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. exosome (RNase complex) Source: UniProtKB
  3. nucleolus Source: UniProtKB-SubCell
  4. nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Exosome, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 276275Exosome complex component RRP43PRO_0000139968Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9D753.
PaxDbiQ9D753.
PRIDEiQ9D753.

PTM databases

PhosphoSiteiQ9D753.

Expressioni

Gene expression databases

BgeeiQ9D753.
CleanExiMM_EXOSC8.
ExpressionAtlasiQ9D753. baseline and differential.
GenevestigatoriQ9D753.

Interactioni

Subunit structurei

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).By similarity

Protein-protein interaction databases

IntActiQ9D753. 1 interaction.
MINTiMINT-4094795.
STRINGi10090.ENSMUSP00000029316.

Structurei

3D structure databases

ProteinModelPortaliQ9D753.
SMRiQ9D753. Positions 7-274.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the RNase PH family.Curated

Phylogenomic databases

eggNOGiCOG2123.
GeneTreeiENSGT00530000063093.
HOVERGENiHBG051522.
InParanoidiQ9D753.
KOiK12586.
OMAiQAASQFI.
OrthoDBiEOG7D59PC.
TreeFamiTF320415.

Family and domain databases

Gene3Di3.30.230.70. 1 hit.
InterProiIPR001247. ExoRNase_PH_dom1.
IPR015847. ExoRNase_PH_dom2.
IPR027408. PNPase/RNase_PH_dom.
IPR020568. Ribosomal_S5_D2-typ_fold.
[Graphical view]
PfamiPF01138. RNase_PH. 1 hit.
PF03725. RNase_PH_C. 1 hit.
[Graphical view]
SUPFAMiSSF54211. SSF54211. 2 hits.
SSF55666. SSF55666. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9D753-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAGFKTVEP LEYYRRFLKE NCRPDGRELG EFRATTVNIG SISTADGSAL
60 70 80 90 100
VKLGNTTVIC GVKAEFAAPP VDAPDRGYVV PNVDLPPLCS SRFRTGPPGE
110 120 130 140 150
EAQVTSQFIA DVVDNSQVIK KEDLCISPGK LAWVLYCDLI CLDYDGNILD
160 170 180 190 200
ACTFALLAAL KNVQLPEVTI NEETALAEVN LKKKSYLNVR TNPVATSFAV
210 220 230 240 250
FDDTLLIVDP TGEEEHLSTG TLTVVTDEDG KLCCLHKPGG SGLTGAKLQD
260 270
CMSRAVTRHK EVSKLLDEVI QSMRHK
Length:276
Mass (Da):29,949
Last modified:June 1, 2001 - v1
Checksum:i297E1E45F5C0F794
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK009584 mRNA. No translation available.
CCDSiCCDS17352.1.
RefSeqiNP_081424.3. NM_027148.3.
UniGeneiMm.29253.

Genome annotation databases

EnsembliENSMUST00000029316; ENSMUSP00000029316; ENSMUSG00000027752.
GeneIDi69639.
KEGGimmu:69639.
UCSCiuc008pfq.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK009584 mRNA. No translation available.
CCDSiCCDS17352.1.
RefSeqiNP_081424.3. NM_027148.3.
UniGeneiMm.29253.

3D structure databases

ProteinModelPortaliQ9D753.
SMRiQ9D753. Positions 7-274.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9D753. 1 interaction.
MINTiMINT-4094795.
STRINGi10090.ENSMUSP00000029316.

PTM databases

PhosphoSiteiQ9D753.

Proteomic databases

MaxQBiQ9D753.
PaxDbiQ9D753.
PRIDEiQ9D753.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000029316; ENSMUSP00000029316; ENSMUSG00000027752.
GeneIDi69639.
KEGGimmu:69639.
UCSCiuc008pfq.2. mouse.

Organism-specific databases

CTDi11340.
MGIiMGI:1916889. Exosc8.

Phylogenomic databases

eggNOGiCOG2123.
GeneTreeiENSGT00530000063093.
HOVERGENiHBG051522.
InParanoidiQ9D753.
KOiK12586.
OMAiQAASQFI.
OrthoDBiEOG7D59PC.
TreeFamiTF320415.

Enzyme and pathway databases

ReactomeiREACT_291652. mRNA decay by 3' to 5' exoribonuclease.
REACT_300665. KSRP destabilizes mRNA.

Miscellaneous databases

NextBioi329962.
PROiQ9D753.
SOURCEiSearch...

Gene expression databases

BgeeiQ9D753.
CleanExiMM_EXOSC8.
ExpressionAtlasiQ9D753. baseline and differential.
GenevestigatoriQ9D753.

Family and domain databases

Gene3Di3.30.230.70. 1 hit.
InterProiIPR001247. ExoRNase_PH_dom1.
IPR015847. ExoRNase_PH_dom2.
IPR027408. PNPase/RNase_PH_dom.
IPR020568. Ribosomal_S5_D2-typ_fold.
[Graphical view]
PfamiPF01138. RNase_PH. 1 hit.
PF03725. RNase_PH_C. 1 hit.
[Graphical view]
SUPFAMiSSF54211. SSF54211. 2 hits.
SSF55666. SSF55666. 1 hit.
ProtoNetiSearch...

Publicationsi

  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.
    , 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].
    Strain: C57BL/6J.
    Tissue: Tongue.

Entry informationi

Entry nameiEXOS8_MOUSE
AccessioniPrimary (citable) accession number: Q9D753
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2002
Last sequence update: June 1, 2001
Last modified: April 1, 2015
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.