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Protein

Exosome complex component RRP46

Gene

Exosc5

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein 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 (By similarity).By similarity

GO - Molecular functioni

  1. RNA binding Source: UniProtKB-KW

GO - Biological processi

  1. defense response to virus Source: MGI
  2. DNA deamination Source: MGI
  3. exonucleolytic nuclear-transcribed mRNA catabolic process involved in deadenylation-dependent decay Source: MGI
  4. RNA catabolic process Source: MGI
  5. rRNA processing Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

rRNA processing

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiREACT_198696. KSRP destabilizes mRNA.
REACT_252013. mRNA decay by 3' to 5' exoribonuclease.

Names & Taxonomyi

Protein namesi
Recommended name:
Exosome complex component RRP46
Alternative name(s):
Exosome component 5
Ribosomal RNA-processing protein 46
Gene namesi
Name:Exosc5
Synonyms:D7Wsu180e, Rrp46
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 7

Organism-specific databases

MGIiMGI:107889. Exosc5.

Subcellular locationi

Nucleusnucleolus By similarity. Cytoplasm By similarity. Nucleus By similarity

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm, Exosome, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 235235Exosome complex component RRP46PRO_0000139976Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei20 – 201PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9CRA8.
PaxDbiQ9CRA8.
PRIDEiQ9CRA8.

PTM databases

PhosphoSiteiQ9CRA8.

Expressioni

Gene expression databases

BgeeiQ9CRA8.
CleanExiMM_EXOSC5.
GenevestigatoriQ9CRA8.

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. Interacts with EXOSC1. 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).By similarity

Protein-protein interaction databases

BioGridi205707. 1 interaction.
IntActiQ9CRA8. 3 interactions.
MINTiMINT-1765755.

Structurei

3D structure databases

ProteinModelPortaliQ9CRA8.
SMRiQ9CRA8. Positions 26-234.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the RNase PH family.Curated

Phylogenomic databases

eggNOGiCOG0689.
GeneTreeiENSGT00550000075002.
HOGENOMiHOG000229515.
HOVERGENiHBG051520.
InParanoidiQ9CRA8.
KOiK12590.
OMAiKIFQFYR.
OrthoDBiEOG7P8P90.
PhylomeDBiQ9CRA8.
TreeFamiTF315920.

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. 1 hit.
SSF55666. SSF55666. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9CRA8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEGAKRADAN LLTDTGTESS PRSPVCSLRH FACEQNLLSR PDGSASFLQG
60 70 80 90 100
DTSVLAGVYG PAEVKVSKEI FNKATLEVIL RPKIGLPGVA EKSRERLVRN
110 120 130 140 150
TCEAVVLGAL HPRTSITVVL QVVSDAGSLL ACCLNAACMA LVDAGVPMRA
160 170 180 190 200
LFCGVTCALD SDGNLVLDPT TKQEKEARAI LTFALDSAEQ KLLMSTTKGL
210 220 230
YSDAELQQCL AAAQAASQHI FRFYRESLQR RYSKS
Length:235
Mass (Da):25,194
Last modified:June 1, 2001 - v1
Checksum:i08752915141CF65D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti11 – 111L → V in AAH34358 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK007372 mRNA. Translation: BAB24993.1.
AK006475 mRNA. Translation: BAB24607.1.
BC034358 mRNA. Translation: AAH34358.1.
CCDSiCCDS20990.1.
RefSeqiNP_613052.1. NM_138586.3.
UniGeneiMm.207484.
Mm.27853.

Genome annotation databases

EnsembliENSMUST00000079634; ENSMUSP00000078580; ENSMUSG00000061286.
GeneIDi27998.
KEGGimmu:27998.
UCSCiuc009fti.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK007372 mRNA. Translation: BAB24993.1.
AK006475 mRNA. Translation: BAB24607.1.
BC034358 mRNA. Translation: AAH34358.1.
CCDSiCCDS20990.1.
RefSeqiNP_613052.1. NM_138586.3.
UniGeneiMm.207484.
Mm.27853.

3D structure databases

ProteinModelPortaliQ9CRA8.
SMRiQ9CRA8. Positions 26-234.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi205707. 1 interaction.
IntActiQ9CRA8. 3 interactions.
MINTiMINT-1765755.

PTM databases

PhosphoSiteiQ9CRA8.

Proteomic databases

MaxQBiQ9CRA8.
PaxDbiQ9CRA8.
PRIDEiQ9CRA8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000079634; ENSMUSP00000078580; ENSMUSG00000061286.
GeneIDi27998.
KEGGimmu:27998.
UCSCiuc009fti.2. mouse.

Organism-specific databases

CTDi56915.
MGIiMGI:107889. Exosc5.

Phylogenomic databases

eggNOGiCOG0689.
GeneTreeiENSGT00550000075002.
HOGENOMiHOG000229515.
HOVERGENiHBG051520.
InParanoidiQ9CRA8.
KOiK12590.
OMAiKIFQFYR.
OrthoDBiEOG7P8P90.
PhylomeDBiQ9CRA8.
TreeFamiTF315920.

Enzyme and pathway databases

ReactomeiREACT_198696. KSRP destabilizes mRNA.
REACT_252013. mRNA decay by 3' to 5' exoribonuclease.

Miscellaneous databases

NextBioi306496.
PROiQ9CRA8.
SOURCEiSearch...

Gene expression databases

BgeeiQ9CRA8.
CleanExiMM_EXOSC5.
GenevestigatoriQ9CRA8.

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. 1 hit.
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: Pancreas and 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].
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiEXOS5_MOUSE
AccessioniPrimary (citable) accession number: Q9CRA8
Secondary accession number(s): Q8K1J2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2002
Last sequence update: June 1, 2001
Last modified: March 4, 2015
This is version 110 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.