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Protein

Exosome complex component MTR3

Gene

Exosc6

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 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. poly(A) RNA binding Source: MGI

GO - Biological processi

  1. DNA deamination Source: MGI
  2. isotype switching Source: UniProtKB
  3. positive regulation of isotype switching Source: MGI
  4. rRNA processing Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

rRNA processing

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

BRENDAi1.8.1.9. 3474.

Names & Taxonomyi

Protein namesi
Recommended name:
Exosome complex component MTR3
Alternative name(s):
Exosome component 6
mRNA transport regulator 3 homolog
Gene namesi
Name:Exosc6
Synonyms:Mtr3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:1919794. Exosc6.

Subcellular locationi

Cytoplasm By similarity. Nucleusnucleolus By similarity. Nucleus By similarity

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm, Exosome, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 273273Exosome complex component MTR3PRO_0000287479Add
BLAST

Proteomic databases

MaxQBiQ8BTW3.
PaxDbiQ8BTW3.
PRIDEiQ8BTW3.

PTM databases

PhosphoSiteiQ8BTW3.

Expressioni

Gene expression databases

CleanExiMM_EXOSC6.
GenevestigatoriQ8BTW3.

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

BioGridi215428. 1 interaction.
IntActiQ8BTW3. 3 interactions.
STRINGi10090.ENSMUSP00000111863.

Structurei

3D structure databases

ProteinModelPortaliQ8BTW3.
SMRiQ8BTW3. Positions 29-261.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the RNase PH family.Curated

Phylogenomic databases

eggNOGiCOG0689.
HOGENOMiHOG000229515.
HOVERGENiHBG057826.
InParanoidiQ8BTW3.
KOiK12587.
PhylomeDBiQ8BTW3.

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.
[Graphical view]
SUPFAMiSSF54211. SSF54211. 1 hit.
SSF55666. SSF55666. 1 hit.

Sequencei

Sequence statusi: Complete.

Q8BTW3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPGDHRRIRG PEESQPPQLY AAEDDETPAA RDPTRLRPVY ARAGLLSQAK
60 70 80 90 100
GSAYLEAGGT KVLCAVSGPR QAEGGERGSG PAGAGGEAPA ALRGRLLCDF
110 120 130 140 150
RRAPFSGRRR RAPQGGGGED RELGLALQEA LEPAVRLGRY PRAQLEVSAL
160 170 180 190 200
LLEDGGCALA AALTAAALAL ADAGVEMYDL VVGCGLSLTP GPSPTWLLDP
210 220 230 240 250
TRLEEEHSAA GLTVALMPVL NQVAGLLGSG EGGQTESWTD AVRLGLEGCQ
260 270
RLYPVLQQCL VRAARRRGAA APP
Length:273
Mass (Da):28,370
Last modified:February 28, 2003 - v1
Checksum:i6AC4310F46742B10
GO

Sequence cautioni

The sequence BAB28033.1 differs from that shown. Reason: Frameshift at position 79. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK012102 mRNA. Translation: BAB28033.1. Frameshift.
AK088532 mRNA. Translation: BAC40407.1.
BC116985 mRNA. Translation: AAI16986.1.
BC119082 mRNA. Translation: AAI19083.1.
RefSeqiNP_082550.1. NM_028274.4.
UniGeneiMm.24174.
Mm.334810.

Genome annotation databases

GeneIDi72544.
KEGGimmu:72544.
UCSCiuc009nlp.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK012102 mRNA. Translation: BAB28033.1. Frameshift.
AK088532 mRNA. Translation: BAC40407.1.
BC116985 mRNA. Translation: AAI16986.1.
BC119082 mRNA. Translation: AAI19083.1.
RefSeqiNP_082550.1. NM_028274.4.
UniGeneiMm.24174.
Mm.334810.

3D structure databases

ProteinModelPortaliQ8BTW3.
SMRiQ8BTW3. Positions 29-261.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi215428. 1 interaction.
IntActiQ8BTW3. 3 interactions.
STRINGi10090.ENSMUSP00000111863.

PTM databases

PhosphoSiteiQ8BTW3.

Proteomic databases

MaxQBiQ8BTW3.
PaxDbiQ8BTW3.
PRIDEiQ8BTW3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi72544.
KEGGimmu:72544.
UCSCiuc009nlp.1. mouse.

Organism-specific databases

CTDi118460.
MGIiMGI:1919794. Exosc6.

Phylogenomic databases

eggNOGiCOG0689.
HOGENOMiHOG000229515.
HOVERGENiHBG057826.
InParanoidiQ8BTW3.
KOiK12587.
PhylomeDBiQ8BTW3.

Enzyme and pathway databases

BRENDAi1.8.1.9. 3474.

Miscellaneous databases

NextBioi336459.
PROiQ8BTW3.
SOURCEiSearch...

Gene expression databases

CleanExiMM_EXOSC6.
GenevestigatoriQ8BTW3.

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.
[Graphical view]
SUPFAMiSSF54211. SSF54211. 1 hit.
SSF55666. SSF55666. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
    Tissue: Thymus.
  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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  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(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN IG CLASS-SWITCH RECOMBINATION.

Entry informationi

Entry nameiEXOS6_MOUSE
AccessioniPrimary (citable) accession number: Q8BTW3
Secondary accession number(s): Q9CSR7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 14, 2007
Last sequence update: February 28, 2003
Last modified: March 31, 2015
This is version 88 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.