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Protein

Exosome complex exonuclease RRP44

Gene

Dis3

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

Functioni

Putative 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. DIS3 has both 3'-5' exonuclease and endonuclease activities (By similarity).By similarity

Cofactori

Mg2+By similarity, Mn2+By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Exonuclease, Hydrolase, Nuclease

Keywords - Biological processi

rRNA processing

Keywords - Ligandi

Magnesium, Manganese, RNA-binding

Enzyme and pathway databases

ReactomeiREACT_288807. Butyrate Response Factor 1 (BRF1) destabilizes mRNA.
REACT_291652. mRNA decay by 3' to 5' exoribonuclease.
REACT_300665. KSRP destabilizes mRNA.
REACT_307913. Tristetraprolin (TTP) destabilizes mRNA.

Names & Taxonomyi

Protein namesi
Recommended name:
Exosome complex exonuclease RRP44 (EC:3.1.13.-, EC:3.1.26.-)
Alternative name(s):
Protein DIS3 homolog
Ribosomal RNA-processing protein 44
Gene namesi
Name:Dis3
Synonyms:Kiaa1008, Rrp44
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 14

Organism-specific databases

MGIiMGI:1919912. Dis3.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Exosome, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 958958Exosome complex exonuclease RRP44PRO_0000314757Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei18 – 181N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9CSH3.
PaxDbiQ9CSH3.
PRIDEiQ9CSH3.

PTM databases

PhosphoSiteiQ9CSH3.

Expressioni

Gene expression databases

BgeeiQ9CSH3.
CleanExiMM_DIS3.
GenevestigatoriQ9CSH3.

Interactioni

Subunit structurei

Component of the RNA exosome complex. The catalytically inactive RNA exosome core (Exo-9) complex is believed to associate with catalytic subunits EXOSC10, and DIS3 or DIS3L in cytoplasmic- and nuclear-specific RNA exosome complex forms (By similarity).By similarity

Protein-protein interaction databases

BioGridi215499. 1 interaction.
IntActiQ9CSH3. 1 interaction.
MINTiMINT-8178486.

Structurei

3D structure databases

ProteinModelPortaliQ9CSH3.
SMRiQ9CSH3. Positions 10-911.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini64 – 182119PINcAdd
BLAST

Sequence similaritiesi

Belongs to the RNR ribonuclease family.Curated
Contains 1 PINc domain.Curated

Phylogenomic databases

eggNOGiCOG0557.
GeneTreeiENSGT00530000063106.
HOGENOMiHOG000191945.
HOVERGENiHBG059397.
InParanoidiQ9CSH3.
KOiK12585.
OMAiPWSITEK.
OrthoDBiEOG7KH9J1.
PhylomeDBiQ9CSH3.
TreeFamiTF105755.

Family and domain databases

Gene3Di3.40.50.1010. 1 hit.
InterProiIPR012340. NA-bd_OB-fold.
IPR002716. PIN_dom.
IPR029060. PIN_domain-like.
IPR022966. RNase_II/R_CS.
[Graphical view]
PfamiPF13638. PIN_4. 1 hit.
[Graphical view]
SMARTiSM00670. PINc. 1 hit.
[Graphical view]
SUPFAMiSSF50249. SSF50249. 4 hits.
SSF88723. SSF88723. 1 hit.
PROSITEiPS01175. RIBONUCLEASE_II. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9CSH3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLRSKTFLKK TRAGGVVKIV REHYLRDDIG CGAPACSACG GAHAGPALEL
60 70 80 90 100
QPRDQASSLC PWPHYLLPDT NVLLHQIDVL EHPAIRNVIV LQTVMQEVRN
110 120 130 140 150
RSAPIYKRIR DVTNNQEKHF YTFTNEHHKE TYIEQEQGEN ANDRNDRAIR
160 170 180 190 200
VAAKWYNEHL KRVAADSQLQ VILITNDRKN KEKAVQEGIP AFTCEEYVKS
210 220 230 240 250
LTANPELIDR LAYLSDEMNE IESGKIIFSE HLPLSKLQQG IKSGSYLQGT
260 270 280 290 300
FRASRENYLE ATVWIHGDKE EEKEILIQGI KHLNRAVHED IVAVELLPRS
310 320 330 340 350
QWVAPSSVVL DDEGQNEDDV EKDEERELLL KTAVSEKMLR PTGRVVGIIK
360 370 380 390 400
RNWRPYCGML SKSDIKESRR HLFTPADKRI PRIRIETRQA SALEGRRIIV
410 420 430 440 450
AIDGWPRNSR YPNGHFVKNL GDVGEKETET EVLLLEHDVP HQPFSQAVLS
460 470 480 490 500
FLPRMPWSIT EEDMKNREDL RHLCVCSVDP PGCTDIDDAL HCRELSNGNL
510 520 530 540 550
EVGVHIADVS HFIRPGNALD QESARRGTTV YLCEKRIDMV PELLSSNLCS
560 570 580 590 600
LRSNVDRLAF SCIWEMNHNA EILKTRFTKS VINSKASLTY AEAQMRIDSA
610 620 630 640 650
AMNDDITTSL RGLNQLAKIL KKGRIEKGAL TLSSPEIRFH MDSETHDPID
660 670 680 690 700
LQTKELRETN SMVEEFMLLA NISVAKKIHE EFSEHALLRK HPAPPPSNYD
710 720 730 740 750
ILVKAAKSKN LQIKTDTAKS LADSLDRAES PDFPYLNTLL RILATRCMMQ
760 770 780 790 800
AVYFCSGMDN DFHHYGLASP IYTHFTSPIR RYADIIVHRL LAVAIGADCT
810 820 830 840 850
YPELTDKHKL SDICKNLNFR HKMAQYAQRA SVAFHTQLFF KSKGIVSEEA
860 870 880 890 900
YILFVRKNAI VVLIPKYGLE GTVFFEEKDK PKPRLAYDDE IPSLRIEGTV
910 920 930 940 950
FHVFDKVKVK ITLDSSNLQH QKIRMALVEP QIPGINIPPN VADKALTAPG

GKKRKLEK
Length:958
Mass (Da):108,838
Last modified:January 15, 2008 - v4
Checksum:i31045737557AB4AE
GO

Sequence cautioni

The sequence BAC98069.1 differs from that shown.Incompletely spliced mRNA.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti586 – 5883ASL → VSV in BAC98069 (PubMed:14621295).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK012840 mRNA. Translation: BAB28503.3.
AK032091 mRNA. Translation: BAC27692.1.
AK129259 Transcribed RNA. Translation: BAC98069.1. Sequence problems.
CCDSiCCDS49555.1.
RefSeqiNP_082591.2. NM_028315.2.
UniGeneiMm.163339.

Genome annotation databases

EnsembliENSMUST00000042471; ENSMUSP00000041906; ENSMUSG00000033166.
GeneIDi72662.
KEGGimmu:72662.
UCSCiuc007uuw.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK012840 mRNA. Translation: BAB28503.3.
AK032091 mRNA. Translation: BAC27692.1.
AK129259 Transcribed RNA. Translation: BAC98069.1. Sequence problems.
CCDSiCCDS49555.1.
RefSeqiNP_082591.2. NM_028315.2.
UniGeneiMm.163339.

3D structure databases

ProteinModelPortaliQ9CSH3.
SMRiQ9CSH3. Positions 10-911.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi215499. 1 interaction.
IntActiQ9CSH3. 1 interaction.
MINTiMINT-8178486.

PTM databases

PhosphoSiteiQ9CSH3.

Proteomic databases

MaxQBiQ9CSH3.
PaxDbiQ9CSH3.
PRIDEiQ9CSH3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000042471; ENSMUSP00000041906; ENSMUSG00000033166.
GeneIDi72662.
KEGGimmu:72662.
UCSCiuc007uuw.1. mouse.

Organism-specific databases

CTDi22894.
MGIiMGI:1919912. Dis3.
RougeiSearch...

Phylogenomic databases

eggNOGiCOG0557.
GeneTreeiENSGT00530000063106.
HOGENOMiHOG000191945.
HOVERGENiHBG059397.
InParanoidiQ9CSH3.
KOiK12585.
OMAiPWSITEK.
OrthoDBiEOG7KH9J1.
PhylomeDBiQ9CSH3.
TreeFamiTF105755.

Enzyme and pathway databases

ReactomeiREACT_288807. Butyrate Response Factor 1 (BRF1) destabilizes mRNA.
REACT_291652. mRNA decay by 3' to 5' exoribonuclease.
REACT_300665. KSRP destabilizes mRNA.
REACT_307913. Tristetraprolin (TTP) destabilizes mRNA.

Miscellaneous databases

NextBioi336687.
PROiQ9CSH3.
SOURCEiSearch...

Gene expression databases

BgeeiQ9CSH3.
CleanExiMM_DIS3.
GenevestigatoriQ9CSH3.

Family and domain databases

Gene3Di3.40.50.1010. 1 hit.
InterProiIPR012340. NA-bd_OB-fold.
IPR002716. PIN_dom.
IPR029060. PIN_domain-like.
IPR022966. RNase_II/R_CS.
[Graphical view]
PfamiPF13638. PIN_4. 1 hit.
[Graphical view]
SMARTiSM00670. PINc. 1 hit.
[Graphical view]
SUPFAMiSSF50249. SSF50249. 4 hits.
SSF88723. SSF88723. 1 hit.
PROSITEiPS01175. RIBONUCLEASE_II. 1 hit.
[Graphical view]
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] OF 1-267 AND 272-958.
    Strain: C57BL/6J.
    Tissue: Medulla oblongata.
  2. "Prediction of the coding sequences of mouse homologues of KIAA gene: III. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Nagase T., Ohara O., Koga H.
    DNA Res. 10:167-180(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 131-588.
    Tissue: Embryonic tail.

Entry informationi

Entry nameiRRP44_MOUSE
AccessioniPrimary (citable) accession number: Q9CSH3
Secondary accession number(s): Q6ZQ07, Q8C074
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 15, 2008
Last modified: May 27, 2015
This is version 98 of the entry and version 4 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.