Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9CSH3 (RRP44_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 88. 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 exonuclease RRP44

EC=3.1.13.-
EC=3.1.26.-
Alternative name(s):
Protein DIS3 homolog
Ribosomal RNA-processing protein 44
Gene names
Name:Dis3
Synonyms:Kiaa1008, Rrp44
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length958 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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.

Cofactor

Magnesium or manganese By similarity.

Subunit structure

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.

Subcellular location

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

Sequence similarities

Belongs to the RNR ribonuclease family.

Contains 1 PINc domain.

Sequence caution

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 958958Exosome complex exonuclease RRP44
PRO_0000314757

Regions

Domain64 – 182119PINc

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue181N6-acetyllysine By similarity

Experimental info

Sequence conflict586 – 5883ASL → VSV in BAC98069. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9CSH3 [UniParc].

Last modified January 15, 2008. Version 4.
Checksum: 31045737557AB4AE

FASTA958108,838
        10         20         30         40         50         60 
MLRSKTFLKK TRAGGVVKIV REHYLRDDIG CGAPACSACG GAHAGPALEL QPRDQASSLC 

        70         80         90        100        110        120 
PWPHYLLPDT NVLLHQIDVL EHPAIRNVIV LQTVMQEVRN RSAPIYKRIR DVTNNQEKHF 

       130        140        150        160        170        180 
YTFTNEHHKE TYIEQEQGEN ANDRNDRAIR VAAKWYNEHL KRVAADSQLQ VILITNDRKN 

       190        200        210        220        230        240 
KEKAVQEGIP AFTCEEYVKS LTANPELIDR LAYLSDEMNE IESGKIIFSE HLPLSKLQQG 

       250        260        270        280        290        300 
IKSGSYLQGT FRASRENYLE ATVWIHGDKE EEKEILIQGI KHLNRAVHED IVAVELLPRS 

       310        320        330        340        350        360 
QWVAPSSVVL DDEGQNEDDV EKDEERELLL KTAVSEKMLR PTGRVVGIIK RNWRPYCGML 

       370        380        390        400        410        420 
SKSDIKESRR HLFTPADKRI PRIRIETRQA SALEGRRIIV AIDGWPRNSR YPNGHFVKNL 

       430        440        450        460        470        480 
GDVGEKETET EVLLLEHDVP HQPFSQAVLS FLPRMPWSIT EEDMKNREDL RHLCVCSVDP 

       490        500        510        520        530        540 
PGCTDIDDAL HCRELSNGNL EVGVHIADVS HFIRPGNALD QESARRGTTV YLCEKRIDMV 

       550        560        570        580        590        600 
PELLSSNLCS LRSNVDRLAF SCIWEMNHNA EILKTRFTKS VINSKASLTY AEAQMRIDSA 

       610        620        630        640        650        660 
AMNDDITTSL RGLNQLAKIL KKGRIEKGAL TLSSPEIRFH MDSETHDPID LQTKELRETN 

       670        680        690        700        710        720 
SMVEEFMLLA NISVAKKIHE EFSEHALLRK HPAPPPSNYD ILVKAAKSKN LQIKTDTAKS 

       730        740        750        760        770        780 
LADSLDRAES PDFPYLNTLL RILATRCMMQ AVYFCSGMDN DFHHYGLASP IYTHFTSPIR 

       790        800        810        820        830        840 
RYADIIVHRL LAVAIGADCT YPELTDKHKL SDICKNLNFR HKMAQYAQRA SVAFHTQLFF 

       850        860        870        880        890        900 
KSKGIVSEEA YILFVRKNAI VVLIPKYGLE GTVFFEEKDK PKPRLAYDDE IPSLRIEGTV 

       910        920        930        940        950 
FHVFDKVKVK ITLDSSNLQH QKIRMALVEP QIPGINIPPN VADKALTAPG GKKRKLEK 

« Hide

References

[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK012840 mRNA. Translation: BAB28503.3.
AK032091 mRNA. Translation: BAC27692.1.
AK129259 Transcribed RNA. Translation: BAC98069.1. Sequence problems.
CCDSCCDS49555.1.
RefSeqNP_082591.2. NM_028315.2.
UniGeneMm.163339.

3D structure databases

ProteinModelPortalQ9CSH3.
SMRQ9CSH3. Positions 10-911.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid215499. 1 interaction.
IntActQ9CSH3. 1 interaction.
MINTMINT-8178486.

PTM databases

PhosphoSiteQ9CSH3.

Proteomic databases

MaxQBQ9CSH3.
PaxDbQ9CSH3.
PRIDEQ9CSH3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000042471; ENSMUSP00000041906; ENSMUSG00000033166.
GeneID72662.
KEGGmmu:72662.
UCSCuc007uuw.1. mouse.

Organism-specific databases

CTD22894.
MGIMGI:1919912. Dis3.
RougeSearch...

Phylogenomic databases

eggNOGCOG0557.
GeneTreeENSGT00530000063106.
HOGENOMHOG000191945.
HOVERGENHBG059397.
InParanoidQ9CSH3.
KOK12585.
OMAENANDRN.
OrthoDBEOG7KH9J1.
PhylomeDBQ9CSH3.
TreeFamTF105755.

Gene expression databases

BgeeQ9CSH3.
CleanExMM_DIS3.
GenevestigatorQ9CSH3.

Family and domain databases

Gene3D3.40.50.1010. 1 hit.
InterProIPR012340. NA-bd_OB-fold.
IPR002716. PIN_dom.
IPR029060. PIN_domain-like.
IPR022966. RNase_II/R_CS.
[Graphical view]
PfamPF13638. PIN_4. 1 hit.
[Graphical view]
SMARTSM00670. PINc. 1 hit.
[Graphical view]
SUPFAMSSF50249. SSF50249. 4 hits.
SSF88723. SSF88723. 1 hit.
PROSITEPS01175. RIBONUCLEASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio336687.
PROQ9CSH3.
SOURCESearch...

Entry information

Entry nameRRP44_MOUSE
AccessionPrimary (citable) accession number: Q9CSH3
Secondary accession number(s): Q6ZQ07, Q8C074
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 15, 2008
Last modified: July 9, 2014
This is version 88 of the entry and version 4 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