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UniProtKB - Q08162 (RRP44_YEAST)

Protein

Exosome complex exonuclease DIS3

Gene

DIS3

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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 cryptic unstable transcripts (CUTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and in RNA surveillance pathways, preventing translation of aberrant mRNAs. 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. DIS3 has both 3'-5' exonuclease and endonuclease activities. The exonuclease activity of DIS3 is down-regulated upon association with Exo-9 possibly involving a conformational change in the catalytic domain and threading of the RNA substrate through the complex central channel. Structured substrates can be degraded if they have a 3' single-stranded extension sufficiently long (such as 35 nt poly(A)) to span the proposed complex inner RNA-binding path and to reach the exonuclease site provided by DIS3. Plays a role in mitotic control.3 Publications

Miscellaneous

Present with 606 molecules/cell in log phase SD medium.1 Publication
Mn2+ doesn't support the hydrolytic activity. Activity is KCl or NaCl dependent and activity is slightly increased in the presence of reducing agents such as DTT or beta-mercaptoethanol and doesn't vary notably between pH 6.8 and 8.8.

Caution

It was originally thought that there are multiple subunits in the exosome that have exonuclease activity but it was later shown (PubMed:17173052 and PubMed:17174896) that only this DIS3/RRP44 subunit of the exosome core has this activity.1 Publication

Cofactori

Mg2+1 Publication

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

Keywordsi

Molecular functionEndonuclease, Exonuclease, Hydrolase, Nuclease, RNA-binding
Biological processrRNA processing

Enzyme and pathway databases

BioCyciYEAST:G3O-33437-MONOMER
BRENDAi3.1.13.1 984
ReactomeiR-SCE-429958 mRNA decay by 3' to 5' exoribonuclease

Names & Taxonomyi

Protein namesi
Recommended name:
Exosome complex exonuclease DIS3 (EC:3.1.13.-, EC:3.1.26.-)
Alternative name(s):
Chromosome disjunction protein 3
Ribosomal RNA-processing protein 44
Gene namesi
Name:DIS3
Synonyms:RRP44
Ordered Locus Names:YOL021C
ORF Names:O2197
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›
Proteomesi
  • UP000002311 Componenti: Chromosome XV

Organism-specific databases

EuPathDBiFungiDB:YOL021C
SGDiS000005381 DIS3

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Exosome, Mitochondrion, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi47C → S: Slow growth; when associated with S-52 and S-55. 1 Publication1
Mutagenesisi52C → S: Slow growth; when associated with S-47 and S-55. 1 Publication1
Mutagenesisi55C → S: Slow growth; when associated with S-47 and S-52. 1 Publication1
Mutagenesisi171D → A: Abolishes endoribonucleolytic activity; no effect on growth. No growth; when associated with N-551. 1 Publication1
Mutagenesisi198D → A: Abolishes endoribonucleolytic activity; no effect on growth. No growth; when associated with N-551. 1 Publication1
Mutagenesisi551D → N: Exoribonucleolytic activity abolished. Accumulation of partially processed 5.8S rRNA and partially degraded 5' ETS. No growth; when associated with A-171. No growth; when associated with A-198. 3 Publications1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001664231 – 1001Exosome complex exonuclease DIS3Add BLAST1001

Proteomic databases

MaxQBiQ08162
PaxDbiQ08162
PRIDEiQ08162

Interactioni

Subunit structurei

Component of the RNA exosome complex. The catalytically inactive RNA exosome core (Exo-9) complex which is believed to associate with catalytic subunits DIS3 and RRP6 in cytoplasmic- and nuclear-specific RNA exosome complex forms. Exo-9 is formed by a hexameric ring of RNase PH domain-containing subunits and peripheral S1 domain-containing components CSL4, RRP4 and RRP40 located on the top of the ring structure. DIS3 associates at the respective bottom side with Exo-9. Interacts with GSP1.7 Publications

Binary interactionsi

Protein-protein interaction databases

BioGridi34381, 220 interactors
ComplexPortaliCPX-599 Nuclear/nucleolar exosome complex, DIS3-RRP6 variant
CPX-603 Cytoplasmic exosome complex, DIS3 variant
DIPiDIP-2355N
IntActiQ08162, 23 interactors
MINTiQ08162
STRINGi4932.YOL021C

Structurei

Secondary structure

11001
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliQ08162
SMRiQ08162
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ08162

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini904 – 1001S1 motifPROSITE-ProRule annotationAdd BLAST98

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 235EndoribonucleaseAdd BLAST235

Sequence similaritiesi

Belongs to the RNR ribonuclease family.Curated

Phylogenomic databases

GeneTreeiENSGT00530000063106
HOGENOMiHOG000191945
InParanoidiQ08162
KOiK12585
OMAiWRQYVGH
OrthoDBiEOG092C0VEN

Family and domain databases

InterProiView protein in InterPro
IPR012340 NA-bd_OB-fold
IPR029060 PIN-like_dom_sf
IPR002716 PIN_dom
IPR022966 RNase_II/R_CS
IPR033771 Rrp44_CSD1
IPR033770 RRP44_S1
IPR022967 S1_dom
IPR003029 S1_domain
PfamiView protein in Pfam
PF13638 PIN_4, 1 hit
PF17216 Rrp44_CSD1, 1 hit
PF17215 Rrp44_S1, 1 hit
SMARTiView protein in SMART
SM00670 PINc, 1 hit
SM00316 S1, 1 hit
SUPFAMiSSF50249 SSF50249, 4 hits
SSF88723 SSF88723, 1 hit
PROSITEiView protein in PROSITE
PS01175 RIBONUCLEASE_II, 1 hit
PS50126 S1, 1 hit

Sequencei

Sequence statusi: Complete.

Q08162-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSVPAIAPRR KRLADGLSVT QKVFVRSRNG GATKIVREHY LRSDIPCLSR 
        60         70         80         90        100
SCTKCPQIVV PDAQNELPKF ILSDSPLELS APIGKHYVVL DTNVVLQAID 
       110        120        130        140        150
LLENPNCFFD VIVPQIVLDE VRNKSYPVYT RLRTLCRDSD DHKRFIVFHN 
       160        170        180        190        200
EFSEHTFVER LPNETINDRN DRAIRKTCQW YSEHLKPYDI NVVLVTNDRL 
       210        220        230        240        250
NREAATKEVE SNIITKSLVQ YIELLPNADD IRDSIPQMDS FDKDLERDTF 
       260        270        280        290        300
SDFTFPEYYS TARVMGGLKN GVLYQGNIQI SEYNFLEGSV SLPRFSKPVL 
       310        320        330        340        350
IVGQKNLNRA FNGDQVIVEL LPQSEWKAPS SIVLDSEHFD VNDNPDIEAG 
       360        370        380        390        400
DDDDNNESSS NTTVISDKQR RLLAKDAMIA QRSKKIQPTA KVVYIQRRSW 
       410        420        430        440        450
RQYVGQLAPS SVDPQSSSTQ NVFVILMDKC LPKVRIRTRR AAELLDKRIV 
       460        470        480        490        500
ISIDSWPTTH KYPLGHFVRD LGTIESAQAE TEALLLEHDV EYRPFSKKVL 
       510        520        530        540        550
ECLPAEGHDW KAPTKLDDPE AVSKDPLLTK RKDLRDKLIC SIDPPGCVDI 
       560        570        580        590        600
DDALHAKKLP NGNWEVGVHI ADVTHFVKPG TALDAEGAAR GTSVYLVDKR 
       610        620        630        640        650
IDMLPMLLGT DLCSLKPYVD RFAFSVIWEL DDSANIVNVN FMKSVIRSRE 
       660        670        680        690        700
AFSYEQAQLR IDDKTQNDEL TMGMRALLKL SVKLKQKRLE AGALNLASPE 
       710        720        730        740        750
VKVHMDSETS DPNEVEIKKL LATNSLVEEF MLLANISVAR KIYDAFPQTA 
       760        770        780        790        800
MLRRHAAPPS TNFEILNEML NTRKNMSISL ESSKALADSL DRCVDPEDPY 
       810        820        830        840        850
FNTLVRIMST RCMMAAQYFY SGAYSYPDFR HYGLAVDIYT HFTSPIRRYC 
       860        870        880        890        900
DVVAHRQLAG AIGYEPLSLT HRDKNKMDMI CRNINRKHRN AQFAGRASIE 
       910        920        930        940        950
YYVGQVMRNN ESTETGYVIK VFNNGIVVLV PKFGVEGLIR LDNLTEDPNS 
       960        970        980        990       1000
AAFDEVEYKL TFVPTNSDKP RDVYVFDKVE VQVRSVMDPI TSKRKAELLL 

K
Length:1,001
Mass (Da):113,707
Last modified:November 1, 1997 - v1
Checksum:i00DD31BD2D6904F4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D76430 Genomic DNA Translation: BAA11176.1
Z74763 Genomic DNA Translation: CAA99021.1
BK006948 Genomic DNA Translation: DAA10760.1
PIRiS66704
RefSeqiNP_014621.1, NM_001183275.1

Genome annotation databases

EnsemblFungiiYOL021C; YOL021C; YOL021C
GeneIDi854138
KEGGisce:YOL021C

Similar proteinsi

Entry informationi

Entry nameiRRP44_YEAST
AccessioniPrimary (citable) accession number: Q08162
Secondary accession number(s): D6W244
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: September 12, 2018
This is version 160 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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