CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-011563
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Exosome complex exonuclease DIS3 
Protein Synonyms/Alias
 Chromosome disjunction protein 3; Ribosomal RNA-processing protein 44 
Gene Name
 DIS3 
Gene Synonyms/Alias
 RRP44; YOL021C; O2197 
Created Date
 July 27, 2013 
Organism
 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 
NCBI Taxa ID
 559292 
Lysine Modification
Position
Peptide
Type
References
375KQRRLLAKDAMIAQRacetylation[1]
Reference
 [1] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae.
 Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C.
 Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [PMID: 22865919
Functional Description
 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. 
Sequence Annotation
 DOMAIN 904 1001 S1 motif.
 REGION 1 235 Endoribonuclease.  
Keyword
 3D-structure; Complete proteome; Cytoplasm; Endonuclease; Exonuclease; Exosome; Hydrolase; Mitochondrion; Nuclease; Nucleus; Reference proteome; RNA-binding; rRNA processing. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1001 AA 
Protein Sequence
MSVPAIAPRR KRLADGLSVT QKVFVRSRNG GATKIVREHY LRSDIPCLSR SCTKCPQIVV 60
PDAQNELPKF ILSDSPLELS APIGKHYVVL DTNVVLQAID LLENPNCFFD VIVPQIVLDE 120
VRNKSYPVYT RLRTLCRDSD DHKRFIVFHN EFSEHTFVER LPNETINDRN DRAIRKTCQW 180
YSEHLKPYDI NVVLVTNDRL NREAATKEVE SNIITKSLVQ YIELLPNADD IRDSIPQMDS 240
FDKDLERDTF SDFTFPEYYS TARVMGGLKN GVLYQGNIQI SEYNFLEGSV SLPRFSKPVL 300
IVGQKNLNRA FNGDQVIVEL LPQSEWKAPS SIVLDSEHFD VNDNPDIEAG DDDDNNESSS 360
NTTVISDKQR RLLAKDAMIA QRSKKIQPTA KVVYIQRRSW RQYVGQLAPS SVDPQSSSTQ 420
NVFVILMDKC LPKVRIRTRR AAELLDKRIV ISIDSWPTTH KYPLGHFVRD LGTIESAQAE 480
TEALLLEHDV EYRPFSKKVL ECLPAEGHDW KAPTKLDDPE AVSKDPLLTK RKDLRDKLIC 540
SIDPPGCVDI DDALHAKKLP NGNWEVGVHI ADVTHFVKPG TALDAEGAAR GTSVYLVDKR 600
IDMLPMLLGT DLCSLKPYVD RFAFSVIWEL DDSANIVNVN FMKSVIRSRE AFSYEQAQLR 660
IDDKTQNDEL TMGMRALLKL SVKLKQKRLE AGALNLASPE VKVHMDSETS DPNEVEIKKL 720
LATNSLVEEF MLLANISVAR KIYDAFPQTA MLRRHAAPPS TNFEILNEML NTRKNMSISL 780
ESSKALADSL DRCVDPEDPY FNTLVRIMST RCMMAAQYFY SGAYSYPDFR HYGLAVDIYT 840
HFTSPIRRYC DVVAHRQLAG AIGYEPLSLT HRDKNKMDMI CRNINRKHRN AQFAGRASIE 900
YYVGQVMRNN ESTETGYVIK VFNNGIVVLV PKFGVEGLIR LDNLTEDPNS AAFDEVEYKL 960
TFVPTNSDKP RDVYVFDKVE VQVRSVMDPI TSKRKAELLL K 1001 
Gene Ontology
 GO:0000177; C:cytoplasmic exosome (RNase complex); IDA:SGD.
 GO:0005739; C:mitochondrion; IDA:SGD.
 GO:0000176; C:nuclear exosome (RNase complex); IDA:SGD.
 GO:0005730; C:nucleolus; IDA:SGD.
 GO:0000175; F:3'-5'-exoribonuclease activity; IDA:SGD.
 GO:0004521; F:endoribonuclease activity; IDA:SGD.
 GO:0000049; F:tRNA binding; IDA:SGD.
 GO:0000467; P:exonucleolytic trimming to generate mature 3'-end of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
 GO:0070651; P:nonfunctional rRNA decay; IMP:SGD.
 GO:0071028; P:nuclear mRNA surveillance; IMP:SGD.
 GO:0071039; P:nuclear polyadenylation-dependent CUT catabolic process; IMP:SGD.
 GO:0071042; P:nuclear polyadenylation-dependent mRNA catabolic process; IC:SGD.
 GO:0071035; P:nuclear polyadenylation-dependent rRNA catabolic process; IMP:SGD.
 GO:0071038; P:nuclear polyadenylation-dependent tRNA catabolic process; IDA:SGD.
 GO:0070478; P:nuclear-transcribed mRNA catabolic process, 3'-5' exonucleolytic nonsense-mediated decay; IC:SGD.
 GO:0070481; P:nuclear-transcribed mRNA catabolic process, non-stop decay; IC:SGD.
 GO:0071051; P:polyadenylation-dependent snoRNA 3'-end processing; IC:SGD. 
Interpro
 IPR002716; PIN_dom.
 IPR006596; PINc_nuc-bd.
 IPR003029; Rbsml_prot_S1_RNA-bd_dom.
 IPR022967; RNA-binding_domain_S1.
 IPR001900; RNase_II/R.
 IPR022966; RNase_II/R_CS. 
Pfam
 PF13638; PIN_4
 PF00773; RNB 
SMART
 SM00670; PINc
 SM00955; RNB
 SM00316; S1 
PROSITE
 PS01175; RIBONUCLEASE_II
 PS50126; S1 
PRINTS