DIS3_SCHPO
ID DIS3_SCHPO Reviewed; 970 AA.
AC P37202;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Exosome complex exonuclease dis3;
DE EC=3.1.13.-;
DE EC=3.1.26.-;
DE AltName: Full=Chromosome disjunction protein 3;
DE AltName: Full=Mitotic control protein dis3;
DE AltName: Full=Ribosomal RNA-processing protein 44;
GN Name=dis3; Synonyms=rrp44; ORFNames=SPBC26H8.10;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=972 / ATCC 24843;
RX PubMed=1944266; DOI=10.1128/mcb.11.12.5839-5847.1991;
RA Kinoshita N., Goebl M., Yanagida M.;
RT "The fission yeast dis3+ gene encodes a 110-kDa essential protein
RT implicated in mitotic control.";
RL Mol. Cell. Biol. 11:5839-5847(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP INTERACTION WITH SPI1 AND PIM1.
RX PubMed=8896453; DOI=10.1002/j.1460-2075.1996.tb00944.x;
RA Noguchi E., Hayashi N., Azuma Y., Seki T., Nakamura M., Nakashima N.,
RA Yanagida M., He X., Mueller U., Sazer S., Nishimoto T.;
RT "Dis3, implicated in mitotic control, binds directly to Ran and enhances
RT the GEF activity of RCC1.";
RL EMBO J. 15:5595-5605(1996).
RN [4]
RP INTERACTION WITH NED1.
RX PubMed=12376568; DOI=10.1242/jcs.00135;
RA Tange Y., Hirata A., Niwa O.;
RT "An evolutionarily conserved fission yeast protein, Ned1, implicated in
RT normal nuclear morphology and chromosome stability, interacts with Dis3,
RT Pim1/RCC1 and an essential nucleoporin.";
RL J. Cell Sci. 115:4375-4385(2002).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: Catalytic component of the RNA exosome complex which has
CC 3'->5' exoribonuclease activity and participates in a multitude of
CC cellular RNA processing and degradation events. In the nucleus, the RNA
CC exosome complex is involved in proper maturation of stable RNA species
CC such as rRNA, snRNA and snoRNA, in the elimination of RNA processing
CC by-products and non-coding 'pervasive' transcripts, such as antisense
CC RNA species and cryptic unstable transcripts (CUTs), and of mRNAs with
CC processing defects, thereby limiting or excluding their export to the
CC cytoplasm. In the cytoplasm, the RNA exosome complex is involved in
CC general mRNA turnover and in RNA surveillance pathways, preventing
CC translation of aberrant mRNAs. The catalytic inactive RNA exosome core
CC complex of 9 subunits (Exo-9) is proposed to play a pivotal role in the
CC binding and presentation of RNA for ribonucleolysis, and to serve as a
CC scaffold for the association with catalytic subunits and accessory
CC proteins or complexes. DIS3 has both 3'-5' exonuclease and endonuclease
CC activities. The exonuclease activity of DIS3 is down-regulated upon
CC association with Exo-9 possibly involving a conformational change in
CC the catalytic domain and threading of the RNA substrate through the
CC complex central channel. Structured substrates can be degraded if they
CC have a 3' single-stranded extension sufficiently long (such as 35 nt
CC poly(A)) to span the proposed complex inner RNA-binding path and to
CC reach the exonuclease site provided by dis3 (By similarity). Implicated
CC in mitotic control. Essential for cell division and spore germination.
CC May be involved in regulating protein dephosphorylation during mitosis.
CC {ECO:0000250, ECO:0000269|PubMed:1944266}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- SUBUNIT: Component of the RNA exosome complex. The catalytically
CC inactive RNA exosome core (Exo-9) complex which is believed to
CC associate with catalytic subunits dis3 and rrp6 in cytoplasmic- and
CC nuclear-specific RNA exosome complex forms. Exo-9 is formed by a
CC hexameric ring of RNase PH domain-containing subunits and peripheral S1
CC domain-containing components csl4, rrp4 and rrp40 located on the top of
CC the ring structure. dis3 associates at the respective bottom side with
CC Exo-9 (By similarity). Oligomer of dis3, pim1 and spi1. Interacts with
CC ned1. {ECO:0000250, ECO:0000269|PubMed:12376568,
CC ECO:0000269|PubMed:8896453}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus {ECO:0000269|PubMed:16823372,
CC ECO:0000269|PubMed:1944266}. Note=Abundant in the nucleus
CC (PubMed:1944266). {ECO:0000269|PubMed:1944266}.
CC -!- SIMILARITY: Belongs to the RNR ribonuclease family. {ECO:0000305}.
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DR EMBL; M74094; AAA35302.1; -; Genomic_DNA.
DR EMBL; CU329671; CAA21102.1; -; Genomic_DNA.
DR PIR; A41944; A41944.
DR RefSeq; NP_596653.1; NM_001022575.2.
DR AlphaFoldDB; P37202; -.
DR SMR; P37202; -.
DR BioGRID; 276926; 379.
DR IntAct; P37202; 3.
DR MINT; P37202; -.
DR STRING; 4896.SPBC26H8.10.1; -.
DR MaxQB; P37202; -.
DR PaxDb; P37202; -.
DR PRIDE; P37202; -.
DR EnsemblFungi; SPBC26H8.10.1; SPBC26H8.10.1:pep; SPBC26H8.10.
DR GeneID; 2540398; -.
DR KEGG; spo:SPBC26H8.10; -.
DR PomBase; SPBC26H8.10; dis3.
DR VEuPathDB; FungiDB:SPBC26H8.10; -.
DR eggNOG; KOG2102; Eukaryota.
DR HOGENOM; CLU_002333_5_0_1; -.
DR InParanoid; P37202; -.
DR OMA; VVKRNWR; -.
DR PhylomeDB; P37202; -.
DR BRENDA; 3.1.13.1; 5613.
DR Reactome; R-SPO-429958; mRNA decay by 3' to 5' exoribonuclease.
DR PRO; PR:P37202; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0000785; C:chromatin; IDA:PomBase.
DR GO; GO:0000177; C:cytoplasmic exosome (RNase complex); ISO:PomBase.
DR GO; GO:0000178; C:exosome (RNase complex); IDA:PomBase.
DR GO; GO:0000176; C:nuclear exosome (RNase complex); EXP:PomBase.
DR GO; GO:1990251; C:nuclear exosome focus; IDA:PomBase.
DR GO; GO:0005730; C:nucleolus; IDA:PomBase.
DR GO; GO:0005654; C:nucleoplasm; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0000175; F:3'-5'-exoribonuclease activity; IMP:PomBase.
DR GO; GO:0004519; F:endonuclease activity; IBA:GO_Central.
DR GO; GO:0004521; F:endoribonuclease activity; ISO:PomBase.
DR GO; GO:0004532; F:exoribonuclease activity; IDA:PomBase.
DR GO; GO:0004540; F:ribonuclease activity; IMP:PomBase.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0031267; F:small GTPase binding; IPI:PomBase.
DR GO; 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); ISO:PomBase.
DR GO; GO:0000465; P:exonucleolytic trimming to generate mature 5'-end of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); ISO:PomBase.
DR GO; GO:0070651; P:nonfunctional rRNA decay; ISO:PomBase.
DR GO; GO:0071031; P:nuclear mRNA surveillance of mRNA 3'-end processing; IMP:PomBase.
DR GO; GO:0071042; P:nuclear polyadenylation-dependent mRNA catabolic process; ISO:PomBase.
DR GO; GO:0071035; P:nuclear polyadenylation-dependent rRNA catabolic process; ISO:PomBase.
DR GO; GO:0071038; P:nuclear polyadenylation-dependent tRNA catabolic process; ISO:PomBase.
DR GO; GO:0071027; P:nuclear RNA surveillance; IMP:PomBase.
DR GO; GO:0070478; P:nuclear-transcribed mRNA catabolic process, 3'-5' exonucleolytic nonsense-mediated decay; ISO:PomBase.
DR GO; GO:0033621; P:nuclear-transcribed mRNA catabolic process, meiosis-specific transcripts; IMP:PomBase.
DR GO; GO:0070481; P:nuclear-transcribed mRNA catabolic process, non-stop decay; ISO:PomBase.
DR GO; GO:0006401; P:RNA catabolic process; IDA:PomBase.
DR GO; GO:0016075; P:rRNA catabolic process; IBA:GO_Central.
DR GO; GO:0030847; P:termination of RNA polymerase II transcription, exosome-dependent; IMP:PomBase.
DR Gene3D; 2.40.50.140; -; 1.
DR InterPro; IPR041505; Dis3_CSD2.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR029060; PIN-like_dom_sf.
DR InterPro; IPR002716; PIN_dom.
DR InterPro; IPR001900; RNase_II/R.
DR InterPro; IPR022966; RNase_II/R_CS.
DR InterPro; IPR033771; Rrp44_CSD1.
DR InterPro; IPR033770; RRP44_S1.
DR InterPro; IPR003029; S1_domain.
DR Pfam; PF17849; OB_Dis3; 1.
DR Pfam; PF13638; PIN_4; 1.
DR Pfam; PF00773; RNB; 1.
DR Pfam; PF17216; Rrp44_CSD1; 1.
DR Pfam; PF17215; Rrp44_S1; 1.
DR SMART; SM00670; PINc; 1.
DR SMART; SM00955; RNB; 1.
DR SUPFAM; SSF50249; SSF50249; 3.
DR SUPFAM; SSF88723; SSF88723; 1.
DR PROSITE; PS01175; RIBONUCLEASE_II; 1.
DR PROSITE; PS50126; S1; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Endonuclease; Exonuclease; Exosome; Hydrolase; Nuclease;
KW Nucleus; Reference proteome; RNA-binding; rRNA processing.
FT CHAIN 1..970
FT /note="Exosome complex exonuclease dis3"
FT /id="PRO_0000166421"
FT DOMAIN 83..198
FT /note="PINc"
FT DOMAIN 869..969
FT /note="S1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT REGION 1..74
FT /note="Not essential for function"
FT REGION 823..970
FT /note="Essential for function"
SQ SEQUENCE 970 AA; 110138 MW; 3802201244B18BAB CRC64;
MSTVSGLKRP QSSEKNHRDR VFVRATRGKV QKVVREQYLR NDIPCQSRAC PLCRSKLPKD
SRGNVLEPIL SEKPMFLEKF GHHYLIPDSN IFYHCIDALE HPNNFFDVII LQTVFSEISS
KSIPLYNRMK RLCQEKTKRF TPFSNEFFVD TFVERLDDES ANDRNDRAIR NAASWFASHL
ASLGIKIVLL TDDRENARLA AEQGIQVSTL KDYVQYLPDS EILLDMVSAI ADAIASKEQV
ESGTKNVYEL HWSMSRLLAC IKNGEVHKGL INISTYNYLE GSVVVPGYNK PVLVSGRENL
NRAVQGDIVC IQILPQDQWK TEAEEIADDD EDVVVSTAAE PDSARINDLE LITKRNAHPT
AKVVGILKRN WRPYVGHVDN ATIAQSKGGS QQTVLLTPMD RRVPKIRFRT RQAPRLVGRR
IVVAIDLWDA SSRYPEGHFV RDLGEMETKE AETEALLLEY DVQHRPFPKA VLDCLPEEGH
NWKVPADKTH PLWKNRKDFR DKLICSIDPP GCQDIDDALH ACVLPNGNYE VGVHIADVTH
FVKPNTSMDS EAASRGTTVY LVDKRIDMLP MLLGTDLCSL RPYVERFAFS CIWEMDENAN
IIKVHFTKSV IASKEAFSYA DAQARIDDQK MQDPLTQGMR VLLKLSKILK QKRMDEGALN
LASPEVRIQT DNETSDPMDV EIKQLLETNS LVEEFMLLAN ISVAQKIYDA FPQTAVLRRH
AAPPLTNFDS LQDILRVCKG MHLKCDTSKS LAKSLDECVD PKEPYFNTLL RILTTRCMLS
AEYFCSGTFA PPDFRHYGLA SPIYTHFTSP IRRYADVLAH RQLAAAIDYE TINPSLSDKS
RLIEICNGIN YRHRMAQMAG RASIEYYVGQ ALKGGVAEED AYVIKVFKNG FVVFIARFGL
EGIVYTKSLS SVLEPNVEYV EDEYKLNIEI RDQPKPQTVQ IQMFQQVRVR VTTVRDEHSG
KQKVQITLVY
