ID   DI3L1_MOUSE             Reviewed;        1053 AA.
AC   Q8C0S1; Q69Z56;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 2.
DT   27-MAR-2024, entry version 145.
DE   RecName: Full=DIS3-like exonuclease 1;
DE            EC=3.1.13.1 {ECO:0000250|UniProtKB:Q8TF46};
GN   Name=Dis3l; Synonyms=Kiaa1955;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Thymus;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT   The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
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 cytoplasm, the
CC       RNA exosome complex is involved in general mRNA turnover and
CC       specifically degrades inherently unstable mRNAs containing AU-rich
CC       elements (AREs) within their 3' untranslated regions, and in RNA
CC       surveillance pathways, preventing translation of aberrant mRNAs. It
CC       seems to be involved in degradation of histone mRNA.
CC       {ECO:0000250|UniProtKB:Q8TF46}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Exonucleolytic cleavage in the 3'- to 5'-direction to yield
CC         nucleoside 5'-phosphates.; EC=3.1.13.1;
CC         Evidence={ECO:0000250|UniProtKB:Q8TF46};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:Q8TF46};
CC   -!- SUBUNIT: Component of the RNA exosome complex. The catalytically
CC       inactive RNA exosome core (Exo-9) complex is believed to associate with
CC       catalytic subunits EXOSC10, and DIS3 or DIS3L in cytoplasmic- and
CC       nuclear-specific RNA exosome complex forms (By similarity).
CC       {ECO:0000250|UniProtKB:Q8TF46}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8TF46}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8C0S1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8C0S1-2; Sequence=VSP_030370;
CC   -!- SIMILARITY: Belongs to the RNR ribonuclease family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH56939.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAD32588.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AK173310; BAD32588.1; ALT_INIT; mRNA.
DR   EMBL; AK029974; BAC26710.1; -; mRNA.
DR   EMBL; BC056939; AAH56939.1; ALT_INIT; mRNA.
DR   CCDS; CCDS23280.1; -. [Q8C0S1-2]
DR   CCDS; CCDS52832.1; -. [Q8C0S1-1]
DR   RefSeq; NP_001001295.2; NM_001001295.2. [Q8C0S1-1]
DR   RefSeq; NP_001171255.1; NM_001177784.1. [Q8C0S1-2]
DR   RefSeq; NP_766107.1; NM_172519.3. [Q8C0S1-2]
DR   RefSeq; XP_006511045.1; XM_006510982.3. [Q8C0S1-2]
DR   AlphaFoldDB; Q8C0S1; -.
DR   SMR; Q8C0S1; -.
DR   BioGRID; 229452; 1.
DR   ComplexPortal; CPX-596; Cytoplasmic exosome complex, Dis3l variant.
DR   ComplexPortal; CPX-601; Cytoplasmic exosome complex, Dis3l-Exosc10 variant.
DR   STRING; 10090.ENSMUSP00000129772; -.
DR   PhosphoSitePlus; Q8C0S1; -.
DR   EPD; Q8C0S1; -.
DR   MaxQB; Q8C0S1; -.
DR   PaxDb; 10090-ENSMUSP00000113503; -.
DR   PeptideAtlas; Q8C0S1; -.
DR   ProteomicsDB; 279656; -. [Q8C0S1-1]
DR   ProteomicsDB; 279657; -. [Q8C0S1-2]
DR   Pumba; Q8C0S1; -.
DR   Antibodypedia; 26111; 161 antibodies from 22 providers.
DR   DNASU; 213550; -.
DR   Ensembl; ENSMUST00000068367.14; ENSMUSP00000063830.8; ENSMUSG00000032396.18. [Q8C0S1-2]
DR   Ensembl; ENSMUST00000113890.2; ENSMUSP00000109522.2; ENSMUSG00000032396.18. [Q8C0S1-2]
DR   Ensembl; ENSMUST00000120760.8; ENSMUSP00000113503.2; ENSMUSG00000032396.18. [Q8C0S1-2]
DR   Ensembl; ENSMUST00000168844.9; ENSMUSP00000129772.3; ENSMUSG00000032396.18. [Q8C0S1-1]
DR   GeneID; 213550; -.
DR   KEGG; mmu:213550; -.
DR   UCSC; uc009qbu.2; mouse. [Q8C0S1-1]
DR   AGR; MGI:2143272; -.
DR   CTD; 115752; -.
DR   MGI; MGI:2143272; Dis3l.
DR   VEuPathDB; HostDB:ENSMUSG00000032396; -.
DR   eggNOG; KOG2102; Eukaryota.
DR   GeneTree; ENSGT00530000063106; -.
DR   HOGENOM; CLU_002333_5_0_1; -.
DR   InParanoid; Q8C0S1; -.
DR   OMA; LPLHEWK; -.
DR   OrthoDB; 945235at2759; -.
DR   PhylomeDB; Q8C0S1; -.
DR   TreeFam; TF105755; -.
DR   BioGRID-ORCS; 213550; 11 hits in 76 CRISPR screens.
DR   PRO; PR:Q8C0S1; -.
DR   Proteomes; UP000000589; Chromosome 9.
DR   RNAct; Q8C0S1; Protein.
DR   Bgee; ENSMUSG00000032396; Expressed in spermatocyte and 205 other cell types or tissues.
DR   ExpressionAtlas; Q8C0S1; baseline and differential.
DR   GO; GO:0005813; C:centrosome; ISO:MGI.
DR   GO; GO:0000177; C:cytoplasmic exosome (RNase complex); ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0000175; F:3'-5'-RNA exonuclease activity; ISS:UniProtKB.
DR   GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR   GO; GO:0008859; F:exoribonuclease II activity; ISS:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006401; P:RNA catabolic process; ISO:MGI.
DR   GO; GO:0006396; P:RNA processing; ISO:MGI.
DR   GO; GO:0016075; P:rRNA catabolic process; ISO:MGI.
DR   CDD; cd09862; PIN_Rrp44-like; 1.
DR   Gene3D; 2.40.50.690; -; 1.
DR   Gene3D; 2.40.50.700; -; 1.
DR   Gene3D; 3.40.50.1010; 5'-nuclease; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   InterPro; IPR041505; Dis3_CSD2.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR001900; RNase_II/R.
DR   InterPro; IPR022966; RNase_II/R_CS.
DR   InterPro; IPR033771; Rrp44_CSD1.
DR   InterPro; IPR033770; RRP44_S1.
DR   PANTHER; PTHR23355:SF30; DIS3-LIKE EXONUCLEASE 1; 1.
DR   PANTHER; PTHR23355; RIBONUCLEASE; 1.
DR   Pfam; PF17849; OB_Dis3; 1.
DR   Pfam; PF00773; RNB; 1.
DR   Pfam; PF17216; Rrp44_CSD1; 1.
DR   Pfam; PF17215; Rrp44_S1; 1.
DR   SMART; SM00955; RNB; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 3.
DR   PROSITE; PS01175; RIBONUCLEASE_II; 1.
DR   Genevisible; Q8C0S1; MM.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; Exonuclease; Exosome; Hydrolase;
KW   Magnesium; Nuclease; Phosphoprotein; Reference proteome; RNA-binding.
FT   CHAIN           1..1053
FT                   /note="DIS3-like exonuclease 1"
FT                   /id="PRO_0000314811"
FT   REGION          306..332
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        308..322
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         989
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8TF46"
FT   VAR_SEQ         1..83
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_030370"
SQ   SEQUENCE   1053 AA;  120284 MW;  A60616AB9A904722 CRC64;
     MLQKREKVLL LRTFQGRTLR IVREHYLRPS VPCNSPLCPQ PAACRNDGKL LAAEVTHYVI
     PDWKVVQDYL EVLEFPELKG VIFMQTACQA VQHQRGRRQY NKLRNLLKDA RHDCVLFANE
     FQQHCYLPRE KGEAMEKWQT RSIYNSAVWY YHHCEDRMPI VMVTEDEEAI QKYGSETEGV
     FVISFKNYLD NFWPDLKAAH DLCDSILQSR RERETESQET HGKEYPEHLP LEVLEAGIKS
     GRYIQGILNV NKHRAQIEAF VRLHGASSKD SGLVSDILIH GSKARNRSIH GDVVVVEMLP
     KSEWKGRTAA LGENDSDDKA SGESPSEPMP TGRVVGILQK NWRDYVVTFP SKEEVQSQGK
     NAQKILVTPW DYRIPKIRIS TQQAEALQDF RVVVRIDSWE ATSVYPNGHF VRVLGRIGDL
     EGEIATILVE NSISVVPFSE AQMCEMPVNT PENPWKVSPK EEQERKDLRT THLVFSIDPK
     GCEDVDDTLS VRTLNNGNLE LGVHIADVTH FVAPNSYIDV EARTRATTYY LADRRYDMLP
     SILSADLCSL LGGVDRYAVS VMWELDKTSY EIKKVWYGRT IIRSAYKLFY EAAQELLDGN
     FSIVDDIPEL KALDKQSQQA KLEELVWAIG KLTDIARHIR AKRDRCGALE LEGVEVRVQL
     DDKKNIRDLI PKQPLEVHET VAECMILANH WVAKKIWESF PHQALLRQHP PPHQEFFSEL
     RECAKAKGFF IDTRSNKTLA DSLDSANDPK DPLVNKLLRS MATQAMSNAL YFSTGSCAEE
     EFHHYGLALD KYTHFTSPIR RYSDIVVHRL LMAAISKDKK MEIKENLFSN KNLEELCRHI
     NNRNRAAQRS QKQSTELFQC MYFKDRDAET EERCIADGVI YSIRTNGVLV FIPRFGIKGA
     AYLKNKDSLV ISCGPEGSSE WKPGSLQRSQ NKIISTTAGG QSVTFHLFDH VTVRISVQAS
     RCHSDTIRLE IVSNKPYMIP NTELCHQSSL LKSELVKEVT RSVEEAQLAQ EVKGKVIQEE
     HQEYCQTKGR SLYTLLEEIR DLALLDVSDS CAM
//