DI3L1_HUMAN
ID DI3L1_HUMAN Reviewed; 1054 AA.
AC Q8TF46; Q8N1N8; Q8WTU9; Q96CM7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=DIS3-like exonuclease 1;
DE EC=3.1.13.-;
GN Name=DIS3L; Synonyms=DIS3L1, KIAA1955;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=11853319; DOI=10.1093/dnares/8.6.319;
RA Nagase T., Kikuno R., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XXII. The
RT complete sequences of 50 new cDNA clones which code for large proteins.";
RL DNA Res. 8:319-327(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT GLY-614.
RC TISSUE=Tongue;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND VARIANT GLY-614.
RC TISSUE=Kidney, and Muscle;
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 [6]
RP ASSOCIATION WITH THE RNA EXOSOME COMPLEX, IDENTIFICATION BY MASS
RP SPECTROMETRY, FUNCTION, COFACTOR, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP ASP-486.
RX PubMed=20531386; DOI=10.1038/emboj.2010.121;
RA Tomecki R., Kristiansen M.S., Lykke-Andersen S., Chlebowski A.,
RA Larsen K.M., Szczesny R.J., Drazkowska K., Pastula A., Andersen J.S.,
RA Stepien P.P., Dziembowski A., Jensen T.H.;
RT "The human core exosome interacts with differentially localized processive
RT RNases: hDIS3 and hDIS3L.";
RL EMBO J. 29:2342-2357(2010).
RN [7]
RP FUNCTION, COFACTOR, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ASP-62;
RP ASP-166 AND ASP-486.
RX PubMed=20531389; DOI=10.1038/emboj.2010.122;
RA Staals R.H., Bronkhorst A.W., Schilders G., Slomovic S., Schuster G.,
RA Heck A.J., Raijmakers R., Pruijn G.J.;
RT "Dis3-like 1: a novel exoribonuclease associated with the human exosome.";
RL EMBO J. 29:2358-2367(2010).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-989, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
CC -!- FUNCTION: Putative cytoplasm-specific catalytic component of the RNA
CC exosome complex which has 3'->5' exoribonuclease activity and
CC participates in a multitude of cellular RNA processing and degradation
CC events. In the cytoplasm, the RNA exosome complex is involved in
CC general mRNA turnover and specifically degrades inherently unstable
CC mRNAs containing AU-rich elements (AREs) within their 3' untranslated
CC regions, and in RNA surveillance pathways, preventing translation of
CC aberrant mRNAs. It seems to be involved in degradation of histone mRNA.
CC {ECO:0000269|PubMed:20531386, ECO:0000269|PubMed:20531389}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:20531386, ECO:0000269|PubMed:20531389};
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.
CC -!- INTERACTION:
CC Q8TF46; Q9NQT5: EXOSC3; NbExp=5; IntAct=EBI-3672244, EBI-371866;
CC Q8TF46-1; Q13868: EXOSC2; NbExp=2; IntAct=EBI-3895807, EBI-301735;
CC Q8TF46-4; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-25933135, EBI-5235340;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20531386,
CC ECO:0000269|PubMed:20531389}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q8TF46-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8TF46-2; Sequence=VSP_030366;
CC Name=3;
CC IsoId=Q8TF46-3; Sequence=VSP_030368, VSP_030369;
CC Name=4;
CC IsoId=Q8TF46-4; Sequence=VSP_030367;
CC -!- SIMILARITY: Belongs to the RNR ribonuclease family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB85541.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB075835; BAB85541.1; ALT_INIT; mRNA.
DR EMBL; AK095407; BAC04542.1; -; mRNA.
DR EMBL; AC055855; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471082; EAW77759.1; -; Genomic_DNA.
DR EMBL; BC014124; AAH14124.2; -; mRNA.
DR EMBL; BC022089; AAH22089.1; -; mRNA.
DR CCDS; CCDS10214.1; -. [Q8TF46-4]
DR CCDS; CCDS45286.1; -. [Q8TF46-1]
DR RefSeq; NP_001137160.1; NM_001143688.2. [Q8TF46-1]
DR RefSeq; NP_001310865.1; NM_001323936.1. [Q8TF46-4]
DR RefSeq; NP_001310867.1; NM_001323938.1. [Q8TF46-2]
DR RefSeq; NP_001310868.1; NM_001323939.1. [Q8TF46-2]
DR RefSeq; NP_001310870.1; NM_001323941.1. [Q8TF46-2]
DR RefSeq; NP_001310874.1; NM_001323945.1. [Q8TF46-4]
DR RefSeq; NP_001310875.1; NM_001323946.1. [Q8TF46-2]
DR RefSeq; NP_588616.1; NM_133375.4. [Q8TF46-4]
DR AlphaFoldDB; Q8TF46; -.
DR SMR; Q8TF46; -.
DR BioGRID; 125453; 48.
DR ComplexPortal; CPX-592; Cytoplasmic exosome complex, DIS3L variant.
DR ComplexPortal; CPX-600; Cytoplasmic exosome complex, DIS3L-EXOSC10 variant.
DR CORUM; Q8TF46; -.
DR IntAct; Q8TF46; 26.
DR MINT; Q8TF46; -.
DR STRING; 9606.ENSP00000321711; -.
DR iPTMnet; Q8TF46; -.
DR PhosphoSitePlus; Q8TF46; -.
DR BioMuta; DIS3L; -.
DR DMDM; 166201903; -.
DR EPD; Q8TF46; -.
DR jPOST; Q8TF46; -.
DR MassIVE; Q8TF46; -.
DR MaxQB; Q8TF46; -.
DR PaxDb; Q8TF46; -.
DR PeptideAtlas; Q8TF46; -.
DR PRIDE; Q8TF46; -.
DR ProteomicsDB; 74555; -. [Q8TF46-1]
DR ProteomicsDB; 74556; -. [Q8TF46-2]
DR ProteomicsDB; 74557; -. [Q8TF46-3]
DR ProteomicsDB; 74558; -. [Q8TF46-4]
DR Antibodypedia; 26111; 139 antibodies from 21 providers.
DR DNASU; 115752; -.
DR Ensembl; ENST00000319194.9; ENSP00000321583.5; ENSG00000166938.13. [Q8TF46-4]
DR Ensembl; ENST00000319212.9; ENSP00000321711.4; ENSG00000166938.13. [Q8TF46-1]
DR GeneID; 115752; -.
DR KEGG; hsa:115752; -.
DR MANE-Select; ENST00000319212.9; ENSP00000321711.4; NM_001143688.3; NP_001137160.1.
DR UCSC; uc002app.4; human. [Q8TF46-1]
DR CTD; 115752; -.
DR DisGeNET; 115752; -.
DR GeneCards; DIS3L; -.
DR HGNC; HGNC:28698; DIS3L.
DR HPA; ENSG00000166938; Low tissue specificity.
DR MIM; 614183; gene.
DR neXtProt; NX_Q8TF46; -.
DR OpenTargets; ENSG00000166938; -.
DR PharmGKB; PA162383675; -.
DR VEuPathDB; HostDB:ENSG00000166938; -.
DR eggNOG; KOG2102; Eukaryota.
DR GeneTree; ENSGT00530000063106; -.
DR HOGENOM; CLU_002333_5_0_1; -.
DR InParanoid; Q8TF46; -.
DR OMA; WKVNPEE; -.
DR OrthoDB; 1104619at2759; -.
DR PhylomeDB; Q8TF46; -.
DR TreeFam; TF105755; -.
DR PathwayCommons; Q8TF46; -.
DR SignaLink; Q8TF46; -.
DR SIGNOR; Q8TF46; -.
DR BioGRID-ORCS; 115752; 23 hits in 1073 CRISPR screens.
DR ChiTaRS; DIS3L; human.
DR GeneWiki; DIS3L; -.
DR GenomeRNAi; 115752; -.
DR Pharos; Q8TF46; Tbio.
DR PRO; PR:Q8TF46; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q8TF46; protein.
DR Bgee; ENSG00000166938; Expressed in left ventricle myocardium and 186 other tissues.
DR ExpressionAtlas; Q8TF46; baseline and differential.
DR Genevisible; Q8TF46; HS.
DR GO; GO:0005813; C:centrosome; IDA:HPA.
DR GO; GO:0000177; C:cytoplasmic exosome (RNase complex); IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0000178; C:exosome (RNase complex); IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0000175; F:3'-5'-exoribonuclease activity; IDA:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006401; P:RNA catabolic process; IDA:ComplexPortal.
DR GO; GO:0006396; P:RNA processing; IDA:ComplexPortal.
DR GO; GO:0016075; P:rRNA catabolic process; IDA:UniProtKB.
DR Gene3D; 2.40.50.140; -; 1.
DR InterPro; IPR041505; Dis3_CSD2.
DR InterPro; IPR031192; DIS3L.
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; PTHR23355:SF30; 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; SSF50249; 3.
DR PROSITE; PS01175; RIBONUCLEASE_II; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Exonuclease; Exosome; Hydrolase;
KW Magnesium; Nuclease; Phosphoprotein; Reference proteome; RNA-binding.
FT CHAIN 1..1054
FT /note="DIS3-like exonuclease 1"
FT /id="PRO_0000314810"
FT MOD_RES 989
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..134
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11853319"
FT /id="VSP_030366"
FT VAR_SEQ 1..83
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_030367"
FT VAR_SEQ 735..750
FT /note="SNKTLADSLDNANDPH -> YSSFEGAEEWSGMLYI (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_030368"
FT VAR_SEQ 751..1054
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_030369"
FT VARIANT 518
FT /note="I -> V (in dbSNP:rs34668776)"
FT /id="VAR_038056"
FT VARIANT 614
FT /note="D -> G (in dbSNP:rs3803412)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_038057"
FT VARIANT 747
FT /note="N -> S (in dbSNP:rs17258507)"
FT /id="VAR_038058"
FT MUTAGEN 62
FT /note="D->N: No change of exonuclease activity."
FT /evidence="ECO:0000269|PubMed:20531389"
FT MUTAGEN 166
FT /note="D->N: No change of exonuclease activity."
FT /evidence="ECO:0000269|PubMed:20531389"
FT MUTAGEN 486
FT /note="D->N: Complete loss of exonuclease activity."
FT /evidence="ECO:0000269|PubMed:20531386,
FT ECO:0000269|PubMed:20531389"
SQ SEQUENCE 1054 AA; 120787 MW; B57B691CC25F65B8 CRC64;
MLQKREKVLL LRTFQGRTLR IVREHYLRPC VPCHSPLCPQ PAACSHDGKL LSSDVTHYVI
PDWKVVQDYL EILEFPELKG IIFMQTACQA VQHQRGRRQY NKLRNLLKDA RHDCILFANE
FQQCCYLPRE RGESMEKWQT RSIYNAAVWY YHHCQDRMPI VMVTEDEEAI QQYGSETEGV
FVITFKNYLD NFWPDLKAAH ELCDSILQSR RERENESQES HGKEYPEHLP LEVLEAGIKS
GRYIQGILNV NKHRAQIEAF VRLQGASSKD SDLVSDILIH GMKARNRSIH GDVVVVELLP
KNEWKGRTVA LCENDCDDKA SGESPSEPMP TGRVVGILQK NWRDYVVTFP SKEEVQSQGK
NAQKILVTPW DYRIPKIRIS TQQAETLQDF RVVVRIDSWE STSVYPNGHF VRVLGRIGDL
EGEIATILVE NSISVIPFSE AQMCEMPVNT PESPWKVSPE EEQKRKDLRK SHLVFSIDPK
GCEDVDDTLS VRTLNNGNLE LGVHIADVTH FVAPNSYIDI EARTRATTYY LADRRYDMLP
SVLSADLCSL LGGVDRYAVS IMWELDKASY EIKKVWYGRT IIRSAYKLFY EAAQELLDGN
LSVVDDIPEF KDLDEKSRQA KLEELVWAIG KLTDIARHVR AKRDGCGALE LEGVEVCVQL
DDKKNIHDLI PKQPLEVHET VAECMILANH WVAKKIWESF PHQALLRQHP PPHQEFFSEL
RECAKAKGFF IDTRSNKTLA DSLDNANDPH DPIVNRLLRS MATQAMSNAL YFSTGSCAEE
EFHHYGLALD KYTHFTSPIR RYSDIVVHRL LMAAISKDKK MEIKGNLFSN KDLEELCRHI
NNRNQAAQHS QKQSTELFQC MYFKDKDPAT EERCISDGVI YSIRTNGVLL FIPRFGIKGA
AYLKNKDGLV ISCGPDSCSE WKPGSLQRFQ NKITSTTTDG ESVTFHLFDH VTVRISIQAS
RCHSDTIRLE IISNKPYKIP NTELIHQSSP LLKSELVKEV TKSVEEAQLA QEVKVNIIQE
EYQEYRQTKG RSLYTLLEEI RDLALLDVSN NYGI
