DI3L1_MOUSE
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 03-AUG-2022, entry version 137.
DE RecName: Full=DIS3-like exonuclease 1;
DE EC=3.1.13.-;
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: 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 -!- 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 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}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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.ENSMUSP00000113503; -.
DR PhosphoSitePlus; Q8C0S1; -.
DR EPD; Q8C0S1; -.
DR MaxQB; Q8C0S1; -.
DR PaxDb; Q8C0S1; -.
DR PeptideAtlas; Q8C0S1; -.
DR PRIDE; Q8C0S1; -.
DR ProteomicsDB; 279656; -. [Q8C0S1-1]
DR ProteomicsDB; 279657; -. [Q8C0S1-2]
DR Antibodypedia; 26111; 139 antibodies from 21 providers.
DR DNASU; 213550; -.
DR Ensembl; ENSMUST00000068367; ENSMUSP00000063830; ENSMUSG00000032396. [Q8C0S1-2]
DR Ensembl; ENSMUST00000113890; ENSMUSP00000109522; ENSMUSG00000032396. [Q8C0S1-2]
DR Ensembl; ENSMUST00000120760; ENSMUSP00000113503; ENSMUSG00000032396. [Q8C0S1-2]
DR Ensembl; ENSMUST00000168844; ENSMUSP00000129772; ENSMUSG00000032396. [Q8C0S1-1]
DR GeneID; 213550; -.
DR KEGG; mmu:213550; -.
DR UCSC; uc009qbu.2; mouse. [Q8C0S1-1]
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; WKVNPEE; -.
DR OrthoDB; 1104619at2759; -.
DR PhylomeDB; Q8C0S1; -.
DR TreeFam; TF105755; -.
DR BioGRID-ORCS; 213550; 11 hits in 71 CRISPR screens.
DR PRO; PR:Q8C0S1; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q8C0S1; protein.
DR Bgee; ENSMUSG00000032396; Expressed in spermatocyte and 202 other tissues.
DR ExpressionAtlas; Q8C0S1; baseline and differential.
DR Genevisible; Q8C0S1; MM.
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:0000178; C:exosome (RNase complex); IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0000175; F:3'-5'-exoribonuclease activity; ISS:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
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 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..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
