ISG20_MOUSE
ID ISG20_MOUSE Reviewed; 300 AA.
AC Q9JL16; Q9CPZ5;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Interferon-stimulated gene 20 kDa protein;
DE EC=3.1.13.1;
DE AltName: Full=Promyelocytic leukemia nuclear body-associated protein ISG20;
DE AltName: Full=Protein DnaQL;
GN Name=Isg20;
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 [MRNA] (ISOFORM 1).
RA Ramirez M.H., Shannon M.E., Thelen M.P.;
RT "Isolation of a novel mouse gene member of the DnaQ superfamily:
RT characterization of the exonuclease protein product.";
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Small intestine;
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 2).
RC STRAIN=FVB/N; TISSUE=Salivary gland;
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=Spleen;
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: Interferon-induced antiviral exoribonuclease that acts on
CC single-stranded RNA and also has minor activity towards single-stranded
CC DNA. Exhibits antiviral activity against RNA viruses in an exonuclease-
CC dependent manner. May also play additional roles in the maturation of
CC snRNAs and rRNAs, and in ribosome biogenesis (By similarity).
CC {ECO:0000250}.
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 -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Note=Binds 2 manganese ions per subunit.;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.0.;
CC -!- SUBUNIT: Associates with PML and SP100 in the PML NB complex.
CC Associates with survival motor neuron protein (SMN)-containing
CC macromolecular nuclear complexes and U1 and U2 snRNAs and U3 snoRNA (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Nucleus, nucleolus
CC {ECO:0000250}. Cytoplasm {ECO:0000250}. Nucleus, Cajal body
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9JL16-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9JL16-2; Sequence=VSP_012431, VSP_012432;
CC -!- INDUCTION: Induced by interferons alpha and beta. Weaker induction was
CC seen with interferon gamma. Increased expression was seen at the
CC transcriptional level (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the exonuclease superfamily. {ECO:0000305}.
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DR EMBL; AF217484; AAF59917.1; -; mRNA.
DR EMBL; AK008139; BAB25487.1; -; mRNA.
DR EMBL; AK008171; BAB25509.1; -; mRNA.
DR EMBL; AK008353; BAB25623.1; -; mRNA.
DR EMBL; BC022751; AAH22751.1; -; mRNA.
DR CCDS; CCDS21376.1; -. [Q9JL16-2]
DR CCDS; CCDS71982.1; -. [Q9JL16-1]
DR RefSeq; NP_001106999.1; NM_001113527.1. [Q9JL16-2]
DR RefSeq; NP_001278149.1; NM_001291220.1. [Q9JL16-1]
DR RefSeq; NP_001278150.1; NM_001291221.1. [Q9JL16-2]
DR RefSeq; NP_065608.2; NM_020583.5. [Q9JL16-2]
DR RefSeq; XP_006541089.1; XM_006541026.2. [Q9JL16-1]
DR RefSeq; XP_006541091.1; XM_006541028.3. [Q9JL16-1]
DR AlphaFoldDB; Q9JL16; -.
DR SMR; Q9JL16; -.
DR STRING; 10090.ENSMUSP00000040080; -.
DR iPTMnet; Q9JL16; -.
DR PhosphoSitePlus; Q9JL16; -.
DR EPD; Q9JL16; -.
DR MaxQB; Q9JL16; -.
DR PaxDb; Q9JL16; -.
DR PRIDE; Q9JL16; -.
DR ProteomicsDB; 269229; -. [Q9JL16-1]
DR ProteomicsDB; 269230; -. [Q9JL16-2]
DR Antibodypedia; 15665; 356 antibodies from 27 providers.
DR DNASU; 57444; -.
DR Ensembl; ENSMUST00000038142; ENSMUSP00000040080; ENSMUSG00000039236. [Q9JL16-2]
DR Ensembl; ENSMUST00000118867; ENSMUSP00000112480; ENSMUSG00000039236. [Q9JL16-2]
DR Ensembl; ENSMUST00000120331; ENSMUSP00000113255; ENSMUSG00000039236. [Q9JL16-2]
DR Ensembl; ENSMUST00000121645; ENSMUSP00000112621; ENSMUSG00000039236. [Q9JL16-1]
DR GeneID; 57444; -.
DR KEGG; mmu:57444; -.
DR UCSC; uc009hxt.2; mouse. [Q9JL16-1]
DR CTD; 3669; -.
DR MGI; MGI:1928895; Isg20.
DR VEuPathDB; HostDB:ENSMUSG00000039236; -.
DR eggNOG; KOG2249; Eukaryota.
DR GeneTree; ENSGT00940000160781; -.
DR HOGENOM; CLU_022453_3_1_1; -.
DR InParanoid; Q9JL16; -.
DR OMA; LSHPRRY; -.
DR OrthoDB; 1562214at2759; -.
DR PhylomeDB; Q9JL16; -.
DR TreeFam; TF354340; -.
DR BioGRID-ORCS; 57444; 2 hits in 77 CRISPR screens.
DR ChiTaRS; Isg20; mouse.
DR PRO; PR:Q9JL16; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9JL16; protein.
DR Bgee; ENSMUSG00000039236; Expressed in femorotibial joint and 126 other tissues.
DR ExpressionAtlas; Q9JL16; baseline and differential.
DR Genevisible; Q9JL16; MM.
DR GO; GO:0015030; C:Cajal body; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0016605; C:PML body; ISO:MGI.
DR GO; GO:0000175; F:3'-5'-exoribonuclease activity; ISO:MGI.
DR GO; GO:0004527; F:exonuclease activity; ISS:UniProtKB.
DR GO; GO:0008859; F:exoribonuclease II activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008310; F:single-stranded DNA 3'-5' exodeoxyribonuclease activity; ISO:MGI.
DR GO; GO:0030619; F:U1 snRNA binding; ISS:UniProtKB.
DR GO; GO:0030620; F:U2 snRNA binding; ISS:UniProtKB.
DR GO; GO:0034511; F:U3 snoRNA binding; ISS:UniProtKB.
DR GO; GO:0051607; P:defense response to virus; ISS:UniProtKB.
DR GO; GO:0000738; P:DNA catabolic process, exonucleolytic; ISO:MGI.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0045071; P:negative regulation of viral genome replication; ISO:MGI.
DR GO; GO:0009615; P:response to virus; ISO:MGI.
DR GO; GO:0006401; P:RNA catabolic process; ISO:MGI.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR Gene3D; 3.30.420.10; -; 1.
DR InterPro; IPR013520; Exonuclease_RNaseT/DNA_pol3.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR Pfam; PF00929; RNase_T; 1.
DR SMART; SM00479; EXOIII; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Antiviral defense; Cytoplasm; Exonuclease; Hydrolase;
KW Immunity; Innate immunity; Manganese; Metal-binding; Nuclease; Nucleus;
KW Reference proteome; RNA-binding; rRNA processing.
FT CHAIN 1..300
FT /note="Interferon-stimulated gene 20 kDa protein"
FT /id="PRO_0000084244"
FT BINDING 11
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 13
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 90
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 93
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT VAR_SEQ 144..181
FT /note="VLPGSLLGVGGCILPGTDILHLLLYVGMVRIADLRLLT -> NNWRGHCSVE
FT DARATMELYKISQRLRAQRGLPCPGTSD (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_012431"
FT VAR_SEQ 182..300
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_012432"
SQ SEQUENCE 300 AA; 32503 MW; 3517E33DBFD8D463 CRC64;
MAGIPEVVAM DCEMVGLGPQ RVSGLARCSI VNIHGAVLYD KYIRPEGEIT DYRTQVSGVT
PQHMVRATPF GEARLEILQL LKGKLVVGHD LKHDFNALKE DMSKYTIYDT STDRLLWHEA
KLQYYSRVSL RLLCKRLLHK NIQVLPGSLL GVGGCILPGT DILHLLLYVG MVRIADLRLL
TPFLPPSCLA CPLLPESLAS ARSHAVISAL SSSSHLLTPL PNPSQGPQGH VDRLSGQLQD
WGGSPLAPAL PVSAEQLAGP LLCGRCQGHN GALQNLSATQ SPARAALPWD VRLNFILIQG
