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Interferon-stimulated gene 20 kDa protein (EC 3.1.13.1) (Estrogen-regulated transcript 45 protein) (Promyelocytic leukemia nuclear body-associated protein ISG20)

 ISG20_HUMAN             Reviewed;         181 AA.
Q96AZ6; O00441; O00586;
04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
04-JAN-2005, sequence version 2.
25-OCT-2017, entry version 130.
RecName: Full=Interferon-stimulated gene 20 kDa protein;
EC=3.1.13.1;
AltName: Full=Estrogen-regulated transcript 45 protein;
AltName: Full=Promyelocytic leukemia nuclear body-associated protein ISG20;
Name=ISG20; Synonyms=HEM45;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, IDENTIFICATION IN PML NB COMPLEX, AND INDUCTION.
PubMed=9235947; DOI=10.1074/jbc.272.31.19457;
Gongora C., David G., Pintard L., Tissot C., Hua T.D., Dejean A.,
Mechti N.;
"Molecular cloning of a new interferon-induced PML nuclear bodies-
associated protein.";
J. Biol. Chem. 272:19457-19463(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
PubMed=9569007; DOI=10.1016/S0960-0760(97)00140-4;
Pentecost B.T.;
"Expression and estrogen regulation of the HEM45 mRNA in human tumor
lines and in the rat uterus.";
J. Steroid Biochem. Mol. Biol. 64:25-33(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=B-cell, and Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
FUNCTION, AND ENZYME REGULATION.
PubMed=11401564; DOI=10.1021/bi010141t;
Nguyen L.H., Espert L., Mechti N., Wilson D.M. III;
"The human interferon- and estrogen-regulated ISG20/HEM45 gene product
degrades single-stranded RNA and DNA in vitro.";
Biochemistry 40:7174-7179(2001).
[7]
FUNCTION.
PubMed=12594219; DOI=10.1074/jbc.M209628200;
Espert L., Degols G., Gongora C., Blondel D., Williams B.R.,
Silverman R.H., Mechti N.;
"ISG20, a new interferon-induced RNase specific for single-stranded
RNA, defines an alternative antiviral pathway against RNA genomic
viruses.";
J. Biol. Chem. 278:16151-16158(2003).
[8]
FUNCTION.
PubMed=16033969; DOI=10.1099/vir.0.81074-0;
Espert L., Degols G., Lin Y.L., Vincent T., Benkirane M., Mechti N.;
"Interferon-induced exonuclease ISG20 exhibits an antiviral activity
against human immunodeficiency virus type 1.";
J. Gen. Virol. 86:2221-2229(2005).
[9]
SUBCELLULAR LOCATION, AND INTERACTION WITH SMN COMPLEX AND SNRNAS.
PubMed=16514659; DOI=10.1002/jcb.20869;
Espert L., Eldin P., Gongora C., Bayard B., Harper F.,
Chelbi-Alix M.K., Bertrand E., Degols G., Mechti N.;
"The exonuclease ISG20 mainly localizes in the nucleolus and the Cajal
(Coiled) bodies and is associated with nuclear SMN protein-containing
complexes.";
J. Cell. Biochem. 98:1320-1333(2006).
[10]
REVIEW ON FUNCTION.
PubMed=17445960; DOI=10.1016/j.biochi.2007.03.006;
Degols G., Eldin P., Mechti N.;
"ISG20, an actor of the innate immune response.";
Biochimie 89:831-835(2007).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[12]
FUNCTION IN HCV; HAV AND YFV RESTRICTION, AND SUBCELLULAR LOCATION.
PubMed=21036379; DOI=10.1016/j.virol.2010.10.008;
Zhou Z., Wang N., Woodson S.E., Dong Q., Wang J., Liang Y.,
Rijnbrand R., Wei L., Nichols J.E., Guo J.T., Holbrook M.R.,
Lemon S.M., Li K.;
"Antiviral activities of ISG20 in positive-strand RNA virus
infections.";
Virology 409:175-188(2011).
[13]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH UMP, COFACTOR,
AND MANGANESE-BINDING SITES.
PubMed=15527770; DOI=10.1016/j.febslet.2004.09.074;
Horio T., Murai M., Inoue T., Hamasaki T., Tanaka T., Ohgi T.;
"Crystal structure of human ISG20, an interferon-induced antiviral
ribonuclease.";
FEBS Lett. 577:111-116(2004).
-!- FUNCTION: Interferon-induced antiviral exoribonuclease that acts
on single-stranded RNA and also has minor activity towards single-
stranded DNA. Exhibits antiviral activity against RNA viruses
including hepatitis C virus (HCV), hepatitis A virus (HAV) and
yellow fever virus (YFV) in an exonuclease-dependent manner. May
also play additional roles in the maturation of snRNAs and rRNAs,
and in ribosome biogenesis. {ECO:0000269|PubMed:11401564,
ECO:0000269|PubMed:12594219, ECO:0000269|PubMed:16033969,
ECO:0000269|PubMed:21036379}.
-!- CATALYTIC ACTIVITY: Exonucleolytic cleavage in the 3'- to 5'-
direction to yield nucleoside 5'-phosphates.
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000269|PubMed:15527770};
Note=Binds 2 manganese ions per subunit.
{ECO:0000269|PubMed:15527770};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
pH dependence:
Optimum pH is 7.0.;
-!- SUBUNIT: Associates with PML and SP100 in the PML NB complex.
Associates with survival motor neuron protein (SMN)-containing
macromolecular nuclear complexes and U1 and U2 snRNAs and U3
snoRNA. {ECO:0000269|PubMed:15527770, ECO:0000269|PubMed:9235947}.
-!- SUBCELLULAR LOCATION: Nucleus. Nucleus, nucleolus. Cytoplasm.
Nucleus, Cajal body.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q96AZ6-1; Sequence=Displayed;
Name=2;
IsoId=Q96AZ6-2; Sequence=VSP_012429, VSP_012430;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Highly expressed in peripheral blood
leukocytes, spleen, thymus, colon and lung. Up regulated by E2 in
estrogen receptor-positive breast cancer lines.
{ECO:0000269|PubMed:9235947, ECO:0000269|PubMed:9569007}.
-!- INDUCTION: Induced by interferons alpha and beta. Weaker induction
was seen with interferon gamma. Increased expression was seen at
the transcriptional level. {ECO:0000269|PubMed:9235947}.
-!- SIMILARITY: Belongs to the exonuclease superfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X89773; CAA61915.2; -; mRNA.
EMBL; U88964; AAB53416.1; -; mRNA.
EMBL; BT006952; AAP35598.1; -; mRNA.
EMBL; CR456942; CAG33223.1; -; mRNA.
EMBL; BC007922; AAH07922.1; -; mRNA.
EMBL; BC016341; AAH16341.1; -; mRNA.
CCDS; CCDS10345.1; -. [Q96AZ6-1]
RefSeq; NP_001290162.1; NM_001303233.1. [Q96AZ6-1]
RefSeq; NP_001290163.1; NM_001303234.1. [Q96AZ6-1]
RefSeq; NP_001290165.1; NM_001303236.1.
RefSeq; NP_002192.2; NM_002201.5. [Q96AZ6-1]
RefSeq; XP_005254956.1; XM_005254899.2. [Q96AZ6-1]
RefSeq; XP_006720551.1; XM_006720488.3. [Q96AZ6-1]
UniGene; Hs.459265; -.
PDB; 1WLJ; X-ray; 1.90 A; A=1-181.
PDBsum; 1WLJ; -.
ProteinModelPortal; Q96AZ6; -.
SMR; Q96AZ6; -.
BioGrid; 109876; 10.
MINT; MINT-4714850; -.
STRING; 9606.ENSP00000306565; -.
DrugBank; DB03685; Uridine-5'-Monophosphate.
iPTMnet; Q96AZ6; -.
PhosphoSitePlus; Q96AZ6; -.
BioMuta; ISG20; -.
DMDM; 57012967; -.
EPD; Q96AZ6; -.
MaxQB; Q96AZ6; -.
PaxDb; Q96AZ6; -.
PeptideAtlas; Q96AZ6; -.
PRIDE; Q96AZ6; -.
DNASU; 3669; -.
Ensembl; ENST00000306072; ENSP00000306565; ENSG00000172183. [Q96AZ6-1]
Ensembl; ENST00000560741; ENSP00000453638; ENSG00000172183. [Q96AZ6-1]
GeneID; 3669; -.
KEGG; hsa:3669; -.
UCSC; uc002bmv.2; human. [Q96AZ6-1]
CTD; 3669; -.
DisGeNET; 3669; -.
EuPathDB; HostDB:ENSG00000172183.14; -.
GeneCards; ISG20; -.
HGNC; HGNC:6130; ISG20.
HPA; HPA058356; -.
MIM; 604533; gene.
neXtProt; NX_Q96AZ6; -.
OpenTargets; ENSG00000172183; -.
PharmGKB; PA29930; -.
eggNOG; KOG2249; Eukaryota.
eggNOG; COG0847; LUCA.
GeneTree; ENSGT00520000055542; -.
HOGENOM; HOG000182422; -.
HOVERGEN; HBG052149; -.
InParanoid; Q96AZ6; -.
KO; K12579; -.
OMA; MLLWREA; -.
OrthoDB; EOG091G0I6S; -.
PhylomeDB; Q96AZ6; -.
TreeFam; TF354340; -.
Reactome; R-HSA-909733; Interferon alpha/beta signaling.
ChiTaRS; ISG20; human.
EvolutionaryTrace; Q96AZ6; -.
GeneWiki; ISG20; -.
GenomeRNAi; 3669; -.
PRO; PR:Q96AZ6; -.
Proteomes; UP000005640; Chromosome 15.
Bgee; ENSG00000172183; -.
CleanEx; HS_ISG20; -.
ExpressionAtlas; Q96AZ6; baseline and differential.
Genevisible; Q96AZ6; HS.
GO; GO:0015030; C:Cajal body; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0016605; C:PML body; IDA:UniProtKB.
GO; GO:0000175; F:3'-5'-exoribonuclease activity; IDA:UniProtKB.
GO; GO:0004527; F:exonuclease activity; IMP:UniProtKB.
GO; GO:0008859; F:exoribonuclease II activity; IEA:UniProtKB-EC.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0008310; F:single-stranded DNA 3'-5' exodeoxyribonuclease activity; IDA:UniProtKB.
GO; GO:0030619; F:U1 snRNA binding; IDA:UniProtKB.
GO; GO:0030620; F:U2 snRNA binding; IDA:UniProtKB.
GO; GO:0034511; F:U3 snoRNA binding; IDA:UniProtKB.
GO; GO:0008283; P:cell proliferation; TAS:ProtInc.
GO; GO:0051607; P:defense response to virus; IMP:UniProtKB.
GO; GO:0000738; P:DNA catabolic process, exonucleolytic; IDA:UniProtKB.
GO; GO:0045071; P:negative regulation of viral genome replication; IMP:UniProtKB.
GO; GO:0009615; P:response to virus; IDA:UniProtKB.
GO; GO:0006401; P:RNA catabolic process; IDA:UniProtKB.
GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
GO; GO:0060337; P:type I interferon signaling pathway; TAS:Reactome.
Gene3D; 3.30.420.10; -; 1.
InterPro; IPR013520; Exonuclease_RNaseT/DNA_pol3.
InterPro; IPR012337; RNaseH-like_sf.
InterPro; IPR036397; RNaseH_sf.
Pfam; PF00929; RNase_T; 1.
SMART; SM00479; EXOIII; 1.
SUPFAM; SSF53098; SSF53098; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Antiviral defense;
Complete proteome; Cytoplasm; Exonuclease; Hydrolase; Immunity;
Innate immunity; Manganese; Metal-binding; Nuclease; Nucleus;
Reference proteome; RNA-binding; rRNA processing.
CHAIN 1 181 Interferon-stimulated gene 20 kDa
protein.
/FTId=PRO_0000084243.
METAL 11 11 Manganese 1.
METAL 13 13 Manganese 1.
METAL 90 90 Manganese 2.
METAL 93 93 Manganese 2.
METAL 154 154 Manganese 1.
VAR_SEQ 77 86 ILQLLKGKLV -> VPFPSSPTAA (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_012429.
VAR_SEQ 87 181 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_012430.
STRAND 7 17 {ECO:0000244|PDB:1WLJ}.
TURN 18 21 {ECO:0000244|PDB:1WLJ}.
STRAND 22 31 {ECO:0000244|PDB:1WLJ}.
STRAND 37 44 {ECO:0000244|PDB:1WLJ}.
STRAND 49 51 {ECO:0000244|PDB:1WLJ}.
HELIX 54 57 {ECO:0000244|PDB:1WLJ}.
HELIX 61 64 {ECO:0000244|PDB:1WLJ}.
HELIX 70 81 {ECO:0000244|PDB:1WLJ}.
STRAND 84 90 {ECO:0000244|PDB:1WLJ}.
HELIX 91 97 {ECO:0000244|PDB:1WLJ}.
STRAND 106 109 {ECO:0000244|PDB:1WLJ}.
HELIX 110 112 {ECO:0000244|PDB:1WLJ}.
HELIX 114 120 {ECO:0000244|PDB:1WLJ}.
HELIX 130 137 {ECO:0000244|PDB:1WLJ}.
HELIX 151 171 {ECO:0000244|PDB:1WLJ}.
SEQUENCE 181 AA; 20363 MW; 24519CB52CEA5581 CRC64;
MAGSREVVAM DCEMVGLGPH RESGLARCSL VNVHGAVLYD KFIRPEGEIT DYRTRVSGVT
PQHMVGATPF AVARLEILQL LKGKLVVGHD LKHDFQALKE DMSGYTIYDT STDRLLWREA
KLDHCRRVSL RVLSERLLHK SIQNSLLGHS SVEDARATME LYQISQRIRA RRGLPRLAVS
D


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