ID   ISG20_PIG               Reviewed;         181 AA.
AC   Q66UW5;
DT   04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT   10-JAN-2006, sequence version 2.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Interferon-stimulated gene 20 kDa protein;
DE            EC=3.1.13.1;
GN   Name=Isg20;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Rowland R.R., Aguirre L.M.N., Schneider P.;
RT   "Porcine interferon-stimulated gene - 20 kDa.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
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   -!- 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; AY702647; AAU09455.2; -; mRNA.
DR   RefSeq; NP_001005351.2; NM_001005351.2.
DR   AlphaFoldDB; Q66UW5; -.
DR   SMR; Q66UW5; -.
DR   GeneID; 448855; -.
DR   CTD; 3669; -.
DR   InParanoid; Q66UW5; -.
DR   OrthoDB; 1562214at2759; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
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: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: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; IBA:GO_Central.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   GO; GO:0045071; P:negative regulation of viral genome replication; IBA:GO_Central.
DR   GO; GO:0006401; P:RNA catabolic process; IBA:GO_Central.
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   Antiviral defense; Cytoplasm; Exonuclease; Hydrolase; Immunity;
KW   Innate immunity; Manganese; Metal-binding; Nuclease; Nucleus;
KW   Reference proteome; RNA-binding; rRNA processing.
FT   CHAIN           1..181
FT                   /note="Interferon-stimulated gene 20 kDa protein"
FT                   /id="PRO_0000084245"
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   BINDING         154
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   181 AA;  20462 MW;  8FBE461A99CEF23D CRC64;
     MAGSREVVAM DCEMVGMGPR RESGLARCSL VNVHGAVLYD KFIQPEGEIT DYRTRVSGVT
     PQHMVGATPF AVARLEILQL LKGKLVVGHD LKHDFQALKE DMNRYTIYDT STDMLLWREA
     KLDHCRRVSL RVLCERLLHK SIQNSLLGHS SVEDAKATME LYQISQRIRA RRGLPRLAVS
     D