ID   OASL2_RAT               Reviewed;         511 AA.
AC   Q5MYT9;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=2'-5'-oligoadenylate synthase-like protein 2;
DE            EC=2.7.7.84;
GN   Name=Oasl2;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sprague-Dawley; TISSUE=Ovary;
RX   PubMed=12080145; DOI=10.1073/pnas.142287799;
RA   Perelygin A.A., Scherbik S.V., Zhulin I.B., Stockman B.M., Li Y.,
RA   Brinton M.A.;
RT   "Positional cloning of the murine flavivirus resistance gene.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:9322-9327(2002).
RN   [2]
RP   REVIEW.
RX   PubMed=17024523; DOI=10.1007/s00239-006-0073-3;
RA   Perelygin A.A., Zharkikh A.A., Scherbik S.V., Brinton M.A.;
RT   "The mammalian 2'-5' oligoadenylate synthetase gene family: evidence for
RT   concerted evolution of paralogous Oas1 genes in Rodentia and
RT   Artiodactyla.";
RL   J. Mol. Evol. 63:562-576(2006).
CC   -!- FUNCTION: Interferon-induced, dsRNA-activated antiviral enzyme which
CC       plays a critical role in cellular innate antiviral response.
CC       Synthesizes oligomers of 2'-5'-oligoadenylates (2-5A) from ATP which
CC       then bind to the inactive monomeric form of ribonuclease L (RNase L)
CC       leading to its dimerization and subsequent activation. Activation of
CC       RNase L leads to degradation of cellular as well as viral RNA,
CC       resulting in the inhibition of protein synthesis, thus terminating
CC       viral replication. Can mediate the antiviral effect via the classical
CC       RNase L-dependent pathway or an alternative antiviral pathway
CC       independent of RNase L (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3 ATP = 5'-triphosphoadenylyl-(2'->5')-adenylyl-(2'->5')-
CC         adenosine + 2 diphosphate; Xref=Rhea:RHEA:34407, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:67143; EC=2.7.7.84;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305};
CC   -!- ACTIVITY REGULATION: Produced as a latent enzyme which is activated by
CC       dsRNA generated during the course of viral infection. The dsRNA
CC       activator must be at least 15 nucleotides long, and no modification of
CC       the 2'-hydroxyl group is tolerated. ssRNA or dsDNA do not act as
CC       activators (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the 2-5A synthase family. {ECO:0000305}.
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DR   EMBL; AY237116; AAP70315.1; -; mRNA.
DR   RefSeq; NP_001009682.1; NM_001009682.1.
DR   AlphaFoldDB; Q5MYT9; -.
DR   SMR; Q5MYT9; -.
DR   STRING; 10116.ENSRNOP00000001600; -.
DR   PaxDb; Q5MYT9; -.
DR   PRIDE; Q5MYT9; -.
DR   GeneID; 304549; -.
DR   KEGG; rno:304549; -.
DR   UCSC; RGD:1307351; rat.
DR   CTD; 23962; -.
DR   RGD; 1307351; Oasl2.
DR   eggNOG; KOG0001; Eukaryota.
DR   HOGENOM; CLU_040930_1_0_1; -.
DR   InParanoid; Q5MYT9; -.
DR   OrthoDB; 611234at2759; -.
DR   PhylomeDB; Q5MYT9; -.
DR   TreeFam; TF329749; -.
DR   PRO; PR:Q5MYT9; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR   GO; GO:0001730; F:2'-5'-oligoadenylate synthetase activity; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003725; F:double-stranded RNA binding; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0051607; P:defense response to virus; 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:0060700; P:regulation of ribonuclease activity; IBA:GO_Central.
DR   GO; GO:0009615; P:response to virus; TAS:UniProtKB.
DR   CDD; cd05400; NT_2-5OAS_ClassI-CCAase; 1.
DR   Gene3D; 3.30.460.10; -; 1.
DR   InterPro; IPR018952; 2-5-oligoAdlate_synth_1_dom2/C.
DR   InterPro; IPR026774; 2-5A_synthase.
DR   InterPro; IPR006117; 2-5OAS_C_CS.
DR   InterPro; IPR043518; 2-5OAS_N_CS.
DR   InterPro; IPR006116; NT_2-5OAS_ClassI-CCAase.
DR   InterPro; IPR043519; NT_sf.
DR   InterPro; IPR000626; Ubiquitin-like_dom.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   PANTHER; PTHR11258; PTHR11258; 1.
DR   Pfam; PF10421; OAS1_C; 1.
DR   Pfam; PF00240; ubiquitin; 1.
DR   SMART; SM00213; UBQ; 2.
DR   SUPFAM; SSF54236; SSF54236; 2.
DR   SUPFAM; SSF81301; SSF81301; 1.
DR   PROSITE; PS00832; 25A_SYNTH_1; 1.
DR   PROSITE; PS00833; 25A_SYNTH_2; 1.
DR   PROSITE; PS50152; 25A_SYNTH_3; 1.
DR   PROSITE; PS50053; UBIQUITIN_2; 1.
PE   2: Evidence at transcript level;
KW   Antiviral defense; ATP-binding; Immunity; Innate immunity; Magnesium;
KW   Metal-binding; Nucleotide-binding; Nucleotidyltransferase;
KW   Reference proteome; RNA-binding; Transferase.
FT   CHAIN           1..511
FT                   /note="2'-5'-oligoadenylate synthase-like protein 2"
FT                   /id="PRO_0000418634"
FT   DOMAIN          439..477
FT                   /note="Ubiquitin-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   BINDING         69
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P00973"
FT   BINDING         81
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255"
FT   BINDING         83
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255"
FT   BINDING         154
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255"
FT   BINDING         213
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P29728"
FT   BINDING         216
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P00973"
SQ   SEQUENCE   511 AA;  59406 MW;  F209B2D883AC7476 CRC64;
     MDTLPDLYGT VGDSLDYFLE HSLQPQRDWK EEGKDAWERI ERFFREKCFC DELLLDQEVR
     VLKVVKGGSS GKGTALNHRS DQDMILFLSC FSSFKQQARD RKAVIDFIKS KLIHCRKSLA
     YNITVRQHKE GKRTPRSLTL EIQSRKSNDI ICMDILPAYN ALGSFSRDCK PEPEIYENLI
     RCKGYPGDFS PSFAELQRHF VKSRPVKLKN LLRLVKFWHL KYLRHKYRRA VLPSKYALEL
     LTIYAWEMGT DSSDNFNLDE GFVAVMELLR DYQDICIYWT KYYDFQNEVV RNFLKEQLKG
     DRPIILDPAD PTNNLGRRGK WELVAKEATY CLLQLCCVTA DRWNVQVSIA HYLRGARDVQ
     VTVKQTGREE WILLTNPHSP IRKLKAKIKK RMNLCGELRI SFQEPGGERQ PLSGRKTLSD
     YGIFSKVNIR VMETFPPEIQ VFVRYPGGQN KPFAIDPDAT ILSLWEKIEE DGGPCTEDWV
     LLFEGEELDD DDNLAELQIK DCDTIQLSRV S