{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"E9Q9A9","secondaryAccessions":["Q8K4E5","Q8VI92"],"uniProtkbId":"OAS2_MOUSE","entryAudit":{"firstPublicDate":"2012-09-05","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2011-04-05","entryVersion":99,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Mus musculus","commonName":"Mouse","taxonId":10090,"lineage":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"value":"2'-5'-oligoadenylate synthase 2"},"shortNames":[{"value":"(2-5')oligo(A) synthase 2"},{"value":"2-5A synthase 2"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15865429"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29117179"}],"value":"2.7.7.84"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"12396720"}],"value":"2',5'-oligoadenylate synthetase-like 11"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000312","source":"MGI","id":"MGI:2180852"}],"value":"Oas2"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"12396720"}],"value":"oasl11"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12396720"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15865429"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29117179"},{"evidenceCode":"ECO:0000303","source":"PubMed","id":"21142819"}],"value":"Interferon-induced, dsRNA-activated antiviral enzyme which plays a critical role in cellular innate antiviral response (PubMed:12396720, PubMed:29117179). Activated by detection of double stranded RNA (dsRNA): catalyzes the formation of 2'-5'-oligoadenylates (2-5A) from polymerization of ATP which then bind to the inactive monomeric form of ribonuclease L (RNASEL) leading to its dimerization and subsequent activation (PubMed:29117179). Activation of RNASEL leads to degradation of cellular as well as viral RNA, resulting in the inhibition of protein synthesis, thus terminating viral replication (PubMed:21142819). Can mediate the antiviral effect via the classical RNASEL-dependent pathway or an alternative antiviral pathway independent of RNASEL (PubMed:21142819). In addition, it may also play a role in other cellular processes such as apoptosis, cell growth, differentiation and gene regulation (PubMed:21142819). May act as a negative regulator of lactation, stopping lactation in virally infected mammary gland lobules, thereby preventing transmission of viruses to neonates (PubMed:29117179). Non-infected lobules would not be affected, allowing efficient pup feeding during infection (PubMed:29117179)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"3 ATP = 5'-triphosphoadenylyl-(2'->5')-adenylyl-(2'->5')-adenosine + 2 diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:34407"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:67143"}],"ecNumber":"2.7.7.84","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15865429"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29117179"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P29728"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P29728"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29117179"}],"value":"Produced as a latent enzyme which is activated by double stranded RNA (dsRNA) generated during the course of viral infection (PubMed:29117179). The dsRNA activator must be at least 15 nucleotides long, and no modification of the 2'-hydroxyl group is tolerated (By similarity). ssRNA or dsDNA do not act as activators (By similarity). Strongly inhibited by copper and iron (By similarity). Down-regulated by Zn(2+); Zn(2+) stabilizes the homodimeric form that is less responsive than monomers to activation by dsRNA (By similarity). Partially inhibited by cobalt and nickel ions (By similarity)"}],"commentType":"ACTIVITY REGULATION"},{"commentType":"BIOPHYSICOCHEMICAL PROPERTIES","kineticParameters":{"michaelisConstants":[{"constant":1.9,"unit":"mM","substrate":"ATP","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15865429"}]}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15865429"}],"value":"kcat is 6.4 sec(-1) for ATP."}]}}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P29728"}],"value":"Homodimer; homodimerization is mediated by coordination of Zn(2+) and down-regulates enzyme activity in response to dsRNA. 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