ID  P29728;
PN  2'-5'-oligoadenylate synthase 2;
GN  OAS2;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:19923450}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:19923450}.
DR  UNIPROT: P29728;
DR  UNIPROT: A8K9T1;
DR  UNIPROT: Q6PJ33;
DR  UNIPROT: Q86XX8;
DR  Pfam: PF01909;
DR  Pfam: PF10421;
DR  PROSITE: PS00832;
DR  PROSITE: PS00833;
DR  PROSITE: PS50152;
DR  OMIM: 603350;
DR  DisGeNET: 4939;
DE  Function: Interferon-induced, dsRNA-activated antiviral enzyme which plays a critical role in cellular innate antiviral response (PubMed:10464285, PubMed:9880569). Activated by detection of double stranded RNA (dsRNA): polymerizes higher oligomers of 2'-5'- oligoadenylates (2-5A) from ATP which then bind to the inactive monomeric form of ribonuclease L (RNASEL) leading to its dimerization and subsequent activation (PubMed:10464285, PubMed:9880569, PubMed:11682059). 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:10464285, PubMed:9880569). 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 (By similarity). Non-infected lobules would not be affected, allowing efficient pup feeding during infection (By similarity). {ECO:0000250|UniProtKB:E9Q9A9, ECO:0000269|PubMed:10464285, ECO:0000269|PubMed:11682059, ECO:0000269|PubMed:19923450, ECO:0000269|PubMed:9880569, ECO:0000303|PubMed:21142819}.
DE  Reference Proteome: Yes;
DE  Interaction: P49761; IntAct: EBI-10211450; Score: 0.67
DE  Interaction: Q96EF6; IntAct: EBI-25275989; Score: 0.56
DE  Interaction: Q8ND71; IntAct: EBI-21862528; Score: 0.35
DE  Interaction: Q13976; IntAct: EBI-21883113; Score: 0.35
DE  Interaction: Q13085; IntAct: EBI-21883113; Score: 0.35
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0043231;
GO  GO:0016020;
GO  GO:0005654;
GO  GO:0048471;
GO  GO:0001730;
GO  GO:0005524;
GO  GO:0003725;
GO  GO:0046872;
GO  GO:0042742;
GO  GO:0051607;
GO  GO:0070106;
GO  GO:0045071;
GO  GO:0006139;
GO  GO:0032728;
GO  GO:0032760;
GO  GO:1903487;
GO  GO:0060700;
GO  GO:0009615;
GO  GO:0006401;
GO  GO:0060337;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:2211721};
SQ  MGNGESQLSSVPAQKLGWFIQEYLKPYEECQTLIDEMVNTICDVLQEPEQFPLVQGVAIGGSYGRKTVLRGNSDGTLVLF
SQ  FSDLKQFQDQKRSQRDILDKTGDKLKFCLFTKWLKNNFEIQKSLDGFTIQVFTKNQRISFEVLAAFNALSLNDNPSPWIY
SQ  RELKRSLDKTNASPGEFAVCFTELQQKFFDNRPGKLKDLILLIKHWHQQCQKKIKDLPSLSPYALELLTVYAWEQGCRKD
SQ  NFDIAEGVRTVLELIKCQEKLCIYWMVNYNFEDETIRNILLHQLQSARPVILDPVDPTNNVSGDKICWQWLKKEAQTWLT
SQ  SPNLDNELPAPSWNVLPAPLFTTPGHLLDKFIKEFLQPNKCFLEQIDSAVNIIRTFLKENCFRQSTAKIQIVRGGSTAKG
SQ  TALKTGSDADLVVFHNSLKSYTSQKNERHKIVKEIHEQLKAFWREKEEELEVSFEPPKWKAPRVLSFSLKSKVLNESVSF
SQ  DVLPAFNALGQLSSGSTPSPEVYAGLIDLYKSSDLPGGEFSTCFTVLQRNFIRSRPTKLKDLIRLVKHWYKECERKLKPK
SQ  GSLPPKYALELLTIYAWEQGSGVPDFDTAEGFRTVLELVTQYQQLCIFWKVNYNFEDETVRKFLLSQLQKTRPVILDPAE
SQ  PTGDVGGGDRWCWHLLAKEAKEWLSSPCFKDGTGNPIPPWKVPTMQTPGSCGARIHPIVNEMFSSRSHRILNNNSKRNF
//