Oas2
entrez
246728
canonical
uniprot
E9Q9A9
canonical
ensembl
ENSMUSG00000032690
resolver
ensp
ENSMUSP00000060082
resolver
ensp
ENSMUSP00000080209
resolver
genesymbol
Oas2
resolver
genesymbol_syn
oasl11
resolver
uniprot
Q8K4E5
resolver
uniprot
Q8VI92
resolver
uniprot_entry
OAS2_MOUSE
resolver
uniprot_sec
Q8K4E5
resolver
uniprot_sec
Q8VI92
resolver
activity_regulation
ACTIVITY REGULATION: 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). {ECO:0000250|UniProtKB:P29728, ECO:0000269|PubMed:29117179}.
uniprot
proteins
amino_acid_sequence
MGNWLTGNWSSDRSSGYSSGWSPGGSSGVPSGPVHKLEKSIQANLTPNENCLKQIAVSSVPSQKLEGYIQENLKPNRESLKQIDQAVDAIWDLLRSQIPVKEVAKGGSYGRETALRGCSDGTLVLFMDCFQQFQDQIKYQDAYLDVIELWLKIHEKKSVKHEHALVVQVSVPGQRILLQLLPVFNPLRSNENPSSCVYVDLKKSMDQVRASPGEFSDCFTTLQQRFFKKYPQRLKDLILLVKHWYEQCQEKWKTPPPQPLLYALELLTVYAWEQGCQAEDFDMAQGVRTVLRLIQRPTELCVYWTVNYNFEDETVRNILLHQLRSQRPVILDPTDPTNNVGKDDGFWELLTEEAMAWLYSPSLNTESPAPYWDVLPMPLFVTPSHLLNKFIKDFLQPNKLFLKQIKEAVDIICSFLKNVCFLNSDTKVLKTVKGGSTAKGTALKRGSDADIVVFLSSLESYDSLKTNRSQFVQEIQKQLEEFVQAQEWEVTFEISKWKAPRVLSFTLKSKTLNESVEFDVLPAYDALGQLRSDFTLRPEAYKDLIELCASQDIKEGEFSICFTELQRNFIQTRPTKLKSLLRLIKHWYKQYERKMKPKASLPPKYALELLTVYAWEQGSGTDDFDIAEGFRTVLDLVIKYRQLCIFWTVNYNFEEEYMRKFLLTQIQKKRPVILDPADPTGDVGGGDRWCWHLLAEEAKEWLSSPCFQVEQKGLVQPWKVPVMQTPGSCGGQIYPTVGGVTK
uniprot
proteins
ec_number
2.7.7.84
uniprot
proteins
function
FUNCTION: 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). {ECO:0000269|PubMed:12396720, ECO:0000269|PubMed:15865429, ECO:0000269|PubMed:29117179, ECO:0000303|PubMed:21142819}.
uniprot
proteins
mass_dalton
85051
uniprot
proteins
mutagenesis
MUTAGEN 405; /note="I->N: Mice display postpartum failure of lactation and strongly reduced milk protein synthesis. Otherwise, mice develop normally and mammary glands are normal. The mutation causes an activation of the OAS2 pathway, characterized by a strong increase of Ribonuclease L (RNASEL) activity."; /evidence="ECO:0000269|PubMed:29117179"; MUTAGEN 444; /note="K->A,G: Strongly reduced 2'-5'-oligoadenylate synthase activity."; /evidence="ECO:0000269|PubMed:15865429"; MUTAGEN 509; /note="S->L: Abolished 2'-5'-oligoadenylate synthase activity."; /evidence="ECO:0000269|PubMed:15865429"; MUTAGEN 538; /note="P->L: Strongly reduced 2'-5'-oligoadenylate synthase activity."; /evidence="ECO:0000269|PubMed:15865429
uniprot
proteins
post_translational_modification
PTM: Myristoylation is not essential for its activity. {ECO:0000250|UniProtKB:P29728}.; PTM: Glycosylated. Glycosylation is essential for its activity. {ECO:0000250|UniProtKB:P29728}.
uniprot
proteins
protein_family
2-5A synthase family
uniprot
proteins
pubmed
12080145
uniprot
proteins
pubmed
12396720
uniprot
proteins
pubmed
15865429
uniprot
proteins
pubmed
17024523
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
21142819
uniprot
proteins
pubmed
29117179
uniprot
proteins
sequence_length
742
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P29728}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P29728}. Golgi apparatus membrane {ECO:0000250|UniProtKB:P29728}.
uniprot
proteins