Q8VI93 · OAS3_MOUSE

  • Protein
    2'-5'-oligoadenylate synthase 3
  • Gene
    Oas3
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Interferon-induced, dsRNA-activated antiviral enzyme which plays a critical role in cellular innate antiviral response. In addition, it may also play a role in other cellular processes such as apoptosis, cell growth, differentiation and gene regulation. Synthesizes preferentially dimers of 2'-5'-oligoadenylates (2-5A) from ATP which then bind to the inactive monomeric form of ribonuclease L (RNase L) leading to its dimerization and subsequent activation. Activation of RNase L leads to degradation of cellular as well as viral RNA, resulting in the inhibition of protein synthesis, thus terminating viral replication. Can mediate the antiviral effect via the classical RNase L-dependent pathway or an alternative antiviral pathway independent of RNase L.

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Activity regulation

Produced as a latent enzyme which is activated by dsRNA generated during the course of viral infection. Strongly activated by long dsRNAs at least 50 nucleotides in length. ssRNA does not activate the enzyme.

Features

Showing features for site, binding site.

TypeIDPosition(s)Description
Site154Interaction with dsRNA
Site242Interaction with dsRNA
Binding site855ATP (UniProtKB | ChEBI)
Binding site867Mg2+ (UniProtKB | ChEBI); catalytic
Binding site869Mg2+ (UniProtKB | ChEBI); catalytic
Binding site939Mg2+ (UniProtKB | ChEBI); catalytic
Binding site998ATP (UniProtKB | ChEBI)
Binding site1001ATP (UniProtKB | ChEBI)
Binding site1020ATP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular Componentcytosol
Cellular Componentmembrane
Cellular Componentnucleoplasm
Cellular Componentplasma membrane
Molecular Function2'-5'-oligoadenylate synthetase activity
Molecular FunctionATP binding
Molecular Functiondouble-stranded RNA binding
Molecular Functionmetal ion binding
Biological Processdefense response to bacterium
Biological Processdefense response to virus
Biological Processinnate immune response
Biological ProcessMDA-5 signaling pathway
Biological Processnegative regulation of chemokine (C-C motif) ligand 5 production
Biological Processnegative regulation of chemokine (C-X-C motif) ligand 2 production
Biological Processnegative regulation of chemokine (C-X-C motif) ligand 9 production
Biological Processnegative regulation of IP-10 production
Biological Processnegative regulation of type I interferon-mediated signaling pathway
Biological Processnegative regulation of viral genome replication
Biological Processpositive regulation of interferon-beta production
Biological Processpositive regulation of monocyte chemotactic protein-1 production
Biological Processpositive regulation of tumor necrosis factor production
Biological Processresponse to virus
Biological ProcessRIG-I signaling pathway

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    2'-5'-oligoadenylate synthase 3
  • EC number
  • Short names
    (2-5')oligo(A) synthase 3; 2-5A synthase 3
  • Alternative names
    • 2',5'-oligoadenylate synthetase-like 10

Gene names

    • Name
      Oas3
    • Synonyms
      oasl10

Organism names

  • Taxonomic identifier
  • Strains
    • C57BL/6J
    • C3H/RV
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    Q8VI93
  • Secondary accessions
    • B9EIU4
    • Q8K4D2

Proteomes

Organism-specific databases

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for modified residue, chain.

TypeIDPosition(s)Description
Modified residue1N-acetylmethionine
ChainPRO_00004186301-11382'-5'-oligoadenylate synthase 3

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Intestine.

Induction

By type I interferon (IFN) and viruses.

Gene expression databases

Interaction

Subunit

Monomer.

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region6-341OAS domain 1
Region12-56Interaction with dsRNA
Region185-199Interaction with dsRNA
Region342-462Linker
Region370-403Disordered
Region434-459Disordered
Region463-793OAS domain 2
Region801-1135OAS domain 3

Domain

OAS domain 3 is catalytically active. OAS domain 1 has no catalytic activity but is essential for recognition of long dsRNAs.

Sequence similarities

Belongs to the 2-5A synthase family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,138
  • Mass (Da)
    126,333
  • Last updated
    2002-03-01 v1
  • Checksum
    64568BA94FC51866
MDLFHTPAGALDKLVAHNLHPAPEFTAAVRGALGSLNITLQQHRARGSQRPRVIRIAKGGAYARGTALRGGTDVELVIFLDCFQSFGDQKTCHSETLGAMRMLLESWGGHPGPGLTFEFSQSKASRILQFRLASADGEHWIDVSLVPAFDVLGQPRSGVKPTPNVYSSLLSSHCQAGEYSACFTEPRKNFVNTRPAKLKNLILLVKHWYHQVQTRAVRATLPPSYALELLTIFAWEQGCGKDSFSLAQGLRTVLALIQHSKYLCIFWTENYGFEDPAVGEFLRRQLKRPRPVILDPADPTWDVGNGTAWRWDVLAQEAESSFSQQCFKQASGVLVQPWEGPGLPRAGILDLGHPIYQGPNQALEDNKGHLAVQSKERSQKPSNSAPGFPEAATKIPAMPNPSANKTRKIRKKAAHPKTVQEAALDSISSHVRITQSTASSHMPPDRSSISTAGSRMSPDLSQIPSKDLDCFIQDHLRPSPQFQQQVKQAIDAILCCLREKSVYKVLRVSKGGSFGRGTDLRGSCDVELVIFYKTLGDFKGQKPHQAEILRDMQAQLRHWCQNPVPGLSLQFIEQKPNALQLQLASTDLSNRVDLSVLPAFDAVGPLKSGTKPQPQVYSSLLSSGCQAGEHAACFAELRRNFINTCPPKLKSLMLLVKHWYRQVVTRYKGGEAAGDAPPPAYALELLTIFAWEQGCGEQKFSLAEGLRTILRLIQQHQSLCIYWTVNYSVQDPAIRAHLLCQLRKARPLVLDPADPTWNVGQGDWKLLAQEAAALGSQVCLQSGDGTLVPPWDVTPALLHQTLAEDLDKFISEFLQPNRHFLTQVKRAVDTICSFLKENCFRNSTIKVLKVVKGGSSAKGTALQGRSDADLVVFLSCFRQFSEQGSHRAEIISEIQAHLEACQQMHSFDVKFEVSKRKNPRVLSFTLTSQTLLDQSVDFDVLPAFDALGQLRSGSRPDPRVYTDLIHSCSNAGEFSTCFTELQRDFITSRPTKLKSLIRLVKYWYQQCNKTIKGKGSLPPQHGLELLTVYAWEQGGQNPQFNMAEGFRTVLELIVQYRQLCVYWTINYSAEDKTIGDFLKMQLRKPRPVILDPADPTGNLGHNARWDLLAKEATVYASALCCVDRDGNPIKPWPVKAAV

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
F7CXR7F7CXR7_MOUSEOas3131

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict215in Ref. 2; AAM47556
Sequence conflict733in Ref. 2; AAM47556
Sequence conflict897in Ref. 2; AAM47556, 4; EDL19752 and 5; AAI41056
Sequence conflict904in Ref. 2; AAM47556

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AB067534
EMBL· GenBank· DDBJ
BAB84134.1
EMBL· GenBank· DDBJ
mRNA
AF453830
EMBL· GenBank· DDBJ
AAM47556.1
EMBL· GenBank· DDBJ
mRNA
AC115937
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
CH466529
EMBL· GenBank· DDBJ
EDL19752.1
EMBL· GenBank· DDBJ
Genomic DNA
BC141055
EMBL· GenBank· DDBJ
AAI41056.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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