Q8VI93 · OAS3_MOUSE
- Protein2'-5'-oligoadenylate synthase 3
- GeneOas3
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1138 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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
- 3 ATP = 5'-triphosphoadenylyl-(2'->5')-adenylyl-(2'->5')-adenosine + 2 diphosphate
Cofactor
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 154 | Interaction with dsRNA | ||||
Sequence: Q | ||||||
Site | 242 | Interaction with dsRNA | ||||
Sequence: D | ||||||
Binding site | 855 | ATP (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 867 | Mg2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Binding site | 869 | Mg2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Binding site | 939 | Mg2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Binding site | 998 | ATP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 1001 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 1020 | ATP (UniProtKB | ChEBI) | ||||
Sequence: Q |
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended name2'-5'-oligoadenylate synthase 3
- EC number
- Short names(2-5')oligo(A) synthase 3; 2-5A synthase 3
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ8VI93
- Secondary accessions
Proteomes
Organism-specific databases
PTM/Processing
Features
Showing features for modified residue, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 1 | N-acetylmethionine | ||||
Sequence: M | ||||||
Chain | PRO_0000418630 | 1-1138 | 2'-5'-oligoadenylate synthase 3 | |||
Sequence: MDLFHTPAGALDKLVAHNLHPAPEFTAAVRGALGSLNITLQQHRARGSQRPRVIRIAKGGAYARGTALRGGTDVELVIFLDCFQSFGDQKTCHSETLGAMRMLLESWGGHPGPGLTFEFSQSKASRILQFRLASADGEHWIDVSLVPAFDVLGQPRSGVKPTPNVYSSLLSSHCQAGEYSACFTEPRKNFVNTRPAKLKNLILLVKHWYHQVQTRAVRATLPPSYALELLTIFAWEQGCGKDSFSLAQGLRTVLALIQHSKYLCIFWTENYGFEDPAVGEFLRRQLKRPRPVILDPADPTWDVGNGTAWRWDVLAQEAESSFSQQCFKQASGVLVQPWEGPGLPRAGILDLGHPIYQGPNQALEDNKGHLAVQSKERSQKPSNSAPGFPEAATKIPAMPNPSANKTRKIRKKAAHPKTVQEAALDSISSHVRITQSTASSHMPPDRSSISTAGSRMSPDLSQIPSKDLDCFIQDHLRPSPQFQQQVKQAIDAILCCLREKSVYKVLRVSKGGSFGRGTDLRGSCDVELVIFYKTLGDFKGQKPHQAEILRDMQAQLRHWCQNPVPGLSLQFIEQKPNALQLQLASTDLSNRVDLSVLPAFDAVGPLKSGTKPQPQVYSSLLSSGCQAGEHAACFAELRRNFINTCPPKLKSLMLLVKHWYRQVVTRYKGGEAAGDAPPPAYALELLTIFAWEQGCGEQKFSLAEGLRTILRLIQQHQSLCIYWTVNYSVQDPAIRAHLLCQLRKARPLVLDPADPTWNVGQGDWKLLAQEAAALGSQVCLQSGDGTLVPPWDVTPALLHQTLAEDLDKFISEFLQPNRHFLTQVKRAVDTICSFLKENCFRNSTIKVLKVVKGGSSAKGTALQGRSDADLVVFLSCFRQFSEQGSHRAEIISEIQAHLEACQQMHSFDVKFEVSKRKNPRVLSFTLTSQTLLDQSVDFDVLPAFDALGQLRSGSRPDPRVYTDLIHSCSNAGEFSTCFTELQRDFITSRPTKLKSLIRLVKYWYQQCNKTIKGKGSLPPQHGLELLTVYAWEQGGQNPQFNMAEGFRTVLELIVQYRQLCVYWTINYSAEDKTIGDFLKMQLRKPRPVILDPADPTGNLGHNARWDLLAKEATVYASALCCVDRDGNPIKPWPVKAAV |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Intestine.
Induction
By type I interferon (IFN) and viruses.
Gene expression databases
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 6-341 | OAS domain 1 | ||||
Sequence: TPAGALDKLVAHNLHPAPEFTAAVRGALGSLNITLQQHRARGSQRPRVIRIAKGGAYARGTALRGGTDVELVIFLDCFQSFGDQKTCHSETLGAMRMLLESWGGHPGPGLTFEFSQSKASRILQFRLASADGEHWIDVSLVPAFDVLGQPRSGVKPTPNVYSSLLSSHCQAGEYSACFTEPRKNFVNTRPAKLKNLILLVKHWYHQVQTRAVRATLPPSYALELLTIFAWEQGCGKDSFSLAQGLRTVLALIQHSKYLCIFWTENYGFEDPAVGEFLRRQLKRPRPVILDPADPTWDVGNGTAWRWDVLAQEAESSFSQQCFKQASGVLVQPWEGP | ||||||
Region | 12-56 | Interaction with dsRNA | ||||
Sequence: DKLVAHNLHPAPEFTAAVRGALGSLNITLQQHRARGSQRPRVIRI | ||||||
Region | 185-199 | Interaction with dsRNA | ||||
Sequence: EPRKNFVNTRPAKLK | ||||||
Region | 342-462 | Linker | ||||
Sequence: GLPRAGILDLGHPIYQGPNQALEDNKGHLAVQSKERSQKPSNSAPGFPEAATKIPAMPNPSANKTRKIRKKAAHPKTVQEAALDSISSHVRITQSTASSHMPPDRSSISTAGSRMSPDLSQ | ||||||
Region | 370-403 | Disordered | ||||
Sequence: LAVQSKERSQKPSNSAPGFPEAATKIPAMPNPSA | ||||||
Region | 434-459 | Disordered | ||||
Sequence: TQSTASSHMPPDRSSISTAGSRMSPD | ||||||
Region | 463-793 | OAS domain 2 | ||||
Sequence: IPSKDLDCFIQDHLRPSPQFQQQVKQAIDAILCCLREKSVYKVLRVSKGGSFGRGTDLRGSCDVELVIFYKTLGDFKGQKPHQAEILRDMQAQLRHWCQNPVPGLSLQFIEQKPNALQLQLASTDLSNRVDLSVLPAFDAVGPLKSGTKPQPQVYSSLLSSGCQAGEHAACFAELRRNFINTCPPKLKSLMLLVKHWYRQVVTRYKGGEAAGDAPPPAYALELLTIFAWEQGCGEQKFSLAEGLRTILRLIQQHQSLCIYWTVNYSVQDPAIRAHLLCQLRKARPLVLDPADPTWNVGQGDWKLLAQEAAALGSQVCLQSGDGTLVPPWDV | ||||||
Region | 801-1135 | OAS domain 3 | ||||
Sequence: TLAEDLDKFISEFLQPNRHFLTQVKRAVDTICSFLKENCFRNSTIKVLKVVKGGSSAKGTALQGRSDADLVVFLSCFRQFSEQGSHRAEIISEIQAHLEACQQMHSFDVKFEVSKRKNPRVLSFTLTSQTLLDQSVDFDVLPAFDALGQLRSGSRPDPRVYTDLIHSCSNAGEFSTCFTELQRDFITSRPTKLKSLIRLVKYWYQQCNKTIKGKGSLPPQHGLELLTVYAWEQGGQNPQFNMAEGFRTVLELIVQYRQLCVYWTINYSAEDKTIGDFLKMQLRKPRPVILDPADPTGNLGHNARWDLLAKEATVYASALCCVDRDGNPIKPWPVK |
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
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,138
- Mass (Da)126,333
- Last updated2002-03-01 v1
- Checksum64568BA94FC51866
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
F7CXR7 | F7CXR7_MOUSE | Oas3 | 131 |
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 215 | in Ref. 2; AAM47556 | ||||
Sequence: R → Q | ||||||
Sequence conflict | 733 | in Ref. 2; AAM47556 | ||||
Sequence: A → T | ||||||
Sequence conflict | 897 | in Ref. 2; AAM47556, 4; EDL19752 and 5; AAI41056 | ||||
Sequence: H → Q | ||||||
Sequence conflict | 904 | in Ref. 2; AAM47556 | ||||
Sequence: M → T |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |