| UniProt functional annotation for Q6L8Q7 | |||
| UniProt code: Q6L8Q7. |
| Organism: | Homo sapiens (Human). | |
| Taxonomy: | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo. | |
| Function: | Enzyme that cleaves 2',5'-phosphodiester bond linking adenosines of the 5'-triphosphorylated oligoadenylates, triphosphorylated oligoadenylates referred as 2-5A modulates the 2-5A system. Degrades triphosphorylated 2-5A to produce AMP and ATP (PubMed:26055709). Also cleaves 3',5'-phosphodiester bond of oligoadenylates (PubMed:21666256, PubMed:30389976, PubMed:26055709). Plays a role as a negative regulator of the 2-5A system that is one of the major pathways for antiviral and antitumor functions induced by interferons (IFNs). Suppression of this enzyme increases cellular 2-5A levels and decreases viral replication in cultured small-airway epithelial cells and Hela cells (PubMed:26055709). {ECO:0000269|PubMed:15231837, ECO:0000269|PubMed:21245038, ECO:0000269|PubMed:21666256, ECO:0000269|PubMed:22285541, ECO:0000269|PubMed:26055709, ECO:0000269|PubMed:30389976}. | |
| Catalytic activity: | Reaction=Exonucleolytic cleavage of poly(A) to 5'-AMP.; EC=3.1.13.4; Evidence={ECO:0000269|PubMed:21245038, ECO:0000269|PubMed:21666256, ECO:0000269|PubMed:22285541, ECO:0000269|PubMed:26055709, ECO:0000269|PubMed:30389976}; | |
| Cofactor: | Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:22285541, ECO:0000269|PubMed:26055709, ECO:0000269|Ref.16}; | |
| Biophysicochemical properties: | pH dependence: Optimum pH is 8.0 for 2'-5' oligoadenylate exonuclease activity. {ECO:0000269|PubMed:22285541}; | |
| Subcellular location: | Mitochondrion matrix {ECO:0000269|PubMed:21245038, ECO:0000269|PubMed:21666256, ECO:0000269|PubMed:22285541}. | |
| Tissue specificity: | Ubiquitous. {ECO:0000269|PubMed:15231837}. | |
| Similarity: | Belongs to the CCR4/nocturin family. {ECO:0000305}. | |
Annotations taken from UniProtKB at the EBI.