OAS1

OAS1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 4IG8
Identifiers
Aliases	OAS1 , IFI-4, OIAS, OIASI, E18/E16, 2'-5'-oligoadenylate synthetase 1
External IDs	OMIM: 164350 MGI: 2180860 HomoloGene: 1903 GeneCards: OAS1
Gene location (Human) Chr. Chromosome 12 (human) [1] Band 12q24.13 Start 112,905,856 bp [1] End 112,933,219 bp [1]
Gene location (Mouse) Chr. Chromosome 5 (mouse) [2] Band 5 F|5 60.65 cM Start 120,896,256 bp [2] End 120,907,521 bp [2]
RNA expression pattern Bgee Top expressed in stomach urinary bladder duodenum colon spleen More reference expression data BioGPS More reference expression data
Gene ontology Molecular function transferase activity nucleotide binding nucleotidyltransferase activity metal ion binding GO:0001948 protein binding RNA binding double-stranded RNA binding ATP binding 2'-5'-oligoadenylate synthetase activity Cellular component cytoplasm intracellular membrane-bounded organelle extracellular region endoplasmic reticulum mitochondrion nucleus cytosol nucleoplasm Biological process purine nucleotide biosynthetic process regulation of ribonuclease activity glucose homeostasis interferon-gamma-mediated signaling pathway immune system process response to virus negative regulation of viral genome replication defense response to virus type I interferon signaling pathway protein complex oligomerization immune response glucose metabolic process cellular response to interferon-alpha innate immune response Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	4938	246730
Ensembl	ENSG00000089127	ENSMUSG00000052776
UniProt	P00973	P11928
RefSeq (mRNA)	NM_001032409 NM_002534 NM_016816 NM_001320151	NM_145211
RefSeq (protein)	NP_001027581 NP_001307080 NP_002525 NP_058132	NP_660212
Location (UCSC)	Chr 12: 112.91 – 112.93 Mb	Chr 5: 120.9 – 120.91 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

2'-5'-oligoadenylate synthetase 1 is an enzyme that in humans is encoded by the OAS1 gene. ^{[5] [6]}

This gene encodes a member of the 2-5A synthetase family, which include essential proteins involved in the innate immune response to viral infection.

The encoded protein is induced by interferons and uses adenosine triphosphate in 2'-specific nucleotidyl transfer reactions to synthesize 2',5'-oligoadenylates (2-5As). These molecules activate latent RNase L, which results in both viral and endogenous RNA degradation and the inhibition of viral replication. The three known members of this gene family are located in a cluster on chromosome 12. Hypomorphic mutations in this gene have been associated with host susceptibility to viral infection, while gain-of-function variants can cause autoinflammatory immunodeficiency. ^[7] Alternatively spliced transcript variants encoding different isoforms have been described. ^[8]

References

1. GRCh38: Ensembl release 89: ENSG00000089127 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000052776 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Renault B, Hovnanian A, Bryce S, Chang JJ, Lau S, Sakuntabhai A, Monk S, Carter S, Ross CJ, Pang J, Twells R, Chamberlain S, Monaco AP, Strachan T, Kucherlapati R (Feb 1998). "A sequence-ready physical map of a region of 12q24.1". Genomics. 45 (2): 271–8. doi:10.1006/geno.1997.4888. PMID   9344649.
6. Nechiporuk T, Nechiporuk A, Sahba S, Figueroa K, Shibata H, Chen XN, Korenberg JR, de Jong P, Pulst SM (Nov 1997). "A high-resolution PAC and BAC map of the SCA2 region". Genomics. 44 (3): 321–9. doi:10.1006/geno.1997.4886. PMID   9325053.
7. Magg, T.; Okano, T.; Koenig, L. M.; Boehmer DFR; Schwartz, S. L.; Inoue, K.; Heimall, J.; Licciardi, F.; Ley-Zaporozhan, J.; Ferdman, R. M.; Caballero-Oteyza, A.; Park, E. N.; Calderon, B. M.; Dey, D.; Kanegane, H.; Cho, K.; Montin, D.; Reiter, K.; Griese, M.; Albert, M. H.; Rohlfs, M.; Gray, P.; Walz, C.; Conn, G. L.; Sullivan, K. E.; Klein, C.; Morio, T.; Hauck, F. (2021). "Heterozygous OAS1 gain-of-function variants cause an autoinflammatory immunodeficiency". Sci Immunol. 6 (60): eabf9564. doi:10.1126/sciimmunol.abf9564. PMC   8392508 . PMID   34145065.
8. "Entrez Gene: OAS1 2',5'-oligoadenylate synthetase 1, 40/46kDa".

Further reading

• Justesen J, Hartmann R, Kjeldgaard NO (2000). "Gene structure and function of the 2'-5'-oligoadenylate synthetase family". Cell. Mol. Life Sci. 57 (11): 1593–612. doi:10.1007/PL00000644. PMID   11092454. S2CID   19154357.
• Ghosh SK, Kusari J, Bandyopadhyay SK, et al. (1991). "Cloning, sequencing, and expression of two murine 2'-5'-oligoadenylate synthetases. Structure-function relationships". J. Biol. Chem. 266 (23): 15293–9. doi: 10.1016/S0021-9258(18)98615-1 . PMID   1651324.
• Silverman RH, Sengupta DN (1991). "Translational regulation by HIV leader RNA, TAT, and interferon-inducible enzymes". J. Exp. Pathol. 5 (2): 69–77. PMID   1708818.
• Saunders ME, Gewert DR, Tugwell ME, et al. (1985). "Human 2-5A synthetase: characterization of a novel cDNA and corresponding gene structure". EMBO J. 4 (7): 1761–8. doi:10.1002/j.1460-2075.1985.tb03848.x. PMC   554415 . PMID   2411547.
• Benech P, Mory Y, Revel M, Chebath J (1986). "Structure of two forms of the interferon-induced (2'-5') oligo A synthetase of human cells based on cDNAs and gene sequences". EMBO J. 4 (9): 2249–56. doi:10.1002/j.1460-2075.1985.tb03922.x. PMC   554493 . PMID   2416561.
• Williams BR, Saunders ME, Willard HF (1986). "Interferon-regulated human 2-5A synthetase gene maps to chromosome 12". Somat. Cell Mol. Genet. 12 (4): 403–8. doi:10.1007/BF01570735. PMID   2426799. S2CID   13077134.
• Hovanessian AG, Laurent AG, Chebath J, et al. (1987). "Identification of 69-kd and 100-kd forms of 2-5A synthetase in interferon-treated human cells by specific monoclonal antibodies". EMBO J. 6 (5): 1273–80. doi:10.1002/j.1460-2075.1987.tb02364.x. PMC   553929 . PMID   2440675.
• Rutherford MN, Hannigan GE, Williams BR (1988). "Interferon-induced binding of nuclear factors to promoter elements of the 2-5A synthetase gene". EMBO J. 7 (3): 751–9. doi:10.1002/j.1460-2075.1988.tb02872.x. PMC   454386 . PMID   2456211.
• Benech P, Vigneron M, Peretz D, et al. (1988). "Interferon-responsive regulatory elements in the promoter of the human 2',5'-oligo(A) synthetase gene". Mol. Cell. Biol. 7 (12): 4498–504. doi:10.1128/MCB.7.12.4498. PMC   368134 . PMID   2830497.
• Wathelet MG, Clauss IM, Nols CB, et al. (1988). "New inducers revealed by the promoter sequence analysis of two interferon-activated human genes". Eur. J. Biochem. 169 (2): 313–21. doi: 10.1111/j.1432-1033.1987.tb13614.x . PMID   3121313.
• Wathelet MG, Szpirer J, Nols CB, et al. (1988). "Cloning and chromosomal location of human genes inducible by type I interferon". Somat. Cell Mol. Genet. 14 (5): 415–26. doi:10.1007/BF01534709. PMID   3175763. S2CID   42406993.
• Wathelet M, Moutschen S, Cravador A, et al. (1986). "Full-length sequence and expression of the 42 kDa 2-5A synthetase induced by human interferon". FEBS Lett. 196 (1): 113–20. doi: 10.1016/0014-5793(86)80224-1 . PMID   3753689. S2CID   38673605.
• Shiojiri S, Fukunaga R, Ichii Y, Sokawa Y (1986). "Structure and expression of a cloned cDNA for human (2'-5')oligoadenylate synthetase". J. Biochem. 99 (5): 1455–64. doi:10.1093/oxfordjournals.jbchem.a135615. PMID   3754863.
• Merlin G, Chebath J, Benech P, et al. (1983). "Molecular cloning and sequence of partial cDNA for interferon-induced (2'-5')oligo(A) synthetase mRNA from human cells". Proc. Natl. Acad. Sci. U.S.A. 80 (16): 4904–8. Bibcode:1983PNAS...80.4904M. doi: 10.1073/pnas.80.16.4904 . PMC   384155 . PMID   6348777.
• Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID   8125298.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID   9373149.
• Ghosh A, Sarkar SN, Guo W, et al. (1998). "Enzymatic activity of 2'-5'-oligoadenylate synthetase is impaired by specific mutations that affect oligomerization of the protein". J. Biol. Chem. 272 (52): 33220–6. doi: 10.1074/jbc.272.52.33220 . PMID   9407111.
• Hovnanian A, Rebouillat D, Mattei MG, et al. (1998). "The human 2',5'-oligoadenylate synthetase locus is composed of three distinct genes clustered on chromosome 12q24.2 encoding the 100-, 69-, and 40-kDa forms". Genomics. 52 (3): 267–77. doi:10.1006/geno.1998.5443. PMID   9790745.
• Sarkar SN, Ghosh A, Wang HW, et al. (1999). "The nature of the catalytic domain of 2'-5'-oligoadenylate synthetases". J. Biol. Chem. 274 (36): 25535–42. doi: 10.1074/jbc.274.36.25535 . PMID   10464285.