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)
End	112,933,219 bp
Gene location (Mouse)
Chr.	Chromosome 5 (mouse)
End	120,907,521 bp
RNA expression pattern
	Top expressed in
	stomach; ; urinary bladder; ; duodenum; ; colon; ; spleen;
	More reference expression data
	; ;
	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
	4938
	246730
	ENSG00000089127
	ENSMUSG00000052776
	P00973
	P11928
	NM_001032409 ; NM_002534 ; NM_016816 ; NM_001320151
	NM_145211
	NP_001027581 ; NP_001307080 ; NP_002525 ; NP_058132
	NP_660212
	Wikidata
View/Edit Human	View/Edit Mouse

Last updated January 26, 2022

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]

Related Research Articles

Ribonuclease L or RNase L, known sometimes as ribonuclease 4 or 2'-5' oligoadenylate synthetase-dependent ribonuclease — is an interferon (IFN)-induced ribonuclease which, upon activation, destroys all RNA within the cell. RNase L is an enzyme that in humans is encoded by the RNASEL gene.

Signal transducer and activator of transcription 2 is a protein that in humans is encoded by the STAT2 gene. It is a member of the STAT protein family. This protein is critical to the biological response of type I interferons (IFNs). STAT2 sequence identity between mouse and human is only 68%.

Fibroblast growth factor receptor 4 is a protein that in humans is encoded by the FGFR4 gene. FGFR4 has also been designated as CD334.

WEE1 homolog , also known as WEE1, is a protein which in humans is encoded by the WEE1 gene.

Receptor-type tyrosine-protein phosphatase alpha is an enzyme that in humans is encoded by the PTPRA gene.

Tryptophanyl-tRNA synthetase, cytoplasmic is an enzyme that in humans is encoded by the WARS gene.

Profilin-2 is a protein that in humans is encoded by the PFN2 gene.

Bifunctional aminoacyl-tRNA synthetase is an enzyme that in humans is encoded by the EPRS gene.

Interferon-induced protein with tetratricopeptide repeats 1 is a protein that in humans is encoded by the IFIT1 gene.

Cleavage and polyadenylation specificity factor subunit 1 is a protein that in humans is encoded by the CPSF1 gene.

ETS domain-containing protein Elk-3 is a protein that in humans is encoded by the ELK3 gene.

2'-5'-oligoadenylate synthetase 2 is an enzyme that in humans is encoded by the OAS2 gene.

Interferon-induced transmembrane protein 1 is a protein that in humans is encoded by the IFITM1 gene. IFITM1 has also recently been designated CD225. This protein has several additional names: fragilis, IFI17 [interferon-induced protein 17], 9-27 [Interferon-inducible protein 9-27] and Leu13.

Protocadherin-1 is a protein that in humans is encoded by the PCDH1 gene.

Interferon alpha-inducible protein 6 is a protein that in humans is encoded by the IFI6 gene.

Zinc finger protein 143 is a protein that in humans is encoded by the ZNF143 gene.

59 kDa 2'-5'-oligoadenylate synthetase-like protein is an enzyme that in humans is encoded by the OASL gene.

2'-5'-oligoadenylate synthetase 3 is an enzyme that in humans is encoded by the OAS3 gene.

Interferon-alpha/beta receptor alpha chain is a protein that in humans is encoded by the IFNAR1 gene.

Interferon alpha-1/13, also known as IFN-alpha-1/13, is a protein that in humans is encoded by the IFNA1 and IFNA13 genes.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000089127 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000052776 - Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ 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.
↑ 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.
↑ 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.
↑ "Entrez Gene: OAS1 2',5'-oligoadenylate synthetase 1, 40/46kDa".

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.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000089127 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 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.

[pmid9344649-5] 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.

[pmid9325053-6] 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.

[entrez-8] "Entrez Gene: OAS1 2',5'-oligoadenylate synthetase 1, 40/46kDa".

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OAS1

Related Research Articles

References

Further reading