OAS1
2'-5'-oligoadenylate synthase 1
Also known as: IFI-4, OAS1_HUMAN, OIAS, OIASI
Cross-references: UniProt · Ensembl · Human Protein Atlas · GeneCards · NCBI Gene
Protein identityUniProt · HPA
- UniProt accession
- P00973
- Gene
- OAS1
- Ensembl
- ENSG00000089127
- Chromosome
- 12
- Canonical length
- 400 aa
- Protein class
- Disease related genes, Enzymes, Potential drug targets, Predicted intracellular proteins
- Subcellular location
- Nucleoplasm,Cytosol
- Secretome location
- Intracellular and membrane
- Quaternary structure
- Homotetramer
OverviewNCBI Gene
This interferon-induced gene encodes a protein that synthesizes 2',5'-oligoadenylates (2-5As). This protein plays a key role in innate cellular antiviral response, and has been implicated in other cellular processes like cell growth and apoptosis. Alternative splicing results in multiple transcript variants with different enzymatic activities. Polymorphisms in this gene have been associated with susceptibility to viral infection, including SARS-CoV-2, and diabetes mellitus, type 1. This gene is located in a cluster of related genes on chromosome 12. [provided by RefSeq, May 2022]
Canonical amino-acid sequenceUniProt
400 residues, UniProt reviewed canonical sequence.
>P00973|OAS1
1 MMDLRNTPAK SLDKFIEDYL LPDTCFRMQI NHAIDIICGF LKERCFRGSS YPVCVSKVVK
61 GGSSGKGTTL RGRSDADLVV FLSPLTTFQD QLNRRGEFIQ EIRRQLEACQ RERAFSVKFE
121 VQAPRWGNPR ALSFVLSSLQ LGEGVEFDVL PAFDALGQLT GGYKPNPQIY VKLIEECTDL
181 QKEGEFSTCF TELQRDFLKQ RPTKLKSLIR LVKHWYQNCK KKLGKLPPQY ALELLTVYAW
241 ERGSMKTHFN TAQGFRTVLE LVINYQQLCI YWTKYYDFKN PIIEKYLRRQ LTKPRPVILD
301 PADPTGNLGG GDPKGWRQLA QEAEAWLNYP CFKNWDGSPV SSWILLAESN SADDETDDPR
361 RYQKYGYIGT HEYPHFSHRP STLQAASTPQ AEEDWTCTILLocalizationUniProt · AlphaFold · HPA
Whether an antibody against OAS1 can act on the native protein depends on physical access: surface and secreted proteins are reachable by circulating antibodies, intracellular proteins usually are not.
- Antibody reachability
- Secreted
- Secreted
- Yes
- Transmembrane segments
- 0
- Mean surface accessibility (rSASA)
- 0.3
- Highest tissue expression
- 104 nTPM
Expression across tissuesHPA
Tissue
- urinary bladder: 104 nTPM
- salivary gland: 86 nTPM
- esophagus: 53 nTPM
- duodenum: 49 nTPM
- colon: 46 nTPM
- spleen: 46 nTPM
Single-cell type
- esophageal apical cells: 840 nCPM
- urothelial cells: 381 nCPM
- esophageal suprabasal cells: 155 nCPM
- hofbauer cells: 152 nCPM
- colonocytes: 129 nCPM
- foveolar cells: 124 nCPM
Immune cell
- non-classical monocyte: 575 nTPM
- intermediate monocyte: 404 nTPM
- classical monocyte: 254 nTPM
- total PBMC: 218 nTPM
- myeloid DC: 154 nTPM
- plasmacytoid DC: 145 nTPM
Brain region
- spinal cord: 37 nTPM
- medulla oblongata: 25 nTPM
- pons: 17 nTPM
- white matter: 13 nTPM
- thalamus: 10 nTPM
- midbrain: 9 nTPM
DiseaseUniProt · ClinVar · IEDB · PubMed
Four sources answering four different questions about OAS1.
Disease | AllUniProt
Conditions OAS1 is implicated in, by any mechanism.
- Immunodeficiency 100 with pulmonary alveolar proteinosis and hypogammaglobulinemia (IMD100) MIM:618042
Disease | GeneticClinVar
2 pathogenic / likely-pathogenic of 393 ClinVar records.
Conditions with pathogenic or likely-pathogenic variants.
- Pulmonary alveolar proteinosis with hypogammaglobulinemia
Genetic constraint and essentialitygnomAD · DepMap
Does the body need this protein intact? Low LOEUF or a strong DepMap dependency means loss or blockade of the protein is likely to be felt.
- gnomAD LOEUF (loss-of-function intolerance)
- 0.93
- gnomAD pLI
- 0
- gnomAD missense Z
- -0.43
- DepMap mean gene effect
- -0.01
- DepMap dependency class
- none
Cancer expressionTCGA
Across TCGA tumor cohorts, this protein is over-expressed in roughly 5% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).
OntologyGO
Biological processes
- antiviral innate immune response
- cellular response to exogenous dsRNA
- cellular response to interferon-alpha
- cellular response to interferon-beta
- cellular response to virus
- defense response to bacterium
- defense response to virus
- glucose homeostasis
- glucose metabolic process
- interleukin-27-mediated signaling pathway
- negative regulation of chemokine (C-X-C motif) ligand 2 production
- negative regulation of IP-10 production
- negative regulation of type I interferon-mediated signaling pathway
- negative regulation of viral genome replication
- positive regulation of cellular respiration
- positive regulation of interferon-beta production
- positive regulation of monocyte chemotactic protein-1 production
- positive regulation of tumor necrosis factor production
- protein complex oligomerization
- regulation of ribonuclease activity
- response to virus
- surfactant homeostasis
- toll-like receptor 3 signaling pathway
- toll-like receptor 4 signaling pathway
- type I interferon-mediated signaling pathway
Molecular functions
Cellular components
Protein domainsUniProt · Pfam · InterPro
- Polymerase, nucleotidyl transferase domain
- 2-5OAS/ClassI-CCAase, nucleotidyltransferase domain
- 2-5-oligoadenylate synthetase, C-terminal conserved site
- 2'-5'-oligoadenylate synthetase 1, domain 2/C-terminal
- 2-5-oligoadenylate synthetase, N-terminal conserved site
- Nucleotidyltransferase superfamily
- Nucleotidyltransferase domain
- 2'-5'-oligoadenylate synthetase 1, domain 2, C-terminus
KeywordsUniProt
InteractionsUniProt · HPA
Protein binding partners of OAS1 in the human serome: UniProt-annotated complex subunits plus reported interactors. Each links to its own Seroatlas record.
Antibody and autoantibody relevanceSeroatlas analysis
Seroatlas reads OAS1 as an antibody target. Whether an autoantibody or antibody against OAS1 could matter depends on whether native OAS1 is physically reachable, whether the body needs it intact, and whether it acts in a disease-relevant tissue.
OAS1 is annotated as secreted, so native OAS1 circulates and is directly accessible to antibodies. Secreted and cell-surface proteins are the autoantibody targets most likely to act like drugs, blocking or depleting the native protein.
Annotation status
The present source text does not explicitly label OAS1 as an autoantigen. Seroatlas presents hypothesis context only and does not manufacture a known-serology claim.
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