UniProt Accession

 OAS1A_MOUSE; P11928; F2Z419; Q3UEC1; Q64440; Q91VI0 

Genbank Protein ID

 X04958; M33863; AK149613; AC015535; CH466529; BC013715; BC057878; X58077 

Genbank Nucleotide ID

 CAA28620.1; AAA37116.1; BAE28990.1; EDL19743.1; AAH13715.1; AAH57878.1; CAA41105.1 

Protein Name

 2'-5'-oligoadenylate synthase 1A 

Protein Synonyms/Alias

 (2-5')oligo(A) synthase 1A; 2-5A synthase 1A; p42 OAS 

Gene Name

 Oas1a 

Gene Synonyms/Alias

 Oias1 

Created Date

 July 27, 2013 

Organism

 Mus musculus (Mouse) 

NCBI Taxa ID

 10090 

Lysine Modification

Position	Peptide	Type	References
43	NVVCDFLKERCFQGA	acetylation	[1, 2]

Reference

 [1] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [2] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337] 

Functional Description

 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 higher oligomers 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. 

Sequence Annotation

 METAL 76 76 Magnesium; catalytic (Potential).
 METAL 78 78 Magnesium; catalytic (Potential).
 METAL 149 149 Magnesium; catalytic (Potential).
 BINDING 211 211 Substrate (By similarity).
 BINDING 214 214 ATP (By similarity).  

Keyword

 Antiviral defense; ATP-binding; Complete proteome; Cytoplasm; Endoplasmic reticulum; Immunity; Innate immunity; Magnesium; Metal-binding; Microsome; Mitochondrion; Nucleotide-binding; Nucleotidyltransferase; Nucleus; Reference proteome; RNA-binding; Transferase. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 367 AA 

Protein Sequence

Gene Ontology

 GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
 GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0001730; F:2'-5'-oligoadenylate synthetase activity; IDA:UniProtKB.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0003725; F:double-stranded RNA binding; IDA:UniProtKB.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
 GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
 GO:0006164; P:purine nucleotide biosynthetic process; IDA:UniProtKB.
 GO:0009615; P:response to virus; TAS:UniProtKB. 

Interpro

 IPR006117; 2-5-oligoadenylate_synth_CS.
 IPR006116; 2-5-oligoadenylate_synth_N.
 IPR018952; 2-5-oligoAdlate_synth_1_dom2/C.
 IPR026774; 2-5A_synthase.
 IPR002934; Nucleotidyltransferase. 

Pfam

 PF01909; NTP_transf_2
 PF10421; OAS1_C 

SMART

  

PROSITE

 PS00832; 25A_SYNTH_1
 PS00833; 25A_SYNTH_2
 PS50152; 25A_SYNTH_3 

PRINTS