LipidDB ID

LipidDB-9606-01037

Entry Name

UniProt Accession

P29728; A8K9T1; Q6PJ33; Q86XX8;

Theoretical PI

8.55

Molecular Weight

82430.62

Genbank Protein ID

AAA60607.1; AAA60606.1; BAF85485.1; EAW98027.1; AAH23637.1; AAH49215.1;

Genbank Nucleotide ID

M87434; M87284; AK292796; AC004551; CH471054; BC023637; BC049215;

Protein Name

2'-5'-oligoadenylate synthase 2

Protein Synonyms/Alias

(2-5')oligo(A) synthase 2; 2-5A synthase 2; 2.7.7.84; p69 OAS / p71 OAS; p69OAS / p71OAS;

Gene Name

OAS2

Gene Synonyms/Alias

Created Date

01-APR-1993

Organism

Homo sapiens (Human)

NCBI Taxa ID

9606

Reference

[1] Sarkar SN, Bandyopadhyay S, Ghosh A, Sen GC. Enzymatic characteristics ofrecombinant medium isozyme of 2'-5' oligoadenylate synthetase. J Biol Chem. 1999 Jan 15;274(3):1848-55.[PMID:9880569]
[2] Marié I, Svab J, Robert N, Galabru J, Hovanessian AG. Differential expression and distinct structure of 69- and 100-kDa forms of 2-5A synthetase in human cellstreated with interferon. J Biol Chem. 1990 Oct 25;265(30):18601-7.[PMID:2211721]

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

Region: 11 335 OAS domain 1.
Region: 343 683 OAS domain 2.
Metal binding site: 408 408 Magnesium; catalytic.
Metal binding site: 410 410 Magnesium; catalytic.
Metal binding site: 481 481 Magnesium; catalytic.
Binding site: 544 544 Substrate.
Binding site: 547 547 ATP.
Modified residue: 378 378 N6-acetyllysine.

Protein Length

719 AA.

Protein Sequence
(Canonical)

FASTA
(Canonical)

Gene Ontology

GO:0005737; C:cytoplasm; IDA:UniProtKB
GO:0005829; C:cytosol; TAS:Reactome
GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW
GO:0043231; C:intracellular membrane-bounded organelle; TAS:ProtInc
GO:0016020; C:membrane; IDA:UniProtKB
GO:0005739; C:mitochondrion; IEA:UniProtKB-KW
GO:0005634; C:nucleus; IEA:UniProtKB-KW
GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB
GO:0001730; F:2'-5'-oligoadenylate synthetase activity; IDA:UniProtKB
GO:0005524; F:ATP binding; IMP:UniProtKB
GO:0003725; F:double-stranded RNA binding; IDA:UniProtKB
GO:0046872; F:metal ion binding; IEA:UniProtKB-KW
GO:0008270; F:zinc ion binding; IDA:UniProtKB
GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome
GO:0051607; P:defense response to virus; IEA:UniProtKB-KW
GO:0060333; P:interferon-gamma-mediated signaling pathway; TAS:Reactome
GO:0006139; P:nucleobase-containing compound metabolic process; TAS:ProtInc
GO:0006486; P:protein glycosylation; IDA:UniProtKB
GO:0018377; P:protein myristoylation; IMP:UniProtKB
GO:0006164; P:purine nucleotide biosynthetic process; IDA:UniProtKB
GO:0009615; P:response to virus; TAS:UniProtKB
GO:0006401; P:RNA catabolic process; IEA:Ensembl
GO:0060337; P:type I interferon signaling pathway; TAS:Reactome

Interpro

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

Pfam

Pfam; PF01909; NTP_transf_2;
Pfam; PF10421; OAS1_C;

SMART

PROSITE

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

PRINTS