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Overview

Uniprot IDQ9Y6K5
Protein Name2'-5'-oligoadenylate synthase 3
Gene NameOAS3
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
370 QKTPENSKSLNAVYP
59 PRVLKTVKGGSSGRG

Function

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. Catalyzes preferentially the dimerization of ATP to form 2'-5'-diadenylate (2-5A), but can also form the trimeric 2'-5'-oligoadenylate. The oligoadenylate then binds 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. Displays antiviral activity against Chikungunya virus (CHIKV), Dengue virus, Sindbis virus (SINV) and Semliki forest virus (SFV)

Protein Sequence

10 MDLYSTPAAA 20 LDRFVARRLQ 30 PRKEFVEKAR 40 RALGALAAAL 50 RERGGRLGAA 60 APRVLKTVKG 70 GSSGRGTALK 80 GGCDSELVIF 90 LDCFKSYVDQ 100 RARRAEILSE 110 MRASLESWWQ 120 NPVPGLRLTF 130 PEQSVPGALQ 140 FRLTSVDLED 150 WMDVSLVPAF 160 NVLGQAGSGV 170 KPKPQVYSTL 180 LNSGCQGGEH 190 AACFTELRRN 200 FVNIRPAKLK 210 NLILLVKHWY 220 HQVCLQGLWK 230 ETLPPVYALE 240 LLTIFAWEQG 250 CKKDAFSLAE 260 GLRTVLGLIQ 270 QHQHLCVFWT 280 VNYGFEDPAV 290 GQFLQRQLKR 300 PRPVILDPAD 310 PTWDLGNGAA 320 WHWDLLAQEA 330 ASCYDHPCFL 340 RGMGDPVQSW 350 KGPGLPRAGC 360 SGLGHPIQLD 370 PNQKTPENSK 380 SLNAVYPRAG 390 SKPPSCPAPG 400 PTGAASIVPS 410 VPGMALDLSQ 420 IPTKELDRFI 430 QDHLKPSPQF 440 QEQVKKAIDI 450 ILRCLHENCV 460 HKASRVSKGG 470 SFGRGTDLRD 480 GCDVELIIFL 490 NCFTDYKDQG 500 PRRAEILDEM 510 RAQLESWWQD 520 QVPSLSLQFP 530 EQNVPEALQF 540 QLVSTALKSW 550 TDVSLLPAFD 560 AVGQLSSGTK 570 PNPQVYSRLL 580 TSGCQEGEHK 590 ACFAELRRNF 600 MNIRPVKLKN 610 LILLVKHWYR 620 QVAAQNKGKG 630 PAPASLPPAY 640 ALELLTIFAW 650 EQGCRQDCFN 660 MAQGFRTVLG 670 LVQQHQQLCV 680 YWTVNYSTED 690 PAMRMHLLGQ 700 LRKPRPLVLD 710 PADPTWNVGH 720 GSWELLAQEA 730 AALGMQACFL 740 SRDGTSVQPW 750 DVMPALLYQT 760 PAGDLDKFIS 770 EFLQPNRQFL 780 AQVNKAVDTI 790 CSFLKENCFR 800 NSPIKVIKVV 810 KGGSSAKGTA 820 LRGRSDADLV 830 VFLSCFSQFT 840 EQGNKRAEII 850 SEIRAQLEAC 860 QQERQFEVKF 870 EVSKWENPRV 880 LSFSLTSQTM 890 LDQSVDFDVL 900 PAFDALGQLV 910 SGSRPSSQVY 920 VDLIHSYSNA 930 GEYSTCFTEL 940 QRDFIISRPT 950 KLKSLIRLVK 960 HWYQQCTKIS 970 KGRGSLPPQH 980 GLELLTVYAW 990 EQGGKDSQFN 1000 MAEGFRTVLE 1010 LVTQYRQLCI 1020 YWTINYNAKD 1030 KTVGDFLKQQ 1040 LQKPRPIILD 1050 PADPTGNLGH 1060 NARWDLLAKE 1070 AAACTSALCC 1080 MGRNGIPIQP WPVKAAV

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0005829 cytosol
Cellular Component GO:0005615 extracellular space
Cellular Component GO:0043231 intracellular membrane-bounded organelle
Cellular Component GO:0016020 membrane
Cellular Component GO:0005654 nucleoplasm
Molecular Function GO:0001730 2'-5'-oligoadenylate synthetase activity
Molecular Function GO:0005524 ATP binding
Molecular Function GO:0003725 double-stranded RNA binding
Molecular Function GO:0046872 metal ion binding
Biological Process GO:0140374 antiviral innate immune response
Biological Process GO:0071360 cellular response to exogenous dsRNA
Biological Process GO:0042742 defense response to bacterium
Biological Process GO:0051607 defense response to virus
Biological Process GO:0070106 interleukin-27-mediated signaling pathway
Biological Process GO:0039530 MDA-5 signaling pathway
Biological Process GO:0071650 negative regulation of chemokine (C-C motif) ligand 5 production
Biological Process GO:2000342 negative regulation of chemokine (C-X-C motif) ligand 2 production
Biological Process GO:0035395 negative regulation of chemokine (C-X-C motif) ligand 9 production
Biological Process GO:0071659 negative regulation of IP-10 production
Biological Process GO:0060339 negative regulation of type I interferon-mediated signaling pathway
Biological Process GO:0045071 negative regulation of viral genome replication
Biological Process GO:0006139 nucleobase-containing compound metabolic process
Biological Process GO:0032728 positive regulation of interferon-beta production
Biological Process GO:0071639 positive regulation of monocyte chemotactic protein-1 production
Biological Process GO:0032760 positive regulation of tumor necrosis factor production
Biological Process GO:0060700 regulation of ribonuclease activity
Biological Process GO:0009615 response to virus
Biological Process GO:0039529 RIG-I signaling pathway
Biological Process GO:0060337 type I interferon-mediated signaling pathway

Reference

[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.

[2] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.

[3] He J, Lai T, Zhou Z, Yang H, Lei Z et al.. Multiomics profiling reveals the involvement of protein lactylation in nonhomologous end joining pathway conferring radioresistance in lung adenocarcinoma cell.. Sci Rep 15(1):24651. 2025 Jul 9. PMID: 40634431.