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Protein

2'-5'-oligoadenylate synthase 3

Gene

OAS3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 preferentially dimers 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. Displays antiviral activity against Chikungunya virus (CHIKV), Dengue virus, Sindbis virus (SINV) and Semliki forest virus (SFV).3 Publications

Catalytic activityi

3 ATP = pppA2'p5'A2'p5'A + 2 diphosphate.

Cofactori

Mg2+Curated

Enzyme regulationi

Produced as a latent enzyme which is activated by dsRNA generated during the course of viral infection. The dsRNA activator must be at least 15 nucleotides long, and no modification of the 2'-hydroxyl group is tolerated. ssRNA or dsDNA do not act as activators.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi816Magnesium; catalyticSequence analysis1
Metal bindingi818Magnesium; catalyticSequence analysis1
Metal bindingi888Magnesium; catalyticSequence analysis1
Binding sitei947SubstrateBy similarity1
Binding sitei950ATPBy similarity1

GO - Molecular functioni

  • 2'-5'-oligoadenylate synthetase activity Source: UniProtKB
  • ATP binding Source: UniProtKB
  • double-stranded RNA binding Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • defense response to virus Source: UniProtKB
  • interferon-gamma-mediated signaling pathway Source: Reactome
  • negative regulation of viral genome replication Source: UniProtKB
  • nucleobase-containing compound metabolic process Source: ProtInc
  • regulation of ribonuclease activity Source: UniProtKB
  • response to virus Source: UniProtKB
  • type I interferon signaling pathway Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Nucleotidyltransferase, Transferase

Keywords - Biological processi

Antiviral defense, Immunity, Innate immunity

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding, RNA-binding

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000111331-MONOMER.
ZFISH:ENSG00000111331-MONOMER.
ReactomeiR-HSA-877300. Interferon gamma signaling.
R-HSA-909733. Interferon alpha/beta signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
2'-5'-oligoadenylate synthase 3 (EC:2.7.7.84)
Short name:
(2-5')oligo(A) synthase 3
Short name:
2-5A synthase 3
Alternative name(s):
p100 OAS
Short name:
p100OAS
Gene namesi
Name:OAS3
ORF Names:P/OKcl.4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:8088. OAS3.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: Reactome
  • extracellular space Source: UniProtKB
  • intracellular membrane-bounded organelle Source: ProtInc
  • nucleoplasm Source: HPA
  • plasma membrane Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

DisGeNETi4940.
OpenTargetsiENSG00000111331.
PharmGKBiPA31877.

Polymorphism and mutation databases

BioMutaiOAS3.
DMDMi317373408.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001602651 – 10872'-5'-oligoadenylate synthase 3Add BLAST1087

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineCombined sources1 Publication1
Modified residuei365PhosphothreonineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9Y6K5.
MaxQBiQ9Y6K5.
PaxDbiQ9Y6K5.
PeptideAtlasiQ9Y6K5.
PRIDEiQ9Y6K5.

PTM databases

iPTMnetiQ9Y6K5.
PhosphoSitePlusiQ9Y6K5.

Expressioni

Tissue specificityi

Present at high level in placenta trophoblast.

Inductioni

By type I interferon (IFN) and viruses.

Gene expression databases

BgeeiENSG00000111331.
CleanExiHS_OAS3.
ExpressionAtlasiQ9Y6K5. baseline and differential.
GenevisibleiQ9Y6K5. HS.

Organism-specific databases

HPAiHPA041253.
HPA041372.

Interactioni

Subunit structurei

Monomer.

Binary interactionsi

WithEntry#Exp.IntActNotes
DHX30Q7L2E32EBI-6115729,EBI-1211456
EIF6P565372EBI-6115729,EBI-372243
FTSJ3Q8IY812EBI-6115729,EBI-744088
IFRD2Q128942EBI-6115729,EBI-2512448
MAVSQ7Z4342EBI-6115729,EBI-995373

Protein-protein interaction databases

BioGridi110994. 17 interactors.
IntActiQ9Y6K5. 15 interactors.
MINTiMINT-4991875.
STRINGi9606.ENSP00000228928.

Structurei

Secondary structure

11087
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi2 – 5Combined sources4
Helixi8 – 10Combined sources3
Helixi11 – 18Combined sources8
Helixi23 – 41Combined sources19
Beta strandi54 – 60Combined sources7
Helixi61 – 65Combined sources5
Beta strandi73 – 81Combined sources9
Helixi89 – 92Combined sources4
Helixi95 – 108Combined sources14
Beta strandi116 – 119Combined sources4
Beta strandi129 – 139Combined sources11
Beta strandi141 – 149Combined sources9
Helixi165 – 172Combined sources8
Turni177 – 180Combined sources4
Helixi181 – 184Combined sources4
Helixi185 – 193Combined sources9
Helixi197 – 215Combined sources19
Helixi226 – 240Combined sources15
Helixi248 – 260Combined sources13
Helixi262 – 264Combined sources3
Beta strandi275 – 277Combined sources3
Helixi278 – 288Combined sources11
Beta strandi290 – 292Combined sources3
Beta strandi294 – 296Combined sources3
Beta strandi304 – 306Combined sources3
Helixi313 – 322Combined sources10
Helixi327 – 329Combined sources3
Turni332 – 334Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4S3NX-ray2.00A1-371[»]
ProteinModelPortaliQ9Y6K5.
SMRiQ9Y6K5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni6 – 343OAS domain 1Add BLAST338
Regioni344 – 410LinkerAdd BLAST67
Regioni411 – 742OAS domain 2Add BLAST332
Regioni750 – 1084OAS domain 3Add BLAST335

Sequence similaritiesi

Belongs to the 2-5A synthase family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0001. Eukaryota.
COG5272. LUCA.
GeneTreeiENSGT00510000046406.
HOGENOMiHOG000013200.
HOVERGENiHBG007856.
KOiK14216.
OMAiCQGGEHA.
OrthoDBiEOG091G0160.
PhylomeDBiQ9Y6K5.
TreeFamiTF329749.

Family and domain databases

Gene3Di1.10.1410.20. 3 hits.
InterProiIPR006117. 2-5-oligoadenylate_synth_CS.
IPR006116. 2-5-oligoadenylate_synth_N.
IPR018952. 2-5-oligoAdlate_synth_1_dom2/C.
IPR026774. 2-5A_synthase.
IPR002934. Polymerase_NTP_transf_dom.
[Graphical view]
PANTHERiPTHR11258. PTHR11258. 3 hits.
PfamiPF01909. NTP_transf_2. 1 hit.
PF10421. OAS1_C. 3 hits.
[Graphical view]
PROSITEiPS00832. 25A_SYNTH_1. 3 hits.
PS00833. 25A_SYNTH_2. 2 hits.
PS50152. 25A_SYNTH_3. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9Y6K5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDLYSTPAAA LDRFVARRLQ PRKEFVEKAR RALGALAAAL RERGGRLGAA
60 70 80 90 100
APRVLKTVKG GSSGRGTALK GGCDSELVIF LDCFKSYVDQ RARRAEILSE
110 120 130 140 150
MRASLESWWQ NPVPGLRLTF PEQSVPGALQ FRLTSVDLED WMDVSLVPAF
160 170 180 190 200
NVLGQAGSGV KPKPQVYSTL LNSGCQGGEH AACFTELRRN FVNIRPAKLK
210 220 230 240 250
NLILLVKHWY HQVCLQGLWK ETLPPVYALE LLTIFAWEQG CKKDAFSLAE
260 270 280 290 300
GLRTVLGLIQ QHQHLCVFWT VNYGFEDPAV GQFLQRQLKR PRPVILDPAD
310 320 330 340 350
PTWDLGNGAA WHWDLLAQEA ASCYDHPCFL RGMGDPVQSW KGPGLPRAGC
360 370 380 390 400
SGLGHPIQLD PNQKTPENSK SLNAVYPRAG SKPPSCPAPG PTGAASIVPS
410 420 430 440 450
VPGMALDLSQ IPTKELDRFI QDHLKPSPQF QEQVKKAIDI ILRCLHENCV
460 470 480 490 500
HKASRVSKGG SFGRGTDLRD GCDVELIIFL NCFTDYKDQG PRRAEILDEM
510 520 530 540 550
RAQLESWWQD QVPSLSLQFP EQNVPEALQF QLVSTALKSW TDVSLLPAFD
560 570 580 590 600
AVGQLSSGTK PNPQVYSRLL TSGCQEGEHK ACFAELRRNF MNIRPVKLKN
610 620 630 640 650
LILLVKHWYR QVAAQNKGKG PAPASLPPAY ALELLTIFAW EQGCRQDCFN
660 670 680 690 700
MAQGFRTVLG LVQQHQQLCV YWTVNYSTED PAMRMHLLGQ LRKPRPLVLD
710 720 730 740 750
PADPTWNVGH GSWELLAQEA AALGMQACFL SRDGTSVQPW DVMPALLYQT
760 770 780 790 800
PAGDLDKFIS EFLQPNRQFL AQVNKAVDTI CSFLKENCFR NSPIKVIKVV
810 820 830 840 850
KGGSSAKGTA LRGRSDADLV VFLSCFSQFT EQGNKRAEII SEIRAQLEAC
860 870 880 890 900
QQERQFEVKF EVSKWENPRV LSFSLTSQTM LDQSVDFDVL PAFDALGQLV
910 920 930 940 950
SGSRPSSQVY VDLIHSYSNA GEYSTCFTEL QRDFIISRPT KLKSLIRLVK
960 970 980 990 1000
HWYQQCTKIS KGRGSLPPQH GLELLTVYAW EQGGKDSQFN MAEGFRTVLE
1010 1020 1030 1040 1050
LVTQYRQLCI YWTINYNAKD KTVGDFLKQQ LQKPRPIILD PADPTGNLGH
1060 1070 1080
NARWDLLAKE AAACTSALCC MGRNGIPIQP WPVKAAV
Length:1,087
Mass (Da):121,170
Last modified:January 11, 2011 - v3
Checksum:i36DAADE4574DE961
GO

Sequence cautioni

The sequence AAD28543 differs from that shown. Reason: Frameshift at positions 394 and 398.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti159G → A in AAD28543 (PubMed:9880533).Curated1
Sequence conflicti249A → G in AAD28543 (PubMed:9880533).Curated1
Sequence conflicti287 – 288QL → HV in AAD28543 (PubMed:9880533).Curated2
Sequence conflicti316L → H in AAD28543 (PubMed:9880533).Curated1
Sequence conflicti393G → A in AAD28543 (PubMed:9880533).Curated1
Sequence conflicti503 – 504QL → HV in AAD28543 (PubMed:9880533).Curated2
Sequence conflicti503 – 504QL → HV in BAB18647 (PubMed:11280764).Curated2
Sequence conflicti984G → R in BAB18647 (PubMed:11280764).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_06007618R → K.1 PublicationCorresponds to variant rs1859330dbSNPEnsembl.1
Natural variantiVAR_06007718R → M.Corresponds to variant rs1859330dbSNPEnsembl.1
Natural variantiVAR_06007818R → T.Corresponds to variant rs1859330dbSNPEnsembl.1
Natural variantiVAR_05766065R → W.Corresponds to variant rs12819767dbSNPEnsembl.1
Natural variantiVAR_062127378R → K.Corresponds to variant rs45519442dbSNPEnsembl.1
Natural variantiVAR_057661381S → R.1 PublicationCorresponds to variant rs2285933dbSNPEnsembl.1
Natural variantiVAR_057662869R → H.Corresponds to variant rs16942374dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF063613 mRNA. Translation: AAD28543.1. Frameshift.
AB044545 mRNA. Translation: BAB18647.1.
AC004551 Genomic DNA. No translation available.
BC113746 mRNA. Translation: AAI13747.1.
AF251351 Genomic DNA. No translation available.
CCDSiCCDS44981.1.
RefSeqiNP_006178.2. NM_006187.3.
UniGeneiHs.528634.
Hs.744211.

Genome annotation databases

EnsembliENST00000228928; ENSP00000228928; ENSG00000111331.
GeneIDi4940.
KEGGihsa:4940.
UCSCiuc001tug.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF063613 mRNA. Translation: AAD28543.1. Frameshift.
AB044545 mRNA. Translation: BAB18647.1.
AC004551 Genomic DNA. No translation available.
BC113746 mRNA. Translation: AAI13747.1.
AF251351 Genomic DNA. No translation available.
CCDSiCCDS44981.1.
RefSeqiNP_006178.2. NM_006187.3.
UniGeneiHs.528634.
Hs.744211.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4S3NX-ray2.00A1-371[»]
ProteinModelPortaliQ9Y6K5.
SMRiQ9Y6K5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110994. 17 interactors.
IntActiQ9Y6K5. 15 interactors.
MINTiMINT-4991875.
STRINGi9606.ENSP00000228928.

PTM databases

iPTMnetiQ9Y6K5.
PhosphoSitePlusiQ9Y6K5.

Polymorphism and mutation databases

BioMutaiOAS3.
DMDMi317373408.

Proteomic databases

EPDiQ9Y6K5.
MaxQBiQ9Y6K5.
PaxDbiQ9Y6K5.
PeptideAtlasiQ9Y6K5.
PRIDEiQ9Y6K5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000228928; ENSP00000228928; ENSG00000111331.
GeneIDi4940.
KEGGihsa:4940.
UCSCiuc001tug.4. human.

Organism-specific databases

CTDi4940.
DisGeNETi4940.
GeneCardsiOAS3.
H-InvDBHIX0201822.
HGNCiHGNC:8088. OAS3.
HPAiHPA041253.
HPA041372.
MIMi603351. gene.
neXtProtiNX_Q9Y6K5.
OpenTargetsiENSG00000111331.
PharmGKBiPA31877.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0001. Eukaryota.
COG5272. LUCA.
GeneTreeiENSGT00510000046406.
HOGENOMiHOG000013200.
HOVERGENiHBG007856.
KOiK14216.
OMAiCQGGEHA.
OrthoDBiEOG091G0160.
PhylomeDBiQ9Y6K5.
TreeFamiTF329749.

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000111331-MONOMER.
ZFISH:ENSG00000111331-MONOMER.
ReactomeiR-HSA-877300. Interferon gamma signaling.
R-HSA-909733. Interferon alpha/beta signaling.

Miscellaneous databases

ChiTaRSiOAS3. human.
GeneWikiiOAS3.
GenomeRNAii4940.
PROiQ9Y6K5.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000111331.
CleanExiHS_OAS3.
ExpressionAtlasiQ9Y6K5. baseline and differential.
GenevisibleiQ9Y6K5. HS.

Family and domain databases

Gene3Di1.10.1410.20. 3 hits.
InterProiIPR006117. 2-5-oligoadenylate_synth_CS.
IPR006116. 2-5-oligoadenylate_synth_N.
IPR018952. 2-5-oligoAdlate_synth_1_dom2/C.
IPR026774. 2-5A_synthase.
IPR002934. Polymerase_NTP_transf_dom.
[Graphical view]
PANTHERiPTHR11258. PTHR11258. 3 hits.
PfamiPF01909. NTP_transf_2. 1 hit.
PF10421. OAS1_C. 3 hits.
[Graphical view]
PROSITEiPS00832. 25A_SYNTH_1. 3 hits.
PS00833. 25A_SYNTH_2. 2 hits.
PS50152. 25A_SYNTH_3. 3 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiOAS3_HUMAN
AccessioniPrimary (citable) accession number: Q9Y6K5
Secondary accession number(s): Q2HJ14, Q9H3P5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: January 11, 2011
Last modified: November 2, 2016
This is version 140 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.