Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

2'-5'-oligoadenylate synthase 1

Gene

OAS1

Organism
Sus scrofa (Pig)
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 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. The secreted form displays antiviral effect against vesicular stomatitis virus (VSV), herpes simplex virus type 2 (HSV-2), and encephalomyocarditis virus (EMCV) and stimulates the alternative antiviral pathway independent of RNase L.1 Publication

Catalytic activityi

3 ATP = pppA2'p5'A2'p5'A + 2 diphosphate.1 Publication

Cofactori

Mg2+By similarity

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 (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei62 – 621ATPBy similarity
Metal bindingi74 – 741Magnesium; catalyticBy similarity
Metal bindingi76 – 761Magnesium; catalyticBy similarity
Metal bindingi147 – 1471Magnesium; catalyticBy similarity
Binding sitei212 – 2121ATP
Binding sitei229 – 2291ATPBy similarity

GO - Molecular functioni

GO - Biological processi

  • defense response to virus Source: UniProtKB
  • innate immune response Source: UniProtKB-KW
  • negative regulation of viral genome replication Source: UniProtKB
  • purine nucleotide biosynthetic process Source: UniProtKB
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

BRENDAi2.7.7.84. 6170.

Names & Taxonomyi

Protein namesi
Recommended name:
2'-5'-oligoadenylate synthase 1 (EC:2.7.7.84)
Short name:
(2-5')oligo(A) synthase 1
Short name:
2-5A synthase 1
Alternative name(s):
p42 OAS
Gene namesi
Name:OAS1
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
Proteomesi
  • UP000008227 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • endoplasmic reticulum Source: UniProtKB-SubCell
  • extracellular region Source: UniProtKB-SubCell
  • mitochondrion Source: UniProtKB-SubCell
  • nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Microsome, Mitochondrion, Nucleus, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi65 – 651K → A: Significant loss of activity. 1 Publication
Mutagenesisi209 – 2091R → A: Significant loss of activity. 1 Publication
Mutagenesisi212 – 2121K → A: Significant loss of activity. 1 Publication
Mutagenesisi230 – 2301Y → A: Significant loss of activity. 1 Publication
Mutagenesisi233 – 2331E → A: Significant loss of activity. 1 Publication
Mutagenesisi300 – 3001D → A: Significant loss of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 3493492'-5'-oligoadenylate synthase 1PRO_0000160262Add
BLAST

Interactioni

Subunit structurei

Monomer. Homotetramer (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei157 – 1571Interaction with dsRNABy similarity

Structurei

Secondary structure

1
349
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 53Combined sources
Helixi8 – 103Combined sources
Helixi11 – 188Combined sources
Helixi23 – 4321Combined sources
Beta strandi47 – 493Combined sources
Beta strandi53 – 6210Combined sources
Turni70 – 723Combined sources
Beta strandi73 – 8311Combined sources
Helixi89 – 924Combined sources
Helixi94 – 11118Combined sources
Beta strandi115 – 1206Combined sources
Beta strandi121 – 1233Combined sources
Beta strandi125 – 1273Combined sources
Beta strandi132 – 1365Combined sources
Turni138 – 1403Combined sources
Beta strandi143 – 15210Combined sources
Helixi166 – 17914Combined sources
Turni182 – 1854Combined sources
Helixi186 – 1894Combined sources
Helixi190 – 1989Combined sources
Helixi202 – 21918Combined sources
Helixi223 – 2253Combined sources
Helixi229 – 24315Combined sources
Beta strandi246 – 2483Combined sources
Helixi251 – 26313Combined sources
Helixi264 – 2674Combined sources
Beta strandi278 – 2803Combined sources
Helixi281 – 29111Combined sources
Beta strandi293 – 2953Combined sources
Beta strandi297 – 2993Combined sources
Turni308 – 3114Combined sources
Helixi313 – 32614Combined sources
Helixi330 – 3323Combined sources
Beta strandi337 – 3393Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PX5X-ray1.74A/B1-349[»]
4RWNX-ray2.00A1-349[»]
4RWOX-ray2.20A1-349[»]
4RWPX-ray2.25A1-349[»]
4RWQX-ray3.10A/B1-349[»]
ProteinModelPortaliQ29599.
SMRiQ29599. Positions 1-349.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ29599.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni12 – 5948Interaction with dsRNABy similarityAdd
BLAST
Regioni199 – 20911Interaction with dsRNABy similarityAdd
BLAST

Sequence similaritiesi

Belongs to the 2-5A synthase family.Curated

Phylogenomic databases

HOVERGENiHBG000994.
InParanoidiQ29599.
KOiK14216.

Family and domain databases

Gene3Di1.10.1410.20. 1 hit.
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. 1 hit.
PfamiPF01909. NTP_transf_2. 1 hit.
PF10421. OAS1_C. 1 hit.
[Graphical view]
PROSITEiPS00832. 25A_SYNTH_1. 1 hit.
PS00833. 25A_SYNTH_2. 1 hit.
PS50152. 25A_SYNTH_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q29599-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MELRHTPARD LDKFIEDHLL PNTCFRTQVK EAIDIVCRFL KERCFQGTAD
60 70 80 90 100
PVRVSKVVKG GSSGKGTTLR GRSDADLVVF LTKLTSFEDQ LRRRGEFIQE
110 120 130 140 150
IRRQLEACQR EQKFKVTFEV QSPRRENPRA LSFVLSSPQL QQEVEFDVLP
160 170 180 190 200
AFDALGQWTP GYKPNPEIYV QLIKECKSRG KEGEFSTCFT ELQRDFLRNR
210 220 230 240 250
PTKLKSLIRL VKHWYQTCKK THGNKLPPQY ALELLTVYAW EQGSRKTDFS
260 270 280 290 300
TAQGFQTVLE LVLKHQKLCI FWEAYYDFTN PVVGRCMLQQ LKKPRPVILD
310 320 330 340
PADPTGNVGG GDTHSWQRLA QEARVWLGYP CCKNLDGSLV GAWTMLQKI
Length:349
Mass (Da):40,246
Last modified:May 30, 2000 - v3
Checksum:i06949A35BFCF7710
GO

Sequence cautioni

The sequence CAA23153.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti54 – 541V → F in CAA23153 (PubMed:8672129).Curated
Sequence conflicti122 – 1221S → R in CAA23153 (PubMed:8672129).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ225090 mRNA. Translation: CAA12397.1.
F14610 mRNA. Translation: CAA23153.1. Different initiation.
RefSeqiNP_999468.1. NM_214303.1.
UniGeneiSsc.1031.

Genome annotation databases

GeneIDi397570.
KEGGissc:397570.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ225090 mRNA. Translation: CAA12397.1.
F14610 mRNA. Translation: CAA23153.1. Different initiation.
RefSeqiNP_999468.1. NM_214303.1.
UniGeneiSsc.1031.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PX5X-ray1.74A/B1-349[»]
4RWNX-ray2.00A1-349[»]
4RWOX-ray2.20A1-349[»]
4RWPX-ray2.25A1-349[»]
4RWQX-ray3.10A/B1-349[»]
ProteinModelPortaliQ29599.
SMRiQ29599. Positions 1-349.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi397570.
KEGGissc:397570.

Organism-specific databases

CTDi4938.

Phylogenomic databases

HOVERGENiHBG000994.
InParanoidiQ29599.
KOiK14216.

Enzyme and pathway databases

BRENDAi2.7.7.84. 6170.

Miscellaneous databases

EvolutionaryTraceiQ29599.

Family and domain databases

Gene3Di1.10.1410.20. 1 hit.
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. 1 hit.
PfamiPF01909. NTP_transf_2. 1 hit.
PF10421. OAS1_C. 1 hit.
[Graphical view]
PROSITEiPS00832. 25A_SYNTH_1. 1 hit.
PS00833. 25A_SYNTH_2. 1 hit.
PS50152. 25A_SYNTH_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Hartmann R.
    Thesis (1997), University of Aarhus, Denmark
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Small intestine.
  2. "Evaluation and characterization of a porcine small intestine cDNA library: analysis of 839 clones."
    Winteroe A.K., Fredholm M., Davies W.
    Mamm. Genome 7:509-517(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-128.
    Tissue: Small intestine.
  3. "2'-5' oligoadenylate synthetase shares active site architecture with the archaeal CCA-adding enzyme."
    Torralba S., Sojat J., Hartmann R.
    Cell. Mol. Life Sci. 65:2613-2620(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF LYS-65; ARG-209; TYR-230; GLU-233 AND ASP-300.
  4. "Extracellular 2'-5' oligoadenylate synthetase stimulates RNase L-independent antiviral activity: a novel mechanism of virus-induced innate immunity."
    Kristiansen H., Scherer C.A., McVean M., Iadonato S.P., Vends S., Thavachelvam K., Steffensen T.B., Horan K.A., Kuri T., Weber F., Paludan S.R., Hartmann R.
    J. Virol. 84:11898-11904(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  5. "Crystal structure of the 2'-specific and double-stranded RNA-activated interferon-induced antiviral protein 2'-5'-oligoadenylate synthetase."
    Hartmann R., Justesen J., Sarkar S.N., Sen G.C., Yee V.C.
    Mol. Cell 12:1173-1185(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF 1-349, CATALYTIC ACTIVITY, SUBUNIT, METAL BINDING, MUTAGENESIS OF LYS-212.

Entry informationi

Entry nameiOAS1_PIG
AccessioniPrimary (citable) accession number: Q29599
Secondary accession number(s): O77734
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: May 30, 2000
Last modified: November 11, 2015
This is version 91 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.