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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)DescriptionActionsGraphical viewLength
Binding sitei62ATPBy similarity1
Metal bindingi74Magnesium; catalyticBy similarity1
Metal bindingi76Magnesium; catalyticBy similarity1
Metal bindingi147Magnesium; catalyticBy similarity1
Binding sitei212ATP1
Binding sitei229ATPBy similarity1

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)DescriptionActionsGraphical viewLength
Mutagenesisi65K → A: Significant loss of activity. 1 Publication1
Mutagenesisi209R → A: Significant loss of activity. 1 Publication1
Mutagenesisi212K → A: Significant loss of activity. 1 Publication1
Mutagenesisi230Y → A: Significant loss of activity. 1 Publication1
Mutagenesisi233E → A: Significant loss of activity. 1 Publication1
Mutagenesisi300D → A: Significant loss of activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001602621 – 3492'-5'-oligoadenylate synthase 1Add BLAST349

Proteomic databases

PeptideAtlasiQ29599.

Interactioni

Subunit structurei

Monomer. Homotetramer (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei157Interaction with dsRNABy similarity1

Structurei

Secondary structure

1349
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 5Combined sources3
Helixi8 – 10Combined sources3
Helixi11 – 18Combined sources8
Helixi23 – 43Combined sources21
Beta strandi47 – 49Combined sources3
Beta strandi53 – 62Combined sources10
Turni70 – 72Combined sources3
Beta strandi73 – 83Combined sources11
Helixi89 – 92Combined sources4
Helixi94 – 111Combined sources18
Beta strandi115 – 120Combined sources6
Beta strandi121 – 123Combined sources3
Beta strandi125 – 127Combined sources3
Beta strandi132 – 136Combined sources5
Turni138 – 140Combined sources3
Beta strandi143 – 152Combined sources10
Helixi166 – 179Combined sources14
Turni182 – 185Combined sources4
Helixi186 – 189Combined sources4
Helixi190 – 198Combined sources9
Helixi202 – 219Combined sources18
Helixi223 – 225Combined sources3
Helixi229 – 243Combined sources15
Beta strandi246 – 248Combined sources3
Helixi251 – 263Combined sources13
Helixi264 – 267Combined sources4
Beta strandi278 – 280Combined sources3
Helixi281 – 291Combined sources11
Beta strandi293 – 295Combined sources3
Beta strandi297 – 299Combined sources3
Turni308 – 311Combined sources4
Helixi313 – 326Combined sources14
Helixi330 – 332Combined sources3
Beta strandi337 – 339Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ29599.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni12 – 59Interaction with dsRNABy similarityAdd BLAST48
Regioni199 – 209Interaction with dsRNABy similarityAdd BLAST11

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 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti54V → F in CAA23153 (PubMed:8672129).Curated1
Sequence conflicti122S → R in CAA23153 (PubMed:8672129).Curated1

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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PeptideAtlasiQ29599.

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...

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 2, 2016
This is version 94 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.