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F1N3B8 (OAS2_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 24. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
2'-5'-oligoadenylate synthase 2

Short name=(2-5')oligo(A) synthase 2
Short name=2-5A synthase 2
EC=2.7.7.84
Gene names
Name:OAS2
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length714 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

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. 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 By similarity.

Catalytic activity

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

Cofactor

Magnesium Potential.

Enzyme regulation

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.

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm By similarity. Cytoplasmperinuclear region By similarity. Mitochondrion By similarity. Nucleus By similarity. Microsome By similarity. Endoplasmic reticulum By similarity. Note: Associated with different subcellular fractions such as mitochondrial, nuclear, and rough/smooth microsomal fractions By similarity.

Post-translational modification

Myristoylation is not essential for its activity By similarity.

Glycosylated. Glycosylation is essential for its activity By similarity.

Sequence similarities

Belongs to the 2-5A synthase family.

Ontologies

Keywords
   Biological processAntiviral defense
Immunity
Innate immunity
   Cellular componentCytoplasm
Endoplasmic reticulum
Microsome
Mitochondrion
Nucleus
   DomainRepeat
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
RNA-binding
   Molecular functionNucleotidyltransferase
Transferase
   PTMGlycoprotein
Lipoprotein
Myristate
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processRNA catabolic process

Inferred from electronic annotation. Source: Ensembl

defense response to virus

Inferred from electronic annotation. Source: UniProtKB-KW

innate immune response

Inferred from electronic annotation. Source: UniProtKB-KW

protein glycosylation

Inferred from sequence or structural similarity. Source: UniProtKB

protein myristoylation

Inferred from sequence or structural similarity. Source: UniProtKB

purine nucleotide biosynthetic process

Inferred from electronic annotation. Source: Ensembl

response to virus

Traceable author statement Ref.1. Source: UniProtKB

   Cellular_componentendoplasmic reticulum

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitochondrion

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

perinuclear region of cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_function2'-5'-oligoadenylate synthetase activity

Inferred from sequence or structural similarity. Source: UniProtKB

ATP binding

Inferred from sequence or structural similarity. Source: UniProtKB

double-stranded RNA binding

Inferred from sequence or structural similarity. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 7147132'-5'-oligoadenylate synthase 2
PRO_0000418627

Regions

Region11 – 336326OAS domain 1
Region344 – 683340OAS domain 2

Sites

Metal binding4091Magnesium; catalytic Potential
Metal binding4801Magnesium; catalytic Potential
Binding site5441ATP By similarity
Binding site5441Substrate By similarity

Amino acid modifications

Lipidation21N-myristoyl glycine By similarity

Experimental info

Sequence conflict1611S → T in AAT44896. Ref.1
Sequence conflict2191S → P in AAT44896. Ref.1
Sequence conflict2771I → T in AAT44896. Ref.1
Sequence conflict5221A → V in AAT44896. Ref.1
Sequence conflict5511C → K in AAT44896. Ref.1
Sequence conflict5731S → T in AAT44896. Ref.1

Sequences

Sequence LengthMass (Da)Tools
F1N3B8 [UniParc].

Last modified May 3, 2011. Version 1.
Checksum: 6962A98CC6D437BA

FASTA71481,967
        10         20         30         40         50         60 
MGSRESHLYE KPSEKLEEFI QNHLRPSEDC QKDIDQSVDT ICEVLQEPCP SLTVTGVAKG 

        70         80         90        100        110        120 
GSYGRRTVLR GNSDGILVVF FGDLEQFQDQ EKRQYELLSK IWAQMKHCES TWKLAAKMEL 

       130        140        150        160        170        180 
QNTNRSSRVT IQLSTKQQSI TFNVLPAFNA LGLSEKSSLW SYRELKRSLD MVKARPGEFS 

       190        200        210        220        230        240 
VCFTELQEKF FSNYPSKLKD LILLVKHWFQ KCQEKLINSS LLPPYALELL TVYAWEQGCG 

       250        260        270        280        290        300 
AEDFDMAEGV RTVLRLIEKQ EQLCVYWTVN YNFGDEIVRN ILLSQLQAPR PVILDPTDPT 

       310        320        330        340        350        360 
NNVSMDNTCW LQLKHEAQNW LRSLRQNESP GPSWNVLPAS LYITPGHLLD KFVKDFLQPN 

       370        380        390        400        410        420 
QTFQDQIKKA LKIICSFLEE NCFRHSTTKI QVIQGGSTVK GTALKTGSDA SLVVFANSLK 

       430        440        450        460        470        480 
SYTSPKNERY NIIKEIHEQL EACRQEKDFE VKFEISKWKP PWVLSFTLKS KVLNESVDFD 

       490        500        510        520        530        540 
VLPAFNALGE LKSGSTPSPR TYTELIHLYK PSDVFLEGEF SACFTKLQRN FVRSLPLKLK 

       550        560        570        580        590        600 
DLIRLLKHWY CGCEKKLKQK GSLPPKYALE LLSIYAWEKG SGAQDFDMAE GFRTVLELVI 

       610        620        630        640        650        660 
QYQHLCVFWT VNYSFDDEIL RNFLLGQIRR TRPVILDPAD PTGDVGGGHR WCWHLLAKEA 

       670        680        690        700        710 
TEWLSSLCFK DKSGCPIQPW NVPKKRVQTP GSCGAGIYSM VNEMHLLRSH RFLD 

« Hide

References

« Hide 'large scale' references
[1]"The mammalian 2'-5' oligoadenylate synthetase gene family: evidence for concerted evolution of paralogous Oas1 genes in Rodentia and Artiodactyla."
Perelygin A.A., Zharkikh A.A., Scherbik S.V., Brinton M.A.
J. Mol. Evol. 63:562-576(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"A whole-genome assembly of the domestic cow, Bos taurus."
Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D., Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G., Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.
Genome Biol. 10:R42.01-R42.10(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Hereford.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY599197 mRNA. Translation: AAT44896.1.
DAAA02045423 Genomic DNA. No translation available.
DAAA02045424 Genomic DNA. No translation available.
DAAA02045425 Genomic DNA. No translation available.
RefSeqNP_001019728.1. NM_001024557.1.
UniGeneBt.41610.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000019477; ENSBTAP00000019477; ENSBTAG00000014628.
GeneID529660.
KEGGbta:529660.

Organism-specific databases

CTD4939.

Phylogenomic databases

GeneTreeENSGT00510000046406.
HOVERGENHBG007855.
KOK14216.
OMAKSYTSQK.
OrthoDBEOG7WDN1R.
TreeFamTF329749.

Family and domain databases

Gene3D1.10.1410.20. 2 hits.
InterProIPR006117. 2-5-oligoadenylate_synth_CS.
IPR006116. 2-5-oligoadenylate_synth_N.
IPR018952. 2-5-oligoAdlate_synth_1_dom2/C.
IPR026774. 2-5A_synthase.
[Graphical view]
PANTHERPTHR11258. PTHR11258. 1 hit.
PfamPF10421. OAS1_C. 2 hits.
[Graphical view]
PROSITEPS00833. 25A_SYNTH_2. 2 hits.
PS50152. 25A_SYNTH_3. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio20875078.

Entry information

Entry nameOAS2_BOVIN
AccessionPrimary (citable) accession number: F1N3B8
Secondary accession number(s): Q53AV7
Entry history
Integrated into UniProtKB/Swiss-Prot: September 5, 2012
Last sequence update: May 3, 2011
Last modified: February 19, 2014
This is version 24 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families