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Protein

2'-5'-oligoadenylate synthase 2

Gene

Oas2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript 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 (By similarity).By similarity

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 (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi439 – 4391Magnesium; catalyticSequence analysis
Metal bindingi441 – 4411Magnesium; catalyticSequence analysis
Binding sitei452 – 4521SubstrateBy similarity
Metal bindingi510 – 5101Magnesium; catalyticSequence analysis
Binding sitei574 – 5741ATPBy similarity
Binding sitei574 – 5741SubstrateBy similarity

GO - Molecular functioni

GO - Biological processi

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

Names & Taxonomyi

Protein namesi
Recommended name:
2'-5'-oligoadenylate synthase 2 (EC:2.7.7.84)
Short name:
(2-5')oligo(A) synthase 2
Short name:
2-5A synthase 2
Gene namesi
Name:Oas2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi1359697. Oas2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Microsome, Mitochondrion, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 7337322'-5'-oligoadenylate synthase 2PRO_0000418629Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycineBy similarity
Modified residuei408 – 4081N6-acetyllysineBy similarity

Post-translational modificationi

Myristoylation is not essential for its activity.By similarity
Glycosylated. Glycosylation is essential for its activity (By similarity).By similarity

Keywords - PTMi

Acetylation, Glycoprotein, Lipoprotein, Myristate

Proteomic databases

PaxDbiQ5MYU0.

PTM databases

PhosphoSiteiQ5MYU0.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000066845.

Structurei

3D structure databases

ProteinModelPortaliQ5MYU0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni47 – 365319OAS domain 1Add
BLAST
Regioni373 – 713341OAS domain 2Add
BLAST

Sequence similaritiesi

Belongs to the 2-5A synthase family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0001. Eukaryota.
COG5272. LUCA.
HOVERGENiHBG007855.
InParanoidiQ5MYU0.
KOiK14216.
PhylomeDBiQ5MYU0.

Family and domain databases

Gene3Di1.10.1410.20. 2 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. 1 hit.
PfamiPF01909. NTP_transf_2. 1 hit.
PF10421. OAS1_C. 2 hits.
[Graphical view]
PROSITEiPS00832. 25A_SYNTH_1. 1 hit.
PS00833. 25A_SYNTH_2. 2 hits.
PS50152. 25A_SYNTH_3. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q5MYU0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGNWMPGWSS SGSLGVPPMP VQKLEKSVQV NLEPDEKCLS QTEVSSVPSQ
60 70 80 90 100
KLEEYIQANL KPDEESLKQI DQAVDAISDL LCSEVMIDVL KVVKGGSYGR
110 120 130 140 150
KTVLRDCSDG TLVLFTGLFK QFQDQKKYQD KLLDLIEQRL KSHEKYKKSV
160 170 180 190 200
KRKLSLLEVQ VSIPGQSILL QLLPTFNPLC ISENPSAQVY QNLKRSMDQV
210 220 230 240 250
KASPGEFSDC FTTLQQRFFE KYPGRLKDLI LLVKHWYKQL QDKWIIPSPP
260 270 280 290 300
PLLYALELLT VYAWEQGCQT KDFDITQGIR TVLQLISQPT NLCVYWLDNY
310 320 330 340 350
NFEDETVRNN LLHQLNSPRP VILDPTDPTN NVGKDDRFWQ LLAEEAQEWL
360 370 380 390 400
NSLRLNKPHK PCWDVLPMPF FITPSHCLDK FIKDFLQPDK VFLNQIKRAV
410 420 430 440 450
DIICSFLKET CFQNSDIKVL KIIKGGSTAK GTALQQRSDA DIIVFLSSLD
460 470 480 490 500
SYDSLETERS QYVQEIRKQL EACQKAFNLG VKFDISKWMA PRVLSFTLES
510 520 530 540 550
KSLKQSVEFD VLPAYDALGQ LRSDYTSRLK AYKKLIELYA SQDSLKGGEF
560 570 580 590 600
SVCFTELQRD FIETRPTKLK GLIRLIKHWY KQCERKMKPK ASLPPKYALE
610 620 630 640 650
LLTVYAWEHG SGTDGFDTAE GFRTVLDLVI RYRQLCVFWT VNYNFEEDHM
660 670 680 690 700
RKFLLTQIQK KRPVILDPAD PTGDVGGGDR WCWHLLAKEA KEWLSSSCFQ
710 720 730
VEPKSPVQPW KVPVVQTPGS CGAQIYPVVG GVY
Length:733
Mass (Da):84,066
Last modified:February 1, 2005 - v1
Checksum:i136B28AAE998544D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY230746 mRNA. Translation: AAP57396.1.
RefSeqiNP_001009715.1. NM_001009715.1.
UniGeneiRn.136740.

Genome annotation databases

GeneIDi363938.
KEGGirno:363938.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY230746 mRNA. Translation: AAP57396.1.
RefSeqiNP_001009715.1. NM_001009715.1.
UniGeneiRn.136740.

3D structure databases

ProteinModelPortaliQ5MYU0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000066845.

PTM databases

PhosphoSiteiQ5MYU0.

Proteomic databases

PaxDbiQ5MYU0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi363938.
KEGGirno:363938.

Organism-specific databases

CTDi4939.
RGDi1359697. Oas2.

Phylogenomic databases

eggNOGiKOG0001. Eukaryota.
COG5272. LUCA.
HOVERGENiHBG007855.
InParanoidiQ5MYU0.
KOiK14216.
PhylomeDBiQ5MYU0.

Miscellaneous databases

NextBioi684524.
PROiQ5MYU0.

Family and domain databases

Gene3Di1.10.1410.20. 2 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. 1 hit.
PfamiPF01909. NTP_transf_2. 1 hit.
PF10421. OAS1_C. 2 hits.
[Graphical view]
PROSITEiPS00832. 25A_SYNTH_1. 1 hit.
PS00833. 25A_SYNTH_2. 2 hits.
PS50152. 25A_SYNTH_3. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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].
    Strain: Sprague-Dawley.
    Tissue: Ovary.

Entry informationi

Entry nameiOAS2_RAT
AccessioniPrimary (citable) accession number: Q5MYU0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 5, 2012
Last sequence update: February 1, 2005
Last modified: November 11, 2015
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 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.