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Protein

2'-5'-oligoadenylate synthase 2

Gene

Oas2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -Experimental evidence at transcript leveli

Functioni

Interferon-induced, dsRNA-activated antiviral enzyme which plays a critical role in cellular innate antiviral response. Activated by detection of double stranded RNA (dsRNA): polymerizes higher oligomers of 2'-5'-oligoadenylates (2-5A) from ATP which then bind to the inactive monomeric form of ribonuclease L (RNASEL) leading to its dimerization and subsequent activation. Activation of RNASEL 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 RNASEL-dependent pathway or an alternative antiviral pathway independent of RNASEL. In addition, it may also play a role in other cellular processes such as apoptosis, cell growth, differentiation and gene regulation (By similarity). May act as a negative regulator of lactation, stopping lactation in virally infected mammary gland lobules, thereby preventing transmission of viruses to neonates (By similarity). Non-infected lobules would not be affected, allowing efficient pup feeding during infection (By similarity).By similarity

Catalytic activityi

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

Cofactori

Mg2+By similarity

Enzyme regulationi

Produced as a latent enzyme which is activated by double stranded RNA (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. Strongly inhibited by copper, iron and zinc ions. Partially inhibited by cobalt and nickel ions.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei427ATPBy similarity1
Metal bindingi439Magnesium; catalyticSequence analysis1
Metal bindingi441Magnesium; catalyticSequence analysis1
Metal bindingi510Magnesium; catalyticSequence analysis1
Binding sitei574ATPBy similarity1
Binding sitei577ATPBy similarity1

GO - Molecular functioni

GO - Biological processi

  • defense response to virus Source: UniProtKB
  • regulation of lactation Source: UniProtKB
  • response to virus Source: UniProtKB
  • type I interferon signaling pathway Source: UniProtKB

Keywordsi

Molecular functionNucleotidyltransferase, RNA-binding, Transferase
Biological processAntiviral defense, Immunity, Innate immunity
LigandATP-binding, Magnesium, Metal-binding, Nucleotide-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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi1359697 Oas2

Subcellular locationi

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00004186292 – 7332'-5'-oligoadenylate synthase 2Add BLAST732

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi2N-myristoyl glycineBy similarity1
Modified residuei408N6-acetyllysineBy similarity1

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Glycoprotein, Lipoprotein, Myristate

Proteomic databases

PaxDbiQ5MYU0
PRIDEiQ5MYU0

PTM databases

iPTMnetiQ5MYU0
PhosphoSitePlusiQ5MYU0

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000066845

Structurei

3D structure databases

ProteinModelPortaliQ5MYU0
SMRiQ5MYU0
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni47 – 365OAS domain 1Add BLAST319
Regioni373 – 713OAS domain 2Add BLAST341

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
InterProiView protein in InterPro
IPR006117 2-5-oligoadenylate_synth_CS
IPR006116 2-5-oligoadenylate_synth_N
IPR018952 2-5-oligoAdlate_synth_1_dom2/C
IPR038121 2-5-oligoAdlate_synth_2_sf
IPR026774 2-5A_synthase
IPR002934 Polymerase_NTP_transf_dom
PANTHERiPTHR11258 PTHR11258, 1 hit
PfamiView protein in Pfam
PF01909 NTP_transf_2, 1 hit
PF10421 OAS1_C, 2 hits
PROSITEiView protein in PROSITE
PS00832 25A_SYNTH_1, 1 hit
PS00833 25A_SYNTH_2, 2 hits
PS50152 25A_SYNTH_3, 2 hits

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

Similar proteinsi

Entry informationi

Entry nameiOAS2_RAT
AccessioniPrimary (citable) accession number: Q5MYU0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 5, 2012
Last sequence update: February 1, 2005
Last modified: May 23, 2018
This is version 67 of the entry and version 1 of the sequence. See 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

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