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Protein

2'-5'-oligoadenylate synthase 2

Gene

Oas2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Interferon-induced, dsRNA-activated antiviral enzyme which plays a critical role in cellular innate antiviral response (PubMed:12396720, PubMed:29117179). 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 (PubMed:29117179). Activation of RNASEL leads to degradation of cellular as well as viral RNA, resulting in the inhibition of protein synthesis, thus terminating viral replication (PubMed:21142819). Can mediate the antiviral effect via the classical RNASEL-dependent pathway or an alternative antiviral pathway independent of RNASEL (PubMed:21142819). In addition, it may also play a role in other cellular processes such as apoptosis, cell growth, differentiation and gene regulation (PubMed:21142819). May act as a negative regulator of lactation, stopping lactation in virally infected mammary gland lobules, thereby preventing transmission of viruses to neonates (PubMed:29117179). Non-infected lobules would not be affected, allowing efficient pup feeding during infection (PubMed:29117179).1 Publication3 Publications

Catalytic activityi

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

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 (PubMed:29117179). The dsRNA activator must be at least 15 nucleotides long, and no modification of the 2'-hydroxyl group is tolerated (By similarity). ssRNA or dsDNA do not act as activators (By similarity). Strongly inhibited by copper, iron and zinc ions (By similarity). Partially inhibited by cobalt and nickel ions (By similarity).By similarity1 Publication

Kineticsi

Kcat is 6.4 sec(-1) for ATP.1 Publication
  1. KM=1.9 mM for ATP1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei436ATPBy similarity1
    Metal bindingi448Magnesium; catalyticSequence analysis1
    Metal bindingi450Magnesium; catalyticSequence analysis1
    Metal bindingi519Magnesium; catalyticSequence analysis1
    Binding sitei582ATPBy similarity1
    Binding sitei585ATPBy similarity1

    GO - Molecular functioni

    • 2'-5'-oligoadenylate synthetase activity Source: UniProtKB
    • ATP binding Source: UniProtKB
    • double-stranded RNA binding Source: MGI
    • metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    • defense response to virus Source: UniProtKB
    • regulation of lactation Source: UniProtKB
    • response to virus Source: UniProtKB
    • RNA catabolic process Source: MGI
    • 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:2.7.7.842 Publications)
    Short name:
    (2-5')oligo(A) synthase 2
    Short name:
    2-5A synthase 2
    Alternative name(s):
    2',5'-oligoadenylate synthetase-like 111 Publication
    Gene namesi
    Name:Oas2Imported
    Synonyms:oasl111 Publication
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
    Proteomesi
    • UP000000589 Componenti: Chromosome 5

    Organism-specific databases

    MGIiMGI:2180852 Oas2

    Subcellular locationi

    Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi405I → N: Mice display postpartum failure of lactation and strongly reduced milk protein synthesis. Otherwise, mice develop normally and mammary glands are normal. The mutation causes an activation of the OAS2 pathway, characterized by a strong increase of Ribonuclease L (RNASEL) activity. 1 Publication1
    Mutagenesisi444K → A or G: Strongly reduced 2'-5'-oligoadenylate synthase activity. 1 Publication1
    Mutagenesisi509S → L: Abolished 2'-5'-oligoadenylate synthase activity. 1 Publication1
    Mutagenesisi538P → L: Strongly reduced 2'-5'-oligoadenylate synthase activity. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Initiator methionineiRemovedBy similarity
    ChainiPRO_00004186282 – 7422'-5'-oligoadenylate synthase 2Add BLAST741

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Lipidationi2N-myristoyl glycineBy similarity1
    Modified residuei417N6-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

    EPDiE9Q9A9
    MaxQBiE9Q9A9
    PaxDbiE9Q9A9
    PeptideAtlasiE9Q9A9
    PRIDEiE9Q9A9

    PTM databases

    iPTMnetiE9Q9A9
    PhosphoSitePlusiE9Q9A9
    SwissPalmiE9Q9A9

    Expressioni

    Tissue specificityi

    Expressed in the uterus (PubMed:12396720). Expressed in mammary glands: expressed at low level before the establishment of lactation, then expression strongly increases, and subsequently decreases during early involution (PubMed:29117179).2 Publications

    Gene expression databases

    BgeeiENSMUSG00000032690
    ExpressionAtlasiE9Q9A9 baseline and differential
    GenevisibleiE9Q9A9 MM

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Protein-protein interaction databases

    STRINGi10090.ENSMUSP00000060082

    Structurei

    3D structure databases

    ProteinModelPortaliE9Q9A9
    SMRiE9Q9A9
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni60 – 374OAS domain 1Add BLAST315
    Regioni382 – 721OAS domain 2Add BLAST340

    Sequence similaritiesi

    Belongs to the 2-5A synthase family.Curated

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiKOG0001 Eukaryota
    COG5272 LUCA
    GeneTreeiENSGT00510000046406
    HOGENOMiHOG000013200
    HOVERGENiHBG007855
    InParanoidiE9Q9A9
    KOiK14216
    OMAiKSYTSQK
    OrthoDBiEOG091G0160
    TreeFamiTF329749

    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, 2 hits
    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

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

    Isoform 1 (identifier: E9Q9A9-1) [UniParc]FASTAAdd to basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

            10         20         30         40         50
    MGNWLTGNWS SDRSSGYSSG WSPGGSSGVP SGPVHKLEKS IQANLTPNEN
    60 70 80 90 100
    CLKQIAVSSV PSQKLEGYIQ ENLKPNRESL KQIDQAVDAI WDLLRSQIPV
    110 120 130 140 150
    KEVAKGGSYG RETALRGCSD GTLVLFMDCF QQFQDQIKYQ DAYLDVIELW
    160 170 180 190 200
    LKIHEKKSVK HEHALVVQVS VPGQRILLQL LPVFNPLRSN ENPSSCVYVD
    210 220 230 240 250
    LKKSMDQVRA SPGEFSDCFT TLQQRFFKKY PQRLKDLILL VKHWYEQCQE
    260 270 280 290 300
    KWKTPPPQPL LYALELLTVY AWEQGCQAED FDMAQGVRTV LRLIQRPTEL
    310 320 330 340 350
    CVYWTVNYNF EDETVRNILL HQLRSQRPVI LDPTDPTNNV GKDDGFWELL
    360 370 380 390 400
    TEEAMAWLYS PSLNTESPAP YWDVLPMPLF VTPSHLLNKF IKDFLQPNKL
    410 420 430 440 450
    FLKQIKEAVD IICSFLKNVC FLNSDTKVLK TVKGGSTAKG TALKRGSDAD
    460 470 480 490 500
    IVVFLSSLES YDSLKTNRSQ FVQEIQKQLE EFVQAQEWEV TFEISKWKAP
    510 520 530 540 550
    RVLSFTLKSK TLNESVEFDV LPAYDALGQL RSDFTLRPEA YKDLIELCAS
    560 570 580 590 600
    QDIKEGEFSI CFTELQRNFI QTRPTKLKSL LRLIKHWYKQ YERKMKPKAS
    610 620 630 640 650
    LPPKYALELL TVYAWEQGSG TDDFDIAEGF RTVLDLVIKY RQLCIFWTVN
    660 670 680 690 700
    YNFEEEYMRK FLLTQIQKKR PVILDPADPT GDVGGGDRWC WHLLAEEAKE
    710 720 730 740
    WLSSPCFQVE QKGLVQPWKV PVMQTPGSCG GQIYPTVGGV TK
    Length:742
    Mass (Da):85,051
    Last modified:April 5, 2011 - v1
    Checksum:iF8F21FB4BEF90C58
    GO
    Isoform 2 (identifier: E9Q9A9-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         723-742: MQTPGSCGGQIYPTVGGVTK → PRDLKTSDMVGVFTTGGILWQDQGFLSFV

    Show »
    Length:751
    Mass (Da):86,285
    Checksum:iB4E650AE78280C49
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti270Y → C in BAB84135 (PubMed:12396720).Curated1
    Sequence conflicti630F → L in BAB84135 (PubMed:12396720).Curated1

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural varianti232Q → R in strain: C3H/He. 2 Publications1

    Alternative sequence

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Alternative sequenceiVSP_044068723 – 742MQTPG…GGVTK → PRDLKTSDMVGVFTTGGILW QDQGFLSFV in isoform 2. 1 PublicationAdd BLAST20

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AB067535 mRNA Translation: BAB84135.1
    AF418010 mRNA Translation: AAM54499.1
    AC115937 Genomic DNA No translation available.
    CH466529 Genomic DNA Translation: EDL19753.1
    CCDSiCCDS19625.2 [E9Q9A9-1]
    CCDS84949.1 [E9Q9A9-2]
    RefSeqiNP_001334377.1, NM_001347448.1 [E9Q9A9-2]
    NP_660262.2, NM_145227.3 [E9Q9A9-1]
    UniGeneiMm.260926

    Genome annotation databases

    EnsembliENSMUST00000053909; ENSMUSP00000060082; ENSMUSG00000032690 [E9Q9A9-1]
    ENSMUST00000081491; ENSMUSP00000080209; ENSMUSG00000032690 [E9Q9A9-2]
    GeneIDi246728
    KEGGimmu:246728
    UCSCiuc008zhw.2 mouse [E9Q9A9-2]
    uc008zhx.2 mouse [E9Q9A9-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Similar proteinsi

    Entry informationi

    Entry nameiOAS2_MOUSE
    AccessioniPrimary (citable) accession number: E9Q9A9
    Secondary accession number(s): Q8K4E5, Q8VI92
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 5, 2012
    Last sequence update: April 5, 2011
    Last modified: May 23, 2018
    This is version 61 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. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

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