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F1N3B8

- OAS2_BOVIN

UniProt

F1N3B8 - OAS2_BOVIN

Protein

2'-5'-oligoadenylate synthase 2

Gene

OAS2

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 25 (01 Oct 2014)
      Sequence version 1 (03 May 2011)
      Previous versions | rss
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    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

    Magnesium.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 bindingi409 – 4091Magnesium; catalyticSequence Analysis
    Metal bindingi480 – 4801Magnesium; catalyticSequence Analysis
    Binding sitei544 – 5441ATPBy similarity
    Binding sitei544 – 5441SubstrateBy similarity

    GO - Molecular functioni

    1. 2'-5'-oligoadenylate synthetase activity Source: UniProtKB
    2. ATP binding Source: UniProtKB
    3. double-stranded RNA binding Source: UniProtKB
    4. zinc ion binding Source: Ensembl

    GO - Biological processi

    1. defense response to virus Source: UniProtKB-KW
    2. innate immune response Source: UniProtKB-KW
    3. protein glycosylation Source: UniProtKB
    4. protein myristoylation Source: UniProtKB
    5. purine nucleotide biosynthetic process Source: Ensembl
    6. response to virus Source: UniProtKB
    7. RNA catabolic process Source: Ensembl

    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
    OrganismiBos taurus (Bovine)
    Taxonomic identifieri9913 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
    ProteomesiUP000009136: Chromosome 17

    Subcellular locationi

    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

    GO - Cellular componenti

    1. endoplasmic reticulum Source: UniProtKB-SubCell
    2. mitochondrion Source: UniProtKB-SubCell
    3. nucleus Source: UniProtKB-SubCell
    4. perinuclear region of cytoplasm Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Endoplasmic reticulum, Microsome, Mitochondrion, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 7147132'-5'-oligoadenylate synthase 2PRO_0000418627Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi2 – 21N-myristoyl glycineBy 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

    Glycoprotein, Lipoprotein, Myristate

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni11 – 336326OAS domain 1Add
    BLAST
    Regioni344 – 683340OAS domain 2Add
    BLAST

    Sequence similaritiesi

    Belongs to the 2-5A synthase family.Curated

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    GeneTreeiENSGT00510000046406.
    HOVERGENiHBG007855.
    KOiK14216.
    OMAiKSYTSQK.
    OrthoDBiEOG7WDN1R.
    TreeFamiTF329749.

    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.
    [Graphical view]
    PANTHERiPTHR11258. PTHR11258. 1 hit.
    PfamiPF10421. OAS1_C. 2 hits.
    [Graphical view]
    PROSITEiPS00833. 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.

    F1N3B8-1 [UniParc]FASTAAdd to Basket

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    MGSRESHLYE KPSEKLEEFI QNHLRPSEDC QKDIDQSVDT ICEVLQEPCP    50
    SLTVTGVAKG GSYGRRTVLR GNSDGILVVF FGDLEQFQDQ EKRQYELLSK 100
    IWAQMKHCES TWKLAAKMEL QNTNRSSRVT IQLSTKQQSI TFNVLPAFNA 150
    LGLSEKSSLW SYRELKRSLD MVKARPGEFS VCFTELQEKF FSNYPSKLKD 200
    LILLVKHWFQ KCQEKLINSS LLPPYALELL TVYAWEQGCG AEDFDMAEGV 250
    RTVLRLIEKQ EQLCVYWTVN YNFGDEIVRN ILLSQLQAPR PVILDPTDPT 300
    NNVSMDNTCW LQLKHEAQNW LRSLRQNESP GPSWNVLPAS LYITPGHLLD 350
    KFVKDFLQPN QTFQDQIKKA LKIICSFLEE NCFRHSTTKI QVIQGGSTVK 400
    GTALKTGSDA SLVVFANSLK SYTSPKNERY NIIKEIHEQL EACRQEKDFE 450
    VKFEISKWKP PWVLSFTLKS KVLNESVDFD VLPAFNALGE LKSGSTPSPR 500
    TYTELIHLYK PSDVFLEGEF SACFTKLQRN FVRSLPLKLK DLIRLLKHWY 550
    CGCEKKLKQK GSLPPKYALE LLSIYAWEKG SGAQDFDMAE GFRTVLELVI 600
    QYQHLCVFWT VNYSFDDEIL RNFLLGQIRR TRPVILDPAD PTGDVGGGHR 650
    WCWHLLAKEA TEWLSSLCFK DKSGCPIQPW NVPKKRVQTP GSCGAGIYSM 700
    VNEMHLLRSH RFLD 714
    Length:714
    Mass (Da):81,967
    Last modified:May 3, 2011 - v1
    Checksum:i6962A98CC6D437BA
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti161 – 1611S → T in AAT44896. (PubMed:17024523)Curated
    Sequence conflicti219 – 2191S → P in AAT44896. (PubMed:17024523)Curated
    Sequence conflicti277 – 2771I → T in AAT44896. (PubMed:17024523)Curated
    Sequence conflicti522 – 5221A → V in AAT44896. (PubMed:17024523)Curated
    Sequence conflicti551 – 5511C → K in AAT44896. (PubMed:17024523)Curated
    Sequence conflicti573 – 5731S → T in AAT44896. (PubMed:17024523)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY599197 mRNA. Translation: AAT44896.1.
    DAAA02045423 Genomic DNA. No translation available.
    DAAA02045424 Genomic DNA. No translation available.
    DAAA02045425 Genomic DNA. No translation available.
    RefSeqiNP_001019728.1. NM_001024557.1.
    UniGeneiBt.41610.

    Genome annotation databases

    EnsembliENSBTAT00000019477; ENSBTAP00000019477; ENSBTAG00000014628.
    GeneIDi529660.
    KEGGibta:529660.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY599197 mRNA. Translation: AAT44896.1 .
    DAAA02045423 Genomic DNA. No translation available.
    DAAA02045424 Genomic DNA. No translation available.
    DAAA02045425 Genomic DNA. No translation available.
    RefSeqi NP_001019728.1. NM_001024557.1.
    UniGenei Bt.41610.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSBTAT00000019477 ; ENSBTAP00000019477 ; ENSBTAG00000014628 .
    GeneIDi 529660.
    KEGGi bta:529660.

    Organism-specific databases

    CTDi 4939.

    Phylogenomic databases

    GeneTreei ENSGT00510000046406.
    HOVERGENi HBG007855.
    KOi K14216.
    OMAi KSYTSQK.
    OrthoDBi EOG7WDN1R.
    TreeFami TF329749.

    Miscellaneous databases

    NextBioi 20875078.

    Family and domain databases

    Gene3Di 1.10.1410.20. 2 hits.
    InterProi IPR006117. 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 ]
    PANTHERi PTHR11258. PTHR11258. 1 hit.
    Pfami PF10421. OAS1_C. 2 hits.
    [Graphical view ]
    PROSITEi PS00833. 25A_SYNTH_2. 2 hits.
    PS50152. 25A_SYNTH_3. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    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].
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Hereford.

    Entry informationi

    Entry nameiOAS2_BOVIN
    AccessioniPrimary (citable) accession number: F1N3B8
    Secondary accession number(s): Q53AV7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 5, 2012
    Last sequence update: May 3, 2011
    Last modified: October 1, 2014
    This is version 25 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

    External Data

    Dasty 3