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Q8VI94

- OASL1_MOUSE

UniProt

Q8VI94 - OASL1_MOUSE

Protein

2'-5'-oligoadenylate synthase-like protein 1

Gene

Oasl1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 97 (01 Oct 2014)
      Sequence version 1 (01 Mar 2002)
      Previous versions | rss
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    Functioni

    Does not have 2'-5'-OAS activity, but can bind double-stranded RNA. Displays antiviral activity via an alternative antiviral pathway independent of RNase L.2 Publications

    GO - Molecular functioni

    1. ATP binding Source: InterPro
    2. DNA binding Source: UniProtKB
    3. double-stranded RNA binding Source: MGI
    4. transferase activity Source: InterPro

    GO - Biological processi

    1. defense response to virus Source: UniProtKB-KW
    2. innate immune response Source: UniProtKB-KW
    3. negative regulation of viral genome replication Source: Ensembl
    4. response to virus Source: UniProtKB

    Keywords - Biological processi

    Antiviral defense, Immunity, Innate immunity

    Keywords - Ligandi

    RNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_198660. Interferon gamma signaling.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    2'-5'-oligoadenylate synthase-like protein 1
    Alternative name(s):
    2',5'-oligoadenylate synthetase-like 9
    Gene namesi
    Name:Oasl1
    Synonyms:oasl9
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 5

    Organism-specific databases

    MGIiMGI:2180849. Oasl1.

    Subcellular locationi

    Nucleusnucleolus By similarity. Cytoplasm By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. nucleolus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 5115112'-5'-oligoadenylate synthase-like protein 1PRO_0000418632Add
    BLAST

    Proteomic databases

    MaxQBiQ8VI94.
    PRIDEiQ8VI94.

    Expressioni

    Inductioni

    By type I interferon (IFN) and viruses.1 Publication

    Gene expression databases

    BgeeiQ8VI94.
    GenevestigatoriQ8VI94.

    Interactioni

    Subunit structurei

    Specifically interacts with the ligand binding domain of the thyroid receptor (TR). TRIP14 does not require the presence of thyroid hormone for its interaction. Binds MBD1 By similarity.By similarity

    Protein-protein interaction databases

    STRINGi10090.ENSMUSP00000031540.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8VI94.
    SMRiQ8VI94. Positions 350-507.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini350 – 42980Ubiquitin-like 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini430 – 50677Ubiquitin-like 2PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the 2-5A synthase family.Curated
    Contains 2 ubiquitin-like domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG309765.
    GeneTreeiENSGT00510000046406.
    HOGENOMiHOG000022614.
    HOVERGENiHBG000994.
    InParanoidiQ8VI94.
    KOiK14608.
    OMAiCFHSFQE.
    OrthoDBiEOG7WDN1R.
    PhylomeDBiQ8VI94.
    TreeFamiTF329749.

    Family and domain databases

    Gene3Di1.10.1410.20. 1 hit.
    InterProiIPR006117. 2-5-oligoadenylate_synth_CS.
    IPR006116. 2-5-oligoadenylate_synth_N.
    IPR018952. 2-5-oligoAdlate_synth_1_dom2/C.
    IPR026774. 2-5A_synthase.
    IPR000626. Ubiquitin-like.
    IPR029071. Ubiquitin-rel_dom.
    [Graphical view]
    PANTHERiPTHR11258. PTHR11258. 1 hit.
    PfamiPF10421. OAS1_C. 1 hit.
    PF00240. ubiquitin. 1 hit.
    [Graphical view]
    SMARTiSM00213. UBQ. 2 hits.
    [Graphical view]
    SUPFAMiSSF54236. SSF54236. 2 hits.
    PROSITEiPS00833. 25A_SYNTH_2. 1 hit.
    PS50152. 25A_SYNTH_3. 1 hit.
    PS50053. UBIQUITIN_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q8VI94-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAVAQELYGF PASKLDSFVA QWLQPTREWK EEVLETVQTV EQFLRQENFR    50
    EDRGPARDVR VLKVLKVGCF GNGTVLRSTT DVELVVFLSC FHSFQEEAKH 100
    HQAVLRLIQK RMYYCQELMD LGLSNLSVTN RVPSSLIFTI QTRETWETIT 150
    VTVVPAYRAL GPSCPSSEVY ANLIKANGYP GNFSPSFSEL QRNFVKHRPT 200
    KLKSLLRLVK HWYQQYVRDK CPRANLPPLY ALELLTVYAW EAGTREDANF 250
    RLDEGLATVM ELLQDHELLC IYWTKHYTLQ HPVIEACVRR QLRGQRPIIL 300
    DPADPTNNVA EGYRWDIVAQ RANQCLKQDC CYDNRDSPVP SWRVKRAPDI 350
    QVTVQEWGHS DLTFWVNPYE PIKKLKEKIQ LSQGYLGLQR LSFQEPGGER 400
    QLIRSHCTLA YYGIFCDTHI CLLDTISPEI QVFVKNPDGR SHAYAIHPLD 450
    YVLNLKQQIE DRQGLRCQEQ RLEFQGHILE DWFDFKSYGI QDSVTVILSK 500
    TTEGAAPFVP S 511
    Length:511
    Mass (Da):59,088
    Last modified:March 1, 2002 - v1
    Checksum:i8E679549424535C1
    GO

    Sequence cautioni

    The sequence BAE29916.1 differs from that shown. Reason: Frameshift at position 509.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti298 – 2981I → V in AAN31518. (PubMed:12169584)Curated
    Sequence conflicti298 – 2981I → V in AAH32152. (PubMed:15489334)Curated
    Sequence conflicti339 – 3391V → I in AAN31518. (PubMed:12169584)Curated
    Sequence conflicti339 – 3391V → I in AAH32152. (PubMed:15489334)Curated
    Sequence conflicti352 – 3521V → L in AAM08092. (PubMed:12222967)Curated
    Sequence conflicti356 – 3561E → D in AAM08092. (PubMed:12222967)Curated
    Sequence conflicti356 – 3561E → Q in AAN31518. (PubMed:12169584)Curated
    Sequence conflicti356 – 3561E → Q in AAH32152. (PubMed:15489334)Curated
    Sequence conflicti360 – 3601S → P in AAN31518. (PubMed:12169584)Curated
    Sequence conflicti360 – 3601S → P in AAH32152. (PubMed:15489334)Curated
    Sequence conflicti382 – 3821S → T in AAM08092. (PubMed:12222967)Curated
    Sequence conflicti383 – 3831Q → R in AAN31518. (PubMed:12169584)Curated
    Sequence conflicti383 – 3831Q → R in AAH32152. (PubMed:15489334)Curated
    Sequence conflicti396 – 3961P → L in AAN31518. (PubMed:12169584)Curated
    Sequence conflicti396 – 3961P → L in AAH32152. (PubMed:15489334)Curated
    Sequence conflicti485 – 4851F → L in AAN31518. (PubMed:12169584)Curated
    Sequence conflicti485 – 4851F → L in AAH32152. (PubMed:15489334)Curated
    Sequence conflicti501 – 5011T → M in AAN31518. (PubMed:12169584)Curated
    Sequence conflicti501 – 5011T → M in AAH32152. (PubMed:15489334)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF426289 mRNA. Translation: AAN31518.1.
    AY089728 mRNA. Translation: AAM08092.1.
    AY057107 mRNA. Translation: AAL12828.1.
    AB067533 mRNA. Translation: BAB84133.1.
    AK078690 mRNA. Translation: BAC37360.1.
    AK149824 mRNA. Translation: BAE29106.1.
    AK150863 mRNA. Translation: BAE29916.1. Frameshift.
    AK165578 mRNA. Translation: BAE38269.1.
    AC116500 Genomic DNA. No translation available.
    BC032152 mRNA. Translation: AAH32152.1.
    CCDSiCCDS19575.1.
    RefSeqiNP_660210.1. NM_145209.3.
    XP_006530357.1. XM_006530294.1.
    UniGeneiMm.95479.

    Genome annotation databases

    EnsembliENSMUST00000031540; ENSMUSP00000031540; ENSMUSG00000041827.
    ENSMUST00000112143; ENSMUSP00000107771; ENSMUSG00000041827.
    GeneIDi231655.
    KEGGimmu:231655.
    UCSCiuc008zcv.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF426289 mRNA. Translation: AAN31518.1 .
    AY089728 mRNA. Translation: AAM08092.1 .
    AY057107 mRNA. Translation: AAL12828.1 .
    AB067533 mRNA. Translation: BAB84133.1 .
    AK078690 mRNA. Translation: BAC37360.1 .
    AK149824 mRNA. Translation: BAE29106.1 .
    AK150863 mRNA. Translation: BAE29916.1 . Frameshift.
    AK165578 mRNA. Translation: BAE38269.1 .
    AC116500 Genomic DNA. No translation available.
    BC032152 mRNA. Translation: AAH32152.1 .
    CCDSi CCDS19575.1.
    RefSeqi NP_660210.1. NM_145209.3.
    XP_006530357.1. XM_006530294.1.
    UniGenei Mm.95479.

    3D structure databases

    ProteinModelPortali Q8VI94.
    SMRi Q8VI94. Positions 350-507.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10090.ENSMUSP00000031540.

    Proteomic databases

    MaxQBi Q8VI94.
    PRIDEi Q8VI94.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000031540 ; ENSMUSP00000031540 ; ENSMUSG00000041827 .
    ENSMUST00000112143 ; ENSMUSP00000107771 ; ENSMUSG00000041827 .
    GeneIDi 231655.
    KEGGi mmu:231655.
    UCSCi uc008zcv.1. mouse.

    Organism-specific databases

    CTDi 231655.
    MGIi MGI:2180849. Oasl1.

    Phylogenomic databases

    eggNOGi NOG309765.
    GeneTreei ENSGT00510000046406.
    HOGENOMi HOG000022614.
    HOVERGENi HBG000994.
    InParanoidi Q8VI94.
    KOi K14608.
    OMAi CFHSFQE.
    OrthoDBi EOG7WDN1R.
    PhylomeDBi Q8VI94.
    TreeFami TF329749.

    Enzyme and pathway databases

    Reactomei REACT_198660. Interferon gamma signaling.

    Miscellaneous databases

    NextBioi 380687.
    PROi Q8VI94.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q8VI94.
    Genevestigatori Q8VI94.

    Family and domain databases

    Gene3Di 1.10.1410.20. 1 hit.
    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.
    IPR000626. Ubiquitin-like.
    IPR029071. Ubiquitin-rel_dom.
    [Graphical view ]
    PANTHERi PTHR11258. PTHR11258. 1 hit.
    Pfami PF10421. OAS1_C. 1 hit.
    PF00240. ubiquitin. 1 hit.
    [Graphical view ]
    SMARTi SM00213. UBQ. 2 hits.
    [Graphical view ]
    SUPFAMi SSF54236. SSF54236. 2 hits.
    PROSITEi PS00833. 25A_SYNTH_2. 1 hit.
    PS50152. 25A_SYNTH_3. 1 hit.
    PS50053. UBIQUITIN_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Glucocorticoid-attenuated response genes induced in the lung during endotoxemia."
      Smith J.B., Nguyen T.T., Hughes H.J., Herschman H.R., Widney D.P., Bui K.C., Rovai L.E.
      Am. J. Physiol. 283:L636-L647(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: Czech II.
    2. "Gene structure of the murine 2'-5'-oligoadenylate synthetase family."
      Eskildsen S., Hartmann R., Kjeldgaard N.O., Justesen J.
      Cell. Mol. Life Sci. 59:1212-1222(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: FVB/N.
      Tissue: Intestine.
    3. "Genomic structure of the mouse 2',5'-oligoadenylate synthetase gene family."
      Kakuta S., Shibata S., Iwakura Y.
      J. Interferon Cytokine Res. 22:981-993(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
      Strain: C57BL/6J.
      Tissue: Colon.
    4. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: C3H/He.
    5. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Bone marrow, Eye and Kidney.
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Czech II.
      Tissue: Mammary tumor.
    8. "Characterization of the 2'-5'-oligoadenylate synthetase ubiquitin-like family."
      Eskildsen S., Justesen J., Schierup M.H., Hartmann R.
      Nucleic Acids Res. 31:3166-3173(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INDUCTION.
    9. "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: REVIEW.

    Entry informationi

    Entry nameiOASL1_MOUSE
    AccessioniPrimary (citable) accession number: Q8VI94
    Secondary accession number(s): Q3UBP8, Q8K2A2, Q8QZV5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 5, 2012
    Last sequence update: March 1, 2002
    Last modified: October 1, 2014
    This is version 97 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. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3