ID   OASL1_MOUSE             Reviewed;         511 AA.
AC   Q8VI94; Q3UBP8; Q8K2A2; Q8QZV5;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   24-JAN-2024, entry version 153.
DE   RecName: Full=2'-5'-oligoadenylate synthase-like protein 1;
DE   AltName: Full=2',5'-oligoadenylate synthetase-like 9;
GN   Name=Oasl1; Synonyms=oasl9;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Czech II;
RX   PubMed=12169584; DOI=10.1152/ajplung.00496.2001;
RA   Smith J.B., Nguyen T.T., Hughes H.J., Herschman H.R., Widney D.P.,
RA   Bui K.C., Rovai L.E.;
RT   "Glucocorticoid-attenuated response genes induced in the lung during
RT   endotoxemia.";
RL   Am. J. Physiol. 283:L636-L647(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=FVB/N; TISSUE=Intestine;
RX   PubMed=12222967; DOI=10.1007/s00018-002-8499-2;
RA   Eskildsen S., Hartmann R., Kjeldgaard N.O., Justesen J.;
RT   "Gene structure of the murine 2'-5'-oligoadenylate synthetase family.";
RL   Cell. Mol. Life Sci. 59:1212-1222(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC   STRAIN=C57BL/6J; TISSUE=Colon;
RX   PubMed=12396720; DOI=10.1089/10799900260286696;
RA   Kakuta S., Shibata S., Iwakura Y.;
RT   "Genomic structure of the mouse 2',5'-oligoadenylate synthetase gene
RT   family.";
RL   J. Interferon Cytokine Res. 22:981-993(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C3H/He;
RX   PubMed=12080145; DOI=10.1073/pnas.142287799;
RA   Perelygin A.A., Scherbik S.V., Zhulin I.B., Stockman B.M., Li Y.,
RA   Brinton M.A.;
RT   "Positional cloning of the murine flavivirus resistance gene.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:9322-9327(2002).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow, Eye, and Kidney;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [8]
RP   FUNCTION, AND INDUCTION.
RX   PubMed=12799444; DOI=10.1093/nar/gkg427;
RA   Eskildsen S., Justesen J., Schierup M.H., Hartmann R.;
RT   "Characterization of the 2'-5'-oligoadenylate synthetase ubiquitin-like
RT   family.";
RL   Nucleic Acids Res. 31:3166-3173(2003).
RN   [9]
RP   REVIEW.
RX   PubMed=17024523; DOI=10.1007/s00239-006-0073-3;
RA   Perelygin A.A., Zharkikh A.A., Scherbik S.V., Brinton M.A.;
RT   "The mammalian 2'-5' oligoadenylate synthetase gene family: evidence for
RT   concerted evolution of paralogous Oas1 genes in Rodentia and
RT   Artiodactyla.";
RL   J. Mol. Evol. 63:562-576(2006).
CC   -!- FUNCTION: Does not have 2'-5'-OAS activity, but can bind double-
CC       stranded RNA. Displays antiviral activity via an alternative antiviral
CC       pathway independent of RNase L. {ECO:0000269|PubMed:12396720,
CC       ECO:0000269|PubMed:12799444}.
CC   -!- SUBUNIT: Specifically interacts with the ligand binding domain of the
CC       thyroid receptor (TR). TRIP14 does not require the presence of thyroid
CC       hormone for its interaction. Binds MBD1 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. Cytoplasm
CC       {ECO:0000250}.
CC   -!- INDUCTION: By type I interferon (IFN) and viruses.
CC       {ECO:0000269|PubMed:12799444}.
CC   -!- SIMILARITY: Belongs to the 2-5A synthase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAE29916.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AF426289; AAN31518.1; -; mRNA.
DR   EMBL; AY089728; AAM08092.1; -; mRNA.
DR   EMBL; AY057107; AAL12828.1; -; mRNA.
DR   EMBL; AB067533; BAB84133.1; -; mRNA.
DR   EMBL; AK078690; BAC37360.1; -; mRNA.
DR   EMBL; AK149824; BAE29106.1; -; mRNA.
DR   EMBL; AK150863; BAE29916.1; ALT_FRAME; mRNA.
DR   EMBL; AK165578; BAE38269.1; -; mRNA.
DR   EMBL; AC116500; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC032152; AAH32152.1; -; mRNA.
DR   CCDS; CCDS19575.1; -.
DR   RefSeq; NP_660210.1; NM_145209.3.
DR   RefSeq; XP_006530357.1; XM_006530294.3.
DR   AlphaFoldDB; Q8VI94; -.
DR   SMR; Q8VI94; -.
DR   STRING; 10090.ENSMUSP00000107771; -.
DR   iPTMnet; Q8VI94; -.
DR   PhosphoSitePlus; Q8VI94; -.
DR   SwissPalm; Q8VI94; -.
DR   EPD; Q8VI94; -.
DR   jPOST; Q8VI94; -.
DR   MaxQB; Q8VI94; -.
DR   PaxDb; 10090-ENSMUSP00000031540; -.
DR   PeptideAtlas; Q8VI94; -.
DR   ProteomicsDB; 294262; -.
DR   Antibodypedia; 808; 191 antibodies from 26 providers.
DR   DNASU; 231655; -.
DR   Ensembl; ENSMUST00000031540.11; ENSMUSP00000031540.5; ENSMUSG00000041827.16.
DR   Ensembl; ENSMUST00000112143.4; ENSMUSP00000107771.4; ENSMUSG00000041827.16.
DR   GeneID; 231655; -.
DR   KEGG; mmu:231655; -.
DR   UCSC; uc008zcv.1; mouse.
DR   AGR; MGI:2180849; -.
DR   CTD; 231655; -.
DR   MGI; MGI:2180849; Oasl1.
DR   VEuPathDB; HostDB:ENSMUSG00000041827; -.
DR   eggNOG; KOG0001; Eukaryota.
DR   GeneTree; ENSGT00510000046406; -.
DR   HOGENOM; CLU_040930_1_0_1; -.
DR   InParanoid; Q8VI94; -.
DR   OMA; VICIYWT; -.
DR   OrthoDB; 4638494at2759; -.
DR   PhylomeDB; Q8VI94; -.
DR   TreeFam; TF329749; -.
DR   Reactome; R-MMU-8983711; OAS antiviral response.
DR   BioGRID-ORCS; 231655; 2 hits in 78 CRISPR screens.
DR   PRO; PR:Q8VI94; -.
DR   Proteomes; UP000000589; Chromosome 5.
DR   RNAct; Q8VI94; Protein.
DR   Bgee; ENSMUSG00000041827; Expressed in small intestine Peyer's patch and 75 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR   GO; GO:0003725; F:double-stranded RNA binding; IDA:MGI.
DR   GO; GO:0016779; F:nucleotidyltransferase activity; IEA:InterPro.
DR   GO; GO:0051607; P:defense response to virus; ISO:MGI.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   GO; GO:0070106; P:interleukin-27-mediated signaling pathway; IEP:ARUK-UCL.
DR   GO; GO:0045071; P:negative regulation of viral genome replication; ISO:MGI.
DR   GO; GO:1900246; P:positive regulation of RIG-I signaling pathway; ISO:MGI.
DR   GO; GO:0009615; P:response to virus; ISS:UniProtKB.
DR   CDD; cd05400; NT_2-5OAS_ClassI-CCAase; 1.
DR   CDD; cd01811; Ubl1_OASL; 1.
DR   Gene3D; 1.10.1410.20; 2'-5'-oligoadenylate synthetase 1, domain 2; 1.
DR   Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR   InterPro; IPR018952; 2-5-oligoAdlate_synth_1_dom2/C.
DR   InterPro; IPR006117; 2-5OAS_C_CS.
DR   InterPro; IPR006116; NT_2-5OAS_ClassI-CCAase.
DR   InterPro; IPR043519; NT_sf.
DR   InterPro; IPR000626; Ubiquitin-like_dom.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   PANTHER; PTHR11258:SF16; 2'-5'-OLIGOADENYLATE SYNTHASE-LIKE PROTEIN; 1.
DR   PANTHER; PTHR11258; 2-5 OLIGOADENYLATE SYNTHETASE; 1.
DR   Pfam; PF10421; OAS1_C; 1.
DR   Pfam; PF00240; ubiquitin; 1.
DR   SMART; SM00213; UBQ; 2.
DR   SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR   SUPFAM; SSF81631; PAP/OAS1 substrate-binding domain; 1.
DR   SUPFAM; SSF54236; Ubiquitin-like; 2.
DR   PROSITE; PS00833; 25A_SYNTH_2; 1.
DR   PROSITE; PS50152; 25A_SYNTH_3; 1.
DR   PROSITE; PS50053; UBIQUITIN_2; 1.
DR   Genevisible; Q8VI94; MM.
PE   2: Evidence at transcript level;
KW   Antiviral defense; Cytoplasm; Immunity; Innate immunity; Nucleus;
KW   Reference proteome; Repeat; RNA-binding.
FT   CHAIN           1..511
FT                   /note="2'-5'-oligoadenylate synthase-like protein 1"
FT                   /id="PRO_0000418632"
FT   DOMAIN          350..429
FT                   /note="Ubiquitin-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   DOMAIN          430..506
FT                   /note="Ubiquitin-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   CONFLICT        298
FT                   /note="I -> V (in Ref. 1; AAN31518 and 7; AAH32152)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        339
FT                   /note="V -> I (in Ref. 1; AAN31518 and 7; AAH32152)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        352
FT                   /note="V -> L (in Ref. 2; AAM08092)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        356
FT                   /note="E -> D (in Ref. 2; AAM08092)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        356
FT                   /note="E -> Q (in Ref. 1; AAN31518 and 7; AAH32152)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        360
FT                   /note="S -> P (in Ref. 1; AAN31518 and 7; AAH32152)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        382
FT                   /note="S -> T (in Ref. 2; AAM08092)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        383
FT                   /note="Q -> R (in Ref. 1; AAN31518 and 7; AAH32152)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        396
FT                   /note="P -> L (in Ref. 1; AAN31518 and 7; AAH32152)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        485
FT                   /note="F -> L (in Ref. 1; AAN31518 and 7; AAH32152)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        501
FT                   /note="T -> M (in Ref. 1; AAN31518 and 7; AAH32152)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   511 AA;  59088 MW;  8E679549424535C1 CRC64;
     MAVAQELYGF PASKLDSFVA QWLQPTREWK EEVLETVQTV EQFLRQENFR EDRGPARDVR
     VLKVLKVGCF GNGTVLRSTT DVELVVFLSC FHSFQEEAKH HQAVLRLIQK RMYYCQELMD
     LGLSNLSVTN RVPSSLIFTI QTRETWETIT VTVVPAYRAL GPSCPSSEVY ANLIKANGYP
     GNFSPSFSEL QRNFVKHRPT KLKSLLRLVK HWYQQYVRDK CPRANLPPLY ALELLTVYAW
     EAGTREDANF RLDEGLATVM ELLQDHELLC IYWTKHYTLQ HPVIEACVRR QLRGQRPIIL
     DPADPTNNVA EGYRWDIVAQ RANQCLKQDC CYDNRDSPVP SWRVKRAPDI QVTVQEWGHS
     DLTFWVNPYE PIKKLKEKIQ LSQGYLGLQR LSFQEPGGER QLIRSHCTLA YYGIFCDTHI
     CLLDTISPEI QVFVKNPDGR SHAYAIHPLD YVLNLKQQIE DRQGLRCQEQ RLEFQGHILE
     DWFDFKSYGI QDSVTVILSK TTEGAAPFVP S
//