OASL1_MOUSE
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 03-AUG-2022, entry version 146.
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};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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.ENSMUSP00000031540; -.
DR iPTMnet; Q8VI94; -.
DR PhosphoSitePlus; Q8VI94; -.
DR SwissPalm; Q8VI94; -.
DR EPD; Q8VI94; -.
DR jPOST; Q8VI94; -.
DR MaxQB; Q8VI94; -.
DR PaxDb; Q8VI94; -.
DR PeptideAtlas; Q8VI94; -.
DR PRIDE; Q8VI94; -.
DR ProteomicsDB; 294262; -.
DR Antibodypedia; 808; 179 antibodies from 26 providers.
DR DNASU; 231655; -.
DR Ensembl; ENSMUST00000031540; ENSMUSP00000031540; ENSMUSG00000041827.
DR Ensembl; ENSMUST00000112143; ENSMUSP00000107771; ENSMUSG00000041827.
DR GeneID; 231655; -.
DR KEGG; mmu:231655; -.
DR UCSC; uc008zcv.1; mouse.
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; 611234at2759; -.
DR PhylomeDB; Q8VI94; -.
DR TreeFam; TF329749; -.
DR Reactome; R-MMU-8983711; OAS antiviral response.
DR BioGRID-ORCS; 231655; 2 hits in 73 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 74 other tissues.
DR Genevisible; Q8VI94; MM.
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:0060700; P:regulation of ribonuclease activity; IBA:GO_Central.
DR GO; GO:0009615; P:response to virus; ISS:UniProtKB.
DR CDD; cd05400; NT_2-5OAS_ClassI-CCAase; 1.
DR Gene3D; 3.30.460.10; -; 1.
DR InterPro; IPR018952; 2-5-oligoAdlate_synth_1_dom2/C.
DR InterPro; IPR026774; 2-5A_synthase.
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; PTHR11258; 1.
DR Pfam; PF10421; OAS1_C; 1.
DR Pfam; PF00240; ubiquitin; 1.
DR SMART; SM00213; UBQ; 2.
DR SUPFAM; SSF54236; SSF54236; 2.
DR SUPFAM; SSF81301; SSF81301; 1.
DR PROSITE; PS00833; 25A_SYNTH_2; 1.
DR PROSITE; PS50152; 25A_SYNTH_3; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
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
