OAS3_MOUSE
ID OAS3_MOUSE Reviewed; 1138 AA.
AC Q8VI93; B9EIU4; Q8K4D2;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=2'-5'-oligoadenylate synthase 3;
DE Short=(2-5')oligo(A) synthase 3;
DE Short=2-5A synthase 3;
DE EC=2.7.7.84 {ECO:0000269|PubMed:12396720};
DE AltName: Full=2',5'-oligoadenylate synthetase-like 10;
GN Name=Oas3; Synonyms=oasl10;
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], FUNCTION, CATALYTIC ACTIVITY, AND TISSUE
RP 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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C3H/RV;
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [6]
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).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP REVIEW ON FUNCTION.
RX PubMed=21142819; DOI=10.1089/jir.2010.0107;
RA Kristiansen H., Gad H.H., Eskildsen-Larsen S., Despres P., Hartmann R.;
RT "The oligoadenylate synthetase family: an ancient protein family with
RT multiple antiviral activities.";
RL J. Interferon Cytokine Res. 31:41-47(2011).
CC -!- FUNCTION: Interferon-induced, dsRNA-activated antiviral enzyme which
CC plays a critical role in cellular innate antiviral response. In
CC addition, it may also play a role in other cellular processes such as
CC apoptosis, cell growth, differentiation and gene regulation.
CC Synthesizes preferentially dimers of 2'-5'-oligoadenylates (2-5A) from
CC ATP which then bind to the inactive monomeric form of ribonuclease L
CC (RNase L) leading to its dimerization and subsequent activation.
CC Activation of RNase L leads to degradation of cellular as well as viral
CC RNA, resulting in the inhibition of protein synthesis, thus terminating
CC viral replication. Can mediate the antiviral effect via the classical
CC RNase L-dependent pathway or an alternative antiviral pathway
CC independent of RNase L. {ECO:0000269|PubMed:12396720}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3 ATP = 5'-triphosphoadenylyl-(2'->5')-adenylyl-(2'->5')-
CC adenosine + 2 diphosphate; Xref=Rhea:RHEA:34407, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:67143; EC=2.7.7.84;
CC Evidence={ECO:0000269|PubMed:12396720};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305};
CC -!- ACTIVITY REGULATION: Produced as a latent enzyme which is activated by
CC dsRNA generated during the course of viral infection. Strongly
CC activated by long dsRNAs at least 50 nucleotides in length. ssRNA does
CC not activate the enzyme. {ECO:0000250|UniProtKB:Q9Y6K5}.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Intestine. {ECO:0000269|PubMed:12396720}.
CC -!- INDUCTION: By type I interferon (IFN) and viruses.
CC -!- DOMAIN: OAS domain 3 is catalytically active. OAS domain 1 has no
CC catalytic activity but is essential for recognition of long dsRNAs.
CC {ECO:0000250|UniProtKB:Q9Y6K5}.
CC -!- SIMILARITY: Belongs to the 2-5A synthase family. {ECO:0000305}.
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DR EMBL; AB067534; BAB84134.1; -; mRNA.
DR EMBL; AF453830; AAM47556.1; -; mRNA.
DR EMBL; AC115937; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466529; EDL19752.1; -; Genomic_DNA.
DR EMBL; BC141055; AAI41056.1; -; mRNA.
DR CCDS; CCDS39242.1; -.
DR RefSeq; NP_660261.1; NM_145226.2.
DR AlphaFoldDB; Q8VI93; -.
DR SMR; Q8VI93; -.
DR BioGRID; 232935; 8.
DR STRING; 10090.ENSMUSP00000035588; -.
DR iPTMnet; Q8VI93; -.
DR PhosphoSitePlus; Q8VI93; -.
DR SwissPalm; Q8VI93; -.
DR EPD; Q8VI93; -.
DR jPOST; Q8VI93; -.
DR MaxQB; Q8VI93; -.
DR PaxDb; Q8VI93; -.
DR PeptideAtlas; Q8VI93; -.
DR PRIDE; Q8VI93; -.
DR ProteomicsDB; 291933; -.
DR Antibodypedia; 31208; 199 antibodies from 32 providers.
DR DNASU; 246727; -.
DR Ensembl; ENSMUST00000044833; ENSMUSP00000035588; ENSMUSG00000032661.
DR GeneID; 246727; -.
DR KEGG; mmu:246727; -.
DR UCSC; uc008zhz.1; mouse.
DR CTD; 4940; -.
DR MGI; MGI:2180850; Oas3.
DR VEuPathDB; HostDB:ENSMUSG00000032661; -.
DR eggNOG; ENOG502S649; Eukaryota.
DR GeneTree; ENSGT00510000046406; -.
DR HOGENOM; CLU_287245_0_0_1; -.
DR InParanoid; Q8VI93; -.
DR OMA; LESWWQD; -.
DR OrthoDB; 611234at2759; -.
DR PhylomeDB; Q8VI93; -.
DR TreeFam; TF329749; -.
DR BioGRID-ORCS; 246727; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Oas3; mouse.
DR PRO; PR:Q8VI93; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q8VI93; protein.
DR Bgee; ENSMUSG00000032661; Expressed in granulocyte and 41 other tissues.
DR ExpressionAtlas; Q8VI93; baseline and differential.
DR Genevisible; Q8VI93; 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:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0001730; F:2'-5'-oligoadenylate synthetase activity; IDA:MGI.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0003725; F:double-stranded RNA binding; IDA:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042742; P:defense response to bacterium; ISO:MGI.
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:0039530; P:MDA-5 signaling pathway; ISO:MGI.
DR GO; GO:0071650; P:negative regulation of chemokine (C-C motif) ligand 5 production; ISO:MGI.
DR GO; GO:2000342; P:negative regulation of chemokine (C-X-C motif) ligand 2 production; ISO:MGI.
DR GO; GO:0035395; P:negative regulation of chemokine (C-X-C motif) ligand 9 production; ISO:MGI.
DR GO; GO:0071659; P:negative regulation of IP-10 production; ISO:MGI.
DR GO; GO:0060339; P:negative regulation of type I interferon-mediated signaling pathway; ISO:MGI.
DR GO; GO:0045071; P:negative regulation of viral genome replication; ISO:MGI.
DR GO; GO:0032728; P:positive regulation of interferon-beta production; ISO:MGI.
DR GO; GO:0071639; P:positive regulation of monocyte chemotactic protein-1 production; ISO:MGI.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; ISO:MGI.
DR GO; GO:0060700; P:regulation of ribonuclease activity; ISO:MGI.
DR GO; GO:0009615; P:response to virus; ISS:UniProtKB.
DR GO; GO:0039529; P:RIG-I signaling pathway; ISO:MGI.
DR CDD; cd05400; NT_2-5OAS_ClassI-CCAase; 3.
DR Gene3D; 3.30.460.10; -; 3.
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; IPR043518; 2-5OAS_N_CS.
DR InterPro; IPR006116; NT_2-5OAS_ClassI-CCAase.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR002934; Polymerase_NTP_transf_dom.
DR PANTHER; PTHR11258; PTHR11258; 2.
DR Pfam; PF01909; NTP_transf_2; 1.
DR Pfam; PF10421; OAS1_C; 3.
DR SUPFAM; SSF81301; SSF81301; 3.
DR PROSITE; PS00832; 25A_SYNTH_1; 1.
DR PROSITE; PS00833; 25A_SYNTH_2; 2.
DR PROSITE; PS50152; 25A_SYNTH_3; 3.
PE 1: Evidence at protein level;
KW Acetylation; Antiviral defense; ATP-binding; Cytoplasm; Immunity;
KW Innate immunity; Magnesium; Metal-binding; Nucleotide-binding;
KW Nucleotidyltransferase; Nucleus; Reference proteome; Repeat; RNA-binding;
KW Transferase.
FT CHAIN 1..1138
FT /note="2'-5'-oligoadenylate synthase 3"
FT /id="PRO_0000418630"
FT REGION 6..341
FT /note="OAS domain 1"
FT /evidence="ECO:0000305"
FT REGION 12..56
FT /note="Interaction with dsRNA"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6K5"
FT REGION 185..199
FT /note="Interaction with dsRNA"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6K5"
FT REGION 342..462
FT /note="Linker"
FT /evidence="ECO:0000305"
FT REGION 370..403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 434..459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 463..793
FT /note="OAS domain 2"
FT /evidence="ECO:0000305"
FT REGION 801..1135
FT /note="OAS domain 3"
FT /evidence="ECO:0000305"
FT BINDING 855
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P00973"
FT BINDING 867
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00973"
FT BINDING 869
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00973"
FT BINDING 939
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00973"
FT BINDING 998
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P29728"
FT BINDING 1001
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P00973"
FT BINDING 1020
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P00973"
FT SITE 154
FT /note="Interaction with dsRNA"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6K5"
FT SITE 242
FT /note="Interaction with dsRNA"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6K5"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6K5"
FT CONFLICT 215
FT /note="R -> Q (in Ref. 2; AAM47556)"
FT /evidence="ECO:0000305"
FT CONFLICT 733
FT /note="A -> T (in Ref. 2; AAM47556)"
FT /evidence="ECO:0000305"
FT CONFLICT 897
FT /note="H -> Q (in Ref. 2; AAM47556, 4; EDL19752 and 5;
FT AAI41056)"
FT /evidence="ECO:0000305"
FT CONFLICT 904
FT /note="M -> T (in Ref. 2; AAM47556)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1138 AA; 126333 MW; 64568BA94FC51866 CRC64;
MDLFHTPAGA LDKLVAHNLH PAPEFTAAVR GALGSLNITL QQHRARGSQR PRVIRIAKGG
AYARGTALRG GTDVELVIFL DCFQSFGDQK TCHSETLGAM RMLLESWGGH PGPGLTFEFS
QSKASRILQF RLASADGEHW IDVSLVPAFD VLGQPRSGVK PTPNVYSSLL SSHCQAGEYS
ACFTEPRKNF VNTRPAKLKN LILLVKHWYH QVQTRAVRAT LPPSYALELL TIFAWEQGCG
KDSFSLAQGL RTVLALIQHS KYLCIFWTEN YGFEDPAVGE FLRRQLKRPR PVILDPADPT
WDVGNGTAWR WDVLAQEAES SFSQQCFKQA SGVLVQPWEG PGLPRAGILD LGHPIYQGPN
QALEDNKGHL AVQSKERSQK PSNSAPGFPE AATKIPAMPN PSANKTRKIR KKAAHPKTVQ
EAALDSISSH VRITQSTASS HMPPDRSSIS TAGSRMSPDL SQIPSKDLDC FIQDHLRPSP
QFQQQVKQAI DAILCCLREK SVYKVLRVSK GGSFGRGTDL RGSCDVELVI FYKTLGDFKG
QKPHQAEILR DMQAQLRHWC QNPVPGLSLQ FIEQKPNALQ LQLASTDLSN RVDLSVLPAF
DAVGPLKSGT KPQPQVYSSL LSSGCQAGEH AACFAELRRN FINTCPPKLK SLMLLVKHWY
RQVVTRYKGG EAAGDAPPPA YALELLTIFA WEQGCGEQKF SLAEGLRTIL RLIQQHQSLC
IYWTVNYSVQ DPAIRAHLLC QLRKARPLVL DPADPTWNVG QGDWKLLAQE AAALGSQVCL
QSGDGTLVPP WDVTPALLHQ TLAEDLDKFI SEFLQPNRHF LTQVKRAVDT ICSFLKENCF
RNSTIKVLKV VKGGSSAKGT ALQGRSDADL VVFLSCFRQF SEQGSHRAEI ISEIQAHLEA
CQQMHSFDVK FEVSKRKNPR VLSFTLTSQT LLDQSVDFDV LPAFDALGQL RSGSRPDPRV
YTDLIHSCSN AGEFSTCFTE LQRDFITSRP TKLKSLIRLV KYWYQQCNKT IKGKGSLPPQ
HGLELLTVYA WEQGGQNPQF NMAEGFRTVL ELIVQYRQLC VYWTINYSAE DKTIGDFLKM
QLRKPRPVIL DPADPTGNLG HNARWDLLAK EATVYASALC CVDRDGNPIK PWPVKAAV
