OAS3_HUMAN
ID OAS3_HUMAN Reviewed; 1087 AA.
AC Q9Y6K5; Q2HJ14; Q9H3P5;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 3.
DT 03-AUG-2022, entry version 172.
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:25775560, ECO:0000269|PubMed:9880533};
DE AltName: Full=p100 OAS;
DE Short=p100OAS;
GN Name=OAS3; ORFNames=P/OKcl.4;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, CATALYTIC
RP ACTIVITY, COFACTOR, AND SUBCELLULAR LOCATION.
RX PubMed=9880533; DOI=10.1074/jbc.274.3.1557;
RA Rebouillat D., Hovnanian A., Marie I., Hovanessian A.G.;
RT "The 100-kDa 2',5'-oligoadenylate synthetase catalyzing preferentially the
RT synthesis of dimeric pppA2'p5'A molecules is composed of three homologous
RT domains.";
RL J. Biol. Chem. 274:1557-1565(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT LYS-18.
RC TISSUE=Pancreatic cancer;
RX PubMed=11280764;
RA Ito M., Shichijo S., Tsuda N., Ochi M., Harashima N., Saito N., Itoh K.;
RT "Molecular basis of T cell-mediated recognition of pancreatic cancer
RT cells.";
RL Cancer Res. 61:2038-2046(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-381.
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-59.
RC TISSUE=Monocyte;
RX PubMed=11112351; DOI=10.1006/geno.2000.6382;
RA Rebouillat D., Hovnanian A., David G., Hovanessian A.G., Williams B.R.;
RT "Characterization of the gene encoding the 100-kDa form of human 2',
RT 5'oligoadenylate synthetase.";
RL Genomics 70:232-240(2000).
RN [6]
RP PROTEIN SEQUENCE OF 1-17; 118-132; 244-253 AND 371-378, ACETYLATION AT
RP MET-1, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Prostatic carcinoma;
RA Bienvenut W.V., Gao M., Leug H.;
RL Submitted (JUN-2009) to UniProtKB.
RN [7]
RP REVIEW ON FUNCTION.
RX PubMed=17408844; DOI=10.1016/j.biochi.2007.02.003;
RA Hovanessian A.G., Justesen J.;
RT "The human 2'-5'oligoadenylate synthetase family: unique interferon-
RT inducible enzymes catalyzing 2'-5' instead of 3'-5' phosphodiester bond
RT formation.";
RL Biochimie 89:779-788(2007).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=19923450; DOI=10.4049/jimmunol.0902728;
RA Lin R.J., Yu H.P., Chang B.L., Tang W.C., Liao C.L., Lin Y.L.;
RT "Distinct antiviral roles for human 2',5'-oligoadenylate synthetase family
RT members against dengue virus infection.";
RL J. Immunol. 183:8035-8043(2009).
RN [9]
RP REVIEW.
RX PubMed=19904482; DOI=10.1007/s00239-009-9299-1;
RA Kjaer K.H., Poulsen J.B., Reintamm T., Saby E., Martensen P.M., Kelve M.,
RA Justesen J.;
RT "Evolution of the 2'-5'-oligoadenylate synthetase family in eukaryotes and
RT bacteria.";
RL J. Mol. Evol. 69:612-624(2009).
RN [10]
RP FUNCTION.
RX PubMed=19056102; DOI=10.1016/j.virol.2008.10.021;
RA Brehin A.C., Casademont I., Frenkiel M.P., Julier C., Sakuntabhai A.,
RA Despres P.;
RT "The large form of human 2',5'-Oligoadenylate Synthetase (OAS3) exerts
RT antiviral effect against Chikungunya virus.";
RL Virology 384:216-222(2009).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
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).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-365, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 1-371 IN COMPLEX WITH DSRNA,
RP CATALYTIC ACTIVITY, SUBUNIT, DOMAIN, AND MUTAGENESIS OF ARG-30; ARG-41;
RP GLU-76; SER-145 AND 816-ASP--ASP-818.
RX PubMed=25775560; DOI=10.1073/pnas.1419409112;
RA Donovan J., Whitney G., Rath S., Korennykh A.;
RT "Structural mechanism of sensing long dsRNA via a noncatalytic domain in
RT human oligoadenylate synthetase 3.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:3949-3954(2015).
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. Displays antiviral activity against Chikungunya
CC virus (CHIKV), Dengue virus, Sindbis virus (SINV) and Semliki forest
CC virus (SFV). {ECO:0000269|PubMed:19056102, ECO:0000269|PubMed:19923450,
CC ECO:0000269|PubMed:9880533}.
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:25775560, ECO:0000269|PubMed:9880533};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000305|PubMed:9880533};
CC -!- ACTIVITY REGULATION: Produced as a latent enzyme which is activated by
CC dsRNA generated during the course of viral infection (Probable).
CC Strongly activated by long dsRNAs at least 50 nucleotides in length
CC (PubMed:25775560). ssRNA does not activate the enzyme
CC (PubMed:25775560). {ECO:0000269|PubMed:25775560, ECO:0000305}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:25775560}.
CC -!- INTERACTION:
CC Q9Y6K5; Q7L2E3: DHX30; NbExp=2; IntAct=EBI-6115729, EBI-1211456;
CC Q9Y6K5; P56537: EIF6; NbExp=2; IntAct=EBI-6115729, EBI-372243;
CC Q9Y6K5; Q8IY81: FTSJ3; NbExp=2; IntAct=EBI-6115729, EBI-744088;
CC Q9Y6K5; Q12894: IFRD2; NbExp=2; IntAct=EBI-6115729, EBI-2512448;
CC Q9Y6K5; Q7Z434: MAVS; NbExp=2; IntAct=EBI-6115729, EBI-995373;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- TISSUE SPECIFICITY: Present at high level in placenta trophoblast.
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:0000269|PubMed:25775560}.
CC -!- SIMILARITY: Belongs to the 2-5A synthase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD28543.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF063613; AAD28543.1; ALT_FRAME; mRNA.
DR EMBL; AB044545; BAB18647.1; -; mRNA.
DR EMBL; AC004551; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC113746; AAI13747.1; -; mRNA.
DR EMBL; AF251351; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS44981.1; -.
DR RefSeq; NP_006178.2; NM_006187.3.
DR PDB; 4S3N; X-ray; 2.00 A; A=1-371.
DR PDBsum; 4S3N; -.
DR AlphaFoldDB; Q9Y6K5; -.
DR SMR; Q9Y6K5; -.
DR BioGRID; 110994; 53.
DR IntAct; Q9Y6K5; 43.
DR MINT; Q9Y6K5; -.
DR STRING; 9606.ENSP00000228928; -.
DR iPTMnet; Q9Y6K5; -.
DR PhosphoSitePlus; Q9Y6K5; -.
DR BioMuta; OAS3; -.
DR DMDM; 317373408; -.
DR EPD; Q9Y6K5; -.
DR jPOST; Q9Y6K5; -.
DR MassIVE; Q9Y6K5; -.
DR MaxQB; Q9Y6K5; -.
DR PaxDb; Q9Y6K5; -.
DR PeptideAtlas; Q9Y6K5; -.
DR PRIDE; Q9Y6K5; -.
DR ProteomicsDB; 86712; -.
DR Antibodypedia; 31208; 199 antibodies from 32 providers.
DR DNASU; 4940; -.
DR Ensembl; ENST00000228928.12; ENSP00000228928.7; ENSG00000111331.14.
DR GeneID; 4940; -.
DR KEGG; hsa:4940; -.
DR MANE-Select; ENST00000228928.12; ENSP00000228928.7; NM_006187.4; NP_006178.2.
DR UCSC; uc001tug.4; human.
DR CTD; 4940; -.
DR DisGeNET; 4940; -.
DR GeneCards; OAS3; -.
DR HGNC; HGNC:8088; OAS3.
DR HPA; ENSG00000111331; Low tissue specificity.
DR MIM; 603351; gene.
DR neXtProt; NX_Q9Y6K5; -.
DR OpenTargets; ENSG00000111331; -.
DR PharmGKB; PA31877; -.
DR VEuPathDB; HostDB:ENSG00000111331; -.
DR eggNOG; ENOG502S649; Eukaryota.
DR GeneTree; ENSGT00510000046406; -.
DR HOGENOM; CLU_287245_0_0_1; -.
DR OMA; LESWWQD; -.
DR OrthoDB; 611234at2759; -.
DR PhylomeDB; Q9Y6K5; -.
DR TreeFam; TF329749; -.
DR BioCyc; MetaCyc:ENSG00000111331-MON; -.
DR BRENDA; 2.7.7.84; 2681.
DR PathwayCommons; Q9Y6K5; -.
DR Reactome; R-HSA-877300; Interferon gamma signaling.
DR Reactome; R-HSA-8983711; OAS antiviral response.
DR Reactome; R-HSA-909733; Interferon alpha/beta signaling.
DR SignaLink; Q9Y6K5; -.
DR BioGRID-ORCS; 4940; 8 hits in 1087 CRISPR screens.
DR ChiTaRS; OAS3; human.
DR GeneWiki; OAS3; -.
DR GenomeRNAi; 4940; -.
DR Pharos; Q9Y6K5; Tbio.
DR PRO; PR:Q9Y6K5; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q9Y6K5; protein.
DR Bgee; ENSG00000111331; Expressed in monocyte and 155 other tissues.
DR ExpressionAtlas; Q9Y6K5; baseline and differential.
DR Genevisible; Q9Y6K5; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; TAS:ProtInc.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0001730; F:2'-5'-oligoadenylate synthetase activity; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0003725; F:double-stranded RNA binding; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042742; P:defense response to bacterium; IMP:ARUK-UCL.
DR GO; GO:0051607; P:defense response to virus; IDA:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0039530; P:MDA-5 signaling pathway; IMP:ARUK-UCL.
DR GO; GO:0071650; P:negative regulation of chemokine (C-C motif) ligand 5 production; IMP:ARUK-UCL.
DR GO; GO:2000342; P:negative regulation of chemokine (C-X-C motif) ligand 2 production; IMP:ARUK-UCL.
DR GO; GO:0035395; P:negative regulation of chemokine (C-X-C motif) ligand 9 production; IMP:ARUK-UCL.
DR GO; GO:0071659; P:negative regulation of IP-10 production; IMP:ARUK-UCL.
DR GO; GO:0060339; P:negative regulation of type I interferon-mediated signaling pathway; IMP:ARUK-UCL.
DR GO; GO:0045071; P:negative regulation of viral genome replication; IDA:UniProtKB.
DR GO; GO:0006139; P:nucleobase-containing compound metabolic process; TAS:ProtInc.
DR GO; GO:0032728; P:positive regulation of interferon-beta production; IMP:ARUK-UCL.
DR GO; GO:0071639; P:positive regulation of monocyte chemotactic protein-1 production; IMP:ARUK-UCL.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IMP:ARUK-UCL.
DR GO; GO:0060700; P:regulation of ribonuclease activity; IDA:UniProtKB.
DR GO; GO:0009615; P:response to virus; IDA:UniProtKB.
DR GO; GO:0039529; P:RIG-I signaling pathway; IMP:ARUK-UCL.
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; 3.
DR PROSITE; PS00833; 25A_SYNTH_2; 2.
DR PROSITE; PS50152; 25A_SYNTH_3; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Antiviral defense; ATP-binding; Cytoplasm;
KW Direct protein sequencing; Immunity; Innate immunity; Magnesium;
KW Metal-binding; Nucleotide-binding; Nucleotidyltransferase; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; RNA-binding; Transferase.
FT CHAIN 1..1087
FT /note="2'-5'-oligoadenylate synthase 3"
FT /id="PRO_0000160265"
FT REGION 6..343
FT /note="OAS domain 1"
FT /evidence="ECO:0000305"
FT REGION 12..57
FT /note="Interaction with dsRNA"
FT /evidence="ECO:0000269|PubMed:25775560"
FT REGION 186..200
FT /note="Interaction with dsRNA"
FT /evidence="ECO:0000269|PubMed:25775560"
FT REGION 344..410
FT /note="Linker"
FT /evidence="ECO:0000305"
FT REGION 411..742
FT /note="OAS domain 2"
FT /evidence="ECO:0000305"
FT REGION 750..1084
FT /note="OAS domain 3"
FT /evidence="ECO:0000305"
FT BINDING 804
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P00973"
FT BINDING 816
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000305|PubMed:25775560"
FT BINDING 818
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000305|PubMed:25775560"
FT BINDING 888
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00973"
FT BINDING 947
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P29728"
FT BINDING 950
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P00973"
FT BINDING 969
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P00973"
FT SITE 155
FT /note="Interaction with dsRNA"
FT /evidence="ECO:0000269|PubMed:25775560"
FT SITE 244
FT /note="Interaction with dsRNA"
FT /evidence="ECO:0000269|PubMed:25775560"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|Ref.6, ECO:0007744|PubMed:22814378"
FT MOD_RES 365
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VARIANT 18
FT /note="R -> K (in dbSNP:rs1859330)"
FT /evidence="ECO:0000269|PubMed:11280764"
FT /id="VAR_060076"
FT VARIANT 18
FT /note="R -> M (in dbSNP:rs1859330)"
FT /id="VAR_060077"
FT VARIANT 18
FT /note="R -> T (in dbSNP:rs1859330)"
FT /id="VAR_060078"
FT VARIANT 65
FT /note="R -> W (in dbSNP:rs12819767)"
FT /id="VAR_057660"
FT VARIANT 378
FT /note="R -> K (in dbSNP:rs45519442)"
FT /id="VAR_062127"
FT VARIANT 381
FT /note="S -> R (in dbSNP:rs2285933)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_057661"
FT VARIANT 869
FT /note="R -> H (in dbSNP:rs16942374)"
FT /id="VAR_057662"
FT MUTAGEN 30
FT /note="R->A: Impaired dsRNA binding."
FT /evidence="ECO:0000269|PubMed:25775560"
FT MUTAGEN 41
FT /note="R->A: Impaired dsRNA binding."
FT /evidence="ECO:0000269|PubMed:25775560"
FT MUTAGEN 76
FT /note="E->D: No effect on catalytic activity; when
FT associated with D-145."
FT /evidence="ECO:0000269|PubMed:25775560"
FT MUTAGEN 145
FT /note="S->D: No effect on catalytic activity. No effect on
FT catalytic activity; when associated with D-76."
FT /evidence="ECO:0000269|PubMed:25775560"
FT MUTAGEN 816..818
FT /note="DAD->AAA: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:25775560"
FT CONFLICT 159
FT /note="G -> A (in Ref. 1; AAD28543)"
FT /evidence="ECO:0000305"
FT CONFLICT 249
FT /note="A -> G (in Ref. 1; AAD28543)"
FT /evidence="ECO:0000305"
FT CONFLICT 287..288
FT /note="QL -> HV (in Ref. 1; AAD28543)"
FT /evidence="ECO:0000305"
FT CONFLICT 316
FT /note="L -> H (in Ref. 1; AAD28543)"
FT /evidence="ECO:0000305"
FT CONFLICT 393
FT /note="G -> A (in Ref. 1; AAD28543)"
FT /evidence="ECO:0000305"
FT CONFLICT 503..504
FT /note="QL -> HV (in Ref. 1; AAD28543 and 2; BAB18647)"
FT /evidence="ECO:0000305"
FT CONFLICT 984
FT /note="G -> R (in Ref. 2; BAB18647)"
FT /evidence="ECO:0000305"
FT HELIX 2..5
FT /evidence="ECO:0007829|PDB:4S3N"
FT HELIX 8..10
FT /evidence="ECO:0007829|PDB:4S3N"
FT HELIX 11..18
FT /evidence="ECO:0007829|PDB:4S3N"
FT HELIX 23..41
FT /evidence="ECO:0007829|PDB:4S3N"
FT STRAND 54..60
FT /evidence="ECO:0007829|PDB:4S3N"
FT HELIX 61..65
FT /evidence="ECO:0007829|PDB:4S3N"
FT STRAND 73..81
FT /evidence="ECO:0007829|PDB:4S3N"
FT HELIX 89..92
FT /evidence="ECO:0007829|PDB:4S3N"
FT HELIX 95..108
FT /evidence="ECO:0007829|PDB:4S3N"
FT STRAND 116..119
FT /evidence="ECO:0007829|PDB:4S3N"
FT STRAND 129..139
FT /evidence="ECO:0007829|PDB:4S3N"
FT STRAND 141..149
FT /evidence="ECO:0007829|PDB:4S3N"
FT HELIX 165..172
FT /evidence="ECO:0007829|PDB:4S3N"
FT TURN 177..180
FT /evidence="ECO:0007829|PDB:4S3N"
FT HELIX 181..184
FT /evidence="ECO:0007829|PDB:4S3N"
FT HELIX 185..193
FT /evidence="ECO:0007829|PDB:4S3N"
FT HELIX 197..215
FT /evidence="ECO:0007829|PDB:4S3N"
FT HELIX 226..240
FT /evidence="ECO:0007829|PDB:4S3N"
FT HELIX 248..260
FT /evidence="ECO:0007829|PDB:4S3N"
FT HELIX 262..264
FT /evidence="ECO:0007829|PDB:4S3N"
FT STRAND 275..277
FT /evidence="ECO:0007829|PDB:4S3N"
FT HELIX 278..288
FT /evidence="ECO:0007829|PDB:4S3N"
FT STRAND 290..292
FT /evidence="ECO:0007829|PDB:4S3N"
FT STRAND 294..296
FT /evidence="ECO:0007829|PDB:4S3N"
FT STRAND 304..306
FT /evidence="ECO:0007829|PDB:4S3N"
FT HELIX 313..322
FT /evidence="ECO:0007829|PDB:4S3N"
FT HELIX 327..329
FT /evidence="ECO:0007829|PDB:4S3N"
FT TURN 332..334
FT /evidence="ECO:0007829|PDB:4S3N"
SQ SEQUENCE 1087 AA; 121170 MW; 36DAADE4574DE961 CRC64;
MDLYSTPAAA LDRFVARRLQ PRKEFVEKAR RALGALAAAL RERGGRLGAA APRVLKTVKG
GSSGRGTALK GGCDSELVIF LDCFKSYVDQ RARRAEILSE MRASLESWWQ NPVPGLRLTF
PEQSVPGALQ FRLTSVDLED WMDVSLVPAF NVLGQAGSGV KPKPQVYSTL LNSGCQGGEH
AACFTELRRN FVNIRPAKLK NLILLVKHWY HQVCLQGLWK ETLPPVYALE LLTIFAWEQG
CKKDAFSLAE GLRTVLGLIQ QHQHLCVFWT VNYGFEDPAV GQFLQRQLKR PRPVILDPAD
PTWDLGNGAA WHWDLLAQEA ASCYDHPCFL RGMGDPVQSW KGPGLPRAGC SGLGHPIQLD
PNQKTPENSK SLNAVYPRAG SKPPSCPAPG PTGAASIVPS VPGMALDLSQ IPTKELDRFI
QDHLKPSPQF QEQVKKAIDI ILRCLHENCV HKASRVSKGG SFGRGTDLRD GCDVELIIFL
NCFTDYKDQG PRRAEILDEM RAQLESWWQD QVPSLSLQFP EQNVPEALQF QLVSTALKSW
TDVSLLPAFD AVGQLSSGTK PNPQVYSRLL TSGCQEGEHK ACFAELRRNF MNIRPVKLKN
LILLVKHWYR QVAAQNKGKG PAPASLPPAY ALELLTIFAW EQGCRQDCFN MAQGFRTVLG
LVQQHQQLCV YWTVNYSTED PAMRMHLLGQ LRKPRPLVLD PADPTWNVGH GSWELLAQEA
AALGMQACFL SRDGTSVQPW DVMPALLYQT PAGDLDKFIS EFLQPNRQFL AQVNKAVDTI
CSFLKENCFR NSPIKVIKVV KGGSSAKGTA LRGRSDADLV VFLSCFSQFT EQGNKRAEII
SEIRAQLEAC QQERQFEVKF EVSKWENPRV LSFSLTSQTM LDQSVDFDVL PAFDALGQLV
SGSRPSSQVY VDLIHSYSNA GEYSTCFTEL QRDFIISRPT KLKSLIRLVK HWYQQCTKIS
KGRGSLPPQH GLELLTVYAW EQGGKDSQFN MAEGFRTVLE LVTQYRQLCI YWTINYNAKD
KTVGDFLKQQ LQKPRPIILD PADPTGNLGH NARWDLLAKE AAACTSALCC MGRNGIPIQP
WPVKAAV
