GenomeNet

Database: UniProt
Entry: O95786
LinkDB: O95786
Original site: O95786 
ID   DDX58_HUMAN             Reviewed;         925 AA.
AC   O95786; A2RU81; Q5HYE1; Q5VYT1; Q9NT04;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 2.
DT   13-NOV-2019, entry version 174.
DE   RecName: Full=Probable ATP-dependent RNA helicase DDX58;
DE            EC=3.6.4.13;
DE   AltName: Full=DEAD box protein 58;
DE   AltName: Full=RIG-I-like receptor 1;
DE            Short=RLR-1;
DE   AltName: Full=Retinoic acid-inducible gene 1 protein;
DE            Short=RIG-1;
DE   AltName: Full=Retinoic acid-inducible gene I protein;
DE            Short=RIG-I;
GN   Name=DDX58;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT GLU-580.
RA   Sun Y.-W.;
RT   "RIG-I, a human homolog gene of RNA helicase, is induced by retinoic
RT   acid during the differentiation of acute promyelocytic leukemia
RT   cell.";
RL   Thesis (1997), Shanghai Institute of Hematology, China.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT GLU-580, AND
RP   INDUCTION.
RX   PubMed=11890704; DOI=10.1006/bbrc.2002.6650;
RA   Imaizumi T., Aratani S., Nakajima T., Carlson M., Matsumiya T.,
RA   Tanji K., Ookawa K., Yoshida H., Tsuchida S., McIntyre T.M.,
RA   Prescott S.M., Zimmerman G.A., Satoh K.;
RT   "Retinoic acid-inducible gene-I is induced in endothelial cells by LPS
RT   and regulates expression of COX-2.";
RL   Biochem. Biophys. Res. Commun. 292:274-279(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164053; DOI=10.1038/nature02465;
RA   Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
RA   Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA   Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA   Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA   Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA   Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA   Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA   Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA   Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA   Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA   Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA   Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA   Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA   Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA   Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA   Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
RA   Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA   Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA   McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA   Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA   Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA   Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA   Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA   Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA   Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA   Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA   Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
RA   Rogers J., Dunham I.;
RT   "DNA sequence and analysis of human chromosome 9.";
RL   Nature 429:369-374(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-748 (ISOFORM 2),
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 528-925 (ISOFORMS 1/2), AND
RP   VARIANT CYS-7.
RC   TISSUE=Skin, and Testis;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA   Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA   Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [7]
RP   INDUCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=15181474; DOI=10.1139/o04-041;
RA   Cui X.-F., Imaizumi T., Yoshida H., Borden E.C., Satoh K.;
RT   "Retinoic acid-inducible gene-I is induced by interferon-gamma and
RT   regulates the expression of interferon-gamma stimulated gene 15 in
RT   MCF-7 cells.";
RL   Biochem. Cell Biol. 82:401-405(2004).
RN   [8]
RP   INDUCTION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX   PubMed=15219805; DOI=10.1016/j.lfs.2004.01.030;
RA   Imaizumi T., Yagihashi N., Hatakeyama M., Yamashita K., Ishikawa A.,
RA   Taima K., Yoshida H., Inoue I., Fujita T., Yagihashi S., Satoh K.;
RT   "Expression of retinoic acid-inducible gene-I in vascular smooth
RT   muscle cells stimulated with interferon-gamma.";
RL   Life Sci. 75:1171-1180(2004).
RN   [9]
RP   INDUCTION, MUTAGENESIS OF LYS-270, SUBCELLULAR LOCATION, BINDING TO
RP   DOUBLE-STRANDED RNA, AND FUNCTION.
RX   PubMed=15208624; DOI=10.1038/ni1087;
RA   Yoneyama M., Kikuchi M., Natsukawa T., Shinobu N., Imaizumi T.,
RA   Miyagishi M., Taira K., Akira S., Fujita T.;
RT   "The RNA helicase RIG-I has an essential function in double-stranded
RT   RNA-induced innate antiviral responses.";
RL   Nat. Immunol. 5:730-737(2004).
RN   [10]
RP   FUNCTION, AND INTERACTION WITH MAVS/IPS1.
RX   PubMed=16125763; DOI=10.1016/j.cell.2005.08.012;
RA   Seth R.B., Sun L., Ea C.-K., Chen Z.J.;
RT   "Identification and characterization of MAVS, a mitochondrial
RT   antiviral signaling protein that activates NF-kappaB and IRF 3.";
RL   Cell 122:669-682(2005).
RN   [11]
RP   INTERACTION WITH IKBKE AND TBK1.
RX   PubMed=16281057; DOI=10.1038/sj.emboj.7600863;
RA   Huang J., Liu T., Xu L.-G., Chen D., Zhai Z., Shu H.-B.;
RT   "SIKE is an IKK epsilon/TBK1-associated suppressor of TLR3- and virus-
RT   triggered IRF-3 activation pathways.";
RL   EMBO J. 24:4018-4028(2005).
RN   [12]
RP   INDUCTION, MUTAGENESIS OF THR-55 AND LYS-270, BINDING TO
RP   DOUBLE-STRANDED RNA, AND FUNCTION.
RX   PubMed=15708988; DOI=10.1128/jvi.79.5.2689-2699.2005;
RA   Sumpter R. Jr., Loo Y.-M., Foy E., Li K., Yoneyama M., Fujita T.,
RA   Lemon S.M., Gale M. Jr.;
RT   "Regulating intracellular antiviral defense and permissiveness to
RT   hepatitis C virus RNA replication through a cellular RNA helicase,
RT   RIG-I.";
RL   J. Virol. 79:2689-2699(2005).
RN   [13]
RP   FUNCTION, AND INTERACTION WITH MAVS/IPS1.
RX   PubMed=16153868; DOI=10.1016/j.molcel.2005.08.014;
RA   Xu L.-G., Wang Y.-Y., Han K.-J., Li L.-Y., Zhai Z., Shu H.-B.;
RT   "VISA is an adapter protein required for virus-triggered IFN-beta
RT   Signaling.";
RL   Mol. Cell 19:727-740(2005).
RN   [14]
RP   FUNCTION, AND INTERACTION WITH MAVS/IPS1.
RX   PubMed=16127453; DOI=10.1038/ni1243;
RA   Kawai T., Takahashi K., Sato S., Coban C., Kumar H., Kato H.,
RA   Ishii K.J., Takeuchi O., Akira S.;
RT   "IPS-1, an adaptor triggering RIG-I- and Mda5-mediated type I
RT   interferon induction.";
RL   Nat. Immunol. 6:981-988(2005).
RN   [15]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND ISGYLATION.
RX   PubMed=16009940; DOI=10.1073/pnas.0504754102;
RA   Zhao C., Denison C., Huibregtse J.M., Gygi S.P., Krug R.M.;
RT   "Human ISG15 conjugation targets both IFN-induced and constitutively
RT   expressed proteins functioning in diverse cellular pathways.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:10200-10205(2005).
RN   [16]
RP   INTERACTION WITH TRIM25, DOMAIN, SUBCELLULAR LOCATION, UBIQUITINATION
RP   AT LYS-172, AND MUTAGENESIS OF LYS-99; LYS-169; LYS-172; LYS-181 AND
RP   LYS-193.
RX   PubMed=17392790; DOI=10.1038/nature05732;
RA   Gack M.U., Shin Y.C., Joo C.H., Urano T., Liang C., Sun L.,
RA   Takeuchi O., Akira S., Chen Z., Inoue S., Jung J.U.;
RT   "TRIM25 RING-finger E3 ubiquitin ligase is essential for RIG-I-
RT   mediated antiviral activity.";
RL   Nature 446:916-920(2007).
RN   [17]
RP   FUNCTION, SUBUNIT, RLR CTR DOMAIN, AND INTERACTION WITH DHX58.
RX   PubMed=17190814; DOI=10.1073/pnas.0606699104;
RA   Saito T., Hirai R., Loo Y.-M., Owen D., Johnson C.L., Sinha S.C.,
RA   Akira S., Fujita T., Gale M. Jr.;
RT   "Regulation of innate antiviral defenses through a shared repressor
RT   domain in RIG-I and LGP2.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:582-587(2007).
RN   [18]
RP   UBIQUITINATION.
RX   PubMed=17460044; DOI=10.1073/pnas.0611551104;
RA   Arimoto K., Takahashi H., Hishiki T., Konishi H., Fujita T.,
RA   Shimotohno K.;
RT   "Negative regulation of the RIG-I signaling by the ubiquitin ligase
RT   RNF125.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:7500-7505(2007).
RN   [19]
RP   FUNCTION, UBIQUITINATION, AND INTERACTION WITH CYLD.
RX   PubMed=18636086; DOI=10.1038/embor.2008.136;
RA   Friedman C.S., O'Donnell M.A., Legarda-Addison D., Ng A.,
RA   Cardenas W.B., Yount J.S., Moran T.M., Basler C.F., Komuro A.,
RA   Horvath C.M., Xavier R., Ting A.T.;
RT   "The tumour suppressor CYLD is a negative regulator of RIG-I-mediated
RT   antiviral response.";
RL   EMBO Rep. 9:930-936(2008).
RN   [20]
RP   ISGYLATION.
RX   PubMed=18057259; DOI=10.1128/jvi.01650-07;
RA   Kim M.J., Hwang S.Y., Imaizumi T., Yoo J.Y.;
RT   "Negative feedback regulation of RIG-I-mediated antiviral signaling by
RT   interferon-induced ISG15 conjugation.";
RL   J. Virol. 82:1474-1483(2008).
RN   [21]
RP   INTERACTION WITH TMEM173.
RX   PubMed=18724357; DOI=10.1038/nature07317;
RA   Ishikawa H., Barber G.N.;
RT   "STING is an endoplasmic reticulum adaptor that facilitates innate
RT   immune signalling.";
RL   Nature 455:674-678(2008).
RN   [22]
RP   FUNCTION.
RX   PubMed=19631370; DOI=10.1016/j.cell.2009.06.015;
RA   Chiu Y.-H., Macmillan J.B., Chen Z.J.;
RT   "RNA polymerase III detects cytosolic DNA and induces type I
RT   interferons through the RIG-I pathway.";
RL   Cell 138:576-591(2009).
RN   [23]
RP   FUNCTION.
RX   PubMed=19576794; DOI=10.1016/j.immuni.2009.05.008;
RA   Schlee M., Roth A., Hornung V., Hagmann C.A., Wimmenauer V.,
RA   Barchet W., Coch C., Janke M., Mihailovic A., Wardle G., Juranek S.,
RA   Kato H., Kawai T., Poeck H., Fitzgerald K.A., Takeuchi O., Akira S.,
RA   Tuschl T., Latz E., Ludwig J., Hartmann G.;
RT   "Recognition of 5' triphosphate by RIG-I helicase requires short blunt
RT   double-stranded RNA as contained in panhandle of negative-strand
RT   virus.";
RL   Immunity 31:25-34(2009).
RN   [24]
RP   UBIQUITINATION, AND INTERACTION WITH RNF135.
RX   PubMed=19017631; DOI=10.1074/jbc.m804259200;
RA   Oshiumi H., Matsumoto M., Hatakeyama S., Seya T.;
RT   "Riplet/RNF135, a RING finger protein, ubiquitinates RIG-I to promote
RT   interferon-beta induction during the early phase of viral infection.";
RL   J. Biol. Chem. 284:807-817(2009).
RN   [25]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=19122199; DOI=10.1074/jbc.m807547200;
RA   Mukherjee A., Morosky S.A., Shen L., Weber C.R., Turner J.R.,
RA   Kim K.S., Wang T., Coyne C.B.;
RT   "Retinoic acid-induced gene-1 (RIG-I) associates with the actin
RT   cytoskeleton via caspase activation and recruitment domain-dependent
RT   interactions.";
RL   J. Biol. Chem. 284:6486-6494(2009).
RN   [26]
RP   FUNCTION.
RX   PubMed=19211564; DOI=10.1074/jbc.m807365200;
RA   Bamming D., Horvath C.M.;
RT   "Regulation of signal transduction by enzymatically inactive antiviral
RT   RNA helicase proteins MDA5, RIG-I, and LGP2.";
RL   J. Biol. Chem. 284:9700-9712(2009).
RN   [27]
RP   INTERACTION WITH SRC.
RX   PubMed=19419966; DOI=10.1074/jbc.m808233200;
RA   Johnsen I.B., Nguyen T.T., Bergstroem B., Fitzgerald K.A.,
RA   Anthonsen M.W.;
RT   "The tyrosine kinase c-Src enhances RIG-I (retinoic acid-inducible
RT   gene I)-elicited antiviral signaling.";
RL   J. Biol. Chem. 284:19122-19131(2009).
RN   [28]
RP   INTERACTION WITH HRSV PROTEIN NS2 (MICROBIAL INFECTION).
RX   PubMed=19193793; DOI=10.1128/jvi.02434-08;
RA   Ling Z., Tran K.C., Teng M.N.;
RT   "Human respiratory syncytial virus nonstructural protein NS2
RT   antagonizes the activation of beta interferon transcription by
RT   interacting with RIG-I.";
RL   J. Virol. 83:3734-3742(2009).
RN   [29]
RP   FUNCTION.
RX   PubMed=19609254; DOI=10.1038/ni.1779;
RA   Ablasser A., Bauernfeind F., Hartmann G., Latz E., Fitzgerald K.A.,
RA   Hornung V.;
RT   "RIG-I-dependent sensing of poly(dA:dT) through the induction of an
RT   RNA polymerase III-transcribed RNA intermediate.";
RL   Nat. Immunol. 10:1065-1072(2009).
RN   [30]
RP   UBIQUITINATION AT LYS-154; LYS-164 AND LYS-172, INTERACTION WITH
RP   RNF135, AND MUTAGENESIS OF LYS-154; LYS-164 AND LYS-172.
RX   PubMed=19484123; DOI=10.1371/journal.pone.0005760;
RA   Gao D., Yang Y.K., Wang R.P., Zhou X., Diao F.C., Li M.D., Zhai Z.H.,
RA   Jiang Z.F., Chen D.Y.;
RT   "REUL is a novel E3 ubiquitin ligase and stimulator of retinoic-acid-
RT   inducible gene-I.";
RL   PLoS ONE 4:E5760-E5760(2009).
RN   [31]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-858, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA   Walther T.C., Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [32]
RP   INTERACTION WITH NLRC5.
RX   PubMed=20434986; DOI=10.1016/j.cell.2010.03.040;
RA   Cui J., Zhu L., Xia X., Wang H.Y., Legras X., Hong J., Ji J., Shen P.,
RA   Zheng S., Chen Z.J., Wang R.F.;
RT   "NLRC5 negatively regulates the NF-kappaB and type I interferon
RT   signaling pathways.";
RL   Cell 141:483-496(2010).
RN   [33]
RP   UBIQUITINATION, AND DEUBIQUITINATION BY USP17L2.
RX   PubMed=20368735; DOI=10.1038/cr.2010.41;
RA   Chen R., Zhang L., Zhong B., Tan B., Liu Y., Shu H.B.;
RT   "The ubiquitin-specific protease 17 is involved in virus-triggered
RT   type I IFN signaling.";
RL   Cell Res. 20:802-811(2010).
RN   [34]
RP   REVIEW ON FUNCTION.
RX   PubMed=21175414; DOI=10.1615/critrevimmunol.v30.i6.10;
RA   Matsumiya T., Stafforini D.M.;
RT   "Function and regulation of retinoic acid-inducible gene-I.";
RL   Crit. Rev. Immunol. 30:489-513(2010).
RN   [35]
RP   INTERACTION WITH NEW WORLD ARENAVIRUSES PROTEIN Z (MICROBIAL
RP   INFECTION).
RX   PubMed=20007272; DOI=10.1128/jvi.01362-09;
RA   Fan L., Briese T., Lipkin W.I.;
RT   "Z proteins of New World arenaviruses bind RIG-I and interfere with
RT   type I interferon induction.";
RL   J. Virol. 84:1785-1791(2010).
RN   [36]
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.,
RA   Buerckstuemmer T., 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   [37]
RP   REVIEW ON FUNCTION.
RX   PubMed=21616437; DOI=10.1016/j.immuni.2011.05.003;
RA   Loo Y.M., Gale M. Jr.;
RT   "Immune signaling by RIG-I-like receptors.";
RL   Immunity 34:680-692(2011).
RN   [38]
RP   REVIEW ON FUNCTION.
RX   PubMed=21884169; DOI=10.1111/j.1600-065x.2011.01052.x;
RA   Kato H., Takahasi K., Fujita T.;
RT   "RIG-I-like receptors: cytoplasmic sensors for non-self RNA.";
RL   Immunol. Rev. 243:91-98(2011).
RN   [39]
RP   FUNCTION.
RX   PubMed=21742966; DOI=10.4049/jimmunol.1100361;
RA   Jiang M., Osterlund P., Sarin L.P., Poranen M.M., Bamford D.H.,
RA   Guo D., Julkunen I.;
RT   "Innate immune responses in human monocyte-derived dendritic cells are
RT   highly dependent on the size and the 5' phosphorylation of RNA
RT   molecules.";
RL   J. Immunol. 187:1713-1721(2011).
RN   [40]
RP   INTERACTION WITH IFIT3.
RX   PubMed=21813773; DOI=10.4049/jimmunol.1100963;
RA   Liu X.Y., Chen W., Wei B., Shan Y.F., Wang C.;
RT   "IFN-induced TPR protein IFIT3 potentiates antiviral signaling by
RT   bridging MAVS and TBK1.";
RL   J. Immunol. 187:2559-2568(2011).
RN   [41]
RP   REVIEW ON FUNCTION.
RX   PubMed=20950133; DOI=10.1089/jir.2010.0057;
RA   Onoguchi K., Yoneyama M., Fujita T.;
RT   "Retinoic acid-inducible gene-I-like receptors.";
RL   J. Interferon Cytokine Res. 31:27-31(2011).
RN   [42]
RP   PHOSPHORYLATION AT THR-770; SER-854 AND SER-855.
RX   PubMed=21068236; DOI=10.1128/jvi.01734-10;
RA   Sun Z., Ren H., Liu Y., Teeling J.L., Gu J.;
RT   "Phosphorylation of RIG-I by casein kinase II inhibits its antiviral
RT   response.";
RL   J. Virol. 85:1036-1047(2011).
RN   [43]
RP   INTERACTION WITH DDX60.
RX   PubMed=21791617; DOI=10.1128/mcb.01368-10;
RA   Miyashita M., Oshiumi H., Matsumoto M., Seya T.;
RT   "DDX60, a DEXD/H box helicase, is a novel antiviral factor promoting
RT   RIG-I-like receptor-mediated signaling.";
RL   Mol. Cell. Biol. 31:3802-3819(2011).
RN   [44]
RP   INTERACTION WITH ZC3HAV1, AND SUBCELLULAR LOCATION.
RX   PubMed=21102435; DOI=10.1038/ni.1963;
RA   Hayakawa S., Shiratori S., Yamato H., Kameyama T., Kitatsuji C.,
RA   Kashigi F., Goto S., Kameoka S., Fujikura D., Yamada T., Mizutani T.,
RA   Kazumata M., Sato M., Tanaka J., Asaka M., Ohba Y., Miyazaki T.,
RA   Imamura M., Takaoka A.;
RT   "ZAPS is a potent stimulator of signaling mediated by the RNA helicase
RT   RIG-I during antiviral responses.";
RL   Nat. Immunol. 12:37-44(2011).
RN   [45]
RP   INTERACTION WITH ROTAVIRUS PROTEIN NSP1 (MICROBIAL INFECTION).
RX   PubMed=22152002; DOI=10.1186/1743-422x-8-526;
RA   Qin L., Ren L., Zhou Z., Lei X., Chen L., Xue Q., Liu X., Wang J.,
RA   Hung T.;
RT   "Rotavirus nonstructural protein 1 antagonizes innate immune response
RT   by interacting with retinoic acid inducible gene I.";
RL   Virol. J. 8:526-526(2011).
RN   [46]
RP   INTERACTION WITH HERPES SIMPLEX VIRUS 1 PROTEIN US11 (MICROBIAL
RP   INFECTION).
RX   PubMed=22301138; DOI=10.1128/jvi.06713-11;
RA   Xing J., Wang S., Lin R., Mossman K.L., Zheng C.;
RT   "Herpes simplex virus 1 tegument protein US11 downmodulates the RLR
RT   signaling pathway via direct interaction with RIG-I and MDA-5.";
RL   J. Virol. 86:3528-3540(2012).
RN   [47]
RP   SUMOYLATION BY MUL1.
RX   PubMed=23399697; DOI=10.1038/icb.2013.7;
RA   Jenkins K., Khoo J.J., Sadler A., Piganis R., Wang D., Borg N.A.,
RA   Hjerrild K., Gould J., Thomas B.J., Nagley P., Hertzog P.J.,
RA   Mansell A.;
RT   "Mitochondrially localised MUL1 is a novel modulator of antiviral
RT   signaling.";
RL   Immunol. Cell Biol. 91:321-330(2013).
RN   [48]
RP   INTERACTION WITH SEC14L1.
RX   PubMed=23843640; DOI=10.1128/jvi.01073-13;
RA   Li M.T., Di W., Xu H., Yang Y.K., Chen H.W., Zhang F.X., Zhai Z.H.,
RA   Chen D.Y.;
RT   "Negative regulation of RIG-I-mediated innate antiviral signaling by
RT   SEC14L1.";
RL   J. Virol. 87:10037-10046(2013).
RN   [49]
RP   UBIQUITINATION AT LYS-154; LYS-164 AND LYS-172 BY TRIM4.
RX   PubMed=24755855; DOI=10.1093/jmcb/mju005;
RA   Yan J., Li Q., Mao A.P., Hu M.M., Shu H.B.;
RT   "TRIM4 modulates type I interferon induction and cellular antiviral
RT   response by targeting RIG-I for K63-linked ubiquitination.";
RL   J. Mol. Cell Biol. 6:154-163(2014).
RN   [50]
RP   PROTEOLYTIC CLEAVAGE (MICROBIAL INFECTION).
RX   PubMed=24390337; DOI=10.1128/jvi.02712-13;
RA   Feng Q., Langereis M.A., Lork M., Nguyen M., Hato S.V., Lanke K.,
RA   Emdad L., Bhoopathi P., Fisher P.B., Lloyd R.E., van Kuppeveld F.J.;
RT   "Enterovirus 2Apro targets MDA5 and MAVS in infected cells.";
RL   J. Virol. 88:3369-3378(2014).
RN   [51]
RP   UBIQUITINATION AT LYS-181 BY RNF125, INTERACTION WITH VCP, AND
RP   MUTAGENESIS OF LYS-181.
RX   PubMed=26471729; DOI=10.15252/embj.201591888;
RA   Hao Q., Jiao S., Shi Z., Li C., Meng X., Zhang Z., Wang Y., Song X.,
RA   Wang W., Zhang R., Zhao Y., Wong C.C., Zhou Z.;
RT   "A non-canonical role of the p97 complex in RIG-I antiviral
RT   signaling.";
RL   EMBO J. 34:2903-2920(2015).
RN   [52]
RP   INTERACTION WITH NOP53.
RX   PubMed=27824081; DOI=10.1038/srep36226;
RA   Wang P., Meng W., Han S.C., Li C.C., Wang X.J., Wang X.J.;
RT   "The nucleolar protein GLTSCR2 is required for efficient viral
RT   replication.";
RL   Sci. Rep. 6:36226-36226(2016).
RN   [53]
RP   INTERACTION WITH HERPES SIMPLEX VIRUS 1 PROTEIN UL37 (MICROBIAL
RP   INFECTION), DEAMIDATION AT ASN-495 AND ASN-549, AND MUTAGENESIS OF
RP   ASN-495 AND ASN-549.
RX   PubMed=27866900; DOI=10.1016/j.chom.2016.10.011;
RA   Zhao J., Zeng Y., Xu S., Chen J., Shen G., Yu C., Knipe D., Yuan W.,
RA   Peng J., Xu W., Zhang C., Xia Z., Feng P.;
RT   "A Viral Deamidase Targets the Helicase Domain of RIG-I to Block RNA-
RT   Induced Activation.";
RL   Cell Host Microbe 20:770-784(2016).
RN   [54]
RP   INVOLVEMENT IN SGMRT2, VARIANTS SGMRT2 PHE-268 AND ALA-373, AND
RP   CHARACTERIZATION OF VARIANTS SGMRT2 PHE-268 AND ALA-373.
RX   PubMed=25620203; DOI=10.1016/j.ajhg.2014.11.019;
RA   Jang M.A., Kim E.K., Now H., Nguyen N.T., Kim W.J., Yoo J.Y., Lee J.,
RA   Jeong Y.M., Kim C.H., Kim O.H., Sohn S., Nam S.H., Hong Y., Lee Y.S.,
RA   Chang S.A., Jang S.Y., Kim J.W., Lee M.S., Lim S.Y., Sung K.S.,
RA   Park K.T., Kim B.J., Lee J.H., Kim D.K., Kee C., Ki C.S.;
RT   "Mutations in DDX58, which encodes RIG-I, cause atypical Singleton-
RT   Merten syndrome.";
RL   Am. J. Hum. Genet. 96:266-274(2015).
RN   [55]
RP   INTERACTION WITH RNF123.
RX   PubMed=27312109; DOI=10.15252/embr.201541703;
RA   Wang S., Yang Y.K., Chen T., Zhang H., Yang W.W., Song S.S.,
RA   Zhai Z.H., Chen D.Y.;
RT   "RNF123 has an E3 ligase-independent function in RIG-I-like receptor-
RT   mediated antiviral signaling.";
RL   EMBO Rep. 17:1155-1168(2016).
RN   [56]
RP   INTERACTION WITH LRRC25.
RX   PubMed=29288164; DOI=10.15252/embj.201796781;
RA   Du Y., Duan T., Feng Y., Liu Q., Lin M., Cui J., Wang R.F.;
RT   "LRRC25 inhibits type I IFN signaling by targeting ISG15-associated
RT   RIG-I for autophagic degradation.";
RL   EMBO J. 37:351-366(2018).
RN   [57]
RP   INTERACTION WITH ZCCHC3, AND UBIQUITINATION.
RX   PubMed=30193849; DOI=10.1016/j.immuni.2018.08.014;
RA   Lian H., Zang R., Wei J., Ye W., Hu M.M., Chen Y.D., Zhang X.N.,
RA   Guo Y., Lei C.Q., Yang Q., Luo W.W., Li S., Shu H.B.;
RT   "The zinc-finger protein ZCCHC3 binds RNA and facilitates viral RNA
RT   sensing and activation of the RIG-I-like receptors.";
RL   Immunity 49:438-448(2018).
RN   [58]
RP   X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 802-925 IN COMPLEX WITH ZINC
RP   IONS.
RX   PubMed=18243112; DOI=10.1016/j.molcel.2007.10.032;
RA   Cui S., Eisenaecher K., Kirchhofer A., Brzozka K., Lammens A.,
RA   Lammens K., Fujita T., Conzelmann K.-K., Krug A., Hopfner K.-P.;
RT   "The C-terminal regulatory domain is the RNA 5'-triphosphate sensor of
RT   RIG-I.";
RL   Mol. Cell 29:169-179(2008).
RN   [59]
RP   STRUCTURE BY NMR OF 792-925.
RX   PubMed=18242112; DOI=10.1016/j.molcel.2007.11.028;
RA   Takahasi K., Yoneyama M., Nishihori T., Hirai R., Kumeta H.,
RA   Narita R., Gale M. Jr., Inagaki F., Fujita T.;
RT   "Nonself RNA-sensing mechanism of RIG-I helicase and activation of
RT   antiviral immune responses.";
RL   Mol. Cell 29:428-440(2008).
RN   [60]
RP   X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) OF 1-201 IN COMPLEX WITH MAVS,
RP   AND SUBUNIT.
RX   PubMed=25018021; DOI=10.1016/j.molcel.2014.06.010;
RA   Wu B., Peisley A., Tetrault D., Li Z., Egelman E.H., Magor K.E.,
RA   Walz T., Penczek P.A., Hur S.;
RT   "Molecular imprinting as a signal-activation mechanism of the viral
RT   RNA sensor RIG-I.";
RL   Mol. Cell 55:511-523(2014).
CC   -!- FUNCTION: Innate immune receptor which acts as a cytoplasmic
CC       sensor of viral nucleic acids and plays a major role in sensing
CC       viral infection and in the activation of a cascade of antiviral
CC       responses including the induction of type I interferons and
CC       proinflammatory cytokines. Its ligands include: 5'-
CC       triphosphorylated ssRNA and dsRNA and short dsRNA (<1 kb in
CC       length). In addition to the 5'-triphosphate moiety, blunt-end base
CC       pairing at the 5'-end of the RNA is very essential. Overhangs at
CC       the non-triphosphorylated end of the dsRNA RNA have no major
CC       impact on its activity. A 3'overhang at the 5'triphosphate end
CC       decreases and any 5'overhang at the 5' triphosphate end abolishes
CC       its activity. Upon ligand binding it associates with mitochondria
CC       antiviral signaling protein (MAVS/IPS1) which activates the IKK-
CC       related kinases: TBK1 and IKBKE which phosphorylate interferon
CC       regulatory factors: IRF3 and IRF7 which in turn activate
CC       transcription of antiviral immunological genes, including
CC       interferons (IFNs); IFN-alpha and IFN-beta. Detects both positive
CC       and negative strand RNA viruses including members of the families
CC       Paramyxoviridae: Human respiratory syncytial virus and measles
CC       virus (MeV), Rhabdoviridae: vesicular stomatitis virus (VSV),
CC       Orthomyxoviridae: influenza A and B virus, Flaviviridae: Japanese
CC       encephalitis virus (JEV), hepatitis C virus (HCV), dengue virus
CC       (DENV) and west Nile virus (WNV). It also detects rotavirus and
CC       reovirus. Also involved in antiviral signaling in response to
CC       viruses containing a dsDNA genome such as Epstein-Barr virus
CC       (EBV). Detects dsRNA produced from non-self dsDNA by RNA
CC       polymerase III, such as Epstein-Barr virus-encoded RNAs (EBERs).
CC       May play important roles in granulocyte production and
CC       differentiation, bacterial phagocytosis and in the regulation of
CC       cell migration. {ECO:0000269|PubMed:15208624,
CC       ECO:0000269|PubMed:15708988, ECO:0000269|PubMed:16125763,
CC       ECO:0000269|PubMed:16127453, ECO:0000269|PubMed:16153868,
CC       ECO:0000269|PubMed:17190814, ECO:0000269|PubMed:18636086,
CC       ECO:0000269|PubMed:19122199, ECO:0000269|PubMed:19211564,
CC       ECO:0000269|PubMed:19576794, ECO:0000269|PubMed:19609254,
CC       ECO:0000269|PubMed:19631370, ECO:0000269|PubMed:21742966}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC   -!- SUBUNIT: Monomer; maintained as a monomer in an autoinhibited
CC       state. Upon viral dsRNA binding and conformation shift,
CC       homomultimerizes and interacts (via tandem CARD domain) with
CC       MAVS/IPS1 promoting its filamentation. Interacts with DHX58/LGP2,
CC       IKBKE, TBK1 and TMEM173/STING. Interacts (via CARD domain) with
CC       TRIM25 (via SPRY domain). Interacts with RNF135. Interacts with
CC       CYLD. Interacts with NLRC5; blocks the interaction of MAVS/IPS1 to
CC       DDX58. Interacts with SRC. Interacts with DDX60. Interacts with
CC       isoform 2 of ZC3HAV1 (via zinc-fingers) in an RNA-dependent
CC       manner. Interacts (via tandem CARD domain) with SEC14L1; the
CC       interaction is direct and impairs the interaction of DDX58 with
CC       MAVS/IPS1. Interacts with VCP/p97; interaction is direct and leads
CC       to recruit RNF125 and subsequent ubiquitination and degradation
CC       (PubMed:26471729). Interacts with NOP53; may regulate DDX58
CC       through USP15-mediated 'Lys-63'-linked deubiquitination
CC       (PubMed:27824081). Interacts with LRRC25 (PubMed:29288164).
CC       Interacts with ZCCHC3; leading to activate DDX58/RIG-I
CC       (PubMed:30193849). Interacts with RNF123 (PubMed:27312109).
CC       {ECO:0000269|PubMed:16125763, ECO:0000269|PubMed:16127453,
CC       ECO:0000269|PubMed:16153868, ECO:0000269|PubMed:16281057,
CC       ECO:0000269|PubMed:17190814, ECO:0000269|PubMed:17392790,
CC       ECO:0000269|PubMed:18243112, ECO:0000269|PubMed:18636086,
CC       ECO:0000269|PubMed:18724357, ECO:0000269|PubMed:19017631,
CC       ECO:0000269|PubMed:19419966, ECO:0000269|PubMed:19484123,
CC       ECO:0000269|PubMed:20434986, ECO:0000269|PubMed:21102435,
CC       ECO:0000269|PubMed:21791617, ECO:0000269|PubMed:21813773,
CC       ECO:0000269|PubMed:23843640, ECO:0000269|PubMed:25018021,
CC       ECO:0000269|PubMed:26471729, ECO:0000269|PubMed:27312109,
CC       ECO:0000269|PubMed:27824081, ECO:0000269|PubMed:29288164,
CC       ECO:0000269|PubMed:30193849}.
CC   -!- SUBUNIT: (Microbial infection) Interacts with protein Z of
CC       Guanarito virus, Machupo virus, Junin arenavirus and Sabia virus.
CC       This interaction disrupts its interaction with MAVS/IPS1, impeding
CC       downstream IRF3 and NF-kappa-B activation and resulting in
CC       decreased IFN-beta induction (PubMed:20007272).
CC       {ECO:0000269|PubMed:20007272}.
CC   -!- SUBUNIT: (Microbial infection) Interacts (via CARD domain) with
CC       Human respiratory syncytial virus A non-structural protein 2 (NS2)
CC       and this interaction disrupts its interaction with MAVS/IPS1,
CC       impeding downstream IRF3 activation (PubMed:19193793).
CC       {ECO:0000269|PubMed:19193793}.
CC   -!- SUBUNIT: (Microbial infection) Interacts with Rotavirus A non-
CC       structural protein 1 (NSP1) and this interaction induces down-
CC       regulation of DDX58/RIG-I (PubMed:22152002).
CC       {ECO:0000269|PubMed:22152002}.
CC   -!- SUBUNIT: (Microbial infection) Interacts with herpes simplex virus
CC       1 protein US11; this interaction prevents the interaction of
CC       MAVS/IPS1 to DDX58 (PubMed:22301138).
CC       {ECO:0000269|PubMed:22301138}.
CC   -!- SUBUNIT: (Microbial infection) Interacts with herpes simplex virus
CC       1 protein UL37; this interaction daeminates DDX58 and inhibits its
CC       activation. {ECO:0000269|PubMed:27866900}.
CC   -!- INTERACTION:
CC       Self; NbExp=2; IntAct=EBI-995350, EBI-995350;
CC       F1BA49:- (xeno); NbExp=5; IntAct=EBI-995350, EBI-9687469;
CC       P04543:1B (xeno); NbExp=2; IntAct=EBI-995350, EBI-3648048;
CC       Q9H1Y0:ATG5; NbExp=4; IntAct=EBI-15577823, EBI-1047414;
CC       Q920D5:Casp12 (xeno); NbExp=4; IntAct=EBI-995350, EBI-1374296;
CC       Q9NQC7:CYLD; NbExp=2; IntAct=EBI-995350, EBI-2117940;
CC       O00571:DDX3X; NbExp=2; IntAct=EBI-995350, EBI-353779;
CC       Q7Z434:MAVS; NbExp=13; IntAct=EBI-995350, EBI-995373;
CC       Q7Z434-1:MAVS; NbExp=8; IntAct=EBI-15577823, EBI-15577799;
CC       Q9NZM5:NOP53; NbExp=2; IntAct=EBI-995350, EBI-720156;
CC       Q99AU3:NS (xeno); NbExp=2; IntAct=EBI-15577823, EBI-6150155;
CC       P21699:NSS (xeno); NbExp=3; IntAct=EBI-995350, EBI-6693910;
CC       O75569:PRKRA; NbExp=2; IntAct=EBI-995350, EBI-713955;
CC       Q96EQ8:RNF125; NbExp=5; IntAct=EBI-15577823, EBI-2339208;
CC       P42224:STAT1; NbExp=4; IntAct=EBI-995350, EBI-1057697;
CC       Q86WV6:TMEM173; NbExp=2; IntAct=EBI-15577823, EBI-2800345;
CC       Q14258:TRIM25; NbExp=4; IntAct=EBI-995350, EBI-2341129;
CC       P04487:US11 (xeno); NbExp=4; IntAct=EBI-995350, EBI-6150681;
CC       Q96S55:WRNIP1; NbExp=2; IntAct=EBI-995350, EBI-2513471;
CC       Q6IUF9:Z (xeno); NbExp=3; IntAct=EBI-995350, EBI-3647473;
CC       Q6IVU5:Z (xeno); NbExp=3; IntAct=EBI-995350, EBI-3647294;
CC       Q6UY62:Z (xeno); NbExp=2; IntAct=EBI-995350, EBI-3647496;
CC       Q6UY71:Z (xeno); NbExp=3; IntAct=EBI-995350, EBI-3647448;
CC       Q7Z2W4:ZC3HAV1; NbExp=3; IntAct=EBI-995350, EBI-922540;
CC       Q7Z2W4-2:ZC3HAV1; NbExp=4; IntAct=EBI-995350, EBI-922559;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Cell projection, ruffle membrane.
CC       Cytoplasm, cytoskeleton. Cell junction, tight junction.
CC       Note=Colocalized with TRIM25 at cytoplasmic perinuclear bodies.
CC       Associated with the actin cytoskeleton at membrane ruffles.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=O95786-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O95786-2; Sequence=VSP_016054;
CC         Note=No experimental confirmation available.;
CC   -!- TISSUE SPECIFICITY: Present in vascular smooth cells (at protein
CC       level). {ECO:0000269|PubMed:15219805}.
CC   -!- INDUCTION: By bacterial lipopolysaccharides (LPS) in endothelial
CC       cells. By interferon (IFN). {ECO:0000269|PubMed:11890704,
CC       ECO:0000269|PubMed:15181474, ECO:0000269|PubMed:15208624,
CC       ECO:0000269|PubMed:15219805, ECO:0000269|PubMed:15708988}.
CC   -!- DOMAIN: The RLR CTR domain controls homomultimerization and
CC       interaction with MAVS/IPS1. In the absence of viral infection, the
CC       protein is maintained as a monomer in an autoinhibited state with
CC       the CARD domains masked through intramolecular interactions
CC       mediated by the RLR CTR domain. Upon binding to viral RNA in the
CC       presence of ATP, the RLR CTR domain induces a conformational
CC       change exposing the CARD domain and promotes dimerization and CARD
CC       interactions with the adapter protein MAVS/IPS1 leading to the
CC       induction of downstream signaling.
CC   -!- DOMAIN: The helicase domain is responsible for dsRNA recognition.
CC   -!- DOMAIN: The 2 CARD domains are responsible for interaction with
CC       and signaling through MAVS/IPS1 and for association with the actin
CC       cytoskeleton.
CC   -!- DOMAIN: The second CARD domain is the primary site for 'Lys-63'-
CC       linked ubiquitination. {ECO:0000269|PubMed:17392790}.
CC   -!- PTM: (Microbial infection) Deamidated on 'Asn-495' and 'Asn-549'
CC       by herpes simplex virus 1 protein UL37. These modifications
CC       eliminate DDX58 detection of viral RNA and restriction of viral
CC       replication. {ECO:0000269|PubMed:27866900}.
CC   -!- PTM: (Microbial infection) Cleaved by the protease 3C of
CC       coxsackievirus B3, poliovirus and enterovirus 71 allowing the
CC       virus to disrupt the host type I interferon production.
CC       {ECO:0000269|PubMed:24390337}.
CC   -!- PTM: Phosphorylated in resting cells and dephosphorylated in RNA
CC       virus-infected cells. Phosphorylation at Thr-770, Ser-854 and Ser-
CC       855 results in inhibition of its activity while dephosphorylation
CC       at these sites results in its activation.
CC       {ECO:0000269|PubMed:21068236}.
CC   -!- PTM: ISGylated. Conjugated to ubiquitin-like protein ISG15 upon
CC       IFN-beta stimulation. ISGylation negatively regulates its function
CC       in antiviral signaling response. {ECO:0000269|PubMed:16009940,
CC       ECO:0000269|PubMed:18057259, ECO:0000269|PubMed:20368735}.
CC   -!- PTM: Sumoylated, probably by MUL1; inhibiting its
CC       polyubiquitination. {ECO:0000269|PubMed:20368735,
CC       ECO:0000269|PubMed:23399697}.
CC   -!- PTM: Ubiquitinated. Undergoes 'Lys-48'- and 'Lys-63'-linked
CC       ubiquitination. Lys-172 is the critical site for TRIM25-mediated
CC       ubiquitination, for MAVS/IPS1 binding and to induce anti-viral
CC       signal transduction (PubMed:17392790, PubMed:30193849). Lys-154,
CC       Lys-164 and Lys-172 are critical sites for RNF135-mediated and
CC       TRIM4-mediated ubiquitination (PubMed:19017631, PubMed:19484123,
CC       PubMed:24755855). Deubiquitinated by CYLD, a protease that
CC       selectively cleaves 'Lys-63'-linked ubiquitin chains
CC       (PubMed:18636086). Also probably deubiquitinated by USP17L2/USP17
CC       that cleaves 'Lys-48'-and 'Lys-63'-linked ubiquitin chains and
CC       positively regulates the receptor (PubMed:20368735). Ubiquitinated
CC       at Lys-181 by RNF125, leading to its degradation: ubiquitination
CC       takes place upon viral infection and is enhanced 'Lys-63'-linked
CC       ubiquitination of the CARD domains, which promote interaction with
CC       VCP/p97 and subsequent recruitment of RNF125 (PubMed:17460044,
CC       PubMed:26471729). Ubiquitinated at Lys-812 by CBL, leading to its
CC       degradation: ubiquitination takes place upon viral infection and
CC       involves 'Lys-48'-linked ubiquitination (By similarity).
CC       {ECO:0000250|UniProtKB:Q6Q899, ECO:0000269|PubMed:17392790,
CC       ECO:0000269|PubMed:17460044, ECO:0000269|PubMed:18636086,
CC       ECO:0000269|PubMed:19017631, ECO:0000269|PubMed:19484123,
CC       ECO:0000269|PubMed:20368735, ECO:0000269|PubMed:24755855,
CC       ECO:0000269|PubMed:26471729, ECO:0000269|PubMed:30193849}.
CC   -!- DISEASE: Singleton-Merten syndrome 2 (SGMRT2) [MIM:616298]: A form
CC       of Singleton-Merten syndrome, an autosomal dominant disorder
CC       characterized by marked aortic calcification, dental anomalies,
CC       osteopenia, acro-osteolysis, and to a lesser extent glaucoma,
CC       psoriasis, muscle weakness, and joint laxity. Additional clinical
CC       manifestations include particular facial characteristics and
CC       abnormal joint and muscle ligaments. SGMRT2 is an atypical form
CC       characterized by variable expression of glaucoma, aortic
CC       calcification, and skeletal abnormalities, without dental
CC       anomalies. {ECO:0000269|PubMed:25620203}. Note=The disease is
CC       caused by mutations affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the helicase family. RLR subfamily.
CC       {ECO:0000305}.
DR   EMBL; AF038963; AAD19826.1; -; mRNA.
DR   EMBL; AL161783; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL353671; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471071; EAW58548.1; -; Genomic_DNA.
DR   EMBL; BC132786; AAI32787.1; -; mRNA.
DR   EMBL; BC136610; AAI36611.1; -; mRNA.
DR   EMBL; BX647917; CAI46068.1; -; mRNA.
DR   EMBL; AL137608; CAB70840.1; -; mRNA.
DR   CCDS; CCDS6526.1; -. [O95786-1]
DR   PIR; T46312; T46312.
DR   RefSeq; NP_055129.2; NM_014314.3. [O95786-1]
DR   PDB; 2LWD; NMR; -; A=95-190.
DR   PDB; 2LWE; NMR; -; A=95-190.
DR   PDB; 2QFB; X-ray; 3.00 A; A/B/C/D/E/F/G/H/I/J=802-925.
DR   PDB; 2QFD; X-ray; 2.70 A; A/B/C/D/E/F/G/H/I/J=802-925.
DR   PDB; 2RMJ; NMR; -; A=792-925.
DR   PDB; 2YKG; X-ray; 2.50 A; A=230-925.
DR   PDB; 3LRN; X-ray; 2.60 A; A/B=803-923.
DR   PDB; 3LRR; X-ray; 2.15 A; A/B=803-923.
DR   PDB; 3NCU; X-ray; 2.55 A; A/B=792-925.
DR   PDB; 3OG8; X-ray; 2.40 A; A/B=802-925.
DR   PDB; 3ZD6; X-ray; 2.80 A; A=230-925.
DR   PDB; 3ZD7; X-ray; 2.50 A; A=230-925.
DR   PDB; 4AY2; X-ray; 2.80 A; A=239-925.
DR   PDB; 4BPB; X-ray; 2.58 A; A=230-925.
DR   PDB; 4NQK; X-ray; 3.70 A; A/B/C/D=1-200.
DR   PDB; 4ON9; X-ray; 2.71 A; A/B=230-793.
DR   PDB; 4P4H; X-ray; 3.40 A; A/B/C/D/E/F/G/H=1-201.
DR   PDB; 5E3H; X-ray; 2.70 A; A=232-925.
DR   PDB; 5F98; X-ray; 3.28 A; A/C/E/G/I/K=232-925.
DR   PDB; 5F9F; X-ray; 2.60 A; A/C/E/G/I/K=232-925.
DR   PDB; 5F9H; X-ray; 3.10 A; A/C/E/G/I/K=232-925.
DR   PDB; 6GPG; X-ray; 2.89 A; A=232-925.
DR   PDBsum; 2LWD; -.
DR   PDBsum; 2LWE; -.
DR   PDBsum; 2QFB; -.
DR   PDBsum; 2QFD; -.
DR   PDBsum; 2RMJ; -.
DR   PDBsum; 2YKG; -.
DR   PDBsum; 3LRN; -.
DR   PDBsum; 3LRR; -.
DR   PDBsum; 3NCU; -.
DR   PDBsum; 3OG8; -.
DR   PDBsum; 3ZD6; -.
DR   PDBsum; 3ZD7; -.
DR   PDBsum; 4AY2; -.
DR   PDBsum; 4BPB; -.
DR   PDBsum; 4NQK; -.
DR   PDBsum; 4ON9; -.
DR   PDBsum; 4P4H; -.
DR   PDBsum; 5E3H; -.
DR   PDBsum; 5F98; -.
DR   PDBsum; 5F9F; -.
DR   PDBsum; 5F9H; -.
DR   PDBsum; 6GPG; -.
DR   SMR; O95786; -.
DR   BioGrid; 117121; 58.
DR   CORUM; O95786; -.
DR   DIP; DIP-35444N; -.
DR   IntAct; O95786; 32.
DR   MINT; O95786; -.
DR   STRING; 9606.ENSP00000369213; -.
DR   iPTMnet; O95786; -.
DR   PhosphoSitePlus; O95786; -.
DR   BioMuta; DDX58; -.
DR   EPD; O95786; -.
DR   jPOST; O95786; -.
DR   MassIVE; O95786; -.
DR   MaxQB; O95786; -.
DR   PaxDb; O95786; -.
DR   PeptideAtlas; O95786; -.
DR   PRIDE; O95786; -.
DR   ProteomicsDB; 51047; -. [O95786-1]
DR   ProteomicsDB; 51048; -. [O95786-2]
DR   Ensembl; ENST00000379883; ENSP00000369213; ENSG00000107201. [O95786-1]
DR   GeneID; 23586; -.
DR   KEGG; hsa:23586; -.
DR   UCSC; uc003zra.4; human. [O95786-1]
DR   CTD; 23586; -.
DR   DisGeNET; 23586; -.
DR   GeneCards; DDX58; -.
DR   HGNC; HGNC:19102; DDX58.
DR   HPA; CAB012643; -.
DR   HPA; HPA047193; -.
DR   MalaCards; DDX58; -.
DR   MIM; 609631; gene.
DR   MIM; 616298; phenotype.
DR   neXtProt; NX_O95786; -.
DR   OpenTargets; ENSG00000107201; -.
DR   Orphanet; 85191; Singleton-Merten dysplasia.
DR   PharmGKB; PA134994272; -.
DR   eggNOG; KOG0354; Eukaryota.
DR   eggNOG; COG1111; LUCA.
DR   GeneTree; ENSGT00940000153173; -.
DR   HOGENOM; HOG000230911; -.
DR   InParanoid; O95786; -.
DR   KO; K12646; -.
DR   OMA; RKCKAFA; -.
DR   OrthoDB; 1337630at2759; -.
DR   PhylomeDB; O95786; -.
DR   TreeFam; TF330258; -.
DR   Reactome; R-HSA-1169408; ISG15 antiviral mechanism.
DR   Reactome; R-HSA-168928; DDX58/IFIH1-mediated induction of interferon-alpha/beta.
DR   Reactome; R-HSA-5689880; Ub-specific processing proteases.
DR   Reactome; R-HSA-5689896; Ovarian tumor domain proteases.
DR   Reactome; R-HSA-8983711; OAS antiviral response.
DR   Reactome; R-HSA-918233; TRAF3-dependent IRF activation pathway.
DR   Reactome; R-HSA-933541; TRAF6 mediated IRF7 activation.
DR   Reactome; R-HSA-933542; TRAF6 mediated NF-kB activation.
DR   Reactome; R-HSA-933543; NF-kB activation through FADD/RIP-1 pathway mediated by caspase-8 and -10.
DR   Reactome; R-HSA-936440; Negative regulators of DDX58/IFIH1 signaling.
DR   SIGNOR; O95786; -.
DR   ChiTaRS; DDX58; human.
DR   EvolutionaryTrace; O95786; -.
DR   GeneWiki; RIG-I; -.
DR   GenomeRNAi; 23586; -.
DR   Pharos; O95786; -.
DR   PRO; PR:O95786; -.
DR   Proteomes; UP000005640; Chromosome 9.
DR   Bgee; ENSG00000107201; Expressed in 216 organ(s), highest expression level in buccal mucosa cell.
DR   ExpressionAtlas; O95786; baseline and differential.
DR   Genevisible; O95786; HS.
DR   GO; GO:0015629; C:actin cytoskeleton; IDA:UniProtKB.
DR   GO; GO:0005923; C:bicellular tight junction; IDA:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR   GO; GO:0032587; C:ruffle membrane; IDA:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003690; F:double-stranded DNA binding; IEA:Ensembl.
DR   GO; GO:0003725; F:double-stranded RNA binding; IDA:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003727; F:single-stranded RNA binding; IMP:UniProtKB.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR   GO; GO:0071360; P:cellular response to exogenous dsRNA; IMP:UniProtKB.
DR   GO; GO:0039528; P:cytoplasmic pattern recognition receptor signaling pathway in response to virus; TAS:UniProtKB.
DR   GO; GO:0051607; P:defense response to virus; IDA:UniProtKB.
DR   GO; GO:0009597; P:detection of virus; IDA:BHF-UCL.
DR   GO; GO:0045087; P:innate immune response; IMP:UniProtKB.
DR   GO; GO:0032480; P:negative regulation of type I interferon production; TAS:Reactome.
DR   GO; GO:0002230; P:positive regulation of defense response to virus by host; IMP:UniProtKB.
DR   GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IDA:BHF-UCL.
DR   GO; GO:0010628; P:positive regulation of gene expression; IDA:CACAO.
DR   GO; GO:0032725; P:positive regulation of granulocyte macrophage colony-stimulating factor production; IDA:CACAO.
DR   GO; GO:0032727; P:positive regulation of interferon-alpha production; IDA:UniProtKB.
DR   GO; GO:1902741; P:positive regulation of interferon-alpha secretion; IMP:UniProtKB.
DR   GO; GO:0032728; P:positive regulation of interferon-beta production; IDA:BHF-UCL.
DR   GO; GO:0035549; P:positive regulation of interferon-beta secretion; IMP:UniProtKB.
DR   GO; GO:0032755; P:positive regulation of interleukin-6 production; IDA:CACAO.
DR   GO; GO:2000778; P:positive regulation of interleukin-6 secretion; IMP:UniProtKB.
DR   GO; GO:0032757; P:positive regulation of interleukin-8 production; IDA:CACAO.
DR   GO; GO:0002735; P:positive regulation of myeloid dendritic cell cytokine production; ISS:UniProtKB.
DR   GO; GO:0060760; P:positive regulation of response to cytokine stimulus; IMP:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR   GO; GO:1904469; P:positive regulation of tumor necrosis factor secretion; IMP:UniProtKB.
DR   GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
DR   GO; GO:0030334; P:regulation of cell migration; IDA:UniProtKB.
DR   GO; GO:0034344; P:regulation of type III interferon production; TAS:UniProtKB.
DR   GO; GO:0043330; P:response to exogenous dsRNA; ISS:UniProtKB.
DR   GO; GO:0009615; P:response to virus; TAS:UniProtKB.
DR   GO; GO:0039529; P:RIG-I signaling pathway; IMP:UniProtKB.
DR   GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
DR   CDD; cd08817; CARD_RIG-I_r2; 1.
DR   Gene3D; 2.170.150.30; -; 1.
DR   InterPro; IPR031964; CARD_dom.
DR   InterPro; IPR042145; CARD_RIG-I_r2.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR041204; RIG-I_C.
DR   InterPro; IPR038557; RLR_C_sf.
DR   InterPro; IPR021673; RLR_CTR.
DR   Pfam; PF16739; CARD_2; 2.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF18119; RIG-I_C; 1.
DR   Pfam; PF11648; RIG-I_C-RD; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51789; RLR_CTR; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Antiviral defense;
KW   ATP-binding; Cell junction; Cell membrane; Cell projection;
KW   Complete proteome; Cytoplasm; Cytoskeleton; Disease mutation;
KW   Helicase; Host-virus interaction; Hydrolase; Immunity;
KW   Innate immunity; Isopeptide bond; Membrane; Metal-binding;
KW   Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome;
KW   Repeat; RNA-binding; Tight junction; Ubl conjugation; Zinc.
FT   CHAIN         1    925       Probable ATP-dependent RNA helicase
FT                                DDX58.
FT                                /FTId=PRO_0000144093.
FT   DOMAIN        1     87       CARD 1.
FT   DOMAIN       92    172       CARD 2.
FT   DOMAIN      251    430       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      610    776       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   DOMAIN      794    925       RLR CTR. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01125}.
FT   NP_BIND     264    271       ATP. {ECO:0000305}.
FT   REGION      218    925       Interaction with ZC3HAV1.
FT                                {ECO:0000269|PubMed:21102435}.
FT   MOTIF       372    375       DECH box.
FT   METAL       810    810       Zinc. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01125}.
FT   METAL       813    813       Zinc. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01125}.
FT   METAL       864    864       Zinc. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01125}.
FT   METAL       869    869       Zinc. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01125}.
FT   MOD_RES     495    495       (Microbial infection) Deamidated
FT                                asparagine; by herpes simplex virus
FT                                1/HHV-1 UL37.
FT                                {ECO:0000269|PubMed:27866900}.
FT   MOD_RES     549    549       (Microbial infection) Deamidated
FT                                asparagine; by herpes simplex virus
FT                                1/HHV-1 UL37.
FT                                {ECO:0000269|PubMed:27866900}.
FT   MOD_RES     770    770       Phosphothreonine; by CK2.
FT                                {ECO:0000269|PubMed:21068236}.
FT   MOD_RES     854    854       Phosphoserine; by CK2.
FT                                {ECO:0000269|PubMed:21068236}.
FT   MOD_RES     855    855       Phosphoserine; by CK2.
FT                                {ECO:0000269|PubMed:21068236}.
FT   MOD_RES     858    858       N6-acetyllysine.
FT                                {ECO:0000244|PubMed:19608861}.
FT   CROSSLNK    154    154       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT                                {ECO:0000269|PubMed:19484123}.
FT   CROSSLNK    164    164       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT                                {ECO:0000269|PubMed:19484123}.
FT   CROSSLNK    172    172       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT                                {ECO:0000269|PubMed:19484123}.
FT   CROSSLNK    181    181       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT                                {ECO:0000269|PubMed:26471729}.
FT   CROSSLNK    812    812       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT                                {ECO:0000250|UniProtKB:Q6Q899}.
FT   VAR_SEQ      36     80       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:17974005}.
FT                                /FTId=VSP_016054.
FT   VARIANT       7      7       R -> C (in dbSNP:rs10813831).
FT                                {ECO:0000269|PubMed:17974005}.
FT                                /FTId=VAR_023747.
FT   VARIANT     268    268       C -> F (in SGMRT2; results in
FT                                constitutive activation and enhanced
FT                                interferon-mediated signaling;
FT                                dbSNP:rs786204848).
FT                                {ECO:0000269|PubMed:25620203}.
FT                                /FTId=VAR_073667.
FT   VARIANT     373    373       E -> A (in SGMRT2; results in
FT                                constitutive activation and enhanced
FT                                interferon-mediated signaling;
FT                                dbSNP:rs786204847).
FT                                {ECO:0000269|PubMed:25620203}.
FT                                /FTId=VAR_073668.
FT   VARIANT     580    580       D -> E (in dbSNP:rs17217280).
FT                                {ECO:0000269|PubMed:11890704,
FT                                ECO:0000269|Ref.1}.
FT                                /FTId=VAR_023748.
FT   MUTAGEN      55     55       T->I: No IRF3 signaling activity; no
FT                                effect on dsRNA binding.
FT                                {ECO:0000269|PubMed:15708988}.
FT   MUTAGEN      99     99       K->R: Little or no effect on
FT                                ubiquitination of the 2 CARD domain.
FT                                Abolishes ubiquitination by RNF125.
FT                                {ECO:0000269|PubMed:17392790,
FT                                ECO:0000269|PubMed:26471729}.
FT   MUTAGEN     154    154       K->R: Reduction of ubiquitination.
FT                                Reduction of INFB induction.
FT                                {ECO:0000269|PubMed:19484123}.
FT   MUTAGEN     164    164       K->R: Reduction of ubiquitination.
FT                                Reduction of INFB induction.
FT                                {ECO:0000269|PubMed:19484123}.
FT   MUTAGEN     169    169       K->R: Little or no effect on
FT                                ubiquitination of the 2 CARD domains.
FT                                {ECO:0000269|PubMed:17392790}.
FT   MUTAGEN     172    172       K->R: Complete loss of ubiquitination; No
FT                                interaction with MAVS/IPS1; No induction
FT                                of IFN-beta.
FT                                {ECO:0000269|PubMed:17392790,
FT                                ECO:0000269|PubMed:19484123}.
FT   MUTAGEN     181    181       K->R: Little or no effect on
FT                                ubiquitination of the 2 CARD domains.
FT                                {ECO:0000269|PubMed:17392790}.
FT   MUTAGEN     190    190       K->R: Little or no effect on
FT                                ubiquitination of the 2 CARD domains.
FT   MUTAGEN     193    193       K->R: Little or no effect on
FT                                ubiquitination of the 2 CARD domains.
FT                                {ECO:0000269|PubMed:17392790}.
FT   MUTAGEN     270    270       K->A: No IRF3 signaling activity.
FT                                {ECO:0000269|PubMed:15208624,
FT                                ECO:0000269|PubMed:15708988}.
FT   MUTAGEN     495    495       N->Q: Complete loss of herpes simplex
FT                                virus 1 UL37-mediated deamidation; when
FT                                associated with Q-549.
FT                                {ECO:0000269|PubMed:27866900}.
FT   MUTAGEN     549    549       N->Q: Complete loss of herpes simplex
FT                                virus 1 UL37-mediated deamidation; when
FT                                associated with Q-495.
FT                                {ECO:0000269|PubMed:27866900}.
FT   HELIX         2     11       {ECO:0000244|PDB:4P4H}.
FT   HELIX        13     19       {ECO:0000244|PDB:4P4H}.
FT   HELIX        22     25       {ECO:0000244|PDB:4P4H}.
FT   TURN         26     32       {ECO:0000244|PDB:4P4H}.
FT   HELIX        35     48       {ECO:0000244|PDB:4P4H}.
FT   HELIX        50     63       {ECO:0000244|PDB:4P4H}.
FT   HELIX        69     80       {ECO:0000244|PDB:4P4H}.
FT   TURN         83     85       {ECO:0000244|PDB:4P4H}.
FT   HELIX        86     91       {ECO:0000244|PDB:4P4H}.
FT   HELIX        95     99       {ECO:0000244|PDB:4P4H}.
FT   HELIX       101    117       {ECO:0000244|PDB:4P4H}.
FT   HELIX       120    127       {ECO:0000244|PDB:4P4H}.
FT   HELIX       128    130       {ECO:0000244|PDB:4P4H}.
FT   HELIX       133    146       {ECO:0000244|PDB:4P4H}.
FT   HELIX       148    160       {ECO:0000244|PDB:4P4H}.
FT   HELIX       167    177       {ECO:0000244|PDB:4P4H}.
FT   TURN        183    185       {ECO:0000244|PDB:4P4H}.
FT   HELIX       245    255       {ECO:0000244|PDB:2YKG}.
FT   STRAND      260    263       {ECO:0000244|PDB:2YKG}.
FT   HELIX       270    284       {ECO:0000244|PDB:2YKG}.
FT   STRAND      293    296       {ECO:0000244|PDB:2YKG}.
FT   HELIX       300    313       {ECO:0000244|PDB:2YKG}.
FT   TURN        314    318       {ECO:0000244|PDB:2YKG}.
FT   STRAND      321    324       {ECO:0000244|PDB:2YKG}.
FT   STRAND      326    328       {ECO:0000244|PDB:2YKG}.
FT   STRAND      330    332       {ECO:0000244|PDB:2YKG}.
FT   HELIX       334    339       {ECO:0000244|PDB:2YKG}.
FT   STRAND      342    346       {ECO:0000244|PDB:2YKG}.
FT   HELIX       348    356       {ECO:0000244|PDB:2YKG}.
FT   STRAND      358    360       {ECO:0000244|PDB:5F9F}.
FT   HELIX       363    365       {ECO:0000244|PDB:2YKG}.
FT   STRAND      367    372       {ECO:0000244|PDB:2YKG}.
FT   HELIX       374    376       {ECO:0000244|PDB:2YKG}.
FT   STRAND      378    381       {ECO:0000244|PDB:6GPG}.
FT   HELIX       382    395       {ECO:0000244|PDB:2YKG}.
FT   STRAND      396    398       {ECO:0000244|PDB:4ON9}.
FT   STRAND      404    410       {ECO:0000244|PDB:2YKG}.
FT   HELIX       420    433       {ECO:0000244|PDB:2YKG}.
FT   STRAND      438    440       {ECO:0000244|PDB:2YKG}.
FT   STRAND      443    445       {ECO:0000244|PDB:5F98}.
FT   HELIX       446    452       {ECO:0000244|PDB:2YKG}.
FT   STRAND      457    462       {ECO:0000244|PDB:2YKG}.
FT   HELIX       470    489       {ECO:0000244|PDB:2YKG}.
FT   HELIX       493    495       {ECO:0000244|PDB:2YKG}.
FT   STRAND      496    498       {ECO:0000244|PDB:2YKG}.
FT   STRAND      504    506       {ECO:0000244|PDB:2YKG}.
FT   HELIX       507    518       {ECO:0000244|PDB:2YKG}.
FT   STRAND      526    528       {ECO:0000244|PDB:5F9F}.
FT   HELIX       531    557       {ECO:0000244|PDB:2YKG}.
FT   HELIX       560    575       {ECO:0000244|PDB:2YKG}.
FT   HELIX       581    591       {ECO:0000244|PDB:2YKG}.
FT   HELIX       594    602       {ECO:0000244|PDB:2YKG}.
FT   HELIX       604    606       {ECO:0000244|PDB:2YKG}.
FT   HELIX       609    622       {ECO:0000244|PDB:2YKG}.
FT   STRAND      630    633       {ECO:0000244|PDB:2YKG}.
FT   HELIX       637    649       {ECO:0000244|PDB:2YKG}.
FT   HELIX       651    653       {ECO:0000244|PDB:3ZD7}.
FT   STRAND      658    660       {ECO:0000244|PDB:3ZD7}.
FT   HELIX       675    683       {ECO:0000244|PDB:5F9F}.
FT   STRAND      686    690       {ECO:0000244|PDB:5F9F}.
FT   STRAND      694    700       {ECO:0000244|PDB:2YKG}.
FT   STRAND      701    703       {ECO:0000244|PDB:4ON9}.
FT   HELIX       706    708       {ECO:0000244|PDB:3ZD7}.
FT   STRAND      710    716       {ECO:0000244|PDB:2YKG}.
FT   HELIX       721    726       {ECO:0000244|PDB:5F9F}.
FT   HELIX       727    731       {ECO:0000244|PDB:5F9F}.
FT   STRAND      737    743       {ECO:0000244|PDB:2YKG}.
FT   HELIX       745    768       {ECO:0000244|PDB:2YKG}.
FT   HELIX       773    793       {ECO:0000244|PDB:2YKG}.
FT   STRAND      801    804       {ECO:0000244|PDB:2RMJ}.
FT   STRAND      806    810       {ECO:0000244|PDB:3LRR}.
FT   TURN        811    813       {ECO:0000244|PDB:3LRR}.
FT   STRAND      816    819       {ECO:0000244|PDB:3LRR}.
FT   HELIX       820    822       {ECO:0000244|PDB:3LRR}.
FT   STRAND      823    826       {ECO:0000244|PDB:3LRR}.
FT   TURN        827    829       {ECO:0000244|PDB:3LRR}.
FT   STRAND      830    833       {ECO:0000244|PDB:3LRR}.
FT   HELIX       836    839       {ECO:0000244|PDB:3LRR}.
FT   STRAND      842    846       {ECO:0000244|PDB:3LRR}.
FT   STRAND      856    864       {ECO:0000244|PDB:3LRR}.
FT   TURN        867    869       {ECO:0000244|PDB:3LRR}.
FT   STRAND      872    879       {ECO:0000244|PDB:3LRR}.
FT   STRAND      882    887       {ECO:0000244|PDB:3LRR}.
FT   HELIX       889    891       {ECO:0000244|PDB:3LRR}.
FT   STRAND      892    896       {ECO:0000244|PDB:3LRR}.
FT   TURN        897    899       {ECO:0000244|PDB:3LRR}.
FT   STRAND      902    904       {ECO:0000244|PDB:4BPB}.
FT   TURN        908    910       {ECO:0000244|PDB:3LRR}.
FT   HELIX       920    922       {ECO:0000244|PDB:3LRR}.
SQ   SEQUENCE   925 AA;  106600 MW;  BF0D501C395BAE25 CRC64;
     MTTEQRRSLQ AFQDYIRKTL DPTYILSYMA PWFREEEVQY IQAEKNNKGP MEAATLFLKF
     LLELQEEGWF RGFLDALDHA GYSGLYEAIE SWDFKKIEKL EEYRLLLKRL QPEFKTRIIP
     TDIISDLSEC LINQECEEIL QICSTKGMMA GAEKLVECLL RSDKENWPKT LKLALEKERN
     KFSELWIVEK GIKDVETEDL EDKMETSDIQ IFYQEDPECQ NLSENSCPPS EVSDTNLYSP
     FKPRNYQLEL ALPAMKGKNT IICAPTGCGK TFVSLLICEH HLKKFPQGQK GKVVFFANQI
     PVYEQQKSVF SKYFERHGYR VTGISGATAE NVPVEQIVEN NDIIILTPQI LVNNLKKGTI
     PSLSIFTLMI FDECHNTSKQ HPYNMIMFNY LDQKLGGSSG PLPQVIGLTA SVGVGDAKNT
     DEALDYICKL CASLDASVIA TVKHNLEELE QVVYKPQKFF RKVESRISDK FKYIIAQLMR
     DTESLAKRIC KDLENLSQIQ NREFGTQKYE QWIVTVQKAC MVFQMPDKDE ESRICKALFL
     YTSHLRKYND ALIISEHARM KDALDYLKDF FSNVRAAGFD EIEQDLTQRF EEKLQELESV
     SRDPSNENPK LEDLCFILQE EYHLNPETIT ILFVKTRALV DALKNWIEGN PKLSFLKPGI
     LTGRGKTNQN TGMTLPAQKC ILDAFKASGD HNILIATSVA DEGIDIAQCN LVILYEYVGN
     VIKMIQTRGR GRARGSKCFL LTSNAGVIEK EQINMYKEKM MNDSILRLQT WDEAVFREKI
     LHIQTHEKFI RDSQEKPKPV PDKENKKLLC RKCKALACYT ADVRVIEECH YTVLGDAFKE
     CFVSRPHPKP KQFSSFEKRA KIFCARQNCS HDWGIHVKYK TFEIPVIKIE SFVVEDIATG
     VQTLYSKWKD FHFEKIPFDP AEMSK
//
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