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Genome polyprotein [Cleaved into: Capsid protein C (Capsid protein) (Core protein); Protein prM (Precursor membrane protein); Peptide pr (Peptide precursor); Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (Non-structural protein 5)]

 POLG_DEN1W              Reviewed;        3392 AA.
P17763; P27910; P89313; P89314;
01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
12-DEC-2006, sequence version 2.
26-FEB-2020, entry version 175.
RecName: Full=Genome polyprotein;
Contains:
RecName: Full=Capsid protein C;
AltName: Full=Capsid protein;
AltName: Full=Core protein;
Contains:
RecName: Full=Protein prM;
AltName: Full=Precursor membrane protein;
Contains:
RecName: Full=Peptide pr;
AltName: Full=Peptide precursor;
Contains:
RecName: Full=Small envelope protein M;
AltName: Full=Matrix protein;
Contains:
RecName: Full=Envelope protein E;
Contains:
RecName: Full=Non-structural protein 1;
Short=NS1;
Contains:
RecName: Full=Non-structural protein 2A;
Short=NS2A;
Contains:
RecName: Full=Serine protease subunit NS2B;
AltName: Full=Flavivirin protease NS2B regulatory subunit;
AltName: Full=Non-structural protein 2B;
Contains:
RecName: Full=Serine protease NS3;
EC=3.4.21.91;
EC=3.6.1.15 {ECO:0000250|UniProtKB:Q9Q6P4};
EC=3.6.4.13 {ECO:0000250|UniProtKB:Q9Q6P4};
AltName: Full=Flavivirin protease NS3 catalytic subunit;
AltName: Full=Non-structural protein 3;
Contains:
RecName: Full=Non-structural protein 4A;
Short=NS4A;
Contains:
RecName: Full=Peptide 2k;
Contains:
RecName: Full=Non-structural protein 4B;
Short=NS4B;
Contains:
RecName: Full=RNA-directed RNA polymerase NS5;
EC=2.1.1.56 {ECO:0000255|PROSITE-ProRule:PRU00924};
EC=2.1.1.57 {ECO:0000255|PROSITE-ProRule:PRU00924};
EC=2.7.7.48 {ECO:0000255|PROSITE-ProRule:PRU00539};
AltName: Full=Non-structural protein 5;
Dengue virus type 1 (strain Nauru/West Pac/1974) (DENV-1).
Viruses; Riboviria; Flaviviridae; Flavivirus.
NCBI_TaxID=11059;
NCBI_TaxID=7159; Aedes aegypti (Yellowfever mosquito) (Culex aegypti).
NCBI_TaxID=7160; Aedes albopictus (Asian tiger mosquito) (Stegomyia albopicta).
NCBI_TaxID=9606; Homo sapiens (Human).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate 45AZ5, and Isolate WestPac;
PubMed=9292016; DOI=10.1099/0022-1317-78-9-2287;
Puri B., Nelson W.M., Henchal E.A., Hoke C.H., Eckels K.H., Dubois D.R.,
Porter K.R., Hayes C.G.;
"Molecular analysis of dengue virus attenuation after serial passage in
primary dog kidney cells.";
J. Gen. Virol. 78:2287-2291(1997).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-1226.
PubMed=3672932; DOI=10.1016/0042-6822(87)90196-6;
Mason P.W., McAda P.C., Mason T.L., Fournier M.J.;
"Sequence of the dengue-1 virus genome in the region encoding the three
structural proteins and the major nonstructural protein NS1.";
Virology 161:262-267(1987).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-792.
STRAIN=Isolate Philippines/836-1/1984;
PubMed=2738579; DOI=10.1099/0022-1317-70-7-1701;
Chu M.C., O'Rourke E.J., Trent D.W.;
"Genetic relatedness among structural protein genes of dengue 1 virus
strains.";
J. Gen. Virol. 70:1701-1712(1989).
[4]
SUBUNIT (NON-STRUCTURAL PROTEIN 1).
PubMed=2827377; DOI=10.1016/0042-6822(88)90408-4;
Winkler G., Randolph V.B., Cleaves G.R., Ryan T.E., Stollar V.;
"Evidence that the mature form of the flavivirus nonstructural protein NS1
is a dimer.";
Virology 162:187-196(1988).
[5]
PROTEOLYTIC CLEAVAGE (PROTEIN PRM).
PubMed=2154882; DOI=10.1016/0042-6822(90)90099-d;
Randolph V.B., Winkler G., Stollar V.;
"Acidotropic amines inhibit proteolytic processing of flavivirus prM
protein.";
Virology 174:450-458(1990).
[6]
GLYCOSYLATION (NON-STRUCTURAL PROTEIN 1).
PubMed=8176380; DOI=10.1099/0022-1317-75-5-1183;
Pryor M.J., Wright P.J.;
"Glycosylation mutants of dengue virus NS1 protein.";
J. Gen. Virol. 75:1183-1187(1994).
[7]
SUBCELLULAR LOCATION (NON-STRUCTURAL PROTEIN 1), SUBUNIT (NON-STRUCTURAL
PROTEIN 1), AND GLYCOSYLATION (NON-STRUCTURAL PROTEIN 1).
PubMed=10364366;
Flamand M., Megret F., Mathieu M., Lepault J., Rey F.A., Deubel V.;
"Dengue virus type 1 nonstructural glycoprotein NS1 is secreted from
mammalian cells as a soluble hexamer in a glycosylation-dependent
fashion.";
J. Virol. 73:6104-6110(1999).
[8]
PHOSPHORYLATION (RNA-DIRECTED RNA POLYMERASE NS5).
PubMed=7642575; DOI=10.1074/jbc.270.32.19100;
Kapoor M., Zhang L., Ramachandra M., Kusukawa J., Ebner K.E.,
Padmanabhan R.;
"Association between NS3 and NS5 proteins of dengue virus type 2 in the
putative RNA replicase is linked to differential phosphorylation of NS5.";
J. Biol. Chem. 270:19100-19106(1995).
[9]
FUNCTION (PROTEIN PRM), INTERACTION WITH ENVELOPE PROTEIN E (PROTEIN PRM),
AND INTERACTION WITH PROTEIN PRM (ENVELOPE PROTEIN E).
PubMed=9971841;
Wang S., He R., Anderson R.;
"PrM- and cell-binding domains of the dengue virus E protein.";
J. Virol. 73:2547-2551(1999).
[10]
FUNCTION (SMALL ENVELOPE PROTEIN M).
PubMed=13679613; DOI=10.1099/vir.0.19163-0;
Catteau A., Kalinina O., Wagner M.C., Deubel V., Courageot M.P.,
Despres P.;
"Dengue virus M protein contains a proapoptotic sequence referred to as
ApoptoM.";
J. Gen. Virol. 84:2781-2793(2003).
[11]
CHARACTERIZATION OF METHYLTRANSFERASE ACTIVITY, AND FUNCTION (RNA-DIRECTED
RNA POLYMERASE NS5).
PubMed=17267492; DOI=10.1128/jvi.02704-06;
Zhou Y., Ray D., Zhao Y., Dong H., Ren S., Li Z., Guo Y., Bernard K.A.,
Shi P.-Y., Li H.;
"Structure and function of flavivirus NS5 methyltransferase.";
J. Virol. 81:3891-3903(2007).
[12]
FUNCTION (CAPSID PROTEIN C), FUNCTION (ENVELOPE PROTEIN E), AND SUBUNIT
(ENVELOPE PROTEIN E).
PubMed=11893341; DOI=10.1016/s0092-8674(02)00660-8;
Kuhn R.J., Zhang W., Rossmann M.G., Pletnev S.V., Corver J., Lenches E.,
Jones C.T., Mukhopadhyay S., Chipman P.R., Strauss E.G., Baker T.S.,
Strauss J.H.;
"Structure of dengue virus: implications for flavivirus organization,
maturation, and fusion.";
Cell 108:717-725(2002).
[13]
DISULFIDE BOND (NON-STRUCTURAL PROTEIN 1).
STRAIN=DENV-2 strain Puerto Rico/PR159-S1/1969;
PubMed=14981082; DOI=10.1074/jbc.m312907200;
Wallis T.P., Huang C.Y., Nimkar S.B., Young P.R., Gorman J.J.;
"Determination of the disulfide bond arrangement of dengue virus NS1
protein.";
J. Biol. Chem. 279:20729-20741(2004).
[14]
DISULFIDE BOND (ENVELOPE PROTEIN E).
STRAIN=DENV-2 strain Thailand/16681/1984;
PubMed=14963174; DOI=10.1128/jvi.78.5.2648-2652.2004;
Roehrig J.T., Volpe K.E., Squires J., Hunt A.R., Davis B.S., Chang G.J.;
"Contribution of disulfide bridging to epitope expression of the dengue
type 2 virus envelope glycoprotein.";
J. Virol. 78:2648-2652(2004).
[15]
FUNCTION (NON-STRUCTURAL PROTEIN 4B).
PubMed=15956546; DOI=10.1128/jvi.79.13.8004-8013.2005;
Munoz-Jordan J.L., Laurent-Rolle M., Ashour J., Martinez-Sobrido L.,
Ashok M., Lipkin W.I., Garcia-Sastre A.;
"Inhibition of alpha/beta interferon signaling by the NS4B protein of
flaviviruses.";
J. Virol. 79:8004-8013(2005).
[16]
FUNCTION (SMALL ENVELOPE PROTEIN M).
PubMed=16007501; DOI=10.1007/s00232-005-0744-9;
Premkumar A., Horan C.R., Gage P.W.;
"Dengue virus M protein C-terminal peptide (DVM-C) forms ion channels.";
J. Membr. Biol. 204:33-38(2005).
[17]
INTERACTION WITH SERINE PROTEASE NS3 (RNA-DIRECTED RNA POLYMERASE NS5),
INTERACTION WITH RNA-DIRECTED RNA POLYMERASE NS5 (SERINE PROTEASE NS3), AND
CATALYTIC ACTIVITY (SERINE PROTEASE NS3).
STRAIN=Thailand/NGS-C/1944;
PubMed=15917225; DOI=10.1074/jbc.m501393200;
Yon C., Teramoto T., Mueller N., Phelan J., Ganesh V.K., Murthy K.H.,
Padmanabhan R.;
"Modulation of the nucleoside triphosphatase/RNA helicase and 5'-RNA
triphosphatase activities of Dengue virus type 2 nonstructural protein 3
(NS3) by interaction with NS5, the RNA-dependent RNA polymerase.";
J. Biol. Chem. 280:27412-27419(2005).
[18]
INTERACTION WITH NON-STRUCTURAL PROTEIN 4B (NON-STRUCTURAL PROTEIN 3), AND
INTERACTION WITH NON-STRUCTURAL PROTEIN 3 (NON-STRUCTURAL PROTEIN 4B).
PubMed=16894199; DOI=10.1099/vir.0.81844-0;
Umareddy I., Chao A., Sampath A., Gu F., Vasudevan S.G.;
"Dengue virus NS4B interacts with NS3 and dissociates it from single-
stranded RNA.";
J. Gen. Virol. 87:2605-2614(2006).
[19]
SUBCELLULAR LOCATION (NON-STRUCTURAL PROTEIN 4B), AND TOPOLOGY
(NON-STRUCTURAL PROTEIN 4B).
PubMed=16436383; DOI=10.1074/jbc.m512697200;
Miller S., Sparacio S., Bartenschlager R.;
"Subcellular localization and membrane topology of the Dengue virus type 2
Non-structural protein 4B.";
J. Biol. Chem. 281:8854-8863(2006).
[20]
SUBCELLULAR LOCATION (RNA-DIRECTED RNA POLYMERASE NS5).
PubMed=16699025; DOI=10.1128/jvi.01982-05;
Uchil P.D., Kumar A.V., Satchidanandam V.;
"Nuclear localization of flavivirus RNA synthesis in infected cells.";
J. Virol. 80:5451-5464(2006).
[21]
SUBCELLULAR LOCATION (NON-STRUCTURAL PROTEIN 4A), AND TOPOLOGY (PEPTIDE
2K).
PubMed=17276984; DOI=10.1074/jbc.m609919200;
Miller S., Kastner S., Krijnse-Locker J., Buhler S., Bartenschlager R.;
"The non-structural protein 4A of dengue virus is an integral membrane
protein inducing membrane alterations in a 2K-regulated manner.";
J. Biol. Chem. 282:8873-8882(2007).
[22]
GLYCOSYLATION AT ASN-347 (ENVELOPE PROTEIN E).
PubMed=17459925; DOI=10.1128/jvi.00116-07;
Mondotte J.A., Lozach P.Y., Amara A., Gamarnik A.V.;
"Essential role of dengue virus envelope protein N glycosylation at
asparagine-67 during viral propagation.";
J. Virol. 81:7136-7148(2007).
[23]
REVIEW.
PubMed=18644250; DOI=10.1016/j.mib.2008.06.004;
Perera R., Kuhn R.J.;
"Structural proteomics of dengue virus.";
Curr. Opin. Microbiol. 11:369-377(2008).
[24]
SUBCELLULAR LOCATION (CAPSID PROTEIN C), AND FUNCTION (CAPSID PROTEIN C).
PubMed=18420804; DOI=10.1099/vir.0.83264-0;
Sangiambut S., Keelapang P., Aaskov J., Puttikhunt C., Kasinrerk W.,
Malasit P., Sittisombut N.;
"Multiple regions in dengue virus capsid protein contribute to nuclear
localization during virus infection.";
J. Gen. Virol. 89:1254-1264(2008).
[25]
FUNCTION (ENVELOPE PROTEIN E), FUNCTION (PROTEIN PRM), AND FUNCTION
(PEPTIDE PR).
PubMed=18369148; DOI=10.1126/science.1153264;
Yu I.M., Zhang W., Holdaway H.A., Li L., Kostyuchenko V.A., Chipman P.R.,
Kuhn R.J., Rossmann M.G., Chen J.;
"Structure of the immature dengue virus at low pH primes proteolytic
maturation.";
Science 319:1834-1837(2008).
[26]
FUNCTION (PROTEIN PR), AND SUBCELLULAR LOCATION (PROTEIN PR).
PubMed=19759134; DOI=10.1128/jvi.01637-09;
Yu I.M., Holdaway H.A., Chipman P.R., Kuhn R.J., Rossmann M.G., Chen J.;
"Association of the pr peptides with dengue virus at acidic pH blocks
membrane fusion.";
J. Virol. 83:12101-12107(2009).
[27]
FUNCTION (RNA-DIRECTED RNA POLYMERASE NS5), AND INTERACTION WITH HUMAN
STAT2 (RNA-DIRECTED RNA POLYMERASE NS5).
PubMed=19279106; DOI=10.1128/jvi.02188-08;
Ashour J., Laurent-Rolle M., Shi P.Y., Garcia-Sastre A.;
"NS5 of dengue virus mediates STAT2 binding and degradation.";
J. Virol. 83:5408-5418(2009).
[28]
FUNCTION (RNA-DIRECTED RNA POLYMERASE NS5), AND INTERACTION WITH
RNA-DIRECTED RNA POLYMERASE NS5 (SERINE PROTEASE NS3).
STRAIN=Thailand/16681/1984;
PubMed=19850911; DOI=10.1261/rna.1609709;
Issur M., Geiss B.J., Bougie I., Picard-Jean F., Despins S., Mayette J.,
Hobdey S.E., Bisaillon M.;
"The flavivirus NS5 protein is a true RNA guanylyltransferase that
catalyzes a two-step reaction to form the RNA cap structure.";
RNA 15:2340-2350(2009).
[29]
DOMAIN (ENVELOPE PROTEIN E).
PubMed=20181718; DOI=10.1128/jvi.01963-09;
Hsieh S.C., Tsai W.Y., Wang W.K.;
"The length of and nonhydrophobic residues in the transmembrane domain of
dengue virus envelope protein are critical for its retention and assembly
in the endoplasmic reticulum.";
J. Virol. 84:4782-4797(2010).
[30]
INTERACTION WITH HUMAN EXOC1 (CAPSID PROTEIN C), AND SUBCELLULAR LOCATION
(CAPSID PROTEIN C).
STRAIN=DENV-2;
PubMed=19889084; DOI=10.1111/j.1462-5822.2009.01407.x;
Bhuvanakantham R., Li J., Tan T.T., Ng M.L.;
"Human Sec3 protein is a novel transcriptional and translational repressor
of flavivirus.";
Cell. Microbiol. 12:453-472(2010).
[31]
INTERACTION WITH HUMAN EXOC1 (CAPSID PROTEIN C), AND FUNCTION (CAPSID
PROTEIN C).
STRAIN=DENV-2;
PubMed=23522008; DOI=10.1111/cmi.12143;
Bhuvanakantham R., Ng M.L.;
"West Nile virus and dengue virus capsid protein negates the antiviral
activity of human Sec3 protein through the proteasome pathway.";
Cell. Microbiol. 15:1688-1706(2013).
[32]
REVIEW.
PubMed=20372965; DOI=10.1007/s00018-010-0357-z;
Rodenhuis-Zybert I.A., Wilschut J., Smit J.M.;
"Dengue virus life cycle: viral and host factors modulating infectivity.";
Cell. Mol. Life Sci. 67:2773-2786(2010).
[33]
FUNCTION (CAPSID PROTEIN C).
PubMed=21909430; DOI=10.1371/journal.pone.0024365;
Colpitts T.M., Barthel S., Wang P., Fikrig E.;
"Dengue virus capsid protein binds core histones and inhibits nucleosome
formation in human liver cells.";
PLoS ONE 6:E24365-E24365(2011).
[34]
REVIEW (PROTEIN PRM).
PubMed=21388812; DOI=10.1016/j.tim.2011.02.002;
Rodenhuis-Zybert I.A., Wilschut J., Smit J.M.;
"Partial maturation: an immune-evasion strategy of dengue virus?";
Trends Microbiol. 19:248-254(2011).
[35]
SUBCELLULAR LOCATION (NON-STRUCTURAL PROTEIN 2A), AND TOPOLOGY
(NON-STRUCTURAL PROTEIN 2A).
STRAIN=DENV-2 strain NGC;
PubMed=23408612; DOI=10.1128/jvi.02424-12;
Xie X., Gayen S., Kang C., Yuan Z., Shi P.Y.;
"Membrane topology and function of dengue virus NS2A protein.";
J. Virol. 87:4609-4622(2013).
[36]
FUNCTION (SMALL ENVELOPE PROTEIN M), AND FUNCTION (PROTEIN PRM).
STRAIN=DENV-1 strain Hawaii;
PubMed=25326389; DOI=10.1074/jbc.m114.610428;
Hsieh S.C., Wu Y.C., Zou G., Nerurkar V.R., Shi P.Y., Wang W.K.;
"Highly conserved residues in the helical domain of dengue virus type 1
precursor membrane protein are involved in assembly, precursor membrane
(prM) protein cleavage, and entry.";
J. Biol. Chem. 289:33149-33160(2014).
[37]
INTERACTION WITH ENVELOPE PROTEIN E (NON-STRUCTURAL PROTEIN 1), INTERACTION
WITH PRM (NON-STRUCTURAL PROTEIN 1), INTERACTION WITH NON-STRUCTURAL
PROTEIN 1 (PROTEIN PRM), AND INTERACTION WITH NON-STRUCTURAL PROTEIN 1
(ENVELOPE PROTEIN E).
STRAIN=DENV-2 strain 16681;
PubMed=26562291; DOI=10.1371/journal.ppat.1005277;
Scaturro P., Cortese M., Chatel-Chaix L., Fischl W., Bartenschlager R.;
"Dengue virus non-structural protein 1 modulates infectious particle
production via interaction with the structural proteins.";
PLoS Pathog. 11:E1005277-E1005277(2015).
[38]
SUBCELLULAR LOCATION (NON-STRUCTURAL PROTEIN 1).
PubMed=26655246; DOI=10.1016/j.virol.2015.11.020;
Alcala A.C., Medina F., Gonzalez-Robles A., Salazar-Villatoro L.,
Fragoso-Soriano R.J., Vasquez C., Cervantes-Salazar M., Del Angel R.M.,
Ludert J.E.;
"The dengue virus non-structural protein 1 (NS1) is secreted efficiently
from infected mosquito cells.";
Virology 488:278-287(2015).
[39]
FUNCTION (NON-STRUCTURAL PROTEIN 2A), AND MUTAGENESIS OF GLY-1138;
GLU-1147; GLU-1227; ASP-1252; GLN-1314; LYS-1315 AND GLY-1327.
PubMed=25392211; DOI=10.1128/jvi.02882-14;
Xie X., Zou J., Puttikhunt C., Yuan Z., Shi P.Y.;
"Two distinct sets of NS2A molecules are responsible for dengue virus RNA
synthesis and virion assembly.";
J. Virol. 89:1298-1313(2015).
[40]
SUBCELLULAR LOCATION (SERINE PROTEASE SUBUNIT NS2B), AND TOPOLOGY (SERINE
PROTEASE SUBUNIT NS2B).
STRAIN=DENV-4;
PubMed=26072288; DOI=10.1016/j.bbamem.2015.06.010;
Li Y., Li Q., Wong Y.L., Liew L.S., Kang C.;
"Membrane topology of NS2B of dengue virus revealed by NMR spectroscopy.";
Biochim. Biophys. Acta 1848:2244-2252(2015).
[41]
FUNCTION (SERINE PROTEASE SUBUNIT NS2B), AND SUBUNIT (SERINE PROTEASE
SUBUNIT NS2B).
STRAIN=DENV-2 New Guinea strain AF0136;
PubMed=26728778; DOI=10.1186/s12985-015-0456-4;
Leon-Juarez M., Martinez-Castillo M., Shrivastava G., Garcia-Cordero J.,
Villegas-Sepulveda N., Mondragon-Castelan M., Mondragon-Flores R.,
Cedillo-Barron L.;
"Recombinant Dengue virus protein NS2B alters membrane permeability in
different membrane models.";
Virol. J. 13:1-1(2016).
[42]
SUBUNIT (RNA-DIRECTED RNA POLYMERASE NS5).
STRAIN=DENV-3;
PubMed=26895240; DOI=10.1371/journal.ppat.1005451;
Klema V.J., Ye M., Hindupur A., Teramoto T., Gottipati K., Padmanabhan R.,
Choi K.H.;
"Dengue virus nonstructural protein 5 (NS5) assembles into a dimer with a
unique methyltransferase and polymerase interface.";
PLoS Pathog. 12:E1005451-E1005451(2016).
[43]
FUNCTION (NON-STRUCTURAL PROTEIN 1).
PubMed=27416066; DOI=10.1371/journal.ppat.1005738;
Puerta-Guardo H., Glasner D.R., Harris E.;
"Dengue virus NS1 disrupts the endothelial glycocalyx, leading to
hyperpermeability.";
PLoS Pathog. 12:E1005738-E1005738(2016).
[44]
REVIEW (NON-STRUCTURAL PROTEIN 1).
PubMed=27473856; DOI=10.1186/s12985-016-0590-7;
Rastogi M., Sharma N., Singh S.K.;
"Flavivirus NS1: a multifaceted enigmatic viral protein.";
Virol. J. 13:131-131(2016).
[45]
FUNCTION, INTERACTION WITH HOST MAVS, AND SUBCELLULAR LOCATION.
PubMed=27252539; DOI=10.1128/jvi.00221-16;
He Z., Zhu X., Wen W., Yuan J., Hu Y., Chen J., An S., Dong X., Lin C.,
Yu J., Wu J., Yang Y., Cai J., Li J., Li M.;
"Dengue virus subverts host innate immunity by targeting adaptor protein
MAVS.";
J. Virol. 90:7219-7230(2016).
[46]
INTERACTION WITH HOST SHFL (SERINE PROTEASE NS3 AND NON-STRUCTURAL PROTEIN
4A).
STRAIN=Tonga/74 type 2;
PubMed=27974568; DOI=10.1128/jvi.01606-16;
Balinsky C.A., Schmeisser H., Wells A.I., Ganesan S., Jin T., Singh K.,
Zoon K.C.;
"IRAV (FLJ11286), an Interferon-Stimulated Gene with Antiviral Activity
against Dengue Virus, Interacts with MOV10.";
J. Virol. 91:0-0(2017).
[47]
REVIEW (RNA-DIRECTED RNA POLYMERASE NS5).
PubMed=28441781; DOI=10.3390/v9040091;
El Sahili A., Lescar J.;
"Dengue virus non-structural protein 5.";
Viruses 9:0-0(2017).
[48]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1394-1661, INTERACTION WITH SERINE
PROTEASE NS3 (SERINE PROTEASE SUBUNIT NS2B), AND INTERACTION WITH SERINE
PROTEASE SUBUNIT NS2B (SERINE PROTEASE NS3).
PubMed=20042502; DOI=10.1128/jvi.02044-09;
Chandramouli S., Joseph J.S., Daudenarde S., Gatchalian J.,
Cornillez-Ty C., Kuhn P.;
"Serotype-specific structural differences in the protease-cofactor
complexes of the dengue virus family.";
J. Virol. 84:3059-3067(2010).
-!- FUNCTION: [Capsid protein C]: Plays a role in virus budding by binding
to the cell membrane and gathering the viral RNA into a nucleocapsid
that forms the core of a mature virus particle (PubMed:11893341).
During virus entry, may induce genome penetration into the host
cytoplasm after hemifusion induced by the surface proteins. Can migrate
to the cell nucleus where it modulates host functions (PubMed:18420804,
PubMed:21909430). Overcomes the anti-viral effects of host EXOC1 by
sequestering and degrading the latter through the proteasome
degradation pathway (PubMed:23522008). {ECO:0000269|PubMed:11893341,
ECO:0000269|PubMed:18420804, ECO:0000269|PubMed:21909430,
ECO:0000269|PubMed:23522008}.
-!- FUNCTION: [Capsid protein C]: Inhibits RNA silencing by interfering
with host Dicer. {ECO:0000250|UniProtKB:P03314}.
-!- FUNCTION: [Peptide pr]: Prevents premature fusion activity of envelope
proteins in trans-Golgi by binding to envelope protein E at pH6.0.
After virion release in extracellular space, gets dissociated from E
dimers. {ECO:0000269|PubMed:18369148, ECO:0000269|PubMed:19759134}.
-!- FUNCTION: [Protein prM]: Acts as a chaperone for envelope protein E
during intracellular virion assembly by masking and inactivating
envelope protein E fusion peptide. prM is the only viral peptide
matured by host furin in the trans-Golgi network probably to avoid
catastrophic activation of the viral fusion activity in acidic Golgi
compartment prior to virion release (PubMed:9971841). prM-E cleavage is
inefficient, and many virions are only partially matured. These
uncleaved prM would play a role in immune evasion (PubMed:21388812).
{ECO:0000269|PubMed:18369148, ECO:0000269|PubMed:25326389,
ECO:0000269|PubMed:9971841, ECO:0000303|PubMed:21388812}.
-!- FUNCTION: [Small envelope protein M]: May play a role in virus budding
(PubMed:25326389). Exerts cytotoxic effects by activating a
mitochondrial apoptotic pathway through M extodomain (PubMed:13679613).
May display a viroporin activity (PubMed:16007501).
{ECO:0000269|PubMed:13679613, ECO:0000269|PubMed:16007501,
ECO:0000269|PubMed:25326389}.
-!- FUNCTION: [Envelope protein E]: Binds to host cell surface receptor and
mediates fusion between viral and cellular membranes. Envelope protein
is synthesized in the endoplasmic reticulum in the form of heterodimer
with protein prM. They play a role in virion budding in the ER, and the
newly formed immature particle is covered with 60 spikes composed of
heterodimer between precursor prM and envelope protein E. The virion is
transported to the Golgi apparatus where the low pH causes dissociation
of PrM-E heterodimers and formation of E homodimers (PubMed:18369148).
prM-E cleavage is ineficient, and many virions are only partially
matured. These uncleaved prM would play a role in immune evasion
(PubMed:11893341). {ECO:0000269|PubMed:11893341,
ECO:0000269|PubMed:18369148}.
-!- FUNCTION: [Non-structural protein 1]: Involved in immune evasion,
pathogenesis and viral replication. Once cleaved off the polyprotein,
is targeted to three destinations: the viral replication cycle, the
plasma membrane and the extracellular compartment. Essential for viral
replication. Required for formation of the replication complex and
recruitment of other non-structural proteins to the ER-derived membrane
structures. Excreted as a hexameric lipoparticle that plays a role
against host immune response. Antagonizing the complement function.
Binds to the host macrophages and dendritic cells. Inhibits signal
transduction originating from Toll-like receptor 3 (TLR3).
{ECO:0000250|UniProtKB:Q9Q6P4}.
-!- FUNCTION: [Non-structural protein 1]: Disrupts the host endothelial
glycocalyx layer of host pulmonary microvascular endothelial cells,
inducing degradation of sialic acid and shedding of heparan sulfate
proteoglycans. NS1 induces expression of sialidases, heparanase, and
activates cathepsin L, which activates heparanase via enzymatic
cleavage. These effects are probably linked to the endothelial
hyperpermeability observed in severe dengue disease.
{ECO:0000269|PubMed:27416066}.
-!- FUNCTION: [Non-structural protein 2A]: Component of the viral RNA
replication complex that functions in virion assembly and antagonizes
the host immune response. {ECO:0000269|PubMed:25392211}.
-!- FUNCTION: [Serine protease subunit NS2B]: Required cofactor for the
serine protease function of NS3. May have membrane-destabilizing
activity and form viroporins (PubMed:26728778). {ECO:0000255|PROSITE-
ProRule:PRU00859, ECO:0000269|PubMed:26728778}.
-!- FUNCTION: [Serine protease NS3]: Displays three enzymatic activities:
serine protease, NTPase and RNA helicase. NS3 serine protease, in
association with NS2B, performs its autocleavage and cleaves the
polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B-
NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and
unwinds dsRNA in the 3' to 5' direction. {ECO:0000255|PROSITE-
ProRule:PRU00860}.
-!- FUNCTION: [Non-structural protein 4A]: Regulates the ATPase activity of
the NS3 helicase activity. NS4A allows NS3 helicase to conserve energy
during unwinding. Plays a role in the inhibition of the host innate
immune response. Interacts with host MAVS and thereby prevents the
interaction between DDX58 and MAVS. In turn, IFN-beta production is
impaired. {ECO:0000250|UniProtKB:Q9Q6P4, ECO:0000269|PubMed:27252539}.
-!- FUNCTION: [Peptide 2k]: Functions as a signal peptide for NS4B and is
required for the interferon antagonism activity of the latter.
{ECO:0000269|PubMed:17276984}.
-!- FUNCTION: [Non-structural protein 4B]: Induces the formation of ER-
derived membrane vesicles where the viral replication takes place (By
similarity). Inhibits interferon (IFN)-induced host STAT1
phosphorylation and nuclear translocation, thereby preventing the
establishment of a cellular antiviral state by blocking the IFN-
alpha/beta pathway (PubMed:15956546). {ECO:0000250|UniProtKB:Q9Q6P4,
ECO:0000269|PubMed:15956546}.
-!- FUNCTION: [RNA-directed RNA polymerase NS5]: Replicates the viral (+)
and (-) RNA genome, and performs the capping of genomes in the
cytoplasm. NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O
positions. Besides its role in RNA genome replication, also prevents
the establishment of cellular antiviral state by blocking the
interferon-alpha/beta (IFN-alpha/beta) signaling pathway. Inhibits host
TYK2 and STAT2 phosphorylation, thereby preventing activation of JAK-
STAT signaling pathway. {ECO:0000269|PubMed:17267492,
ECO:0000269|PubMed:19279106, ECO:0000269|PubMed:19850911}.
-!- CATALYTIC ACTIVITY:
Reaction=Selective hydrolysis of -Xaa-Xaa-|-Yaa- bonds in which each of
the Xaa can be either Arg or Lys and Yaa can be either Ser or Ala.;
EC=3.4.21.91; Evidence={ECO:0000269|PubMed:15917225};
-!- CATALYTIC ACTIVITY:
Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:11128, Rhea:RHEA-
COMP:11129, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:83400;
EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539};
-!- CATALYTIC ACTIVITY:
Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-
diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680,
ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15;
-!- CATALYTIC ACTIVITY:
Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
-!- CATALYTIC ACTIVITY:
Reaction=a 5'-end (5'-triphosphoguanosine)-guanosine in mRNA + S-
adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-
triphosphoguanosine)-guanosine in mRNA + S-adenosyl-L-homocysteine;
Xref=Rhea:RHEA:60856, Rhea:RHEA-COMP:15681, Rhea:RHEA-COMP:15683,
ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:143971,
ChEBI:CHEBI:143975; EC=2.1.1.56; Evidence={ECO:0000255|PROSITE-
ProRule:PRU00924};
-!- CATALYTIC ACTIVITY:
Reaction=a 5'-end (5'-triphosphoguanosine)-adenosine in mRNA + S-
adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-
triphosphoguanosine)-adenosine in mRNA + S-adenosyl-L-homocysteine;
Xref=Rhea:RHEA:60852, Rhea:RHEA-COMP:15680, Rhea:RHEA-COMP:15682,
ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:143973,
ChEBI:CHEBI:143974; EC=2.1.1.56; Evidence={ECO:0000255|PROSITE-
ProRule:PRU00924};
-!- CATALYTIC ACTIVITY:
Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-guanosine in
mRNA + S-adenosyl-L-methionine = a 5'-end (N7-methyl 5'-
triphosphoguanosine)-(2'-O-methyl-guanosine) in mRNA + H(+) + S-
adenosyl-L-homocysteine; Xref=Rhea:RHEA:60864, Rhea:RHEA-COMP:15683,
Rhea:RHEA-COMP:15685, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
ChEBI:CHEBI:59789, ChEBI:CHEBI:143975, ChEBI:CHEBI:143977;
EC=2.1.1.57; Evidence={ECO:0000255|PROSITE-ProRule:PRU00924};
-!- CATALYTIC ACTIVITY:
Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-adenosine in
mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-
triphosphoguanosine)-(2'-O-methyl-adenosine) in mRNA + H(+) + S-
adenosyl-L-homocysteine; Xref=Rhea:RHEA:60860, Rhea:RHEA-COMP:15682,
Rhea:RHEA-COMP:15684, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
ChEBI:CHEBI:59789, ChEBI:CHEBI:143974, ChEBI:CHEBI:143976;
EC=2.1.1.57; Evidence={ECO:0000255|PROSITE-ProRule:PRU00924};
-!- SUBUNIT: [Capsid protein C]: Homodimer. Interacts (via N-terminus) with
host EXOC1 (via C-terminus) (PubMed:19889084, PubMed:23522008); this
interaction results in EXOC1 degradation through the proteasome
degradation pathway (PubMed:23522008). {ECO:0000269|PubMed:19889084,
ECO:0000269|PubMed:23522008}.
-!- SUBUNIT: [Protein prM]: Forms heterodimers with envelope protein E in
the endoplasmic reticulum and Golgi (PubMed:9971841).
{ECO:0000269|PubMed:9971841}.
-!- SUBUNIT: [Envelope protein E]: Homodimer; in the endoplasmic reticulum
and Golgi (PubMed:11893341). Interacts with protein prM
(PubMed:9971841). Interacts with non-structural protein 1
(PubMed:26562291). {ECO:0000269|PubMed:11893341,
ECO:0000269|PubMed:26562291, ECO:0000269|PubMed:9971841}.
-!- SUBUNIT: [Non-structural protein 1]: Homodimer; Homohexamer when
secreted (PubMed:2827377, PubMed:10364366). Interacts with envelope
protein E (PubMed:26562291). {ECO:0000269|PubMed:10364366,
ECO:0000269|PubMed:26562291, ECO:0000269|PubMed:2827377}.
-!- SUBUNIT: [Non-structural protein 2A]: Interacts (via N-terminus) with
serine protease NS3. {ECO:0000250|UniProtKB:P03314}.
-!- SUBUNIT: [Serine protease subunit NS2B]: Forms a heterodimer with
serine protease NS3 (PubMed:20042502). May form homooligomers
(PubMed:26728778). {ECO:0000269|PubMed:20042502,
ECO:0000269|PubMed:26728778}.
-!- SUBUNIT: [Serine protease NS3]: Forms a heterodimer with NS2B
(PubMed:20042502). Interacts with NS4B (PubMed:16894199). Interacts
with unphosphorylated RNA-directed RNA polymerase NS5; this interaction
stimulates RNA-directed RNA polymerase NS5 guanylyltransferase activity
(PubMed:19850911, PubMed:15917225). Interacts with host SHFL
(PubMed:27974568). {ECO:0000269|PubMed:15917225,
ECO:0000269|PubMed:16894199, ECO:0000269|PubMed:19850911,
ECO:0000269|PubMed:20042502, ECO:0000269|PubMed:27974568}.
-!- SUBUNIT: [Non-structural protein 4A]: Interacts with host MAVS; this
interaction inhibits the synthesis of IFN-beta (PubMed:27252539).
Interacts with host SHFL (PubMed:27974568).
{ECO:0000269|PubMed:27252539, ECO:0000269|PubMed:27974568}.
-!- SUBUNIT: [Non-structural protein 4B]: Interacts with serine protease
NS3 (PubMed:16894199). {ECO:0000269|PubMed:16894199}.
-!- SUBUNIT: [RNA-directed RNA polymerase NS5]: Homodimer
(PubMed:26895240). Interacts with host STAT2; this interaction inhibits
the phosphorylation of the latter, and, when all viral proteins are
present (polyprotein), targets STAT2 for degradation (PubMed:19279106).
Interacts with serine protease NS3 (PubMed:15917225, PubMed:19850911).
{ECO:0000269|PubMed:15917225, ECO:0000269|PubMed:19279106,
ECO:0000269|PubMed:19850911, ECO:0000269|PubMed:26895240}.
-!- SUBCELLULAR LOCATION: [Capsid protein C]: Virion. Host nucleus
{ECO:0000269|PubMed:18420804}. Host cytoplasm
{ECO:0000269|PubMed:19889084}. Host cytoplasm, host perinuclear region
{ECO:0000269|PubMed:19889084}.
-!- SUBCELLULAR LOCATION: [Peptide pr]: Secreted
{ECO:0000269|PubMed:19759134}.
-!- SUBCELLULAR LOCATION: [Small envelope protein M]: Virion membrane
{ECO:0000269|PubMed:9971841}; Multi-pass membrane protein
{ECO:0000255}. Host endoplasmic reticulum membrane
{ECO:0000269|PubMed:9971841}; Multi-pass membrane protein
{ECO:0000255}.
-!- SUBCELLULAR LOCATION: [Envelope protein E]: Virion membrane
{ECO:0000269|PubMed:20181718}; Multi-pass membrane protein
{ECO:0000255}. Host endoplasmic reticulum membrane
{ECO:0000269|PubMed:20181718}; Multi-pass membrane protein
{ECO:0000255}.
-!- SUBCELLULAR LOCATION: [Non-structural protein 1]: Secreted
{ECO:0000269|PubMed:10364366, ECO:0000269|PubMed:26655246}. Host
endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal
side {ECO:0000305}. Note=Located in RE-derived vesicles hosting the
replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}.
-!- SUBCELLULAR LOCATION: [Non-structural protein 2A]: Host endoplasmic
reticulum membrane {ECO:0000269|PubMed:23408612}; Multi-pass membrane
protein {ECO:0000269|PubMed:23408612}.
-!- SUBCELLULAR LOCATION: [Serine protease subunit NS2B]: Host endoplasmic
reticulum membrane; Multi-pass membrane protein
{ECO:0000269|PubMed:26072288}.
-!- SUBCELLULAR LOCATION: [Serine protease NS3]: Host endoplasmic reticulum
membrane {ECO:0000255|PROSITE-ProRule:PRU00860}; Peripheral membrane
protein {ECO:0000255|PROSITE-ProRule:PRU00860}; Cytoplasmic side
{ECO:0000255|PROSITE-ProRule:PRU00860}. Note=Remains non-covalently
associated to serine protease subunit NS2B. {ECO:0000255|PROSITE-
ProRule:PRU00860}.
-!- SUBCELLULAR LOCATION: [Non-structural protein 4A]: Host endoplasmic
reticulum membrane {ECO:0000269|PubMed:17276984}; Multi-pass membrane
protein {ECO:0000269|PubMed:17276984}. Host mitochondrion
{ECO:0000269|PubMed:27252539}. Note=Located in RE-associated vesicles
hosting the replication complex. Interacts with host MAVS in the
mitochondrion-associated endoplasmic reticulum membranes.
{ECO:0000269|PubMed:17276984, ECO:0000269|PubMed:27252539}.
-!- SUBCELLULAR LOCATION: [Non-structural protein 4B]: Host endoplasmic
reticulum membrane {ECO:0000269|PubMed:16436383}; Multi-pass membrane
protein {ECO:0000269|PubMed:16436383}. Note=Located in RE-derived
vesicles hosting the replication complex.
{ECO:0000250|UniProtKB:Q9Q6P4}.
-!- SUBCELLULAR LOCATION: [RNA-directed RNA polymerase NS5]: Host
endoplasmic reticulum membrane {ECO:0000305}; Peripheral membrane
protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Host nucleus
{ECO:0000269|PubMed:16699025}. Note=Located in RE-associated vesicles
hosting the replication complex. NS5 protein is mainly localized in the
nucleus rather than in ER vesicles, especially in the DENV 2, 3, 4
serotypes. {ECO:0000303|PubMed:28441781}.
-!- DOMAIN: The transmembrane domains of the small envelope protein M and
envelope protein E contain an endoplasmic reticulum retention signal.
{ECO:0000269|PubMed:20181718}.
-!- PTM: [RNA-directed RNA polymerase NS5]: Sumoylation of RNA-directed RNA
polymerase NS5 increases NS5 protein stability allowing proper viral
RNA replication. {ECO:0000250|UniProtKB:P29990}.
-!- PTM: [Genome polyprotein]: Specific enzymatic cleavages in vivo yield
mature proteins. Cleavages in the lumen of endoplasmic reticulum are
performed by host signal peptidase, whereas cleavages in the
cytoplasmic side are performed by the Serine protease NS3. Signal
cleavage at the 2K-4B site requires a prior NS3 protease-mediated
cleavage at the 4A-2K site.
-!- PTM: [Protein prM]: Cleaved in post-Golgi vesicles by a host furin,
releasing the mature small envelope protein M, and peptide pr. This
cleavage is incomplete as up to 30% of viral particles still carry
uncleaved prM. {ECO:0000269|PubMed:21388812,
ECO:0000269|PubMed:2154882}.
-!- PTM: [Non-structural protein 1]: N-glycosylated (PubMed:8176380,
PubMed:10364366). The excreted form is glycosylated and this is
required for efficient secretion of the protein from infected cells.
{ECO:0000269|PubMed:10364366, ECO:0000269|PubMed:8176380}.
-!- PTM: [RNA-directed RNA polymerase NS5]: Phosphorylated on serines
residues. This phosphorylation may trigger NS5 nuclear localization.
{ECO:0000269|PubMed:7642575}.
-!- PTM: [Envelope protein E]: N-glycosylated.
{ECO:0000269|PubMed:17459925}.
-!- SIMILARITY: In the N-terminal section; belongs to the class I-like SAM-
binding methyltransferase superfamily. mRNA cap 0-1 NS5-type
methyltransferase family. {ECO:0000255|PROSITE-ProRule:PRU00924}.
-!- WEB RESOURCE: Name=Virus Pathogen Resource;
URL="http://www.viprbrc.org/brc/home.do?decorator=flavi_dengue";
---------------------------------------------------------------------------
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EMBL; U88535; AAB70694.1; -; Genomic_RNA.
EMBL; U88536; AAB70695.1; -; Genomic_RNA.
EMBL; M23027; AAA42940.1; -; Genomic_RNA.
EMBL; D00503; BAA00395.1; -; Genomic_RNA.
PIR; A27032; GNWVWP.
RefSeq; NP_059433.1; NC_001477.1.
PDB; 3J8D; EM; 26.00 A; B/F=579-675.
PDB; 3L6P; X-ray; 2.20 A; A=1476-1648.
PDB; 3LKW; X-ray; 2.00 A; A=1476-1657.
PDB; 4AL8; X-ray; 1.66 A; C=575-675.
PDB; 4GSX; X-ray; 1.90 A; A/B=281-691.
PDB; 4GT0; X-ray; 2.57 A; A/B=281-701.
PDB; 4LCY; X-ray; 1.60 A; C/J=1741-1749.
PDB; 4OIG; X-ray; 2.69 A; A/B/D/E=947-1127.
PDB; 5VIC; X-ray; 3.00 A; E=578-676.
PDB; 5WJL; X-ray; 3.15 A; C/F/I=1608-1617.
PDB; 5WKF; X-ray; 2.95 A; C/H=1608-1617.
PDBsum; 3J8D; -.
PDBsum; 3L6P; -.
PDBsum; 3LKW; -.
PDBsum; 4AL8; -.
PDBsum; 4GSX; -.
PDBsum; 4GT0; -.
PDBsum; 4LCY; -.
PDBsum; 4OIG; -.
PDBsum; 5VIC; -.
PDBsum; 5WJL; -.
PDBsum; 5WKF; -.
SMR; P17763; -.
IntAct; P17763; 1.
PRIDE; P17763; -.
ABCD; P17763; -.
GeneID; 5075725; -.
KEGG; vg:5075725; -.
EvolutionaryTrace; P17763; -.
PRO; PR:P17763; -.
Proteomes; UP000002500; Genome.
GO; GO:0039714; C:cytoplasmic viral factory; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0033650; C:host cell mitochondrion; IEA:UniProtKB-SubCell.
GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
GO; GO:0044220; C:host cell perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0044385; C:integral to membrane of host cell; IEA:UniProtKB-KW.
GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0003725; F:double-stranded RNA binding; IEA:InterPro.
GO; GO:0005216; F:ion channel activity; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004482; F:mRNA (guanine-N7-)-methyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0004483; F:mRNA (nucleoside-2'-O-)-methyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
GO; GO:0075512; P:clathrin-dependent endocytosis of virus by host cell; IEA:UniProtKB-KW.
GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
GO; GO:0039520; P:induction by virus of host autophagy; IEA:UniProtKB-KW.
GO; GO:0039707; P:pore formation by virus in membrane of host cell; IEA:UniProtKB-KW.
GO; GO:0051259; P:protein complex oligomerization; IEA:UniProtKB-KW.
GO; GO:0039545; P:suppression by virus of host MAVS activity; IEA:UniProtKB-KW.
GO; GO:0039564; P:suppression by virus of host STAT2 activity; IEA:UniProtKB-KW.
GO; GO:0039574; P:suppression by virus of host TYK2 activity; IEA:UniProtKB-KW.
GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; IEA:UniProtKB-KW.
GO; GO:0046762; P:viral budding from ER membrane; IDA:UniProtKB.
GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
CDD; cd12149; Flavi_E_C; 1.
DisProt; DP01929; -.
Gene3D; 1.10.10.930; -; 1.
Gene3D; 1.10.8.970; -; 1.
Gene3D; 1.20.1280.260; -; 1.
Gene3D; 2.60.260.50; -; 1.
Gene3D; 2.60.40.350; -; 1.
Gene3D; 2.60.98.10; -; 1.
Gene3D; 3.30.387.10; -; 1.
Gene3D; 3.30.67.10; -; 1.
InterPro; IPR011492; DEAD_Flavivir.
InterPro; IPR000069; Env_glycoprot_M_flavivir.
InterPro; IPR038302; Env_glycoprot_M_sf_flavivir.
InterPro; IPR013755; Flav_gly_cen_dom_subdom1.
InterPro; IPR001122; Flavi_capsidC.
InterPro; IPR037172; Flavi_capsidC_sf.
InterPro; IPR027287; Flavi_E_Ig-like.
InterPro; IPR026470; Flavi_E_Stem/Anchor_dom.
InterPro; IPR038345; Flavi_E_Stem/Anchor_dom_sf.
InterPro; IPR001157; Flavi_NS1.
InterPro; IPR000752; Flavi_NS2A.
InterPro; IPR000487; Flavi_NS2B.
InterPro; IPR000404; Flavi_NS4A.
InterPro; IPR001528; Flavi_NS4B.
InterPro; IPR002535; Flavi_propep.
InterPro; IPR038688; Flavi_propep_sf.
InterPro; IPR000336; Flavivir/Alphavir_Ig-like_sf.
InterPro; IPR001850; Flavivirus_NS3_S7.
InterPro; IPR014412; Gen_Poly_FLV.
InterPro; IPR011998; Glycoprot_cen/dimer.
InterPro; IPR036253; Glycoprot_cen/dimer_sf.
InterPro; IPR038055; Glycoprot_E_dimer_dom.
InterPro; IPR013756; GlyE_cen_dom_subdom2.
InterPro; IPR014001; Helicase_ATP-bd.
InterPro; IPR001650; Helicase_C.
InterPro; IPR014756; Ig_E-set.
InterPro; IPR026490; mRNA_cap_0/1_MeTrfase.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR000208; RNA-dir_pol_flavivirus.
InterPro; IPR007094; RNA-dir_pol_PSvirus.
InterPro; IPR002877; rRNA_MeTrfase_FtsJ_dom.
InterPro; IPR029063; SAM-dependent_MTases.
Pfam; PF01003; Flavi_capsid; 1.
Pfam; PF07652; Flavi_DEAD; 1.
Pfam; PF02832; Flavi_glycop_C; 1.
Pfam; PF00869; Flavi_glycoprot; 1.
Pfam; PF01004; Flavi_M; 1.
Pfam; PF00948; Flavi_NS1; 1.
Pfam; PF01005; Flavi_NS2A; 1.
Pfam; PF01002; Flavi_NS2B; 1.
Pfam; PF01350; Flavi_NS4A; 1.
Pfam; PF01349; Flavi_NS4B; 1.
Pfam; PF00972; Flavi_NS5; 1.
Pfam; PF01570; Flavi_propep; 1.
Pfam; PF01728; FtsJ; 1.
Pfam; PF00949; Peptidase_S7; 1.
PIRSF; PIRSF003817; Gen_Poly_FLV; 1.
SMART; SM00487; DEXDc; 1.
SMART; SM00490; HELICc; 1.
SUPFAM; SSF101257; SSF101257; 1.
SUPFAM; SSF50494; SSF50494; 1.
SUPFAM; SSF52540; SSF52540; 2.
SUPFAM; SSF53335; SSF53335; 1.
SUPFAM; SSF56983; SSF56983; 1.
SUPFAM; SSF81296; SSF81296; 1.
TIGRFAMs; TIGR04240; flavi_E_stem; 1.
PROSITE; PS51527; FLAVIVIRUS_NS2B; 1.
PROSITE; PS51528; FLAVIVIRUS_NS3PRO; 1.
PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PROSITE; PS51194; HELICASE_CTER; 1.
PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PROSITE; PS51591; RNA_CAP01_NS5_MT; 1.
1: Evidence at protein level;
3D-structure; Activation of host autophagy by virus; ATP-binding;
Capsid protein; Clathrin-mediated endocytosis of virus by host;
Cleavage on pair of basic residues; Disulfide bond;
Fusion of virus membrane with host endosomal membrane;
Fusion of virus membrane with host membrane; Glycoprotein; Helicase;
Host cytoplasm; Host endoplasmic reticulum; Host membrane;
Host mitochondrion; Host nucleus; Host-virus interaction; Hydrolase;
Inhibition of host innate immune response by virus;
Inhibition of host interferon signaling pathway by virus;
Inhibition of host MAVS by virus; Inhibition of host RLR pathway by virus;
Inhibition of host STAT2 by virus; Inhibition of host TYK2 by virus;
Ion channel; Ion transport; Membrane; Metal-binding; Methyltransferase;
mRNA capping; mRNA processing; Multifunctional enzyme; Nucleotide-binding;
Nucleotidyltransferase; Phosphoprotein; Protease; Reference proteome;
RNA-binding; RNA-directed RNA polymerase; S-adenosyl-L-methionine;
Secreted; Serine protease; Suppressor of RNA silencing; Transcription;
Transcription regulation; Transferase; Transmembrane; Transmembrane helix;
Transport; Ubl conjugation; Viral attachment to host cell;
Viral envelope protein; Viral immunoevasion; Viral ion channel;
Viral penetration into host cytoplasm; Viral RNA replication; Virion;
Virus endocytosis by host; Virus entry into host cell; Zinc.
CHAIN 1..3392
/note="Genome polyprotein"
/id="PRO_0000405207"
CHAIN 1..100
/note="Capsid protein C"
/evidence="ECO:0000250|UniProtKB:P29990"
/id="PRO_0000264658"
PROPEP 101..114
/note="ER anchor for the capsid protein C, removed in
mature form by serine protease NS3"
/evidence="ECO:0000250|UniProtKB:P29990"
/id="PRO_0000264659"
CHAIN 115..280
/note="Protein prM"
/evidence="ECO:0000250|UniProtKB:P29990"
/id="PRO_0000264660"
CHAIN 115..205
/note="Peptide pr"
/evidence="ECO:0000250|UniProtKB:P29990"
/id="PRO_0000264661"
CHAIN 206..280
/note="Small envelope protein M"
/evidence="ECO:0000250|UniProtKB:P29990"
/id="PRO_0000264662"
CHAIN 281..775
/note="Envelope protein E"
/evidence="ECO:0000250|UniProtKB:P29990"
/id="PRO_0000264663"
CHAIN 776..1127
/note="Non-structural protein 1"
/evidence="ECO:0000250|UniProtKB:P29990"
/id="PRO_0000264664"
CHAIN 1128..1345
/note="Non-structural protein 2A"
/evidence="ECO:0000250|UniProtKB:P29990"
/id="PRO_0000264666"
CHAIN 1346..1475
/note="Serine protease subunit NS2B"
/evidence="ECO:0000250|UniProtKB:P29990"
/id="PRO_0000264667"
CHAIN 1476..2094
/note="Serine protease NS3"
/evidence="ECO:0000250|UniProtKB:P29990"
/id="PRO_0000264668"
CHAIN 2095..2221
/note="Non-structural protein 4A"
/evidence="ECO:0000250|UniProtKB:P29990"
/id="PRO_0000264669"
PEPTIDE 2222..2244
/note="Peptide 2k"
/evidence="ECO:0000250|UniProtKB:P29990"
/id="PRO_0000264670"
CHAIN 2245..2493
/note="Non-structural protein 4B"
/evidence="ECO:0000250|UniProtKB:P29990"
/id="PRO_0000264671"
CHAIN 2494..3392
/note="RNA-directed RNA polymerase NS5"
/evidence="ECO:0000250|UniProtKB:P29990"
/id="PRO_0000264672"
TOPO_DOM 1..101
/note="Cytoplasmic"
/evidence="ECO:0000255"
TRANSMEM 102..119
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 120..242
/note="Extracellular"
/evidence="ECO:0000255"
TRANSMEM 243..260
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 261
/note="Cytoplasmic"
/evidence="ECO:0000255"
TRANSMEM 262..280
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 281..725
/note="Extracellular"
/evidence="ECO:0000255"
TRANSMEM 726..746
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 747..752
/note="Cytoplasmic"
/evidence="ECO:0000255"
TRANSMEM 753..773
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 774..1195
/note="Extracellular"
/evidence="ECO:0000255"
TRANSMEM 1196..1220
/note="Helical"
/evidence="ECO:0000255, ECO:0000303|PubMed:23408612"
TOPO_DOM 1221..1226
/note="Cytoplasmic"
/evidence="ECO:0000255, ECO:0000303|PubMed:23408612"
TRANSMEM 1227..1245
/note="Helical"
/evidence="ECO:0000255, ECO:0000303|PubMed:23408612"
TOPO_DOM 1246..1269
/note="Lumenal"
/evidence="ECO:0000255, ECO:0000303|PubMed:23408612"
TRANSMEM 1270..1290
/note="Helical"
/evidence="ECO:0000255, ECO:0000303|PubMed:23408612"
TOPO_DOM 1291
/note="Cytoplasmic"
/evidence="ECO:0000255, ECO:0000303|PubMed:23408612"
TRANSMEM 1292..1310
/note="Helical"
/evidence="ECO:0000255, ECO:0000303|PubMed:23408612"
TOPO_DOM 1311..1315
/note="Lumenal"
/evidence="ECO:0000255, ECO:0000303|PubMed:23408612"
TRANSMEM 1316..1336
/note="Helical"
/evidence="ECO:0000255, ECO:0000303|PubMed:23408612"
TOPO_DOM 1337..1351
/note="Cytoplasmic"
/evidence="ECO:0000255, ECO:0000303|PubMed:23408612"
TRANSMEM 1352..1370
/note="Helical"
/evidence="ECO:0000269|PubMed:26072288"
TOPO_DOM 1371
/note="Lumenal"
/evidence="ECO:0000269|PubMed:26072288"
TRANSMEM 1372..1391
/note="Helical"
/evidence="ECO:0000269|PubMed:26072288"
TOPO_DOM 1392..1447
/note="Cytoplasmic"
/evidence="ECO:0000269|PubMed:26072288"
INTRAMEM 1448..1468
/note="Helical"
/evidence="ECO:0000269|PubMed:26072288"
TOPO_DOM 1469..2148
/note="Cytoplasmic"
/evidence="ECO:0000255"
TRANSMEM 2149..2169
/note="Helical"
/evidence="ECO:0000269|PubMed:17276984"
TOPO_DOM 2170..2171
/note="Lumenal"
/evidence="ECO:0000269|PubMed:17276984"
INTRAMEM 2172..2192
/note="Helical"
/evidence="ECO:0000269|PubMed:17276984"
TOPO_DOM 2193
/note="Lumenal"
/evidence="ECO:0000269|PubMed:17276984"
TRANSMEM 2194..2214
/note="Helical"
/evidence="ECO:0000269|PubMed:17276984"
TOPO_DOM 2215..2229
/note="Cytoplasmic"
/evidence="ECO:0000269|PubMed:17276984"
TRANSMEM 2230..2244
/note="Helical; Note=Signal for NS4B"
/evidence="ECO:0000255, ECO:0000269|PubMed:17276984,
ECO:0000305|PubMed:16436383"
TOPO_DOM 2245..2276
/note="Lumenal"
/evidence="ECO:0000305|PubMed:16436383"
INTRAMEM 2277..2297
/note="Helical"
/evidence="ECO:0000255, ECO:0000305|PubMed:16436383"
TOPO_DOM 2298..2349
/note="Lumenal"
/evidence="ECO:0000305|PubMed:16436383"
TRANSMEM 2350..2370
/note="Helical"
/evidence="ECO:0000255, ECO:0000305|PubMed:16436383"
TOPO_DOM 2371..2415
/note="Cytoplasmic"
/evidence="ECO:0000305|PubMed:16436383"
TRANSMEM 2416..2436
/note="Helical"
/evidence="ECO:0000255, ECO:0000305|PubMed:16436383"
TOPO_DOM 2437..2461
/note="Lumenal"
/evidence="ECO:0000305|PubMed:16436383"
TRANSMEM 2462..2482
/note="Helical"
/evidence="ECO:0000255, ECO:0000305|PubMed:16436383"
TOPO_DOM 2483..3392
/note="Cytoplasmic"
/evidence="ECO:0000305|PubMed:26072288"
DOMAIN 1476..1653
/note="Peptidase S7"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00860"
DOMAIN 1656..1812
/note="Helicase ATP-binding"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
DOMAIN 1822..1988
/note="Helicase C-terminal"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
DOMAIN 2495..2756
/note="mRNA cap 0-1 NS5-type MT"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
DOMAIN 3020..3169
/note="RdRp catalytic"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
NP_BIND 1669..1676
/note="ATP"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
REGION 1..15
/note="Interaction with host EXOC1"
/evidence="ECO:0000269|PubMed:19889084"
REGION 37..72
/note="Hydrophobic; homodimerization of capsid protein C"
/evidence="ECO:0000250|UniProtKB:P29990"
REGION 378..391
/note="Fusion peptide"
/evidence="ECO:0000250|UniProtKB:P14336"
REGION 1398..1437
/note="Interacts with and activates NS3 protease"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00859"
REGION 1660..1663
/note="Important for RNA-binding"
/evidence="ECO:0000250|UniProtKB:P14340"
MOTIF 1760..1763
/note="DEAH box"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
MOTIF 2570..2573
/note="SUMO-interacting motif"
/evidence="ECO:0000250|UniProtKB:P29990"
ACT_SITE 1526
/note="Charge relay system; for serine protease NS3
activity"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00860"
ACT_SITE 1550
/note="Charge relay system; for serine protease NS3
activity"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00860"
ACT_SITE 1610
/note="Charge relay system; for serine protease NS3
activity"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00860"
ACT_SITE 2554
/note="For 2'-O-MTase activity"
/evidence="ECO:0000250|UniProtKB:Q6YMS4"
ACT_SITE 2639
/note="For 2'-O-MTase activity"
/evidence="ECO:0000250|UniProtKB:Q6YMS4"
ACT_SITE 2673
/note="For 2'-O-MTase activity"
/evidence="ECO:0000250|UniProtKB:Q6YMS4"
ACT_SITE 2709
/note="For 2'-O-MTase activity"
/evidence="ECO:0000250|UniProtKB:Q6YMS4"
METAL 2930
/note="Zinc 1"
/evidence="ECO:0000250|UniProtKB:Q6YMS4"
METAL 2934
/note="Zinc 1; via tele nitrogen"
/evidence="ECO:0000250|UniProtKB:Q6YMS4"
METAL 2939
/note="Zinc 1"
/evidence="ECO:0000250|UniProtKB:Q6YMS4"
METAL 2942
/note="Zinc 1"
/evidence="ECO:0000250|UniProtKB:Q6YMS4"
METAL 3204
/note="Zinc 2; via tele nitrogen"
/evidence="ECO:0000250|UniProtKB:Q6YMS4"
METAL 3220
/note="Zinc 2"
/evidence="ECO:0000250|UniProtKB:Q6YMS4"
METAL 3339
/note="Zinc 2"
/evidence="ECO:0000250|UniProtKB:Q6YMS4"
BINDING 2549
/note="S-adenosyl-L-methionine"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
BINDING 2579
/note="S-adenosyl-L-methionine; via carbonyl oxygen"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
BINDING 2580
/note="S-adenosyl-L-methionine; via carbonyl oxygen"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
BINDING 2597
/note="S-adenosyl-L-methionine"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
BINDING 2598
/note="S-adenosyl-L-methionine; via carbonyl oxygen"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
BINDING 2624
/note="S-adenosyl-L-methionine"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
BINDING 2625
/note="S-adenosyl-L-methionine; via carbonyl oxygen"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
BINDING 2640
/note="S-adenosyl-L-methionine"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
BINDING 2711
/note="S-adenosyl-L-methionine"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
SITE 100..101
/note="Cleavage; by viral protease NS3"
/evidence="ECO:0000250|UniProtKB:P29990"
SITE 114..115
/note="Cleavage; by host signal peptidase"
/evidence="ECO:0000250|UniProtKB:P29990"
SITE 205..206
/note="Cleavage; by host furin"
/evidence="ECO:0000250|UniProtKB:P29990, ECO:0000255"
SITE 280..281
/note="Cleavage; by host signal peptidase"
/evidence="ECO:0000250|UniProtKB:P29990"
SITE 775..776
/note="Cleavage; by host signal peptidase"
/evidence="ECO:0000250|UniProtKB:P29990"
SITE 1127..1128
/note="Cleavage; by host"
/evidence="ECO:0000250|UniProtKB:P29990"
SITE 1345..1346
/note="Cleavage; by viral protease NS3"
/evidence="ECO:0000250|UniProtKB:P29990"
SITE 1475..1476
/note="Cleavage; by autolysis"
/evidence="ECO:0000250|UniProtKB:P29990"
SITE 1933
/note="Involved in NS3 ATPase and RTPase activities"
/evidence="ECO:0000250|UniProtKB:P14335"
SITE 1936
/note="Involved in NS3 ATPase and RTPase activities"
/evidence="ECO:0000250|UniProtKB:P14335"
SITE 2094..2095
/note="Cleavage; by autolysis"
/evidence="ECO:0000250|UniProtKB:P29990"
SITE 2221..2222
/note="Cleavage; by viral protease NS3"
/evidence="ECO:0000250|UniProtKB:P29990"
SITE 2244..2245
/note="Cleavage; by host signal peptidase"
/evidence="ECO:0000250|UniProtKB:P29990"
SITE 2493..2494
/note="Cleavage; by viral protease NS3"
/evidence="ECO:0000250|UniProtKB:P29990"
SITE 2507
/note="mRNA cap binding"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
SITE 2510
/note="mRNA cap binding; via carbonyl oxygen"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
SITE 2511
/note="mRNA cap binding"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
SITE 2513
/note="mRNA cap binding; via carbonyl oxygen"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
SITE 2518
/note="mRNA cap binding"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
SITE 2522
/note="mRNA cap binding"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
SITE 2554
/note="Essential for 2'-O-methyltransferase activity"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
SITE 2639
/note="Essential for 2'-O-methyltransferase and N-7
methyltransferase activity"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
SITE 2643
/note="mRNA cap binding"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
SITE 2673
/note="Essential for 2'-O-methyltransferase activity"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
SITE 2704
/note="mRNA cap binding"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
SITE 2706
/note="mRNA cap binding"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
SITE 2709
/note="Essential for 2'-O-methyltransferase activity"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
MOD_RES 2549
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P03314"
CARBOHYD 183
/note="N-linked (GlcNAc...) asparagine; by host"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
CARBOHYD 347
/note="N-linked (GlcNAc...) asparagine; by host"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
CARBOHYD 433
/note="N-linked (GlcNAc...) asparagine; by host"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
CARBOHYD 905
/note="N-linked (GlcNAc...) asparagine; by host"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
CARBOHYD 982
/note="N-linked (GlcNAc...) asparagine; by host"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
CARBOHYD 1190
/note="N-linked (GlcNAc...) asparagine; by host"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
CARBOHYD 2303
/note="N-linked (GlcNAc...) asparagine; by host"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
CARBOHYD 2307
/note="N-linked (GlcNAc...) asparagine; by host"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
CARBOHYD 2459
/note="N-linked (GlcNAc...) asparagine; by host"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
DISULFID 283..310
/evidence="ECO:0000269|PubMed:14963174"
DISULFID 340..401
/evidence="ECO:0000269|PubMed:14963174"
DISULFID 354..385
/evidence="ECO:0000269|PubMed:14963174"
DISULFID 372..396
/evidence="ECO:0000269|PubMed:14963174"
DISULFID 465..565
/evidence="ECO:0000269|PubMed:14963174"
DISULFID 582..613
/evidence="ECO:0000269|PubMed:14963174"
DISULFID 779..790
/evidence="ECO:0000269|PubMed:14981082"
DISULFID 830..918
/evidence="ECO:0000269|PubMed:14981082"
DISULFID 954..998
/evidence="ECO:0000269|PubMed:14981082"
DISULFID 1055..1104
/evidence="ECO:0000269|PubMed:14981082"
DISULFID 1066..1088
/evidence="ECO:0000269|PubMed:14981082"
DISULFID 1087..1091
/evidence="ECO:0000269|PubMed:14981082"
VARIANT 125..126
/note="HM -> TL (in strain: Isolate Philippines/836-1/
1984)"
VARIANT 142
/note="S -> P (in strain: Isolate Philippines/836-1/1984)"
VARIANT 171..173
/note="TET -> AEA (in strain: Isolate Philippines/836-1/
1984)"
VARIANT 186
/note="E -> D (in strain: Isolate Philippines/836-1/1984)"
VARIANT 210
/note="A -> D (in strain: Isolate Philippines/836-1/1984)"
VARIANT 251
/note="A -> G (in strain: Isolate Philippines/836-1/1984)"
VARIANT 441
/note="T -> I (in strain: Isolate Philippines/836-1/1984)"
VARIANT 475
/note="E -> R (in strain: Isolate Philippines/836-1/1984)"
VARIANT 482
/note="E -> K (in strain: Isolate 45AZ5)"
VARIANT 573
/note="T -> I (in strain: Isolate 45AZ5)"
VARIANT 677
/note="S -> T (in strain: Isolate Philippines/836-1/1984)"
VARIANT 786
/note="R -> K (in strain: Isolate Philippines/836-1/1984)"
VARIANT 1689..1692
/note="RRNV -> KRKL (in strain: Isolate 45AZ5)"
VARIANT 2242
/note="A -> V (in strain: Isolate 45AZ5)"
VARIANT 2357
/note="F -> L (in strain: Isolate 45AZ5)"
VARIANT 2543
/note="P -> T (in strain: Isolate 45AZ5)"
VARIANT 2779
/note="G -> E (in strain: Isolate 45AZ5)"
VARIANT 3337
/note="R -> Q (in strain: Isolate 45AZ5)"
MUTAGEN 1138
/note="G->A: Impaired virion assembly."
/evidence="ECO:0000269|PubMed:25392211"
MUTAGEN 1147
/note="E->A: Impaired virion assembly."
/evidence="ECO:0000269|PubMed:25392211"
MUTAGEN 1227
/note="E->A: Impaired virion assembly."
/evidence="ECO:0000269|PubMed:25392211"
MUTAGEN 1252
/note="D->A: Complete loss of viral RNA synthesis."
/evidence="ECO:0000269|PubMed:25392211"
MUTAGEN 1314
/note="Q->A: Impaired virion assembly."
/evidence="ECO:0000269|PubMed:25392211"
MUTAGEN 1315
/note="K->A: Impaired virion assembly."
/evidence="ECO:0000269|PubMed:25392211"
MUTAGEN 1327
/note="G->A: Complete loss of viral RNA synthesis."
/evidence="ECO:0000269|PubMed:25392211"
HELIX 288..290
/evidence="ECO:0000244|PDB:4GSX"
STRAND 291..293
/evidence="ECO:0000244|PDB:4GSX"
STRAND 295..308
/evidence="ECO:0000244|PDB:4GSX"
STRAND 311..313
/evidence="ECO:0000244|PDB:4GSX"
STRAND 321..332
/evidence="ECO:0000244|PDB:4GSX"
STRAND 334..352
/evidence="ECO:0000244|PDB:4GSX"
HELIX 363..366
/evidence="ECO:0000244|PDB:4GSX"
STRAND 370..379
/evidence="ECO:0000244|PDB:4GSX"
HELIX 381..383
/evidence="ECO:0000244|PDB:4GSX"
STRAND 389..409
/evidence="ECO:0000244|PDB:4GSX"
HELIX 412..414
/evidence="ECO:0000244|PDB:4GSX"
STRAND 415..423
/evidence="ECO:0000244|PDB:4GSX"
STRAND 440..444
/evidence="ECO:0000244|PDB:4GSX"
STRAND 450..455
/evidence="ECO:0000244|PDB:4GSX"
TURN 456..458
/evidence="ECO:0000244|PDB:4GSX"
STRAND 459..467
/evidence="ECO:0000244|PDB:4GSX"
TURN 473..475
/evidence="ECO:0000244|PDB:4GSX"
STRAND 476..481
/evidence="ECO:0000244|PDB:4GSX"
STRAND 484..489
/evidence="ECO:0000244|PDB:4GSX"
HELIX 490..494
/evidence="ECO:0000244|PDB:4GSX"
STRAND 500..504
/evidence="ECO:0000244|PDB:4GSX"
HELIX 514..516
/evidence="ECO:0000244|PDB:4GSX"
STRAND 518..520
/evidence="ECO:0000244|PDB:4GSX"
STRAND 530..532
/evidence="ECO:0000244|PDB:4GSX"
HELIX 537..543
/evidence="ECO:0000244|PDB:4GSX"
TURN 544..546
/evidence="ECO:0000244|PDB:4GSX"
STRAND 547..553
/evidence="ECO:0000244|PDB:4GSX"
STRAND 556..559
/evidence="ECO:0000244|PDB:4GSX"
STRAND 562..571
/evidence="ECO:0000244|PDB:4GSX"
STRAND 586..590
/evidence="ECO:0000244|PDB:4AL8"
STRAND 596..598
/evidence="ECO:0000244|PDB:4GT0"
STRAND 600..606
/evidence="ECO:0000244|PDB:4AL8"
STRAND 612..614
/evidence="ECO:0000244|PDB:4AL8"
STRAND 617..620
/evidence="ECO:0000244|PDB:4AL8"
STRAND 633..635
/evidence="ECO:0000244|PDB:4AL8"
STRAND 637..639
/evidence="ECO:0000244|PDB:4AL8"
STRAND 645..649
/evidence="ECO:0000244|PDB:4AL8"
STRAND 653..663
/evidence="ECO:0000244|PDB:4AL8"
STRAND 667..673
/evidence="ECO:0000244|PDB:4AL8"
TURN 956..958
/evidence="ECO:0000244|PDB:4OIG"
STRAND 960..964
/evidence="ECO:0000244|PDB:4OIG"
STRAND 967..971
/evidence="ECO:0000244|PDB:4OIG"
STRAND 973..994
/evidence="ECO:0000244|PDB:4OIG"
HELIX 1002..1004
/evidence="ECO:0000244|PDB:4OIG"
HELIX 1013..1015
/evidence="ECO:0000244|PDB:4OIG"
HELIX 1020..1022
/evidence="ECO:0000244|PDB:4OIG"
HELIX 1028..1030
/evidence="ECO:0000244|PDB:4OIG"
HELIX 1043..1045
/evidence="ECO:0000244|PDB:4OIG"
STRAND 1046..1053
/evidence="ECO:0000244|PDB:4OIG"
STRAND 1059..1062
/evidence="ECO:0000244|PDB:4OIG"
STRAND 1073..1076
/evidence="ECO:0000244|PDB:4OIG"
STRAND 1085..1090
/evidence="ECO:0000244|PDB:4OIG"
STRAND 1096..1099
/evidence="ECO:0000244|PDB:4OIG"
STRAND 1104..1106
/evidence="ECO:0000244|PDB:4OIG"
STRAND 1111..1114
/evidence="ECO:0000244|PDB:4OIG"
STRAND 1501..1504
/evidence="ECO:0000244|PDB:3LKW"
STRAND 1507..1517
/evidence="ECO:0000244|PDB:3LKW"
STRAND 1520..1523
/evidence="ECO:0000244|PDB:3LKW"
HELIX 1525..1528
/evidence="ECO:0000244|PDB:3LKW"
STRAND 1533..1535
/evidence="ECO:0000244|PDB:3LKW"
STRAND 1538..1540
/evidence="ECO:0000244|PDB:3LKW"
STRAND 1542..1546
/evidence="ECO:0000244|PDB:3LKW"
TURN 1547..1550
/evidence="ECO:0000244|PDB:3LKW"
STRAND 1551..1557
/evidence="ECO:0000244|PDB:3LKW"
STRAND 1570..1574
/evidence="ECO:0000244|PDB:3LKW"
STRAND 1582..1586
/evidence="ECO:0000244|PDB:3LKW"
STRAND 1589..1593
/evidence="ECO:0000244|PDB:3LKW"
STRAND 1596..1601
/evidence="ECO:0000244|PDB:3LKW"
STRAND 1613..1615
/evidence="ECO:0000244|PDB:3LKW"
STRAND 1621..1625
/evidence="ECO:0000244|PDB:3LKW"
STRAND 1628..1630
/evidence="ECO:0000244|PDB:3LKW"
STRAND 1636..1639
/evidence="ECO:0000244|PDB:3LKW"
SEQUENCE 3392 AA; 378702 MW; 3A7C57D3054D2972 CRC64;
MNNQRKKTGR PSFNMLKRAR NRVSTVSQLA KRFSKGLLSG QGPMKLVMAF IAFLRFLAIP
PTAGILARWG SFKKNGAIKV LRGFKKEISN MLNIMNRRKR SVTMLLMLLP TALAFHLTTR
GGEPHMIVSK QERGKSLLFK TSAGVNMCTL IAMDLGELCE DTMTYKCPRI TETEPDDVDC
WCNATETWVT YGTCSQTGEH RRDKRSVALA PHVGLGLETR TETWMSSEGA WKQIQKVETW
ALRHPGFTVI ALFLAHAIGT SITQKGIIFI LLMLVTPSMA MRCVGIGNRD FVEGLSGATW
VDVVLEHGSC VTTMAKDKPT LDIELLKTEV TNPAVLRKLC IEAKISNTTT DSRCPTQGEA
TLVEEQDTNF VCRRTFVDRG WGNGCGLFGK GSLITCAKFK CVTKLEGKIV QYENLKYSVI
VTVHTGDQHQ VGNETTEHGT TATITPQAPT SEIQLTDYGA LTLDCSPRTG LDFNEMVLLT
MEKKSWLVHK QWFLDLPLPW TSGASTSQET WNRQDLLVTF KTAHAKKQEV VVLGSQEGAM
HTALTGATEI QTSGTTTIFA GHLKCRLKMD KLTLKGMSYV MCTGSFKLEK EVAETQHGTV
LVQVKYEGTD APCKIPFSSQ DEKGVTQNGR LITANPIVTD KEKPVNIEAE PPFGESYIVV
GAGEKALKLS WFKKGSSIGK MFEATARGAR RMAILGDTAW DFGSIGGVFT SVGKLIHQIF
GTAYGVLFSG VSWTMKIGIG ILLTWLGLNS RSTSLSMTCI AVGMVTLYLG VMVQADSGCV
INWKGRELKC GSGIFVTNEV HTWTEQYKFQ ADSPKRLSAA IGKAWEEGVC GIRSATRLEN
IMWKQISNEL NHILLENDMK FTVVVGDVSG ILAQGKKMIR PQPMEHKYSW KSWGKAKIIG
ADVQNTTFII DGPNTPECPD NQRAWNIWEV EDYGFGIFTT NIWLKLRDSY TQVCDHRLMS
AAIKDSKAVH ADMGYWIESE KNETWKLARA SFIEVKTCIW PKSHTLWSNG VLESEMIIPK
IYGGPISQHN YRPGYFTQTA GPWHLGKLEL DFDLCEGTTV VVDEHCGNRG PSLRTTTVTG
KTIHEWCCRS CTLPPLRFKG EDGCWYGMEI RPVKEKEENL VKSMVSAGSG EVDSFSLGLL
CISIMIEEVM RSRWSRKMLM TGTLAVFLLL TMGQLTWNDL IRLCIMVGAN ASDKMGMGTT
YLALMATFRM RPMFAVGLLF RRLTSREVLL LTVGLSLVAS VELPNSLEEL GDGLAMGIMM
LKLLTDFQSH QLWATLLSLT FVKTTFSLHY AWKTMAMILS IVSLFPLCLS TTSQKTTWLP
VLLGSLGCKP LTMFLITENK IWGRKSWPLN EGIMAVGIVS ILLSSLLKND VPLAGPLIAG
GMLIACYVIS GSSADLSLEK AAEVSWEEEA EHSGASHNIL VEVQDDGTMK IKDEERDDTL
TILLKATLLA ISGVYPMSIP ATLFVWYFWQ KKKQRSGVLW DTPSPPEVER AVLDDGIYRI
LQRGLLGRSQ VGVGVFQEGV FHTMWHVTRG AVLMYQGKRL EPSWASVKKD LISYGGGWRF
QGSWNAGEEV QVIAVEPGKN PKNVQTAPGT FKTPEGEVGA IALDFKPGTS GSPIVNREGK
IVGLYGNGVV TTSGTYVSAI AQAKASQEGP LPEIEDEVFR KRNLTIMDLH PGSGKTRRYL
PAIVREAIRR NVRTLVLAPT RVVASEMAEA LKGMPIRYQT TAVKSEHTGK EIVDLMCHAT
FTMRLLSPVR VPNYNMIIMD EAHFTDPASI AARGYISTRV GMGEAAAIFM TATPPGSVEA
FPQSNAVIQD EERDIPERSW NSGYDWITDF PGKTVWFVPS IKSGNDIANC LRKNGKRVVQ
LSRKTFDTEY QKTKNNDWDY VVTTDISEMG ANFRADRVID PRRCLKPVIL KDGPERVILA
GPMPVTVASA AQRRGRIGRN QNKEGDQYIY MGQPLNNDED HAHWTEAKML LDNINTPEGI
IPALFEPERE KSAAIDGEYR LRGEARKTFV ELMRRGDLPV WLSYKVASEG FQYSDRRWCF
DGERNNQVLE ENMDVEIWTK EGERKKLRPR WLDARTYSDP LALREFKEFA AGRRSVSGDL
ILEIGKLPQH LTQRAQNALD NLVMLHNSEQ GGKAYRHAME ELPDTIETLM LLALIAVLTG
GVTLFFLSGR GLGKTSIGLL CVIASSALLW MASVEPHWIA ASIILEFFLM VLLIPEPDRQ
RTPQDNQLAY VVIGLLFMIL TAAANEMGLL ETTKKDLGIG HAAAENHHHA AMLDVDLHPA
SAWTLYAVAT TIITPMMRHT IENTTANISL TAIANQAAIL MGLDKGWPIS KMDIGVPLLA
LGCYSQVNPL TLTAAVFMLV AHYAIIGPGL QAKATREAQK RTAAGIMKNP TVDGIVAIDL
DPVVYDAKFE KQLGQIMLLI LCTSQILLMR TTWALCESIT LATGPLTTLW EGSPGKFWNT
TIAVSMANIF RGSYLAGAGL AFSLMKSLGG GRRGTGAQGE TLGEKWKRQL NQLSKSEFNT
YKRSGIIEVD RSEAKEGLKR GEPTKHAVSR GTAKLRWFVE RNLVKPEGKV IDLGCGRGGW
SYYCAGLKKV TEVKGYTKGG PGHEEPIPMA TYGWNLVKLY SGKDVFFTPP EKCDTLLCDI
GESSPNPTIE EGRTLRVLKM VEPWLRGNQF CIKILNPYMP SVVETLEQMQ RKHGGMLVRN
PLSRNSTHEM YWVSCGTGNI VSAVNMTSRM LLNRFTMAHR KPTYERDVDL GAGTRHVAVE
PEVANLDIIG QRIENIKNGH KSTWHYDEDN PYKTWAYHGS YEVKPSGSAS SMVNGVVRLL
TKPWDVIPMV TQIAMTDTTP FGQQRVFKEK VDTRTPKAKR GTAQIMEVTA RWLWGFLSRN
KKPRICTREE FTRKVRSNAA IGAVFVDENQ WNSAKEAVED ERFWDLVHRE RELHKQGKCA
TCVYNMMGKR EKKLGEFGKA KGSRAIWYMW LGARFLEFEA LGFMNEDHWF SRENSLSGVE
GEGLHKLGYI LRDISKIPGG NMYADDTAGW DTRITEDDLQ NEAKITDIME PEHALLATSI
FKLTYQNKVV RVQRPAKNGT VMDVISRRDQ RGSGQVGTYG LNTFTNMEAQ LIRQMESEGI
FSPSELETPN LAERVLDWLK KHGTERLKRM AISGDDCVVK PIDDRFATAL TALNDMGKVR
KDIPQWEPSK GWNDWQQVPF CSHHFHQLIM KDGREIVVPC RNQDELVGRA RVSQGAGWSL
RETACLGKSY AQMWQLMYFH RRDLRLAANA ICSAVPVDWV PTSRTTWSIH AHHQWMTTED
MLSVWNRVWI EENPWMEDKT HVSSWEDVPY LGKREDRWCG SLIGLTARAT WATNIQVAIN
QVRRLIGNEN YLDFMTSMKR FKNESDPEGA LW


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