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 POLG_DEN1W              Reviewed;        3392 AA.
P17763; P27910; P89313; P89314;
01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
12-DEC-2006, sequence version 2.
25-OCT-2017, entry version 156.
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; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Flaviviridae; Flavivirus; Dengue virus group.
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;
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]
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).
[46]
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 particule 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: Non-structural protein 2B: 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. {ECO:0000250|UniProtKB:Q9Q6P4}.
-!- 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: 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. {ECO:0000269|PubMed:15917225}.
-!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate
+ RNA(n+1). {ECO:0000255|PROSITE-ProRule:PRU00539}.
-!- CATALYTIC ACTIVITY: NTP + H(2)O = NDP + phosphate.
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + G(5')pppR-RNA = S-
adenosyl-L-homocysteine + m(7)G(5')pppR-RNA. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + a 5'-(N(7)-methyl
5'-triphosphoguanosine)-(purine-ribonucleotide)-[mRNA] = S-
adenosyl-L-homocysteine + a 5'-(N(7)-methyl 5'-
triphosphoguanosine)-(2'-O-methyl-purine-ribonucleotide)-[mRNA].
{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).
Protein prM: Forms heterodimers with envelope protein E in the
endoplasmic reticulum and Golgi (PubMed:9971841). 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). Non-
structural protein 1: Homodimer; Homohexamer when secreted
(PubMed:2827377, PubMed:10364366). Interacts with envelope protein
E (PubMed:26562291). Non-structural protein 2A: Interacts (via N-
terminus) with serine protease NS3. Non-structural protein 2B:
Forms a heterodimer with serine protease NS3 (PubMed:20042502).
May form homooligomers (PubMed:26728778). 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). Non-structural protein 4B:
Interacts with serine protease NS3 (PubMed:16894199). 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:10364366, ECO:0000269|PubMed:11893341,
ECO:0000269|PubMed:15917225, ECO:0000269|PubMed:16894199,
ECO:0000269|PubMed:19279106, ECO:0000269|PubMed:19850911,
ECO:0000269|PubMed:19889084, ECO:0000269|PubMed:20042502,
ECO:0000269|PubMed:23522008, ECO:0000269|PubMed:26562291,
ECO:0000269|PubMed:26728778, ECO:0000269|PubMed:26895240,
ECO:0000269|PubMed:2827377, ECO:0000269|PubMed:9971841}.
-!- 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}. Note=Located in
RE-associated vesicles hosting the replication complex.
{ECO:0000269|PubMed:17276984}.
-!- 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; 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.
PDBsum; 3L6P; -.
PDBsum; 3LKW; -.
PDBsum; 4AL8; -.
PDBsum; 4GSX; -.
PDBsum; 4GT0; -.
PDBsum; 4LCY; -.
PDBsum; 4OIG; -.
PDBsum; 5VIC; -.
ProteinModelPortal; P17763; -.
SMR; P17763; -.
IntAct; P17763; 1.
GeneID; 5075725; -.
KEGG; vg:5075725; -.
OrthoDB; VOG0900007N; -.
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: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:0008026; F:ATP-dependent helicase activity; IEA:InterPro.
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:InterPro.
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:0070008; F:serine-type exopeptidase 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 oligomerization; IEA:UniProtKB-KW.
GO; GO:0006355; P:regulation of transcription, DNA-templated; 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:0006351; P:transcription, DNA-templated; 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.
CDD; cd00079; HELICc; 1.
Gene3D; 2.60.40.350; -; 1.
Gene3D; 3.30.387.10; -; 1.
Gene3D; 3.30.67.10; -; 1.
InterPro; IPR011492; DEAD_Flavivir.
InterPro; IPR000069; Env_glycoprot_M_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; IPR001157; Flavi_NS1.
InterPro; IPR000752; Flavi_NS2A.
InterPro; IPR000487; Flavi_NS2B.
InterPro; IPR000404; Flavi_NS4A.
InterPro; IPR001528; Flavi_NS4B.
InterPro; IPR002535; Flavi_propep.
InterPro; IPR000336; Flavivir/Alphavir_Ig-like.
InterPro; IPR001850; Flavivirus_NS3_S7.
InterPro; IPR014412; Gen_Poly_FLV.
InterPro; IPR011998; Glycoprot_cen/dimer.
InterPro; IPR036253; Glycoprot_cen/dimer_sf.
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; Complete proteome; 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 nucleus; Host-virus interaction; Hydrolase;
Inhibition of host innate immune response by virus;
Inhibition of host interferon signaling 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 Genome polyprotein.
/FTId=PRO_0000405207.
CHAIN 1 100 Capsid protein C.
{ECO:0000250|UniProtKB:P29990}.
/FTId=PRO_0000264658.
PROPEP 101 114 ER anchor for the capsid protein C,
removed in mature form by serine protease
NS3. {ECO:0000250|UniProtKB:P29990}.
/FTId=PRO_0000264659.
CHAIN 115 280 Protein prM.
{ECO:0000250|UniProtKB:P29990}.
/FTId=PRO_0000264660.
CHAIN 115 205 Peptide pr.
{ECO:0000250|UniProtKB:P29990}.
/FTId=PRO_0000264661.
CHAIN 206 280 Small envelope protein M.
{ECO:0000250|UniProtKB:P29990}.
/FTId=PRO_0000264662.
CHAIN 281 775 Envelope protein E.
{ECO:0000250|UniProtKB:P29990}.
/FTId=PRO_0000264663.
CHAIN 776 1127 Non-structural protein 1.
{ECO:0000250|UniProtKB:P29990}.
/FTId=PRO_0000264664.
CHAIN 1128 1345 Non-structural protein 2A.
{ECO:0000250|UniProtKB:P29990}.
/FTId=PRO_0000264666.
CHAIN 1346 1475 Serine protease subunit NS2B.
{ECO:0000250|UniProtKB:P29990}.
/FTId=PRO_0000264667.
CHAIN 1476 2094 Serine protease NS3.
{ECO:0000250|UniProtKB:P29990}.
/FTId=PRO_0000264668.
CHAIN 2095 2221 Non-structural protein 4A.
{ECO:0000250|UniProtKB:P29990}.
/FTId=PRO_0000264669.
PEPTIDE 2222 2244 Peptide 2k.
{ECO:0000250|UniProtKB:P29990}.
/FTId=PRO_0000264670.
CHAIN 2245 2493 Non-structural protein 4B.
{ECO:0000250|UniProtKB:P29990}.
/FTId=PRO_0000264671.
CHAIN 2494 3392 RNA-directed RNA polymerase NS5.
{ECO:0000250|UniProtKB:P29990}.
/FTId=PRO_0000264672.
TOPO_DOM 1 101 Cytoplasmic. {ECO:0000255}.
TRANSMEM 102 119 Helical. {ECO:0000255}.
TOPO_DOM 120 242 Extracellular. {ECO:0000255}.
TRANSMEM 243 260 Helical. {ECO:0000255}.
TOPO_DOM 261 261 Cytoplasmic. {ECO:0000255}.
TRANSMEM 262 280 Helical. {ECO:0000255}.
TOPO_DOM 281 725 Extracellular. {ECO:0000255}.
TRANSMEM 726 746 Helical. {ECO:0000255}.
TOPO_DOM 747 752 Cytoplasmic. {ECO:0000255}.
TRANSMEM 753 773 Helical. {ECO:0000255}.
TOPO_DOM 774 1195 Extracellular. {ECO:0000255}.
TRANSMEM 1196 1220 Helical. {ECO:0000255,
ECO:0000303|PubMed:23408612}.
TOPO_DOM 1221 1226 Cytoplasmic. {ECO:0000255,
ECO:0000303|PubMed:23408612}.
TRANSMEM 1227 1245 Helical. {ECO:0000255,
ECO:0000303|PubMed:23408612}.
TOPO_DOM 1246 1269 Lumenal. {ECO:0000255,
ECO:0000303|PubMed:23408612}.
TRANSMEM 1270 1290 Helical. {ECO:0000255,
ECO:0000303|PubMed:23408612}.
TOPO_DOM 1291 1291 Cytoplasmic. {ECO:0000255,
ECO:0000303|PubMed:23408612}.
TRANSMEM 1292 1310 Helical. {ECO:0000255,
ECO:0000303|PubMed:23408612}.
TOPO_DOM 1311 1315 Lumenal. {ECO:0000255,
ECO:0000303|PubMed:23408612}.
TRANSMEM 1316 1336 Helical. {ECO:0000255,
ECO:0000303|PubMed:23408612}.
TOPO_DOM 1337 1351 Cytoplasmic. {ECO:0000255,
ECO:0000303|PubMed:23408612}.
TRANSMEM 1352 1370 Helical. {ECO:0000269|PubMed:26072288}.
TOPO_DOM 1371 1371 Lumenal. {ECO:0000269|PubMed:26072288}.
TRANSMEM 1372 1391 Helical. {ECO:0000269|PubMed:26072288}.
TOPO_DOM 1392 1447 Cytoplasmic.
{ECO:0000269|PubMed:26072288}.
INTRAMEM 1448 1468 Helical. {ECO:0000269|PubMed:26072288}.
TOPO_DOM 1469 2148 Cytoplasmic. {ECO:0000255}.
TRANSMEM 2149 2169 Helical. {ECO:0000269|PubMed:17276984}.
TOPO_DOM 2170 2171 Lumenal. {ECO:0000269|PubMed:17276984}.
INTRAMEM 2172 2192 Helical. {ECO:0000269|PubMed:17276984}.
TOPO_DOM 2193 2193 Lumenal. {ECO:0000269|PubMed:17276984}.
TRANSMEM 2194 2214 Helical. {ECO:0000269|PubMed:17276984}.
TOPO_DOM 2215 2229 Cytoplasmic.
{ECO:0000269|PubMed:17276984}.
TRANSMEM 2230 2244 Helical; Note=Signal for NS4B.
{ECO:0000255,
ECO:0000269|PubMed:17276984,
ECO:0000305|PubMed:16436383}.
TOPO_DOM 2245 2276 Lumenal. {ECO:0000305|PubMed:16436383}.
INTRAMEM 2277 2297 Helical. {ECO:0000255,
ECO:0000305|PubMed:16436383}.
TOPO_DOM 2298 2349 Lumenal. {ECO:0000305|PubMed:16436383}.
TRANSMEM 2350 2370 Helical. {ECO:0000255,
ECO:0000305|PubMed:16436383}.
TOPO_DOM 2371 2415 Cytoplasmic.
{ECO:0000305|PubMed:16436383}.
TRANSMEM 2416 2436 Helical. {ECO:0000255,
ECO:0000305|PubMed:16436383}.
TOPO_DOM 2437 2461 Lumenal. {ECO:0000305|PubMed:16436383}.
TRANSMEM 2462 2482 Helical. {ECO:0000255,
ECO:0000305|PubMed:16436383}.
TOPO_DOM 2483 3392 Cytoplasmic.
{ECO:0000305|PubMed:26072288}.
DOMAIN 1476 1653 Peptidase S7. {ECO:0000255|PROSITE-
ProRule:PRU00860}.
DOMAIN 1656 1812 Helicase ATP-binding.
{ECO:0000255|PROSITE-ProRule:PRU00541}.
DOMAIN 1822 1988 Helicase C-terminal.
{ECO:0000255|PROSITE-ProRule:PRU00542}.
DOMAIN 2495 2756 mRNA cap 0-1 NS5-type MT.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
DOMAIN 3020 3169 RdRp catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00539}.
NP_BIND 1669 1676 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00541}.
REGION 1 15 Interaction with host EXOC1.
{ECO:0000269|PubMed:19889084}.
REGION 37 72 Hydrophobic; homodimerization of capsid
protein C.
{ECO:0000250|UniProtKB:P29990}.
REGION 378 391 Fusion peptide.
{ECO:0000250|UniProtKB:P14336}.
REGION 1398 1437 Interacts with and activates NS3
protease. {ECO:0000255|PROSITE-
ProRule:PRU00859}.
REGION 1660 1663 Important for RNA-binding.
{ECO:0000250|UniProtKB:P14340}.
MOTIF 1760 1763 DEAH box. {ECO:0000255|PROSITE-
ProRule:PRU00541}.
MOTIF 2570 2573 SUMO-interacting motif.
{ECO:0000250|UniProtKB:P29990}.
ACT_SITE 1526 1526 Charge relay system; for serine protease
NS3 activity. {ECO:0000255|PROSITE-
ProRule:PRU00860}.
ACT_SITE 1550 1550 Charge relay system; for serine protease
NS3 activity. {ECO:0000255|PROSITE-
ProRule:PRU00860}.
ACT_SITE 1610 1610 Charge relay system; for serine protease
NS3 activity. {ECO:0000255|PROSITE-
ProRule:PRU00860}.
ACT_SITE 2554 2554 For 2'-O-MTase activity.
{ECO:0000250|UniProtKB:Q6YMS4}.
ACT_SITE 2639 2639 For 2'-O-MTase activity.
{ECO:0000250|UniProtKB:Q6YMS4}.
ACT_SITE 2673 2673 For 2'-O-MTase activity.
{ECO:0000250|UniProtKB:Q6YMS4}.
ACT_SITE 2709 2709 For 2'-O-MTase activity.
{ECO:0000250|UniProtKB:Q6YMS4}.
METAL 2930 2930 Zinc 1. {ECO:0000250|UniProtKB:Q6YMS4}.
METAL 2934 2934 Zinc 1; via tele nitrogen.
{ECO:0000250|UniProtKB:Q6YMS4}.
METAL 2939 2939 Zinc 1. {ECO:0000250|UniProtKB:Q6YMS4}.
METAL 2942 2942 Zinc 1. {ECO:0000250|UniProtKB:Q6YMS4}.
METAL 3204 3204 Zinc 2; via tele nitrogen.
{ECO:0000250|UniProtKB:Q6YMS4}.
METAL 3220 3220 Zinc 2. {ECO:0000250|UniProtKB:Q6YMS4}.
METAL 3339 3339 Zinc 2. {ECO:0000250|UniProtKB:Q6YMS4}.
BINDING 2507 2507 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2510 2510 mRNA cap; via carbonyl oxygen.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
BINDING 2511 2511 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2513 2513 mRNA cap; via carbonyl oxygen.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
BINDING 2522 2522 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2549 2549 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
BINDING 2579 2579 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2580 2580 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2597 2597 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
BINDING 2598 2598 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2624 2624 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
BINDING 2625 2625 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2643 2643 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2704 2704 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2706 2706 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2711 2711 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
SITE 100 101 Cleavage; by viral protease NS3.
{ECO:0000250|UniProtKB:P29990}.
SITE 114 115 Cleavage; by host signal peptidase.
{ECO:0000250|UniProtKB:P29990}.
SITE 205 206 Cleavage; by host furin.
{ECO:0000250|UniProtKB:P29990,
ECO:0000255}.
SITE 280 281 Cleavage; by host signal peptidase.
{ECO:0000250|UniProtKB:P29990}.
SITE 775 776 Cleavage; by host signal peptidase.
{ECO:0000250|UniProtKB:P29990}.
SITE 1127 1128 Cleavage; by host.
{ECO:0000250|UniProtKB:P29990}.
SITE 1345 1346 Cleavage; by viral protease NS3.
{ECO:0000250|UniProtKB:P29990}.
SITE 1475 1476 Cleavage; by autolysis.
{ECO:0000250|UniProtKB:P29990}.
SITE 1933 1933 Involved in NS3 ATPase and RTPase
activities.
{ECO:0000250|UniProtKB:P14335}.
SITE 1936 1936 Involved in NS3 ATPase and RTPase
activities.
{ECO:0000250|UniProtKB:P14335}.
SITE 2094 2095 Cleavage; by autolysis.
{ECO:0000250|UniProtKB:P29990}.
SITE 2221 2222 Cleavage; by viral protease NS3.
{ECO:0000250|UniProtKB:P29990}.
SITE 2244 2245 Cleavage; by host signal peptidase.
{ECO:0000250|UniProtKB:P29990}.
SITE 2493 2494 Cleavage; by viral protease NS3.
{ECO:0000250|UniProtKB:P29990}.
SITE 2518 2518 mRNA cap binding. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
SITE 2554 2554 Essential for 2'-O-methyltransferase
activity. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
SITE 2639 2639 Essential for 2'-O-methyltransferase and
N-7 methyltransferase activity.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
SITE 2640 2640 S-adenosyl-L-methionine binding.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
SITE 2673 2673 Essential for 2'-O-methyltransferase
activity. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
SITE 2709 2709 Essential for 2'-O-methyltransferase
activity. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
MOD_RES 2549 2549 Phosphoserine.
{ECO:0000250|UniProtKB:P03314}.
CARBOHYD 183 183 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 347 347 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 433 433 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 905 905 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 982 982 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 1190 1190 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 2303 2303 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 2307 2307 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 2459 2459 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
DISULFID 283 310 {ECO:0000269|PubMed:14963174}.
DISULFID 340 401 {ECO:0000269|PubMed:14963174}.
DISULFID 354 385 {ECO:0000269|PubMed:14963174}.
DISULFID 372 396 {ECO:0000269|PubMed:14963174}.
DISULFID 465 565 {ECO:0000269|PubMed:14963174}.
DISULFID 582 613 {ECO:0000269|PubMed:14963174}.
DISULFID 779 790 {ECO:0000269|PubMed:14981082}.
DISULFID 830 918 {ECO:0000269|PubMed:14981082}.
DISULFID 954 998 {ECO:0000269|PubMed:14981082}.
DISULFID 1055 1104 {ECO:0000269|PubMed:14981082}.
DISULFID 1066 1088 {ECO:0000269|PubMed:14981082}.
DISULFID 1087 1091 {ECO:0000269|PubMed:14981082}.
VARIANT 125 126 HM -> TL (in strain: Isolate Philippines/
836-1/1984).
VARIANT 142 142 S -> P (in strain: Isolate Philippines/
836-1/1984).
VARIANT 171 173 TET -> AEA (in strain: Isolate
Philippines/836-1/1984).
VARIANT 186 186 E -> D (in strain: Isolate Philippines/
836-1/1984).
VARIANT 210 210 A -> D (in strain: Isolate Philippines/
836-1/1984).
VARIANT 251 251 A -> G (in strain: Isolate Philippines/
836-1/1984).
VARIANT 441 441 T -> I (in strain: Isolate Philippines/
836-1/1984).
VARIANT 475 475 E -> R (in strain: Isolate Philippines/
836-1/1984).
VARIANT 482 482 E -> K (in strain: Isolate 45AZ5).
VARIANT 573 573 T -> I (in strain: Isolate 45AZ5).
VARIANT 677 677 S -> T (in strain: Isolate Philippines/
836-1/1984).
VARIANT 786 786 R -> K (in strain: Isolate Philippines/
836-1/1984).
VARIANT 1689 1692 RRNV -> KRKL (in strain: Isolate 45AZ5).
VARIANT 2242 2242 A -> V (in strain: Isolate 45AZ5).
VARIANT 2357 2357 F -> L (in strain: Isolate 45AZ5).
VARIANT 2543 2543 P -> T (in strain: Isolate 45AZ5).
VARIANT 2779 2779 G -> E (in strain: Isolate 45AZ5).
VARIANT 3337 3337 R -> Q (in strain: Isolate 45AZ5).
MUTAGEN 1138 1138 G->A: Impaired virion assembly.
{ECO:0000269|PubMed:25392211}.
MUTAGEN 1147 1147 E->A: Impaired virion assembly.
{ECO:0000269|PubMed:25392211}.
MUTAGEN 1227 1227 E->A: Impaired virion assembly.
{ECO:0000269|PubMed:25392211}.
MUTAGEN 1252 1252 D->A: Complete loss of viral RNA
synthesis. {ECO:0000269|PubMed:25392211}.
MUTAGEN 1314 1314 Q->A: Impaired virion assembly.
{ECO:0000269|PubMed:25392211}.
MUTAGEN 1315 1315 K->A: Impaired virion assembly.
{ECO:0000269|PubMed:25392211}.
MUTAGEN 1327 1327 G->A: Complete loss of viral RNA
synthesis. {ECO:0000269|PubMed:25392211}.
HELIX 288 290 {ECO:0000244|PDB:4GSX}.
STRAND 291 293 {ECO:0000244|PDB:4GSX}.
STRAND 295 308 {ECO:0000244|PDB:4GSX}.
STRAND 311 313 {ECO:0000244|PDB:4GSX}.
STRAND 321 332 {ECO:0000244|PDB:4GSX}.
STRAND 334 352 {ECO:0000244|PDB:4GSX}.
HELIX 363 366 {ECO:0000244|PDB:4GSX}.
STRAND 370 379 {ECO:0000244|PDB:4GSX}.
HELIX 381 383 {ECO:0000244|PDB:4GSX}.
STRAND 389 409 {ECO:0000244|PDB:4GSX}.
HELIX 412 414 {ECO:0000244|PDB:4GSX}.
STRAND 415 423 {ECO:0000244|PDB:4GSX}.
STRAND 440 444 {ECO:0000244|PDB:4GSX}.
STRAND 450 455 {ECO:0000244|PDB:4GSX}.
TURN 456 458 {ECO:0000244|PDB:4GSX}.
STRAND 459 467 {ECO:0000244|PDB:4GSX}.
TURN 473 475 {ECO:0000244|PDB:4GSX}.
STRAND 476 481 {ECO:0000244|PDB:4GSX}.
STRAND 484 489 {ECO:0000244|PDB:4GSX}.
HELIX 490 494 {ECO:0000244|PDB:4GSX}.
STRAND 500 504 {ECO:0000244|PDB:4GSX}.
HELIX 514 516 {ECO:0000244|PDB:4GSX}.
STRAND 518 520 {ECO:0000244|PDB:4GSX}.
STRAND 530 532 {ECO:0000244|PDB:4GSX}.
HELIX 537 543 {ECO:0000244|PDB:4GSX}.
TURN 544 546 {ECO:0000244|PDB:4GSX}.
STRAND 547 553 {ECO:0000244|PDB:4GSX}.
STRAND 556 559 {ECO:0000244|PDB:4GSX}.
STRAND 562 571 {ECO:0000244|PDB:4GSX}.
STRAND 586 590 {ECO:0000244|PDB:4AL8}.
STRAND 596 598 {ECO:0000244|PDB:4GT0}.
STRAND 600 606 {ECO:0000244|PDB:4AL8}.
STRAND 612 614 {ECO:0000244|PDB:4AL8}.
STRAND 617 620 {ECO:0000244|PDB:4AL8}.
STRAND 633 635 {ECO:0000244|PDB:4AL8}.
STRAND 637 639 {ECO:0000244|PDB:4AL8}.
STRAND 645 649 {ECO:0000244|PDB:4AL8}.
STRAND 653 663 {ECO:0000244|PDB:4AL8}.
STRAND 667 673 {ECO:0000244|PDB:4AL8}.
TURN 956 958 {ECO:0000244|PDB:4OIG}.
STRAND 960 964 {ECO:0000244|PDB:4OIG}.
STRAND 967 971 {ECO:0000244|PDB:4OIG}.
STRAND 973 994 {ECO:0000244|PDB:4OIG}.
HELIX 1002 1004 {ECO:0000244|PDB:4OIG}.
HELIX 1013 1015 {ECO:0000244|PDB:4OIG}.
HELIX 1020 1022 {ECO:0000244|PDB:4OIG}.
HELIX 1028 1030 {ECO:0000244|PDB:4OIG}.
HELIX 1043 1045 {ECO:0000244|PDB:4OIG}.
STRAND 1046 1053 {ECO:0000244|PDB:4OIG}.
STRAND 1059 1062 {ECO:0000244|PDB:4OIG}.
STRAND 1073 1076 {ECO:0000244|PDB:4OIG}.
STRAND 1085 1090 {ECO:0000244|PDB:4OIG}.
STRAND 1096 1099 {ECO:0000244|PDB:4OIG}.
STRAND 1104 1106 {ECO:0000244|PDB:4OIG}.
STRAND 1111 1114 {ECO:0000244|PDB:4OIG}.
STRAND 1496 1504 {ECO:0000244|PDB:3LKW}.
STRAND 1507 1517 {ECO:0000244|PDB:3LKW}.
STRAND 1520 1523 {ECO:0000244|PDB:3LKW}.
HELIX 1525 1528 {ECO:0000244|PDB:3LKW}.
STRAND 1533 1535 {ECO:0000244|PDB:3LKW}.
STRAND 1538 1540 {ECO:0000244|PDB:3LKW}.
STRAND 1542 1546 {ECO:0000244|PDB:3LKW}.
TURN 1547 1550 {ECO:0000244|PDB:3LKW}.
STRAND 1551 1557 {ECO:0000244|PDB:3LKW}.
STRAND 1570 1574 {ECO:0000244|PDB:3LKW}.
STRAND 1582 1586 {ECO:0000244|PDB:3LKW}.
STRAND 1589 1593 {ECO:0000244|PDB:3LKW}.
STRAND 1596 1601 {ECO:0000244|PDB:3LKW}.
STRAND 1613 1615 {ECO:0000244|PDB:3LKW}.
STRAND 1621 1625 {ECO:0000244|PDB:3LKW}.
STRAND 1628 1630 {ECO:0000244|PDB:3LKW}.
STRAND 1636 1639 {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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