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 POLG_DEN26              Reviewed;        3391 AA.
P29990;
01-APR-1993, integrated into UniProtKB/Swiss-Prot.
01-APR-1993, sequence version 1.
25-OCT-2017, entry version 158.
RecName: Full=Genome polyprotein;
Contains:
RecName: Full=Capsid protein C;
AltName: Full=Core protein;
Contains:
RecName: Full=Protein prM;
Contains:
RecName: Full=Peptide pr;
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 2 (strain Thailand/16681/1984) (DENV-2).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Flaviviridae; Flavivirus; Dengue virus group.
NCBI_TaxID=31634;
NCBI_TaxID=7159; Aedes aegypti (Yellowfever mosquito) (Culex aegypti).
NCBI_TaxID=299627; Aedes furcifer (Mosquito).
NCBI_TaxID=299628; Aedes taylori (Mosquito).
NCBI_TaxID=9538; Erythrocebus patas (Red guenon) (Cercopithecus patas).
NCBI_TaxID=9606; Homo sapiens (Human).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=1312269; DOI=10.1016/0042-6822(92)90460-7;
Blok J., McWilliam S.M., Butler H.C., Gibbs A.J., Weiller G.,
Herring B.L., Hemsley A.C., Aaskov J.G., Yoksan S., Bhamarapravati N.;
"Comparison of a dengue-2 virus and its candidate vaccine derivative:
sequence relationships with the flaviviruses and other viruses.";
Virology 187:573-590(1992).
[2]
SUBUNIT (CAPSID PROTEIN C).
PubMed=12768036; DOI=10.1128/JVI.77.12.7143-7149.2003;
Jones C.T., Ma L., Burgner J.W., Groesch T.D., Post C.B., Kuhn R.J.;
"Flavivirus capsid is a dimeric alpha-helical protein.";
J. Virol. 77:7143-7149(2003).
[3]
PROTEOLYTIC PROCESSING (GENOME POLYPROTEIN).
PubMed=14963133; DOI=10.1128/JVI.78.5.2367-2381.2004;
Keelapang P., Sriburi R., Supasa S., Panyadee N., Songjaeng A.,
Jairungsri A., Puttikhunt C., Kasinrerk W., Malasit P.,
Sittisombut N.;
"Alterations of pr-M cleavage and virus export in pr-M junction
chimeric dengue viruses.";
J. Virol. 78:2367-2381(2004).
[4]
SUBUNIT (CAPSID PROTEIN C), AND REGION OF HOMODIMERIZATION (CAPSID
PROTEIN C).
PubMed=15269372; DOI=10.1099/vir.0.80067-0;
Wang S.H., Syu W.J., Hu S.T.;
"Identification of the homotypic interaction domain of the core
protein of dengue virus type 2.";
J. Gen. Virol. 85:2307-2314(2004).
[5]
FUNCTION (NON-STRUCTURAL PROTEIN 4B), AND FUNCTION (PEPTIDE 2K).
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).
[6]
FUNCTION (NON-STRUCTURAL PROTEIN 1).
PubMed=16544248; DOI=10.1086/500949;
Avirutnan P., Punyadee N., Noisakran S., Komoltri C., Thiemmeca S.,
Auethavornanan K., Jairungsri A., Kanlaya R., Tangthawornchaikul N.,
Puttikhunt C., Pattanakitsakul S.N., Yenchitsomanus P.T.,
Mongkolsapaya J., Kasinrerk W., Sittisombut N., Husmann M.,
Blettner M., Vasanawathana S., Bhakdi S., Malasit P.;
"Vascular leakage in severe dengue virus infections: a potential role
for the nonstructural viral protein NS1 and complement.";
J. Infect. Dis. 193:1078-1088(2006).
[7]
SUBCELLULAR LOCATION (SERINE PROTEASE NS3), AND SUBCELLULAR LOCATION
(RNA-DIRECTED RNA POLYMERASE NS5).
STRAIN=TR 1751;
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).
[8]
PROTEOLYTIC PROCESSING (GENOME POLYPROTEIN).
PubMed=17067286; DOI=10.1042/BJ20061136;
Shiryaev S.A., Kozlov I.A., Ratnikov B.I., Smith J.W., Lebl M.,
Strongin A.Y.;
"Cleavage preference distinguishes the two-component NS2B-NS3 serine
proteinases of Dengue and West Nile viruses.";
Biochem. J. 401:743-752(2007).
[9]
DISULFIDE BOND (ENVELOPE PROTEIN E).
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).
[10]
FUNCTION (RNA-DIRECTED RNA POLYMERASE NS5).
PubMed=15944325; DOI=10.4049/jimmunol.174.12.8163;
Ho L.J., Hung L.F., Weng C.Y., Wu W.L., Chou P., Lin Y.L., Chang D.M.,
Tai T.Y., Lai J.H.;
"Dengue virus type 2 antagonizes IFN-alpha but not IFN-gamma antiviral
effect via down-regulating Tyk2-STAT signaling in the human dendritic
cell.";
J. Immunol. 174:8163-8172(2005).
[11]
CHARACTERIZATION (NON-STRUCTURAL PROTEIN 1).
PubMed=17331594; DOI=10.1016/j.jviromet.2007.01.008;
Noisakran S., Dechtawewat T., Rinkaewkan P., Puttikhunt C.,
Kanjanahaluethai A., Kasinrerk W., Sittisombut N., Malasit P.;
"Characterization of dengue virus NS1 stably expressed in 293T cell
lines.";
J. Virol. Methods 142:67-80(2007).
[12]
FUNCTION (RNA-DIRECTED RNA POLYMERASE NS5), INTERACTION WITH
RNA-DIRECTED RNA POLYMERASE NS5 (SERINE PROTEASE NS3), AND INTERACTION
WITH SERINE PROTEASE NS3 (RNA-DIRECTED RNA POLYMERASE NS5).
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).
[13]
FUNCTION (RNA-DIRECTED RNA POLYMERASE NS5), AND INTERACTION WITH HUMAN
STAT2 (RNA-DIRECTED RNA POLYMERASE NS5).
PubMed=19754307; DOI=10.1086/605847;
Mazzon M., Jones M., Davidson A., Chain B., Jacobs M.;
"Dengue virus NS5 inhibits interferon-alpha signaling by blocking
signal transducer and activator of transcription 2 phosphorylation.";
J. Infect. Dis. 200:1261-1270(2009).
[14]
FUNCTION (ENVELOPE PROTEIN E).
PubMed=19272179; DOI=10.1186/1423-0127-16-17;
Suksanpaisan L., Susantad T., Smith D.R.;
"Characterization of dengue virus entry into HepG2 cells.";
J. Biomed. Sci. 16:17-17(2009).
[15]
INTERACTION WITH HUMAN EXOC1 (CAPSID PROTEIN C), AND SUBCELLULAR
LOCATION (CAPSID PROTEIN C).
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).
[16]
INTERACTION WITH HUMAN EXOC1 (CAPSID PROTEIN C), FUNCTION (CAPSID
PROTEIN C), AND MUTAGENESIS OF PHE-13.
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).
[17]
SUMOYLATION (RNA-DIRECTED RNA POLYMERASE NS5), AND MUTAGENESIS OF
2568-VAL--LEU-2571.
PubMed=26889037; DOI=10.1128/JVI.00223-16;
Su C.I., Tseng C.H., Yu C.Y., Lai M.M.;
"SUMO modification stabilizes dengue virus nonstructural protein 5 to
support virus replication.";
J. Virol. 90:4308-4319(2016).
[18]
X-RAY CRYSTALLOGRAPHY (3.8 ANGSTROMS) OF 578-674.
PubMed=18264114; DOI=10.1038/nsmb.1382;
Lok S.M., Kostyuchenko V., Nybakken G.E., Holdaway H.A.,
Battisti A.J., Sukupolvi-Petty S., Sedlak D., Fremont D.H.,
Chipman P.R., Roehrig J.T., Diamond M.S., Kuhn R.J., Rossmann M.G.;
"Binding of a neutralizing antibody to dengue virus alters the
arrangement of surface glycoproteins.";
Nat. Struct. Mol. Biol. 15:312-317(2008).
-!- 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.
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.
Overcomes the anti-viral effects of host EXOC1 by sequestering and
degrading the latter through the proteasome degradation pathway
(PubMed:23522008). {ECO:0000250|UniProtKB:P17763,
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:0000250|UniProtKB:P17763}.
-!- 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. prM-E cleavage is
inefficient, and many virions are only partially matured. These
uncleaved prM would play a role in immune evasion.
{ECO:0000250|UniProtKB:P17763}.
-!- FUNCTION: Small envelope protein M: May play a role in virus
budding. Exerts cytotoxic effects by activating a mitochondrial
apoptotic pathway through M ectodomain. May display a viroporin
activity. {ECO:0000250|UniProtKB:P17763}.
-!- FUNCTION: Envelope protein E: Binds to host cell surface receptor
and mediates fusion between viral and cellular membranes
(PubMed:19272179). Envelope protein is synthesized in the
endoplasmic reticulum in the form of heterodimer with protein prM
(By similarity). 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 (By similarity). The virion is transported to the Golgi
apparatus where the low pH causes dissociation of PrM-E
heterodimers and formation of E homodimers (By similarity). prM-E
cleavage is inefficient, and many virions are only partially
matured. These uncleaved prM would play a role in immune evasion
(By similarity). {ECO:0000250|UniProtKB:P17763}.
-!- 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
(By similarity). Mediates complement activation, which may
contribute to the pathogenesis of the vascular leakage that occurs
in severe dengue disease (PubMed:16544248).
{ECO:0000250|UniProtKB:P17763, ECO:0000269|PubMed:16544248}.
-!- FUNCTION: Non-structural protein 2A: Component of the viral RNA
replication complex that functions in virion assembly and
antagonizes the host immune response.
{ECO:0000250|UniProtKB:P17763}.
-!- FUNCTION: Serine protease subunit NS2B: Required cofactor for the
serine protease function of NS3. May have membrane-destabilizing
activity and form viroporins (By similarity).
{ECO:0000250|UniProtKB:P17763, ECO:0000255|PROSITE-
ProRule:PRU00859}.
-!- 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:15956546}.
-!- FUNCTION: Non-structural protein 4B: Induces the formation of ER-
derived membrane vesicles where the viral replication takes place.
Inhibits interferon (IFN)-induced host STAT1 phosphorylation and
nuclear translocation, thereby preventing the establishment of
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 (By similarity). NS5 methylates viral RNA cap at guanine
N-7 and ribose 2'-O positions (PubMed:19850911). 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 (PubMed:15944325). Inhibits
host TYK2 and STAT2 phosphorylation, thereby preventing activation
of JAK-STAT signaling pathway (PubMed:19754307).
{ECO:0000250|UniProtKB:P17763, ECO:0000269|PubMed:15944325,
ECO:0000269|PubMed:19754307, 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.
-!- 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 (PubMed:12768036,
PubMed:15269372). Interacts (via N-terminus) with host EXOC1 (via
C-terminus); this interaction results in EXOC1 degradation through
the proteasome degradation pathway (PubMed:19889084,
PubMed:23522008). Protein prM: Forms heterodimers with envelope
protein E in the endoplasmic reticulum and Golgi (By similarity).
Envelope protein E: Homodimer; in the endoplasmic reticulum and
Golgi. Interacts with protein prM. Interacts with non-structural
protein 1 (By similarity). Non-structural protein 1: Homodimer;
Homohexamer when secreted. Interacts with envelope protein E (By
similarity). Non-structural protein 2A: Interacts (via N-terminus)
with serine protease NS3 (By similarity). Non-structural protein
2B: Forms a heterodimer with serine protease NS3. May form
homooligomers (By similarity). Serine protease NS3: Forms a
heterodimer with NS2B (By similarity). Interacts with NS4B (By
similarity). Interacts with unphosphorylated RNA-directed RNA
polymerase NS5; this interaction stimulates RNA-directed RNA
polymerase NS5 guanylyltransferase activity (PubMed:19850911).
Non-structural protein 4B: Interacts with serine protease NS3 (By
similarity). RNA-directed RNA polymerase NS5: Homodimer (By
similarity). 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:19754307). Interacts with serine protease NS3
(PubMed:19850911). {ECO:0000250|UniProtKB:P17763,
ECO:0000269|PubMed:12768036, ECO:0000269|PubMed:15269372,
ECO:0000269|PubMed:19754307, ECO:0000269|PubMed:19850911,
ECO:0000269|PubMed:19889084, ECO:0000269|PubMed:23522008}.
-!- SUBCELLULAR LOCATION: Capsid protein C: Virion
{ECO:0000250|UniProtKB:P17763}. Host nucleus
{ECO:0000250|UniProtKB:P17763}. Host cytoplasm
{ECO:0000269|PubMed:19889084}. Host cytoplasm, host perinuclear
region {ECO:0000269|PubMed:19889084}.
-!- SUBCELLULAR LOCATION: Peptide pr: Secreted
{ECO:0000250|UniProtKB:P17763}.
-!- SUBCELLULAR LOCATION: Small envelope protein M: Virion membrane
{ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein
{ECO:0000255}. Host endoplasmic reticulum membrane
{ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein
{ECO:0000255}.
-!- SUBCELLULAR LOCATION: Envelope protein E: Virion membrane
{ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein
{ECO:0000255}. Host endoplasmic reticulum membrane
{ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein
{ECO:0000255}.
-!- SUBCELLULAR LOCATION: Non-structural protein 1: Secreted
{ECO:0000250|UniProtKB:P17763}. Host endoplasmic reticulum
membrane; Peripheral membrane protein; Lumenal side
{ECO:0000250|UniProtKB:P17763}. 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:0000250|UniProtKB:P17763}; Multi-pass
membrane protein {ECO:0000250|UniProtKB:P17763}.
-!- SUBCELLULAR LOCATION: Serine protease subunit NS2B: Host
endoplasmic reticulum membrane; Multi-pass membrane protein
{ECO:0000250|UniProtKB:P17763}.
-!- 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}. Host nucleus {ECO:0000269|PubMed:16699025}.
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:0000250|UniProtKB:P17763}; Multi-pass
membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in
RE-associated vesicles hosting the replication complex.
{ECO:0000250|UniProtKB:P17763}.
-!- SUBCELLULAR LOCATION: Non-structural protein 4B: Host endoplasmic
reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass
membrane protein {ECO:0000250|UniProtKB:P17763}. 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; Peripheral membrane protein;
Cytoplasmic side. 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:0000250|UniProtKB:P17763}.
-!- DOMAIN: The transmembrane domains of the small envelope protein M
and envelope protein E contain an endoplasmic reticulum retention
signal. {ECO:0000250|UniProtKB:P17763}.
-!- 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 serine protease
NS3. Signal cleavage at the 2K-4B site requires a prior NS3
protease-mediated cleavage at the 4A-2K site.
{ECO:0000250|UniProtKB:P17763, ECO:0000269|PubMed:17067286}.
-!- 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:0000250|UniProtKB:P17763,
ECO:0000269|PubMed:14963133}.
-!- PTM: Envelope protein E: N-glycosylated.
{ECO:0000250|UniProtKB:P17763}.
-!- PTM: Non-structural protein 1: N-glycosylated. The excreted form
is glycosylated and this is required for efficient secretion of
the protein from infected cells. {ECO:0000250|UniProtKB:P17763}.
-!- PTM: RNA-directed RNA polymerase NS5: Sumoylation of RNA-directed
RNA polymerase NS5 increases NS5 protein stability allowing proper
viral RNA replication. {ECO:0000269|PubMed:26889037}.
-!- PTM: RNA-directed RNA polymerase NS5: Phosphorylated on serines
residues. This phosphorylation may trigger NS5 nuclear
localization. {ECO:0000250|UniProtKB:P17763}.
-!- 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; M84727; AAA73185.1; -; Genomic_RNA.
PIR; A42451; GNWV16.
PDB; 2R69; X-ray; 3.80 A; A=578-674.
PDB; 4O6B; X-ray; 3.00 A; A/B=775-1127.
PDBsum; 2R69; -.
PDBsum; 4O6B; -.
ProteinModelPortal; P29990; -.
SMR; P29990; -.
IntAct; P29990; 1.
BindingDB; P29990; -.
ChEMBL; CHEMBL5980; -.
iPTMnet; P29990; -.
OrthoDB; VOG090000KT; -.
BRENDA; 2.7.7.50; 1867.
EvolutionaryTrace; P29990; -.
PRO; PR:P29990; -.
Proteomes; UP000002324; Genome.
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: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.
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; 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; 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 3391 Genome polyprotein.
/FTId=PRO_0000405213.
CHAIN 1 100 Capsid protein C.
{ECO:0000269|PubMed:17067286}.
/FTId=PRO_0000037925.
PROPEP 101 114 ER anchor for the capsid protein C,
removed in mature form by serine protease
NS3. {ECO:0000269|PubMed:17067286}.
/FTId=PRO_0000037926.
CHAIN 115 280 Protein prM.
{ECO:0000269|PubMed:17067286}.
/FTId=PRO_0000264673.
CHAIN 115 205 Peptide pr.
{ECO:0000269|PubMed:14963133}.
/FTId=PRO_0000264674.
CHAIN 206 280 Small envelope protein M.
{ECO:0000269|PubMed:17067286}.
/FTId=PRO_0000037927.
CHAIN 281 775 Envelope protein E.
{ECO:0000269|PubMed:17067286}.
/FTId=PRO_0000037928.
CHAIN 776 1127 Non-structural protein 1.
{ECO:0000269|PubMed:17067286}.
/FTId=PRO_0000037929.
CHAIN 1128 1345 Non-structural protein 2A.
{ECO:0000269|PubMed:17067286}.
/FTId=PRO_0000037930.
CHAIN 1346 1475 Serine protease subunit NS2B.
{ECO:0000269|PubMed:17067286}.
/FTId=PRO_0000037931.
CHAIN 1476 2093 Serine protease NS3.
{ECO:0000269|PubMed:17067286}.
/FTId=PRO_0000037932.
CHAIN 2094 2220 Non-structural protein 4A.
{ECO:0000269|PubMed:17067286}.
/FTId=PRO_0000037933.
PEPTIDE 2221 2243 Peptide 2k.
{ECO:0000269|PubMed:17067286}.
/FTId=PRO_0000264676.
CHAIN 2244 2491 Non-structural protein 4B.
{ECO:0000269|PubMed:17067286}.
/FTId=PRO_0000037934.
CHAIN 2492 3391 RNA-directed RNA polymerase NS5.
{ECO:0000269|PubMed:17067286}.
/FTId=PRO_0000037935.
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}.
TOPO_DOM 1221 1226 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1227 1245 Helical. {ECO:0000255}.
TOPO_DOM 1246 1269 Lumenal. {ECO:0000255}.
TRANSMEM 1270 1290 Helical. {ECO:0000255}.
TOPO_DOM 1291 1291 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1292 1310 Helical. {ECO:0000255}.
TOPO_DOM 1311 1317 Lumenal. {ECO:0000255}.
TRANSMEM 1318 1338 Helical. {ECO:0000255}.
TOPO_DOM 1339 1346 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1347 1367 Helical. {ECO:0000255}.
TOPO_DOM 1368 1370 Lumenal. {ECO:0000255}.
TRANSMEM 1371 1391 Helical. {ECO:0000255}.
TOPO_DOM 1392 1447 Cytoplasmic. {ECO:0000255}.
INTRAMEM 1448 1468 Helical. {ECO:0000255}.
TOPO_DOM 1469 2147 Cytoplasmic. {ECO:0000255}.
TRANSMEM 2148 2168 Helical. {ECO:0000255}.
TOPO_DOM 2169 2170 Lumenal. {ECO:0000255}.
INTRAMEM 2171 2191 Helical. {ECO:0000255}.
TOPO_DOM 2192 2192 Lumenal. {ECO:0000255}.
TRANSMEM 2193 2213 Helical. {ECO:0000255}.
TOPO_DOM 2214 2228 Cytoplasmic. {ECO:0000255}.
TRANSMEM 2229 2249 Helical; Note=Signal for NS4B.
{ECO:0000255}.
TOPO_DOM 2250 2274 Lumenal. {ECO:0000255}.
INTRAMEM 2275 2295 Helical. {ECO:0000255}.
TOPO_DOM 2296 2316 Lumenal. {ECO:0000255}.
INTRAMEM 2317 2337 Helical. {ECO:0000255}.
TOPO_DOM 2338 2347 Lumenal. {ECO:0000255}.
TRANSMEM 2348 2368 Helical. {ECO:0000255}.
TOPO_DOM 2369 2413 Cytoplasmic. {ECO:0000255}.
TRANSMEM 2414 2434 Helical. {ECO:0000255}.
TOPO_DOM 2435 2459 Lumenal. {ECO:0000255}.
TRANSMEM 2460 2480 Helical. {ECO:0000255}.
TOPO_DOM 2481 3391 Cytoplasmic. {ECO:0000255}.
DOMAIN 1476 1653 Peptidase S7. {ECO:0000255|PROSITE-
ProRule:PRU00860}.
DOMAIN 1655 1811 Helicase ATP-binding.
{ECO:0000255|PROSITE-ProRule:PRU00541}.
DOMAIN 1821 1988 Helicase C-terminal.
DOMAIN 2493 2755 mRNA cap 0-1 NS5-type MT.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
DOMAIN 3020 3169 RdRp catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00539}.
NP_BIND 1668 1675 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00541}.
REGION 1 15 Interaction with host EXOC1.
{ECO:0000250|UniProtKB:P17763}.
REGION 37 72 Hydrophobic; homodimerization of capsid
protein C. {ECO:0000269|PubMed:15269372}.
REGION 378 391 Fusion peptide.
{ECO:0000250|UniProtKB:P14336}.
REGION 1398 1437 Interacts with and activates NS3
protease. {ECO:0000255|PROSITE-
ProRule:PRU00859}.
REGION 1659 1662 Important for RNA-binding.
{ECO:0000250|UniProtKB:P14340}.
MOTIF 1759 1762 DEAH box. {ECO:0000255|PROSITE-
ProRule:PRU00541}.
MOTIF 2568 2571 SUMO-interacting motif.
{ECO:0000269|PubMed:26889037}.
COMPBIAS 97 100 Poly-Arg.
COMPBIAS 1434 1437 Poly-Glu.
COMPBIAS 2148 2154 Poly-Leu.
COMPBIAS 3383 3386 Poly-Glu.
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 2552 2552 For 2'-O-MTase activity.
{ECO:0000250|UniProtKB:Q6YMS4}.
ACT_SITE 2637 2637 For 2'-O-MTase activity.
{ECO:0000250|UniProtKB:Q6YMS4}.
ACT_SITE 2672 2672 For 2'-O-MTase activity.
{ECO:0000250|UniProtKB:Q6YMS4}.
ACT_SITE 2708 2708 For 2'-O-MTase activity.
{ECO:0000250|UniProtKB:Q6YMS4}.
METAL 2929 2929 Zinc 1. {ECO:0000250|UniProtKB:Q6YMS4}.
METAL 2933 2933 Zinc 1; via tele nitrogen.
{ECO:0000250|UniProtKB:Q6YMS4}.
METAL 2938 2938 Zinc 1. {ECO:0000250|UniProtKB:Q6YMS4}.
METAL 2941 2941 Zinc 1. {ECO:0000250|UniProtKB:Q6YMS4}.
METAL 3203 3203 Zinc 2; via tele nitrogen.
{ECO:0000250|UniProtKB:Q6YMS4}.
METAL 3219 3219 Zinc 2. {ECO:0000250|UniProtKB:Q6YMS4}.
METAL 3338 3338 Zinc 2. {ECO:0000250|UniProtKB:Q6YMS4}.
BINDING 2505 2505 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2508 2508 mRNA cap; via carbonyl oxygen.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
BINDING 2509 2509 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2511 2511 mRNA cap; via carbonyl oxygen.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
BINDING 2520 2520 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2547 2547 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
BINDING 2577 2577 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2578 2578 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2595 2595 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
BINDING 2596 2596 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2622 2622 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
BINDING 2623 2623 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2641 2641 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2703 2703 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2705 2705 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2710 2710 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
SITE 100 101 Cleavage; by viral protease NS3.
{ECO:0000269|PubMed:17067286}.
SITE 114 115 Cleavage; by host signal peptidase.
{ECO:0000269|PubMed:17067286}.
SITE 205 206 Cleavage; by host furin. {ECO:0000255,
ECO:0000269|PubMed:14963133}.
SITE 280 281 Cleavage; by host signal peptidase.
{ECO:0000269|PubMed:17067286}.
SITE 775 776 Cleavage; by host signal peptidase.
{ECO:0000269|PubMed:17067286}.
SITE 1127 1128 Cleavage; by host.
{ECO:0000269|PubMed:17067286}.
SITE 1345 1346 Cleavage; by viral protease NS3.
{ECO:0000269|PubMed:17067286}.
SITE 1475 1476 Cleavage; by autolysis.
{ECO:0000269|PubMed:17067286}.
SITE 1932 1932 Involved in NS3 ATPase and RTPase
activities.
{ECO:0000250|UniProtKB:P14335}.
SITE 1935 1935 Involved in NS3 ATPase and RTPase
activities.
{ECO:0000250|UniProtKB:P14335}.
SITE 2093 2094 Cleavage; by autolysis.
{ECO:0000269|PubMed:17067286}.
SITE 2220 2221 Cleavage; by viral protease NS3.
{ECO:0000269|PubMed:17067286}.
SITE 2243 2244 Cleavage; by host signal peptidase.
{ECO:0000269|PubMed:17067286}.
SITE 2491 2492 Cleavage; by viral protease NS3.
{ECO:0000269|PubMed:17067286}.
SITE 2516 2516 mRNA cap binding. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
SITE 2552 2552 Essential for 2'-O-methyltransferase
activity. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
SITE 2637 2637 Essential for 2'-O-methyltransferase and
N-7 methyltransferase activity.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
SITE 2638 2638 S-adenosyl-L-methionine binding.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
SITE 2672 2672 Essential for 2'-O-methyltransferase
activity. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
SITE 2708 2708 Essential for 2'-O-methyltransferase
activity. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
MOD_RES 2547 2547 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 1134 1134 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 1174 1174 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 2301 2301 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 2305 2305 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 2457 2457 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:0000250|UniProtKB:P17763}.
DISULFID 830 918 {ECO:0000250|UniProtKB:P17763}.
DISULFID 954 998 {ECO:0000250|UniProtKB:P17763}.
DISULFID 1055 1104 {ECO:0000250|UniProtKB:P17763}.
DISULFID 1066 1088 {ECO:0000250|UniProtKB:P17763}.
DISULFID 1087 1091 {ECO:0000250|UniProtKB:P17763}.
MUTAGEN 13 13 F->A: Loss of degradation of hSec3p.
{ECO:0000269|PubMed:23522008}.
MUTAGEN 2568 2571 VVDL->AAAA: Complete loss of NS5
sumoylation and decreased viral
replication.
{ECO:0000269|PubMed:26889037}.
STRAND 776 781 {ECO:0000244|PDB:4O6B}.
TURN 783 785 {ECO:0000244|PDB:4O6B}.
STRAND 788 797 {ECO:0000244|PDB:4O6B}.
HELIX 814 826 {ECO:0000244|PDB:4O6B}.
HELIX 837 856 {ECO:0000244|PDB:4O6B}.
STRAND 862 865 {ECO:0000244|PDB:4O6B}.
STRAND 870 872 {ECO:0000244|PDB:4O6B}.
STRAND 907 913 {ECO:0000244|PDB:4O6B}.
STRAND 916 918 {ECO:0000244|PDB:4O6B}.
HELIX 920 922 {ECO:0000244|PDB:4O6B}.
STRAND 928 932 {ECO:0000244|PDB:4O6B}.
STRAND 942 946 {ECO:0000244|PDB:4O6B}.
TURN 956 958 {ECO:0000244|PDB:4O6B}.
STRAND 960 964 {ECO:0000244|PDB:4O6B}.
STRAND 967 971 {ECO:0000244|PDB:4O6B}.
STRAND 973 993 {ECO:0000244|PDB:4O6B}.
TURN 1013 1015 {ECO:0000244|PDB:4O6B}.
HELIX 1020 1022 {ECO:0000244|PDB:4O6B}.
HELIX 1043 1045 {ECO:0000244|PDB:4O6B}.
STRAND 1046 1053 {ECO:0000244|PDB:4O6B}.
STRAND 1059 1062 {ECO:0000244|PDB:4O6B}.
STRAND 1073 1076 {ECO:0000244|PDB:4O6B}.
STRAND 1085 1090 {ECO:0000244|PDB:4O6B}.
STRAND 1096 1099 {ECO:0000244|PDB:4O6B}.
STRAND 1104 1106 {ECO:0000244|PDB:4O6B}.
STRAND 1110 1115 {ECO:0000244|PDB:4O6B}.
HELIX 1117 1119 {ECO:0000244|PDB:4O6B}.
SEQUENCE 3391 AA; 379547 MW; 2E20AD0D6C978ECC CRC64;
MNDQRKKAKN TPFNMLKRER NRVSTVQQLT KRFSLGMLQG RGPLKLYMAL VAFLRFLTIP
PTAGILKRWG TIKKSKAINV LRGFRKEIGR MLNILNRRRR SAGMIIMLIP TVMAFHLTTR
NGEPHMIVSR QEKGKSLLFK TEDGVNMCTL MAMDLGELCE DTITYKCPLL RQNEPEDIDC
WCNSTSTWVT YGTCTTMGEH RRQKRSVALV PHVGMGLETR TETWMSSEGA WKHVQRIETW
ILRHPGFTMM AAILAYTIGT THFQRALIFI LLTAVTPSMT MRCIGMSNRD FVEGVSGGSW
VDIVLEHGSC VTTMAKNKPT LDFELIKTEA KQPATLRKYC IEAKLTNTTT ESRCPTQGEP
SLNEEQDKRF VCKHSMVDRG WGNGCGLFGK GGIVTCAMFR CKKNMEGKVV QPENLEYTIV
ITPHSGEEHA VGNDTGKHGK EIKITPQSST TEAELTGYGT VTMECSPRTG LDFNEMVLLQ
MENKAWLVHR QWFLDLPLPW LPGADTQGSN WIQKETLVTF KNPHAKKQDV VVLGSQEGAM
HTALTGATEI QMSSGNLLFT GHLKCRLRMD KLQLKGMSYS MCTGKFKVVK EIAETQHGTI
VIRVQYEGDG SPCKIPFEIM DLEKRHVLGR LITVNPIVTE KDSPVNIEAE PPFGDSYIII
GVEPGQLKLN WFKKGSSIGQ MFETTMRGAK RMAILGDTAW DFGSLGGVFT SIGKALHQVF
GAIYGAAFSG VSWTMKILIG VIITWIGMNS RSTSLSVTLV LVGIVTLYLG VMVQADSGCV
VSWKNKELKC GSGIFITDNV HTWTEQYKFQ PESPSKLASA IQKAHEEGIC GIRSVTRLEN
LMWKQITPEL NHILSENEVK LTIMTGDIKG IMQAGKRSLR PQPTELKYSW KTWGKAKMLS
TESHNQTFLI DGPETAECPN TNRAWNSLEV EDYGFGVFTT NIWLKLKEKQ DVFCDSKLMS
AAIKDNRAVH ADMGYWIESA LNDTWKIEKA SFIEVKNCHW PKSHTLWSNG VLESEMIIPK
NLAGPVSQHN YRPGYHTQIT GPWHLGKLEM DFDFCDGTTV VVTEDCGNRG PSLRTTTASG
KLITEWCCRS CTLPPLRYRG EDGCWYGMEI RPLKEKEENL VNSLVTAGHG QVDNFSLGVL
GMALFLEEML RTRVGTKHAI LLVAVSFVTL IIGNMSFRDL GRVMVMVGAT MTDDIGMGVT
YLALLAAFKV RPTFAAGLLL RKLTSKALMM TTIGIVLSSQ STTPETILEL TDALALGMMV
LKMVRNMEKY QLAVTIMAIL CVPNAVILQN AWKVSCTILA VVSVSPLFLT SSQQKTDWIP
LALTIKGLNP TAIFLTTLSR TSKKRSWPLN EAIMAVGMVS ILASSLLKND IPMTGPLVAG
GPLTVCYVLT GRSADLELER AADVKWEDQA EISGSSPILS ITISEDGSMS IKNEEEEQTL
TILIRTGLLV ISGLFPVSIP ITAAAWYLWE VKKQRAGVLW DVPSPPPMGK AELEDGAYRI
KQKGILGYSQ IGAGVYKEGT FHTMWHVTRG AVLMHKGKRI EPSWADVKKD LISYGGGWKL
EGEWKEGEEV QVLALEPGKN PRAVQTKPGL FKTNAGTIGA VSLDFSPGTS GSPIIDKKGK
VVGLYGNGVV TRSGAYVSAI AQTEKSIEDN PEIEDDIFRK RRLTIMDLHP GAGKTKRYLP
AIVREAIKRG LRTLILAPTR VVAAEMEEAL RGLPIRYQTP AIRAEHTGRE IVDLMCHATF
TMRLLSPVRV PNYNLIIMDE AHFTDPASIA ARGYISTRVE MGEAAGIFMT ATPPGSRDPF
PQSNAPIIDE EREIPERSWN SGHEWVTDFK GKTVWFVPSI KAGNDIAACL SKNGKKVIQL
SRKTFDSEYA KTRTNDWDFV VTTDISEMGA NFKAERVIDP RRCMKPVILT DGEERVILAG
PMPVTHSSAA QRRGRIGRNP KNENDQYIYM GEPLENDEDC AHWKEAKMLL DNINTPEGII
PSMFEPEREK VDAIDGEYRL RGEARTTFVD LMRRGDLPVW LAYRVAAEGI NYADRRWCFD
GVKNNQILEE NVEVEIWTKE GERKKLKPRW LDARIYSDPL ALKEFKEFAA GRKSLTLNLI
TEMGRLPTFM TQKARDALDN LAVLHTAEAG GRAYNHALSE LPETLETLLL LTLLATVTGG
ILLFLMSGRG IGKMTLGMCC IITASILLWY AQIQPHWIAA SIILEFFLIV LLIPEPEKQR
TPQDNQLTYV VIAILTVVAA TMANEMGFLE KTKKDLGLGS IATQQPESNI LDIDLRPASA
WTLYAVATTF VTPMLRHSIE NSSVNVSLTA IANQATVLMG LGKGWPLSKM DIGVPLLAIG
CYSQVNPTTL TAALFLLVAH YAIIGPALQA KASREAQKRA AAGIMKNPTV DGITVIDLDP
IPYDPKFEKQ LGQVMLLVLC VTQVLMMRTT WALCEVLTLA TGPISTLWEG NPGRFWNTTI
AVSMANIFRG SYLAGAGLLF SIMKNTTNAR RGTGNIGETL GEKWKSRLNA LGKSEFQIYK
KSGIQEVDRT LAKEGIKRGE TDHHAVSRGS AKLRWFVERN MVTPEGKVVD LGCGRGGWSY
YCGGLKNVRE VKGLTKGGPG HEEPIPMSTY GWNLVRLQSG VDVFFIPPEK CDTLLCDIGE
SSPNPTVEAG RTLRVLNLVE NWLNNNTQFC IKVLNPYMPS VIEKMEALQR KYGGALVRNP
LSRNSTHEMY WVSNASGNIV SSVNMISRML INRFTMRYKK ATYEPDVDLG SGTRNIGIES
EIPNLDIIGK RIEKIKQEHE TSWHYDQDHP YKTWAYHGSY ETKQTGSASS MVNGVFRLLT
KPWDVVPMVT QMAMTDTTPF GQQRVFKEKV DTRTQEPKEG TKKLMKITAE WLWKELGKKK
TPRMCTREEF TRKVRSNAAL GAIFTDENKW KSAREAVEDS RFWELVDKER NLHLEGKCET
CVYNIMGKRE KKLGEFGKAK GSRAIWYMWL GARFLEFEAL GFLNEDHWFS RENSLSGVEG
EGLHKLGYIL RDVSKKEGGA MYADDTAGWD TRITLEDLKN EAMVTNHMEG EHKKLAEAIF
KLTYQNKVVR VQRPTPRGTV MDIISRRDQR GSGQVGTYGL NTFTNMEAQL IRQMEGEGVF
KSIQHLTITE EIAVQNWLAR VGRERLSRMA ISGDDCVVKP LDDRLPSALT ALNDTGKIRK
DIQQWEPSRG WNDWTQVPFC SHHFHELIMK DGRVLVVPCR NQDELIGRAR ISQGAGWSLR
ETACLGKSYD QMWSLMYFHR RDLRLAANAI CSAVPSHWVP TSRTTWSIHA KHEWMTTEDM
LTVWNRVWIQ ENPWMEDKTP VESWEEIPYL GKREDQWCGS LIGLTSRATW AKNIQAAINQ
VRSLIGNEEY TDYMPSMKRF RREEEEAGVL W


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