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Genome polyprotein [Cleaved into: Capsid protein C (Core protein); Protein prM; Peptide pr; Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1)] (Fragment)

 POLG_DEN1C              Reviewed;         791 AA.
P27913;
01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
01-AUG-1992, sequence version 1.
25-APR-2018, entry version 118.
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;
Flags: Fragment;
Dengue virus type 1 (strain Jamaica/CV1636/1977) (DENV-1).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Flaviviridae; Flavivirus; Dengue virus group.
NCBI_TaxID=11058;
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].
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).
-!- 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.
{ECO:0000250|UniProtKB:P17763}.
-!- 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. Envelope
protein is synthesized in the endoplasmic reticulum in the form of
heterodimer with protein prM. They play a role in virion budding
in the ER, and the newly formed immature particle is covered with
60 spikes composed of heterodimer between precursor prM and
envelope protein E. The virion is transported to the Golgi
apparatus where the low pH causes dissociation of PrM-E
heterodimers and formation of E homodimers. 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: 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:0000250|UniProtKB:P17763}.
-!- SUBUNIT: Capsid protein C: Homodimer. Interacts (via N-terminus)
with host EXOC1 (via C-terminus); this interaction results in
EXOC1 degradation through the proteasome degradation pathway.
Protein prM: Forms heterodimers with envelope protein E in the
endoplasmic reticulum and Golgi. Envelope protein E: Homodimer; in
the endoplasmic reticulum and Golgi. Interacts with protein prM.
Interacts with non-structural protein 1. Non-structural protein 1:
Homodimer; Homohexamer when secreted. Interacts with envelope
protein E. Non-structural protein 2A: Interacts (via N-terminus)
with serine protease NS3. {ECO:0000250|UniProtKB:P17763}.
-!- SUBCELLULAR LOCATION: Capsid protein C: Virion
{ECO:0000250|UniProtKB:P17763}. Host nucleus
{ECO:0000250|UniProtKB:P17763}. Host cytoplasm
{ECO:0000250|UniProtKB:P17763}. Host cytoplasm, host perinuclear
region {ECO:0000250|UniProtKB:P17763}.
-!- 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}.
-!- 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, wereas 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}.
-!- PTM: Envelope protein E: N-glycosylated.
{ECO:0000250|UniProtKB:P17763}.
-!- PTM: Non-structural protein 1: 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}.
-!- WEB RESOURCE: Name=Virus Pathogen Resource;
URL="http://www.viprbrc.org/brc/home.do?decorator=flavi_dengue";
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; D00501; BAA00393.1; -; Genomic_RNA.
PIR; A32401; A32401.
ProteinModelPortal; P27913; -.
SMR; P27913; -.
PRIDE; P27913; -.
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:0019031; C:viral envelope; IEA:UniProtKB-KW.
GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-KW.
GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
GO; GO:0046983; F:protein dimerization 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:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
CDD; cd12149; Flavi_E_C; 1.
Gene3D; 1.10.10.930; -; 1.
Gene3D; 1.10.8.970; -; 1.
Gene3D; 1.20.1280.260; -; 1.
Gene3D; 2.60.260.50; -; 1.
Gene3D; 2.60.40.350; -; 1.
Gene3D; 2.60.98.10; -; 3.
Gene3D; 3.30.387.10; -; 2.
Gene3D; 3.30.67.10; -; 4.
InterPro; IPR000069; Env_glycoprot_M_flavivir.
InterPro; IPR038302; Env_glycoprot_M_sf_flavivir.
InterPro; IPR013755; Flav_gly_cen_dom_subdom1.
InterPro; IPR001122; Flavi_capsidC.
InterPro; IPR037172; Flavi_capsidC_sf.
InterPro; IPR027287; Flavi_E_Ig-like.
InterPro; IPR026470; Flavi_E_Stem/Anchor_dom.
InterPro; IPR038345; Flavi_E_Stem/Anchor_dom_sf.
InterPro; IPR002535; Flavi_propep.
InterPro; IPR038688; Flavi_propep_sf.
InterPro; IPR000336; Flavivir/Alphavir_Ig-like_sf.
InterPro; IPR011998; Glycoprot_cen/dimer.
InterPro; IPR036253; Glycoprot_cen/dimer_sf.
InterPro; IPR038055; Glycoprot_E_dimer_dom.
InterPro; IPR013756; GlyE_cen_dom_subdom2.
InterPro; IPR014756; Ig_E-set.
Pfam; PF01003; Flavi_capsid; 1.
Pfam; PF02832; Flavi_glycop_C; 1.
Pfam; PF00869; Flavi_glycoprot; 1.
Pfam; PF01004; Flavi_M; 1.
Pfam; PF01570; Flavi_propep; 1.
SUPFAM; SSF101257; SSF101257; 1.
SUPFAM; SSF56983; SSF56983; 1.
SUPFAM; SSF81296; SSF81296; 1.
TIGRFAMs; TIGR04240; flavi_E_stem; 1.
3: Inferred from homology;
Capsid protein; Clathrin-mediated endocytosis of virus by host;
Cleavage on pair of basic residues; Disulfide bond;
Fusion of virus membrane with host endosomal membrane;
Fusion of virus membrane with host membrane; Glycoprotein;
Host cytoplasm; Host endoplasmic reticulum; Host membrane;
Host nucleus; Host-virus interaction; Membrane; Secreted;
Suppressor of RNA silencing; Transmembrane; Transmembrane helix;
Viral attachment to host cell; Viral envelope protein;
Viral nucleoprotein; Viral penetration into host cytoplasm; Virion;
Virus endocytosis by host; Virus entry into host cell; Zinc.
CHAIN 1 >791 Genome polyprotein.
/FTId=PRO_0000405205.
CHAIN 1 100 Capsid protein C.
{ECO:0000250|UniProtKB:P29990}.
/FTId=PRO_0000037889.
PROPEP 101 114 ER anchor for the capsid protein C,
removed in mature form by serine protease
NS3. {ECO:0000250|UniProtKB:P29990}.
/FTId=PRO_0000037890.
CHAIN 115 280 Protein prM.
{ECO:0000250|UniProtKB:P29990}.
/FTId=PRO_0000264652.
CHAIN 115 205 Peptide pr.
{ECO:0000250|UniProtKB:P29990}.
/FTId=PRO_0000264653.
CHAIN 206 280 Small envelope protein M.
{ECO:0000250|UniProtKB:P29990}.
/FTId=PRO_0000037891.
CHAIN 281 775 Envelope protein E.
{ECO:0000250|UniProtKB:P29990}.
/FTId=PRO_0000037892.
CHAIN 776 >791 Non-structural protein 1.
{ECO:0000250|UniProtKB:P29990}.
/FTId=PRO_0000037893.
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 753 775 Helical. {ECO:0000255}.
TOPO_DOM 776 >791 Extracellular. {ECO:0000255}.
REGION 1 15 Interaction with host EXOC1.
{ECO:0000250|UniProtKB:P17763}.
REGION 37 72 Hydrophobic; homodimerization of capsid
protein C.
{ECO:0000250|UniProtKB:P29990}.
REGION 378 391 Fusion peptide.
{ECO:0000250|UniProtKB:P14336}.
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}.
CARBOHYD 183 183 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 347 347 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 433 433 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
DISULFID 283 310 {ECO:0000250|UniProtKB:P17763}.
DISULFID 340 401 {ECO:0000250|UniProtKB:P17763}.
DISULFID 354 385 {ECO:0000250|UniProtKB:P17763}.
DISULFID 372 396 {ECO:0000250|UniProtKB:P17763}.
DISULFID 465 565 {ECO:0000250|UniProtKB:P17763}.
DISULFID 582 613 {ECO:0000250|UniProtKB:P17763}.
DISULFID 779 790 {ECO:0000250|UniProtKB:P17763}.
NON_TER 791 791
SEQUENCE 791 AA; 86845 MW; FFAE6F7E1C42F5C1 CRC64;
MNNQRKKTGR PSFNMLKRAR NRVSTGSQLA KRFSKGLLSG QGPMKLVMAF IAFLRFLAIP
PTAGILARWS SFKKNGAIKV LRGFKKEISS MLNIMNRRKR SVTMLLMLLP TALAFHLTTR
GGEPTLIVSK QERGKSLLFK TSAGVNMCTL IAMDLGELCE DTMTYKCPRI TERQPDDVDC
WCNATDTWVT YGTCSQTGEH RRDKRSVALA PHVGLGLETR TETWMSSEGA WKQIQKVETW
ALRHPGFTVI GLFLAHAIGT SITQKGIIFI LLMLVTPSMA MRCVGIGNRD FVEGLSGATW
VDVVLEHGSC VTTMAKNKPT LDIELLKTEV TNPAVLRKLC IEAKISNTTT DSRCPTQGEA
TLVEEQDANF VCRRTFVDRG WGNGCGLFGK GSFLTCAKFK CVTKLEGKIV QYENLKYSVI
VTVHTGDQHQ VGNETTEHGT IATITPQAPT SEIQLTDYGA LTLDCSPRTG LDFNRVVLLT
MKKKSWLVHK QWFLDLPLPW TSGASTSQET WNRQDLLVTF KTAHAKKQEV VVLGSQEGAM
HTALTGATEI QTSGTTTIFA GHLKCRLKMD KLTLKGMSYV MCTGSFKLEK EVAETQHGTV
LVQVKYEGTD APCKIPFSSQ DEKGVTQNGR LITANPIVID KEKPVNIEAE PPFGESYIVV
GSGEKALKLS WFKKGSSIGK MFEATARGAR RMAILGDTAW DFGSIGGVFT SVGKLIHQIF
GTAYGILFSG VSWTMKIGIG ILLTWLGLNS RSTSLSMTCI AVGMVTLYLG VMVQADSGCV
INWKGKELKC G


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