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

 POLG_DEN2U              Reviewed;         679 AA.
P18356;
01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 2.
20-JUN-2018, entry version 121.
RecName: Full=Genome polyprotein;
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 2 (strain Thailand/PUO-218/1980) (DENV-2).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Flaviviridae; Flavivirus.
NCBI_TaxID=11068;
NCBI_TaxID=53540; Aedimorphus.
NCBI_TaxID=53539; Diceromyia.
NCBI_TaxID=9538; Erythrocebus patas (Red guenon) (Cercopithecus patas).
NCBI_TaxID=9606; Homo sapiens (Human).
NCBI_TaxID=53541; Stegomyia.
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=3385407; DOI=10.1099/0022-1317-69-6-1391;
Gruenberg A., Woo W.S., Biedrzycka A., Wright P.J.;
"Partial nucleotide sequence and deduced amino acid sequence of the
structural proteins of dengue virus type 2, New Guinea C and PUO-218
strains.";
J. Gen. Virol. 69:1391-1398(1988).
[2]
STRUCTURE BY NMR OF 469-577.
PubMed=18004779; DOI=10.1002/prot.21806;
Huang K.C., Lee M.C., Wu C.W., Huang K.J., Lei H.Y., Cheng J.W.;
"Solution structure and neutralizing antibody binding studies of
domain III of the dengue-2 virus envelope protein.";
Proteins 70:1116-1119(2008).
[3]
STRUCTURE BY ELECTRON MICROSCOPY (24.0 ANGSTROMS) OF 15-95 AND
181-570.
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).
[4]
STRUCTURE BY ELECTRON MICROSCOPY (24.0 ANGSTROMS) OF 15-95 AND
181-575.
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).
-!- 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: 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.
{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: 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}.
-!- 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}.
-!- 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}.
-!- 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 (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; D00345; BAA00254.1; -; Genomic_RNA.
PIR; PS0043; PS0043.
PDB; 2JSF; NMR; -; A=469-577.
PDB; 2R6P; EM; 24.00 A; A/B/C=181-570.
PDB; 3C6R; EM; 25.00 A; A/B/C=181-575, D/E/F=15-95.
PDB; 3IXY; EM; -; D/E/F=15-95.
PDB; 3IYA; EM; -; A/B/C=181-575, D/E/F=15-95.
PDBsum; 2JSF; -.
PDBsum; 2R6P; -.
PDBsum; 3C6R; -.
PDBsum; 3IXY; -.
PDBsum; 3IYA; -.
ProteinModelPortal; P18356; -.
SMR; P18356; -.
PRIDE; P18356; -.
EvolutionaryTrace; P18356; -.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0044167; C:host cell endoplasmic reticulum membrane; 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: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; 1.10.8.970; -; 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; 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; PF02832; Flavi_glycop_C; 1.
Pfam; PF00869; Flavi_glycoprot; 1.
Pfam; PF01004; Flavi_M; 1.
Pfam; PF01570; Flavi_propep; 1.
SUPFAM; SSF56983; SSF56983; 1.
SUPFAM; SSF81296; SSF81296; 1.
TIGRFAMs; TIGR04240; flavi_E_stem; 1.
1: Evidence at protein level;
3D-structure; 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 endoplasmic reticulum; Host membrane; 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 >679 Genome polyprotein.
/FTId=PRO_0000405220.
PROPEP 1 14 ER anchor for the capsid protein C,
removed in mature form by serine protease
NS3. {ECO:0000250|UniProtKB:P29990}.
/FTId=PRO_0000037985.
CHAIN 15 180 Protein prM.
{ECO:0000250|UniProtKB:P29990}.
/FTId=PRO_0000308291.
CHAIN 15 105 Peptide pr.
{ECO:0000250|UniProtKB:P29990}.
/FTId=PRO_0000308292.
CHAIN 106 180 Small envelope protein M.
{ECO:0000250|UniProtKB:P29990}.
/FTId=PRO_0000037986.
CHAIN 181 675 Envelope protein E.
{ECO:0000250|UniProtKB:P29990}.
/FTId=PRO_0000037987.
CHAIN 676 >679 Non-structural protein 1.
{ECO:0000250|UniProtKB:P29990}.
/FTId=PRO_0000037988.
TRANSMEM 2 22 Helical. {ECO:0000255}.
TOPO_DOM 23 138 Extracellular. {ECO:0000255}.
TRANSMEM 139 159 Helical. {ECO:0000255}.
TOPO_DOM 160 165 Cytoplasmic. {ECO:0000255}.
TRANSMEM 166 180 Helical. {ECO:0000255}.
TOPO_DOM 181 625 Extracellular. {ECO:0000255}.
TRANSMEM 626 646 Helical. {ECO:0000255}.
TOPO_DOM 647 652 Cytoplasmic. {ECO:0000255}.
TRANSMEM 653 673 Helical. {ECO:0000255}.
TOPO_DOM 674 >679 Extracellular. {ECO:0000255}.
REGION 278 291 Fusion peptide.
{ECO:0000250|UniProtKB:P14336}.
SITE 14 15 Cleavage; by host signal peptidase.
{ECO:0000250|UniProtKB:P29990}.
SITE 105 106 Cleavage; by host furin.
{ECO:0000250|UniProtKB:P29990,
ECO:0000255}.
SITE 180 181 Cleavage; by host signal peptidase.
{ECO:0000250|UniProtKB:P29990}.
SITE 675 676 Cleavage; by host signal peptidase.
{ECO:0000250|UniProtKB:P29990}.
CARBOHYD 83 83 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 247 247 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 333 333 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
DISULFID 183 210 {ECO:0000250|UniProtKB:P17763}.
DISULFID 240 301 {ECO:0000250|UniProtKB:P17763}.
DISULFID 254 285 {ECO:0000250|UniProtKB:P17763}.
DISULFID 272 296 {ECO:0000250|UniProtKB:P17763}.
DISULFID 365 465 {ECO:0000250|UniProtKB:P17763}.
DISULFID 482 513 {ECO:0000250|UniProtKB:P17763}.
NON_TER 1 1
NON_TER 679 679
STRAND 484 494 {ECO:0000244|PDB:2JSF}.
STRAND 496 498 {ECO:0000244|PDB:2JSF}.
STRAND 500 509 {ECO:0000244|PDB:2JSF}.
STRAND 511 514 {ECO:0000244|PDB:2JSF}.
HELIX 522 524 {ECO:0000244|PDB:2JSF}.
STRAND 525 527 {ECO:0000244|PDB:2JSF}.
STRAND 537 541 {ECO:0000244|PDB:2JSF}.
STRAND 545 550 {ECO:0000244|PDB:2JSF}.
STRAND 553 561 {ECO:0000244|PDB:2JSF}.
TURN 563 565 {ECO:0000244|PDB:2JSF}.
STRAND 567 575 {ECO:0000244|PDB:2JSF}.
SEQUENCE 679 AA; 74932 MW; 1B5B881FC015F46B CRC64;
SAGMIIMLIP TVMAFHLTTR NGEPHMIVSR QEKGKSLLFK TEDGVNMCTL MAMDLGELCE
DTITYKCPLL RQNEPEDIDC WCNSTSTWVT YGTCTTTGEH RREKRSVALV PHVGMGLETR
TETWMSSEGA WKHAQRIEIW ILRHPGFTIM AAILAYTIGT THFQRALIFI LLTAVAPSMT
MRCIGISNRD FVEGVSGGSW VDIVLEHGSC VTTMAKNKPT LDFELIKTEA KQPATLRKYC
IEAKLTNTTT ESRCPTQGEP SLNEEQDKRF VCKHSMVDRG WGNGCGLFGK GGIVTCAMFT
CKKNMEGKVV QPENLEYTIV VTPHSGEEHA VGNDTGKHGK EIKVTPQSSI 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 RSTSLSVSLV
LVGIVTLYLG VMVQADSGC


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