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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); Non-structural protein 2A (NS2A)] (Fragment)

 POLG_YEFV8              Reviewed;        1163 AA.
P29165;
01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
01-DEC-1992, sequence version 1.
20-JUN-2018, entry version 124.
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;
Flags: Fragment;
Yellow fever virus (isolate Peru/1899/1981) (YFV).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Flaviviridae; Flavivirus.
NCBI_TaxID=31641;
NCBI_TaxID=7159; Aedes aegypti (Yellowfever mosquito) (Culex aegypti).
NCBI_TaxID=299629; Aedes luteocephalus (Mosquito).
NCBI_TaxID=7161; Aedes simpsoni.
NCBI_TaxID=9606; Homo sapiens (Human).
NCBI_TaxID=314293; Simiiformes.
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=2145394; DOI=10.1099/0022-1317-71-9-2115;
Ballinger-Crabtree M.E., Miller B.R.;
"Partial nucleotide sequence of South American yellow fever virus
strain 1899/81: structural proteins and NS1.";
J. Gen. Virol. 71:2115-2121(1990).
-!- 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.
{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 2A: Component of the viral RNA
replication complex that functions in virion assembly and
antagonizes the host immune response.
{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. {ECO:0000250|UniProtKB:P17763}.
-!- SUBCELLULAR LOCATION: Capsid protein C: Virion
{ECO:0000250|UniProtKB:P17763}. Host nucleus
{ECO:0000250|UniProtKB:P17763}. Host cytoplasm, host perinuclear
region {ECO:0000250|UniProtKB:P17763}. Host cytoplasm
{ECO:0000250|UniProtKB:P17763}.
-!- SUBCELLULAR LOCATION: Peptide pr: Secreted
{ECO:0000250|UniProtKB:P17763}.
-!- SUBCELLULAR LOCATION: Small envelope protein M: Virion membrane
{ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein
{ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum
membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane
protein {ECO:0000255}. Note=ER membrane retention is mediated by
the transmembrane domains. {ECO:0000250|UniProtKB:P03314}.
-!- SUBCELLULAR LOCATION: Envelope protein E: Virion membrane
{ECO:0000305}; Multi-pass membrane protein
{ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum
membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane
protein {ECO:0000255}. Note=ER membrane retention is mediated by
the transmembrane domains. {ECO:0000250|UniProtKB:P03314}.
-!- 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}.
-!- 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. The nascent capsid protein C contains a C-
terminal hydrophobic domain that act as a signal sequence for
translocation of prM into the lumen of the ER. Mature capsid
protein C is cleaved at a site upstream of this hydrophobic domain
by NS3. prM is cleaved in post-Golgi vesicles by a host furin,
releasing the mature small envelope protein M, and peptide pr.
Non-structural protein 2A-alpha, a C-terminally truncated form of
non-structural protein 2A, results from partial cleavage by NS3.
Specific enzymatic cleavages in vivo yield mature proteins peptide
2K acts as a signal sequence and is removed from the N-terminus of
NS4B by the host signal peptidase in the ER lumen. Signal cleavage
at the 2K-4B site requires a prior NS3 protease-mediated cleavage
at the 4A-2K site. {ECO:0000250|UniProtKB:P03314}.
-!- 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: N-glycosylated. The excreted form
is glycosylated and this is required for efficient secretion of
the protein from infected cells. {ECO:0000250|UniProtKB:P17763}.
-----------------------------------------------------------------------
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EMBL; D14458; BAA03355.1; -; Genomic_RNA.
PIR; JU0374; GNWVY8.
ProteinModelPortal; P29165; -.
SMR; P29165; -.
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: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:0004386; F:helicase activity; IEA:UniProtKB-KW.
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; 1.10.8.970; -; 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; IPR027287; Flavi_E_Ig-like.
InterPro; IPR026470; Flavi_E_Stem/Anchor_dom.
InterPro; IPR038345; Flavi_E_Stem/Anchor_dom_sf.
InterPro; IPR001157; Flavi_NS1.
InterPro; 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; PF00948; Flavi_NS1; 1.
Pfam; PF01570; Flavi_propep; 1.
SUPFAM; SSF56983; SSF56983; 1.
SUPFAM; SSF81296; SSF81296; 1.
TIGRFAMs; TIGR04240; flavi_E_stem; 1.
3: Inferred from homology;
ATP-binding; Capsid protein;
Clathrin-mediated endocytosis of virus by host;
Cleavage on pair of basic residues; Disulfide bond;
Fusion of virus membrane with host endosomal membrane;
Fusion of virus membrane with host membrane; Glycoprotein; Helicase;
Host cytoplasm; Host endoplasmic reticulum; Host membrane;
Host nucleus; Host-virus interaction; Hydrolase; Membrane;
Nucleotide-binding; Secreted; Suppressor of RNA silencing;
Transmembrane; Transmembrane helix; Viral attachment to host cell;
Viral envelope protein; Viral penetration into host cytoplasm; Virion;
Virus endocytosis by host; Virus entry into host cell; Zinc.
CHAIN 1 >1163 Genome polyprotein.
/FTId=PRO_0000405154.
CHAIN 1 101 Capsid protein C.
{ECO:0000250|UniProtKB:P03314}.
/FTId=PRO_0000037776.
PROPEP 102 121 ER anchor for the capsid protein C,
removed in mature form by serine protease
NS3. {ECO:0000250|UniProtKB:P03314}.
/FTId=PRO_0000037777.
CHAIN 122 285 Protein prM.
{ECO:0000250|UniProtKB:P29990}.
/FTId=PRO_0000261453.
CHAIN 122 210 Peptide pr.
{ECO:0000250|UniProtKB:P29990}.
/FTId=PRO_0000261454.
CHAIN 211 285 Small envelope protein M.
{ECO:0000250|UniProtKB:P29990}.
/FTId=PRO_0000037778.
CHAIN 286 778 Envelope protein E.
{ECO:0000250|UniProtKB:P29990}.
/FTId=PRO_0000037779.
CHAIN 779 1130 Non-structural protein 1.
{ECO:0000250|UniProtKB:P03314}.
/FTId=PRO_0000037780.
CHAIN 1131 >1163 Non-structural protein 2A.
{ECO:0000250|UniProtKB:P29990}.
/FTId=PRO_0000037781.
TOPO_DOM 1 104 Cytoplasmic. {ECO:0000255}.
TRANSMEM 105 125 Helical. {ECO:0000255}.
TOPO_DOM 126 244 Extracellular. {ECO:0000255}.
TRANSMEM 245 265 Helical. {ECO:0000255}.
TOPO_DOM 266 270 Cytoplasmic. {ECO:0000255}.
TRANSMEM 271 285 Helical. {ECO:0000305}.
TOPO_DOM 286 730 Extracellular. {ECO:0000255}.
TRANSMEM 731 751 Helical. {ECO:0000255}.
TOPO_DOM 752 757 Extracellular. {ECO:0000255}.
TRANSMEM 758 778 Helical. {ECO:0000255}.
TOPO_DOM 779 >1163 Extracellular. {ECO:0000255}.
REGION 38 72 Hydrophobic; homodimerization of capsid
protein C.
{ECO:0000250|UniProtKB:P29990}.
REGION 383 396 Fusion peptide.
{ECO:0000250|UniProtKB:P14336}.
SITE 101 102 Cleavage; by viral protease NS3.
{ECO:0000250|UniProtKB:P03314}.
SITE 121 122 Cleavage; by host signal peptidase.
{ECO:0000250|UniProtKB:P03314}.
SITE 210 211 Cleavage; by host furin.
{ECO:0000250|UniProtKB:P29990}.
SITE 285 286 Cleavage; by host signal peptidase.
{ECO:0000250|UniProtKB:P29990}.
SITE 778 779 Cleavage; by host signal peptidase.
{ECO:0000250|UniProtKB:P03314}.
SITE 1130 1131 Cleavage; by host.
{ECO:0000250|UniProtKB:P29990}.
CARBOHYD 134 134 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 150 150 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 908 908 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 986 986 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
DISULFID 288 315 {ECO:0000250|UniProtKB:P17763}.
DISULFID 345 406 {ECO:0000250|UniProtKB:P17763}.
DISULFID 359 390 {ECO:0000250|UniProtKB:P17763}.
DISULFID 377 401 {ECO:0000250|UniProtKB:P17763}.
DISULFID 467 568 {ECO:0000250|UniProtKB:P17763}.
DISULFID 585 615 {ECO:0000250|UniProtKB:P17763}.
DISULFID 782 793 {ECO:0000250|UniProtKB:P17763}.
DISULFID 833 921 {ECO:0000250|UniProtKB:P17763}.
DISULFID 957 1002 {ECO:0000250|UniProtKB:P17763}.
DISULFID 1058 1107 {ECO:0000250|UniProtKB:P17763}.
DISULFID 1069 1091 {ECO:0000250|UniProtKB:P17763}.
DISULFID 1090 1094 {ECO:0000250|UniProtKB:P17763}.
NON_TER 1163 1163
SEQUENCE 1163 AA; 128521 MW; 6BEBDA317D722E01 CRC64;
MSGRKAQGKT LGVNMVRQGV RSLSNKIKQK TKQIGNRPGP SRGVQGFIFF FLFNVLTGRK
ITAHLKKLWR MLDPRQGLAV LKKVKRVVAS LMRGLSSRKR RSYEVLTVQF LILGMLLMTG
GVTLVRKSRW LLLNVTSEDL GKTFSVGTGN CTTNILEAKN WCPDSMEYNC PNLSPREEPD
DIDCWCYGVE NVRVAYGKCD SAGRSRRSRR AIDLPTHENH GLKTRQEKWM TGRMGERQLQ
KIERWLVRNP FFAVTALAIA YLVGSNMTQR VVIALLVLAV GPAYSAHCIG ITDRDFIEGV
HGGTWVSATL EQDKCVTVMA PDKPSLDISL ETVAIDGPAE ARKVCYSAVL THVKINDKCP
STGEAHLAEE NEGDHACKRT YSDRGWGNGC GLFGKGSIVA CAKFTCAKSM SLFEVDQTKI
QYVIRAQLHV GAKQENWNAD IKTLKFDALS GSQEAEFTGY GKATLECQVQ TAVDFSNSYI
AEMEKESWIV DRQWAQDLTL PWQSGSGGVW REMHHLVEFE PPHAATIKVL ALGNQEGSLK
TALTGAMRVT KDTNGSNLYK LHGGHVSCRV KLSALTLKGT SYKMCTDKMS FVKNPTDTGH
GTAVMQVKVP KGAPCRIPVM VADDLTASVN KGILVTVNPI ASTNEDEVLI EVNPPFGDSY
IIVGTGDSRL TYQWHKEGSS IGKLFTQTMK GAERLAVMGD AAWDFSSAGG FFTSVGKGIH
MVFGSAFQGL FGGLSWITKV IMGAVLIWVG INMRNMTMSM SMILVGVIMM FLSLGVGADQ
GCAINFGKRE LKCGDGVFIF RDSDDWLNKY SYYPEDPVKL ASIVKASFEE GKCGLNSVDS
LEHEMWRSRA DEINAILEEN EVDISVVVQD PKNIYQRGTH PFSRIRDGLQ YGWKTWGKNL
VFSPGRKNGS FIIDGKSRKE CPFSNRVWNS LQIEEFGTGV FTTRVYMDAV FEYTMDCDGS
ILGAAVNGKK SAHGSPTFWM GSHEVNGTWM IHTLETLDYK ECEWPLTHTI GTSVEESDMF
MPRSIGGPVS SHNHIPGYKV QTNGPWMQVP LEVKREACPG TSVVVDGGCD GRGKSTRSTT
DSGKIIPEWC CRSCTMPPVS FHGSDGCWYP MEIRPRKTHD NHLVRSWVTA GEVHAVPFGL
VSMMIAMEVF LKKRQGPKQI LVG


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