ID   POLG_JAEVN              Reviewed;        1440 AA.
AC   P14403; P08769;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   25-OCT-2017, entry version 119.
DE   RecName: Full=Genome polyprotein;
DE   Contains:
DE     RecName: Full=Capsid protein C;
DE     AltName: Full=Core protein;
DE   Contains:
DE     RecName: Full=Protein prM;
DE   Contains:
DE     RecName: Full=Peptide pr;
DE   Contains:
DE     RecName: Full=Small envelope protein M;
DE     AltName: Full=Matrix protein;
DE   Contains:
DE     RecName: Full=Envelope protein E;
DE   Contains:
DE     RecName: Full=Non-structural protein 1;
DE              Short=NS1;
DE   Contains:
DE     RecName: Full=Non-structural protein 2A;
DE              Short=NS2A;
DE   Contains:
DE     RecName: Full=Serine protease subunit NS2B;
DE     AltName: Full=Flavivirin protease NS2B regulatory subunit;
DE     AltName: Full=Non-structural protein 2B;
DE   Contains:
DE     RecName: Full=Serine protease NS3;
DE              EC=3.4.21.91;
DE              EC=3.6.1.15;
DE              EC=3.6.4.13;
DE     AltName: Full=Flavivirin protease NS3 catalytic subunit;
DE     AltName: Full=Non-structural protein 3;
DE   Flags: Fragment;
OS   Japanese encephalitis virus (strain Nakayama).
OC   Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
OC   Flaviviridae; Flavivirus; Japanese encephalitis virus group.
OX   NCBI_TaxID=11076;
OH   NCBI_TaxID=8899; Ardeidae (herons).
OH   NCBI_TaxID=9913; Bos taurus (Bovine).
OH   NCBI_TaxID=308713; Culex gelidus.
OH   NCBI_TaxID=7178; Culex tritaeniorhynchus (Mosquito).
OH   NCBI_TaxID=9796; Equus caballus (Horse).
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=9823; Sus scrofa (Pig).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=3035787; DOI=10.1016/0042-6822(87)90207-8;
RA   McAda P.C., Mason P.W., Schmaljohn C.S., Dalrymple J.M., Mason T.L.,
RA   Fournier M.J.;
RT   "Partial nucleotide sequence of the Japanese encephalitis virus
RT   genome.";
RL   Virology 158:348-360(1987).
CC   -!- FUNCTION: Capsid protein C: Plays a role in virus budding by
CC       binding to the cell membrane and gathering the viral RNA into a
CC       nucleocapsid that forms the core of a mature virus particle.
CC       During virus entry, may induce genome penetration into the host
CC       cytoplasm after hemifusion induced by the surface proteins. Can
CC       migrate to the cell nucleus where it modulates host functions.
CC       Overcomes the anti-viral effects of host EXOC1 by sequestering and
CC       degrading the latter through the proteasome degradation pathway.
CC       {ECO:0000250|UniProtKB:P17763}.
CC   -!- FUNCTION: Capsid protein C: Inhibits RNA silencing by interfering
CC       with host Dicer. {ECO:0000250|UniProtKB:P03314}.
CC   -!- FUNCTION: Peptide pr: Prevents premature fusion activity of
CC       envelope proteins in trans-Golgi by binding to envelope protein E
CC       at pH6.0. After virion release in extracellular space, gets
CC       dissociated from E dimers. {ECO:0000250|UniProtKB:P17763}.
CC   -!- FUNCTION: Protein prM: Acts as a chaperone for envelope protein E
CC       during intracellular virion assembly by masking and inactivating
CC       envelope protein E fusion peptide. prM is the only viral peptide
CC       matured by host furin in the trans-Golgi network probably to avoid
CC       catastrophic activation of the viral fusion activity in acidic
CC       Golgi compartment prior to virion release. prM-E cleavage is
CC       inefficient, and many virions are only partially matured. These
CC       uncleaved prM would play a role in immune evasion.
CC       {ECO:0000250|UniProtKB:P17763}.
CC   -!- FUNCTION: Small envelope protein M: May play a role in virus
CC       budding. Exerts cytotoxic effects by activating a mitochondrial
CC       apoptotic pathway through M ectodomain. May display a viroporin
CC       activity. {ECO:0000250|UniProtKB:P17763}.
CC   -!- FUNCTION: Envelope protein E: Binds to host cell surface receptor
CC       and mediates fusion between viral and cellular membranes. Envelope
CC       protein is synthesized in the endoplasmic reticulum in the form of
CC       heterodimer with protein prM. They play a role in virion budding
CC       in the ER, and the newly formed immature particule is covered with
CC       60 spikes composed of heterodimer between precursor prM and
CC       envelope protein E. The virion is transported to the Golgi
CC       apparatus where the low pH causes dissociation of PrM-E
CC       heterodimers and formation of E homodimers. prM-E cleavage is
CC       inefficient, and many virions are only partially matured. These
CC       uncleaved prM would play a role in immune evasion.
CC       {ECO:0000250|UniProtKB:P17763}.
CC   -!- FUNCTION: Non-structural protein 1: Involved in immune evasion,
CC       pathogenesis and viral replication. Once cleaved off the
CC       polyprotein, is targeted to three destinations: the viral
CC       replication cycle, the plasma membrane and the extracellular
CC       compartment. Essential for viral replication. Required for
CC       formation of the replication complex and recruitment of other non-
CC       structural proteins to the ER-derived membrane structures.
CC       Excreted as a hexameric lipoparticle that plays a role against
CC       host immune response. Antagonizing the complement function. Binds
CC       to the host macrophages and dendritic cells. Inhibits signal
CC       transduction originating from Toll-like receptor 3 (TLR3).
CC       {ECO:0000250|UniProtKB:Q9Q6P4}.
CC   -!- FUNCTION: Non-structural protein 2A: Component of the viral RNA
CC       replication complex that functions in virion assembly and
CC       antagonizes the host alpha/beta interferon antiviral response.
CC       {ECO:0000250|UniProtKB:P14335}.
CC   -!- FUNCTION: Serine protease subunit NS2B: Required cofactor for the
CC       serine protease function of NS3. May have membrane-destabilizing
CC       activity and form viroporins (By similarity).
CC       {ECO:0000250|UniProtKB:P17763, ECO:0000255|PROSITE-
CC       ProRule:PRU00859}.
CC   -!- FUNCTION: Serine protease NS3: Displays three enzymatic
CC       activities: serine protease, NTPase and RNA helicase. NS3 serine
CC       protease, in association with NS2B, performs its autocleavage and
CC       cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM,
CC       NS2A-NS2B, NS2B-NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA
CC       helicase binds RNA and unwinds dsRNA in the 3' to 5' direction.
CC       {ECO:0000255|PROSITE-ProRule:PRU00860}.
CC   -!- FUNCTION: Non-structural protein 4A: Regulates the ATPase activity
CC       of the NS3 helicase activity. NS4A allows NS3 helicase to conserve
CC       energy during unwinding. {ECO:0000250|UniProtKB:Q9Q6P4}.
CC   -!- FUNCTION: Peptide 2k: Functions as a signal peptide for NS4B and
CC       is required for the interferon antagonism activity of the latter.
CC       {ECO:0000250|UniProtKB:P17763}.
CC   -!- FUNCTION: Non-structural protein 4B: Induces the formation of ER-
CC       derived membrane vesicles where the viral replication takes place.
CC       Inhibits interferon (IFN)-induced host STAT1 phosphorylation and
CC       nuclear translocation, thereby preventing the establishment of
CC       cellular antiviral state by blocking the IFN-alpha/beta pathway.
CC       Inhibits STAT2 translocation in the nucleus after IFN-alpha
CC       treatment. {ECO:0000250|UniProtKB:Q9Q6P4}.
CC   -!- FUNCTION: RNA-directed RNA polymerase NS5: Replicates the viral
CC       (+) and (-) RNA genome, and performs the capping of genomes in the
CC       cytoplasm. NS5 methylates viral RNA cap at guanine N-7 and ribose
CC       2'-O positions. Besides its role in RNA genome replication, also
CC       prevents the establishment of cellular antiviral state by blocking
CC       the interferon-alpha/beta (IFN-alpha/beta) signaling pathway.
CC       Inhibits host TYK2 and STAT2 phosphorylation, thereby preventing
CC       activation of JAK-STAT signaling pathway.
CC       {ECO:0000250|UniProtKB:Q9Q6P4}.
CC   -!- CATALYTIC ACTIVITY: Selective hydrolysis of -Xaa-Xaa-|-Yaa- bonds
CC       in which each of the Xaa can be either Arg or Lys and Yaa can be
CC       either Ser or Ala.
CC   -!- CATALYTIC ACTIVITY: NTP + H(2)O = NDP + phosphate.
CC   -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
CC       {ECO:0000250|UniProtKB:Q9Q6P4}.
CC   -!- SUBUNIT: Capsid protein C: Homodimer. Interacts (via N-terminus)
CC       with host EXOC1 (via C-terminus); this interaction results in
CC       EXOC1 degradation through the proteasome degradation pathway.
CC       Protein prM: Forms heterodimers with envelope protein E in the
CC       endoplasmic reticulum and Golgi. Envelope protein E: Homodimer; in
CC       the endoplasmic reticulum and Golgi. Interacts with protein prM.
CC       Interacts with non-structural protein 1. Non-structural protein 1:
CC       Homohexamer when secreted. NS1 interacts with NS4B. Interacts with
CC       host complement protein CFH; this interaction leads to the
CC       degradation of C3. Non-structural protein 2A: Interacts (via N-
CC       terminus) with serine protease NS3. Non-structural protein 2B:
CC       Forms a heterodimer with serine protease NS3. May form
CC       homooligomers. Serine protease NS3: Forms a heterodimer with NS2B.
CC       Interacts with NS4B. Interacts with unphosphorylated RNA-directed
CC       RNA polymerase NS5; this interaction stimulates RNA-directed RNA
CC       polymerase NS5 guanylyltransferase activity. Non-structural
CC       protein 4B: Interacts with serine protease NS3. RNA-directed RNA
CC       polymerase NS5: Homodimer. Interacts with host STAT2; this
CC       interaction inhibits the phosphorylation of the latter, and, when
CC       all viral proteins are present (polyprotein), targets STAT2 for
CC       degradation. Interacts with serine protease NS3.
CC       {ECO:0000250|UniProtKB:P17763}.
CC   -!- SUBCELLULAR LOCATION: Capsid protein C: Virion
CC       {ECO:0000250|UniProtKB:P17763}. Host nucleus
CC       {ECO:0000250|UniProtKB:P17763}. Host cytoplasm
CC       {ECO:0000250|UniProtKB:P06935}. Host cytoplasm, host perinuclear
CC       region {ECO:0000250|UniProtKB:P06935}.
CC   -!- SUBCELLULAR LOCATION: Peptide pr: Secreted
CC       {ECO:0000250|UniProtKB:P17763}.
CC   -!- SUBCELLULAR LOCATION: Small envelope protein M: Virion membrane
CC       {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum
CC       membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane
CC       protein {ECO:0000255}. Note=ER membrane retention is mediated by
CC       the transmembrane domains. {ECO:0000250|UniProtKB:P03314}.
CC   -!- SUBCELLULAR LOCATION: Envelope protein E: Virion membrane
CC       {ECO:0000305}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum
CC       membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane
CC       protein {ECO:0000255}. Note=ER membrane retention is mediated by
CC       the transmembrane domains. {ECO:0000250|UniProtKB:P03314}.
CC   -!- SUBCELLULAR LOCATION: Non-structural protein 1: Secreted
CC       {ECO:0000250|UniProtKB:P17763}. Host endoplasmic reticulum
CC       membrane; Peripheral membrane protein; Lumenal side
CC       {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived
CC       vesicles hosting the replication complex.
CC       {ECO:0000250|UniProtKB:Q9Q6P4}.
CC   -!- SUBCELLULAR LOCATION: Non-structural protein 2A: Host endoplasmic
CC       reticulum membrane {ECO:0000250|UniProtKB:P14335}; Multi-pass
CC       membrane protein {ECO:0000250|UniProtKB:P17763}.
CC   -!- SUBCELLULAR LOCATION: Serine protease subunit NS2B: Host
CC       endoplasmic reticulum membrane; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:P17763}.
CC   -!- SUBCELLULAR LOCATION: Serine protease NS3: Host endoplasmic
CC       reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860};
CC       Peripheral membrane protein {ECO:0000255|PROSITE-
CC       ProRule:PRU00860}; Cytoplasmic side {ECO:0000255|PROSITE-
CC       ProRule:PRU00860}. Note=Remains non-covalently associated to
CC       serine protease subunit NS2B. {ECO:0000255|PROSITE-
CC       ProRule:PRU00860}.
CC   -!- DOMAIN: The transmembrane domains of the small envelope protein M
CC       and envelope protein E contain an endoplasmic reticulum retention
CC       signal. {ECO:0000250|UniProtKB:P17763}.
CC   -!- PTM: Genome polyprotein: Specific enzymatic cleavages in vivo
CC       yield mature proteins. Cleavages in the lumen of endoplasmic
CC       reticulum are performed by host signal peptidase, whereas
CC       cleavages in the cytoplasmic side are performed by serine protease
CC       NS3. Signal cleavage at the 2K-4B site requires a prior NS3
CC       protease-mediated cleavage at the 4A-2K site.
CC       {ECO:0000250|UniProtKB:P17763}.
CC   -!- PTM: Protein prM: Cleaved in post-Golgi vesicles by a host furin,
CC       releasing the mature small envelope protein M, and peptide pr.
CC       This cleavage is incomplete as up to 30% of viral particles still
CC       carry uncleaved prM. {ECO:0000250|UniProtKB:P17763}.
CC   -!- PTM: Envelope protein E: N-glycosylated.
CC       {ECO:0000250|UniProtKB:P17763}.
CC   -!- PTM: Non-structural protein 1: N-glycosylated. The excreted form
CC       is glycosylated and this is required for efficient secretion of
CC       the protein from infected cells. {ECO:0000250|UniProtKB:P17763}.
CC   -!- PTM: RNA-directed RNA polymerase NS5: Phosphorylated on serines
CC       residues. This phosphorylation may trigger NS5 nuclear
CC       localization. {ECO:0000250|UniProtKB:P17763}.
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DR   EMBL; M16574; AAA46251.1; -; Genomic_RNA.
DR   PIR; A27844; GNWVJF.
DR   PDB; 4R8T; X-ray; 2.13 A; A=1352-1369.
DR   PDBsum; 4R8T; -.
DR   ProteinModelPortal; P14403; -.
DR   SMR; P14403; -.
DR   PRIDE; P14403; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0044220; C:host cell perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
DR   GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
DR   GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003725; F:double-stranded RNA binding; IEA:InterPro.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0075512; P:clathrin-dependent endocytosis of virus by host cell; IEA:UniProtKB-KW.
DR   GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
DR   GO; GO:0039563; P:suppression by virus of host STAT1 activity; IEA:UniProtKB-KW.
DR   GO; GO:0039564; P:suppression by virus of host STAT2 activity; IEA:UniProtKB-KW.
DR   GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; IEA:UniProtKB-KW.
DR   GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR   CDD; cd12149; Flavi_E_C; 1.
DR   Gene3D; 2.60.40.350; -; 1.
DR   Gene3D; 3.30.387.10; -; 1.
DR   Gene3D; 3.30.67.10; -; 1.
DR   InterPro; IPR000069; Env_glycoprot_M_flavivir.
DR   InterPro; IPR013755; Flav_gly_cen_dom_subdom1.
DR   InterPro; IPR001122; Flavi_capsidC.
DR   InterPro; IPR027287; Flavi_E_Ig-like.
DR   InterPro; IPR026470; Flavi_E_Stem/Anchor_dom.
DR   InterPro; IPR001157; Flavi_NS1.
DR   InterPro; IPR000752; Flavi_NS2A.
DR   InterPro; IPR000487; Flavi_NS2B.
DR   InterPro; IPR002535; Flavi_propep.
DR   InterPro; IPR000336; Flavivir/Alphavir_Ig-like.
DR   InterPro; IPR011998; Glycoprot_cen/dimer.
DR   InterPro; IPR036253; Glycoprot_cen/dimer_sf.
DR   InterPro; IPR013756; GlyE_cen_dom_subdom2.
DR   InterPro; IPR014756; Ig_E-set.
DR   Pfam; PF01003; Flavi_capsid; 1.
DR   Pfam; PF02832; Flavi_glycop_C; 1.
DR   Pfam; PF00869; Flavi_glycoprot; 1.
DR   Pfam; PF01004; Flavi_M; 1.
DR   Pfam; PF00948; Flavi_NS1; 1.
DR   Pfam; PF01005; Flavi_NS2A; 1.
DR   Pfam; PF01002; Flavi_NS2B; 1.
DR   Pfam; PF01570; Flavi_propep; 1.
DR   SUPFAM; SSF56983; SSF56983; 1.
DR   SUPFAM; SSF81296; SSF81296; 1.
DR   TIGRFAMs; TIGR04240; flavi_E_stem; 1.
DR   PROSITE; PS51527; FLAVIVIRUS_NS2B; 1.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Capsid protein;
KW   Clathrin-mediated endocytosis of virus by host;
KW   Cleavage on pair of basic residues; Disulfide bond;
KW   Fusion of virus membrane with host endosomal membrane;
KW   Fusion of virus membrane with host membrane; Glycoprotein; Helicase;
KW   Host cytoplasm; Host endoplasmic reticulum; Host membrane;
KW   Host nucleus; Host-virus interaction; Hydrolase;
KW   Inhibition of host innate immune response by virus;
KW   Inhibition of host interferon signaling pathway by virus;
KW   Inhibition of host STAT1 by virus; Inhibition of host STAT2 by virus;
KW   Membrane; Multifunctional enzyme; Nucleotide-binding; Protease;
KW   Secreted; Serine protease; Suppressor of RNA silencing; Transmembrane;
KW   Transmembrane helix; Viral attachment to host cell;
KW   Viral envelope protein; Viral immunoevasion;
KW   Viral penetration into host cytoplasm; Virion;
KW   Virus endocytosis by host; Virus entry into host cell; Zinc.
FT   CHAIN        <1  >1440       Genome polyprotein.
FT                                /FTId=PRO_0000405200.
FT   CHAIN        <1     31       Capsid protein C.
FT                                {ECO:0000250|UniProtKB:P06935}.
FT                                /FTId=PRO_0000037869.
FT   PROPEP       32     53       ER anchor for the capsid protein C,
FT                                removed in mature form by serine protease
FT                                NS3. {ECO:0000250|UniProtKB:P06935}.
FT                                /FTId=PRO_0000405201.
FT   CHAIN        54    222       Protein prM.
FT                                {ECO:0000250|UniProtKB:P06935}.
FT                                /FTId=PRO_0000405202.
FT   CHAIN        54    146       Peptide pr.
FT                                {ECO:0000250|UniProtKB:P06935}.
FT                                /FTId=PRO_0000037870.
FT   CHAIN       147    222       Small envelope protein M.
FT                                {ECO:0000250|UniProtKB:P06935}.
FT                                /FTId=PRO_0000037871.
FT   CHAIN       223    722       Envelope protein E.
FT                                {ECO:0000250|UniProtKB:P06935}.
FT                                /FTId=PRO_0000037872.
FT   CHAIN       723   1074       Non-structural protein 1.
FT                                {ECO:0000250|UniProtKB:P06935}.
FT                                /FTId=PRO_0000037873.
FT   CHAIN      1075   1301       Non-structural protein 2A.
FT                                {ECO:0000250|UniProtKB:P06935}.
FT                                /FTId=PRO_0000037874.
FT   CHAIN      1302   1432       Serine protease subunit NS2B.
FT                                {ECO:0000250|UniProtKB:P06935}.
FT                                /FTId=PRO_0000037875.
FT   CHAIN      1433  >1440       Serine protease NS3.
FT                                {ECO:0000250|UniProtKB:P06935}.
FT                                /FTId=PRO_0000037876.
FT   TRANSMEM     36     56       Helical. {ECO:0000255}.
FT   TOPO_DOM     57    180       Extracellular. {ECO:0000255}.
FT   TRANSMEM    181    201       Helical. {ECO:0000255}.
FT   TOPO_DOM    202    207       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    208    222       Helical. {ECO:0000305}.
FT   TOPO_DOM    223    674       Extracellular. {ECO:0000255}.
FT   TRANSMEM    675    695       Helical. {ECO:0000255}.
FT   TOPO_DOM    696    701       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    702    722       Helical. {ECO:0000255}.
FT   TOPO_DOM    723   1147       Extracellular. {ECO:0000255}.
FT   TRANSMEM   1148   1168       Helical. {ECO:0000255}.
FT   TOPO_DOM   1169   1178       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   1179   1199       Helical. {ECO:0000255}.
FT   TOPO_DOM   1200   1200       Lumenal. {ECO:0000255}.
FT   TRANSMEM   1201   1221       Helical. {ECO:0000255}.
FT   TOPO_DOM   1222   1237       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   1238   1258       Helical. {ECO:0000255}.
FT   TOPO_DOM   1259   1269       Lumenal. {ECO:0000255}.
FT   TRANSMEM   1270   1290       Helical. {ECO:0000255}.
FT   TOPO_DOM   1291   1302       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   1303   1323       Helical. {ECO:0000255}.
FT   TOPO_DOM   1324   1326       Lumenal. {ECO:0000255}.
FT   TRANSMEM   1327   1347       Helical. {ECO:0000255}.
FT   TOPO_DOM   1348   1404       Cytoplasmic. {ECO:0000255}.
FT   INTRAMEM   1405   1425       Helical. {ECO:0000255}.
FT   TOPO_DOM   1426  >1440       Cytoplasmic. {ECO:0000255}.
FT   REGION      320    333       Fusion peptide.
FT                                {ECO:0000250|UniProtKB:P14336}.
FT   REGION     1355   1394       Interacts with and activates NS3
FT                                protease. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00859}.
FT   SITE         31     32       Cleavage; by viral protease NS3.
FT                                {ECO:0000250|UniProtKB:P06935}.
FT   SITE         53     54       Cleavage; by host signal peptidase.
FT                                {ECO:0000250|UniProtKB:P06935}.
FT   SITE        146    147       Cleavage; by host furin.
FT                                {ECO:0000250|UniProtKB:P06935}.
FT   SITE        222    223       Cleavage; by host signal peptidase.
FT                                {ECO:0000250|UniProtKB:P06935}.
FT   SITE        722    723       Cleavage; by host signal peptidase.
FT                                {ECO:0000250|UniProtKB:P06935}.
FT   SITE       1074   1075       Cleavage; by host.
FT                                {ECO:0000250|UniProtKB:P06935}.
FT   SITE       1301   1302       Cleavage; by viral protease NS3.
FT                                {ECO:0000250|UniProtKB:P06935}.
FT   SITE       1432   1433       Cleavage; by autolysis.
FT                                {ECO:0000250|UniProtKB:P06935}.
FT   CARBOHYD     68     68       N-linked (GlcNAc...) asparagine; by host.
FT                                {ECO:0000250|UniProtKB:P14335}.
FT   CARBOHYD    376    376       N-linked (GlcNAc...) asparagine; by host.
FT                                {ECO:0000255}.
FT   CARBOHYD    852    852       N-linked (GlcNAc...) asparagine; by host.
FT                                {ECO:0000250|UniProtKB:Q9Q6P4}.
FT   CARBOHYD    929    929       N-linked (GlcNAc...) asparagine; by host.
FT                                {ECO:0000250|UniProtKB:Q9Q6P4}.
FT   DISULFID    225    252       {ECO:0000250|UniProtKB:Q9Q6P4}.
FT   DISULFID    282    343       {ECO:0000250|UniProtKB:Q9Q6P4}.
FT   DISULFID    282    338       {ECO:0000250|UniProtKB:P06935}.
FT   DISULFID    296    327       {ECO:0000250|UniProtKB:Q9Q6P4}.
FT   DISULFID    314    343       {ECO:0000250|UniProtKB:P06935}.
FT   DISULFID    314    338       {ECO:0000250|UniProtKB:Q9Q6P4}.
FT   DISULFID    412    509       {ECO:0000250|UniProtKB:Q9Q6P4}.
FT   DISULFID    526    557       {ECO:0000250|UniProtKB:Q9Q6P4}.
FT   DISULFID    726    737       {ECO:0000250|UniProtKB:Q9Q6P4}.
FT   DISULFID    777    865       {ECO:0000250|UniProtKB:Q9Q6P4}.
FT   DISULFID    901    945       {ECO:0000250|UniProtKB:Q9Q6P4}.
FT   DISULFID   1002   1051       {ECO:0000250|UniProtKB:Q9Q6P4}.
FT   DISULFID   1013   1034       {ECO:0000250|UniProtKB:Q9Q6P4}.
FT   DISULFID   1035   1038       {ECO:0000250|UniProtKB:Q9Q6P4}.
FT   NON_TER       1      1
FT   NON_TER    1440   1440
FT   STRAND     1352   1359       {ECO:0000244|PDB:4R8T}.
FT   HELIX      1365   1368       {ECO:0000244|PDB:4R8T}.
SQ   SEQUENCE   1440 AA;  158185 MW;  4D489A365A3C2E6E CRC64;
     SVAMKHLTSF KRELGTLIDA VNKRGRKQNK RGGNEGSIMW LASLAVVIAC AGAMKLSNFQ
     GKLLMTVNNT DIADVIVIPN PSKGENRCWV RAIDVGYMCE DTITYECPKL TMGNDPEDVD
     CWCDNQEVYV QYGRCTRTRH SKRSRRSVSV QTHGESSLVN KKEAWLDSTK ATRYLMKTEN
     WIVRNPGYAF LAAILGWMLG SNNGQRRWYF TILLLLVAPA YSFNCLGMGN RDFIEGASGA
     TWVDLVLEGD SCLTIMANDK PTLDVRMINI EAVQLAEVRS YCYHASVTDI STVARCPTTG
     EAHNEKRADS SYVCKQGFTD RGWGNGCGLF GKGSIDTCAK FSCTSKAIGR TIQPENIKYE
     VGIFVHGTTT SENHGNYSAQ VGASQAAKFT VTPNAPSITL KLGDYGEVTL DCEPRSGLNT
     EAFYVMTVGS KSFLVHREWF HDLALPWTPP SSTAWRNREL LMEFEEAHAT KQSVVALGSQ
     EGGLHQALAG AIVVEYSSSV KLTSGHLKCR LKMDKLALKG TTYGMCTEKF SFAKNPADTG
     HGTVVIELSY SGSDGPCKIP IVSVASLNDM TPVGRLVTVN PFVATSSANS KVLVEMEPPF
     GDSYIVVGRG DKQINHHWHK AGSTLGKAFS TTLKGAQRLA ALGDTAWDFG SIGGVFNSIG
     KAVHQVFGGA FRTLFGGMSW ITQGLMGALL LWMGVNARDR SIALAFLATG GVLVFLATNV
     HADTGCAIDI TRKEMRCGSG IFVHNDVEAW VDRYKYLPET PRSLAKIVHK AHKEGVCGVR
     SVTRLEHQMW EAVRDELNVL LKENAVDLSV VVNKPVGRYR SAPKRLSMTQ EKFEMGWKAW
     GKSILFAPEL ANSTFVVDGP ETKECPDEHR AWNSIEIEDF GFGITSTRVW LKIREESTDE
     CDGAIIGTAV KGHVAVHSDL SYWIESRYND TWKLERAVFG EVKSCTWPET HTLWGDGVEE
     SELIIPHTIA GPKSKHNRRE GYKTQNQGPW DENGIVLDFD YCPGTKVTIT EDCGKRGPSV
     RTTTDSGKLI TDWCCRSCSL PPLRFRTENG CWYGMEIRPV RHDETTLVRS QVDAFNGEMV
     DPFQLGLLVM FLATQEVLRK RWTARLTIPA VLGALLVLML GGITYTDLAR YVVLVAAAFA
     EANSGGDVLH LALIAVFKIQ PAFLVMNMLS TRWTNQENVV LVLGAAFFHL ASVDLQIGVH
     GILNAAAIAW MIVRAITFPT TSSVTMPVLA LLTPGMRALY LDTYRIILLV IGICSLLQER
     KKTMAKKKGA VLLGLALTST GWFSPTTIAA GLMVCNPNKK RGWPATEFLS AVGLMFAIVG
     GLAELDIESM SIPFMLAGLM AVSYVVSGKA TDMWLERAAD ISWEMDAAIT GSSRRLDVKL
     DDDGDFHLID DPGVPWKVWV LRMSCIGLAA LTPWAIVPAA FGYWLTLKTT KRGGVFWDTP
//