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   22-FEB-2023, entry version 143.
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 {ECO:0000250|UniProtKB:P27395};
DE              EC=3.6.1.15 {ECO:0000250|UniProtKB:P27395};
DE              EC=3.6.4.13 {ECO:0000250|UniProtKB:P27395};
DE     AltName: Full=Flavivirin protease NS3 catalytic subunit;
DE     AltName: Full=Non-structural protein 3;
DE   Flags: Fragment;
OS   Japanese encephalitis virus (strain Nakayama) (JEV).
OC   Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Flasuviricetes;
OC   Amarillovirales; Flaviviridae; Flavivirus.
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 genome.";
RL   Virology 158:348-360(1987).
CC   -!- FUNCTION: [Capsid protein C]: Plays a role in virus budding by binding
CC       to the cell membrane and gathering the viral RNA into a nucleocapsid
CC       that forms the core of a mature virus particle. During virus entry, may
CC       induce genome penetration into the host cytoplasm after hemifusion
CC       induced by the surface proteins. Can migrate to the cell nucleus where
CC       it modulates host functions. Overcomes the anti-viral effects of host
CC       EXOC1 by sequestering and degrading the latter through the proteasome
CC       degradation pathway. {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 envelope
CC       proteins in trans-Golgi by binding to envelope protein E at pH 6.0.
CC       After virion release in extracellular space, gets dissociated from E
CC       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 Golgi
CC       compartment prior to virion release. prM-E cleavage is inefficient, and
CC       many virions are only partially matured. These uncleaved prM would play
CC       a role in immune evasion. {ECO:0000250|UniProtKB:P17763}.
CC   -!- FUNCTION: [Small envelope protein M]: May play a role in virus budding.
CC       Exerts cytotoxic effects by activating a mitochondrial apoptotic
CC       pathway through M ectodomain. May display a viroporin activity.
CC       {ECO:0000250|UniProtKB:P17763}.
CC   -!- FUNCTION: [Envelope protein E]: Binds to host cell surface receptor and
CC       mediates fusion between viral and cellular membranes. Envelope protein
CC       is synthesized in the endoplasmic reticulum in the form of heterodimer
CC       with protein prM. They play a role in virion budding in the ER, and the
CC       newly formed immature particle is covered with 60 spikes composed of
CC       heterodimer between precursor prM and envelope protein E. The virion is
CC       transported to the Golgi apparatus where the low pH causes dissociation
CC       of PrM-E 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 polyprotein,
CC       is targeted to three destinations: the viral replication cycle, the
CC       plasma membrane and the extracellular compartment. Essential for viral
CC       replication. Required for formation of the replication complex and
CC       recruitment of other non-structural proteins to the ER-derived membrane
CC       structures. Excreted as a hexameric lipoparticle that plays a role
CC       against host immune response. Antagonizing the complement function.
CC       Binds 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 antagonizes
CC       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-ProRule:PRU00859}.
CC   -!- FUNCTION: [Serine protease NS3]: Displays three enzymatic activities:
CC       serine protease, NTPase and RNA helicase. NS3 serine protease, in
CC       association with NS2B, performs its autocleavage and cleaves the
CC       polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B-
CC       NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and
CC       unwinds dsRNA in the 3' to 5' direction. {ECO:0000255|PROSITE-
CC       ProRule:PRU00860}.
CC   -!- FUNCTION: Non-structural protein 4A: Regulates the ATPase activity of
CC       the NS3 helicase activity. NS4A allows NS3 helicase to conserve energy
CC       during unwinding. {ECO:0000250|UniProtKB:Q9Q6P4}.
CC   -!- FUNCTION: Peptide 2k: Functions as a signal peptide for NS4B and is
CC       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 (By
CC       similarity). Inhibits interferon (IFN)-induced host STAT1
CC       phosphorylation and nuclear translocation, thereby preventing the
CC       establishment of cellular antiviral state by blocking the IFN-
CC       alpha/beta pathway (By similarity). Inhibits STAT2 translocation in the
CC       nucleus after IFN-alpha treatment (By similarity).
CC       {ECO:0000250|UniProtKB:Q9Q6P4}.
CC   -!- FUNCTION: RNA-directed RNA polymerase NS5: Replicates the viral (+) and
CC       (-) RNA genome (By similarity). Performs the capping of genomes in the
CC       cytoplasm. NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O
CC       positions (By similarity). Besides its role in RNA genome replication,
CC       also prevents the establishment of cellular antiviral state by blocking
CC       the interferon-alpha/beta (IFN-alpha/beta) signaling pathway (By
CC       similarity). Inhibits host TYK2 and STAT2 phosphorylation, thereby
CC       preventing activation of JAK-STAT signaling pathway (By similarity).
CC       {ECO:0000250|UniProtKB:P27395, ECO:0000250|UniProtKB:Q9Q6P4}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Selective hydrolysis of -Xaa-Xaa-|-Yaa- bonds in which each of
CC         the Xaa can be either Arg or Lys and Yaa can be either Ser or Ala.;
CC         EC=3.4.21.91;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-
CC         diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC         Evidence={ECO:0000250|UniProtKB:Q9Q6P4};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC       Note=For RNA-directed RNA polymerase NS5 activity; Mn(2+) is more
CC       effective than Mg(2+). {ECO:0000250|UniProtKB:P27395};
CC   -!- SUBUNIT: [Capsid protein C]: Homodimer (By similarity). Interacts (via
CC       N-terminus) with host EXOC1 (via C-terminus); this interaction results
CC       in EXOC1 degradation through the proteasome degradation pathway (By
CC       similarity). {ECO:0000250|UniProtKB:P17763}.
CC   -!- SUBUNIT: [Protein prM]: Forms heterodimers with envelope protein E in
CC       the endoplasmic reticulum and Golgi. {ECO:0000250|UniProtKB:P17763}.
CC   -!- SUBUNIT: [Envelope protein E]: Homodimer; in the endoplasmic reticulum
CC       and Golgi (By similarity). Interacts with protein prM (By similarity).
CC       Interacts with non-structural protein 1 (By similarity).
CC       {ECO:0000250|UniProtKB:P17763}.
CC   -!- SUBUNIT: [Non-structural protein 1]: Homodimer; Homohexamer when
CC       secreted (By similarity). Interacts with envelope protein E (By
CC       similarity). NS1 interacts with NS4B (By similarity). Interacts with
CC       host complement protein CFH; this interaction leads to the degradation
CC       of C3 (By similarity). {ECO:0000250|UniProtKB:Q9Q6P4}.
CC   -!- SUBUNIT: [Non-structural protein 2A]: Interacts (via N-terminus) with
CC       serine protease NS3. {ECO:0000250|UniProtKB:P03314}.
CC   -!- SUBUNIT: [Serine protease subunit NS2B]: Forms a heterodimer with
CC       serine protease NS3 (By similarity). May form homooligomers (By
CC       similarity). {ECO:0000250|UniProtKB:P17763}.
CC   -!- SUBUNIT: [Serine protease NS3]: Forms a heterodimer with NS2B (By
CC       similarity). Interacts with non-structural protein 2A (via N-terminus)
CC       (By similarity). Interacts with NS4B (By similarity). Interacts with
CC       unphosphorylated RNA-directed RNA polymerase NS5; this interaction
CC       stimulates RNA-directed RNA polymerase NS5 guanylyltransferase activity
CC       (By similarity). {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 region
CC       {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 membrane
CC       {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein
CC       {ECO:0000255}. Note=ER membrane retention is mediated by the
CC       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 membrane
CC       {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein
CC       {ECO:0000255}. Note=ER membrane retention is mediated by the
CC       transmembrane domains. {ECO:0000250|UniProtKB:P03314}.
CC   -!- SUBCELLULAR LOCATION: [Non-structural protein 1]: Secreted
CC       {ECO:0000250|UniProtKB:P17763}. Host endoplasmic reticulum membrane;
CC       Peripheral membrane protein; Lumenal side
CC       {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles
CC       hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}.
CC   -!- SUBCELLULAR LOCATION: [Non-structural protein 2A]: Host endoplasmic
CC       reticulum membrane {ECO:0000250|UniProtKB:P14335}; Multi-pass membrane
CC       protein {ECO:0000250|UniProtKB:P17763}.
CC   -!- SUBCELLULAR LOCATION: [Serine protease subunit NS2B]: Host endoplasmic
CC       reticulum membrane; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:P17763}.
CC   -!- SUBCELLULAR LOCATION: [Serine protease NS3]: Host endoplasmic reticulum
CC       membrane {ECO:0000255|PROSITE-ProRule:PRU00860}; Peripheral membrane
CC       protein {ECO:0000255|PROSITE-ProRule:PRU00860}; Cytoplasmic side
CC       {ECO:0000255|PROSITE-ProRule:PRU00860}. Note=Remains non-covalently
CC       associated to serine protease subunit NS2B. {ECO:0000255|PROSITE-
CC       ProRule:PRU00860}.
CC   -!- DOMAIN: The transmembrane domains of the small envelope protein M and
CC       envelope protein E contain an endoplasmic reticulum retention signal.
CC       {ECO:0000250|UniProtKB:P17763}.
CC   -!- PTM: [Genome polyprotein]: Specific enzymatic cleavages in vivo yield
CC       mature proteins. Cleavages in the lumen of endoplasmic reticulum are
CC       performed by host signal peptidase, whereas cleavages in the
CC       cytoplasmic side are performed by serine protease NS3. Signal cleavage
CC       at the 2K-4B site requires a prior NS3 protease-mediated cleavage at
CC       the 4A-2K site. {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. This
CC       cleavage is incomplete as up to 30% of viral particles still carry
CC       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 is
CC       glycosylated and this is required for efficient secretion of the
CC       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 localization.
CC       {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   SMR; P14403; -.
DR   ABCD; P14403; 1 sequenced antibody.
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:0016020; C: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:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003725; F:double-stranded RNA binding; IEA:InterPro.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
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:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0039563; P:suppression by virus of host JAK-STAT cascade via inhibition of STAT1 activity; IEA:UniProtKB-KW.
DR   GO; GO:0039564; P:suppression by virus of host JAK-STAT cascade via inhibition of 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   CDD; cd17038; Flavi_M; 1.
DR   Gene3D; 1.10.10.930; -; 1.
DR   Gene3D; 1.20.1280.260; -; 1.
DR   Gene3D; 2.40.10.120; -; 1.
DR   Gene3D; 2.60.40.350; -; 1.
DR   Gene3D; 1.10.8.970; Flavivirus envelope glycoprotein M-like; 1.
DR   Gene3D; 2.60.260.50; Flavivirus polyprotein propeptide domain; 1.
DR   Gene3D; 2.60.98.10; Tick-borne Encephalitis virus Glycoprotein, domain 1; 1.
DR   Gene3D; 3.30.67.10; Viral Envelope Glycoprotein, domain 2; 1.
DR   Gene3D; 3.30.387.10; Viral Envelope Glycoprotein, domain 3; 1.
DR   InterPro; IPR000069; Env_glycoprot_M_flavivir.
DR   InterPro; IPR038302; Env_glycoprot_M_sf_flavivir.
DR   InterPro; IPR013755; Flav_gly_cen_dom_subdom1.
DR   InterPro; IPR001122; Flavi_capsidC.
DR   InterPro; IPR037172; Flavi_capsidC_sf.
DR   InterPro; IPR027287; Flavi_E_Ig-like.
DR   InterPro; IPR026470; Flavi_E_Stem/Anchor_dom.
DR   InterPro; IPR038345; Flavi_E_Stem/Anchor_dom_sf.
DR   InterPro; IPR001157; Flavi_NS1.
DR   InterPro; IPR000752; Flavi_NS2A.
DR   InterPro; IPR000487; Flavi_NS2B.
DR   InterPro; IPR002535; Flavi_propep.
DR   InterPro; IPR038688; Flavi_propep_sf.
DR   InterPro; IPR000336; Flavivir/Alphavir_Ig-like_sf.
DR   InterPro; IPR011998; Glycoprot_cen/dimer.
DR   InterPro; IPR036253; Glycoprot_cen/dimer_sf.
DR   InterPro; IPR038055; Glycoprot_E_dimer_dom.
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; SSF81296; E set domains; 1.
DR   SUPFAM; SSF56983; Viral glycoprotein, central and dimerisation domains; 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; Host nucleus;
KW   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; Secreted;
KW   Serine protease; Suppressor of RNA silencing; Transmembrane;
KW   Transmembrane helix; Viral attachment to host cell; Viral envelope protein;
KW   Viral immunoevasion; Viral penetration into host cytoplasm; Virion;
KW   Virus endocytosis by host; Virus entry into host cell; Zinc.
FT   CHAIN           <1..>1440
FT                   /note="Genome polyprotein"
FT                   /id="PRO_0000405200"
FT   CHAIN           <1..31
FT                   /note="Capsid protein C"
FT                   /evidence="ECO:0000250|UniProtKB:P06935"
FT                   /id="PRO_0000037869"
FT   PROPEP          32..53
FT                   /note="ER anchor for the capsid protein C, removed in
FT                   mature form by serine protease NS3"
FT                   /evidence="ECO:0000250|UniProtKB:P06935"
FT                   /id="PRO_0000405201"
FT   CHAIN           54..222
FT                   /note="Protein prM"
FT                   /evidence="ECO:0000250|UniProtKB:P06935"
FT                   /id="PRO_0000405202"
FT   CHAIN           54..146
FT                   /note="Peptide pr"
FT                   /evidence="ECO:0000250|UniProtKB:P06935"
FT                   /id="PRO_0000037870"
FT   CHAIN           147..222
FT                   /note="Small envelope protein M"
FT                   /evidence="ECO:0000250|UniProtKB:P06935"
FT                   /id="PRO_0000037871"
FT   CHAIN           223..722
FT                   /note="Envelope protein E"
FT                   /evidence="ECO:0000250|UniProtKB:P06935"
FT                   /id="PRO_0000037872"
FT   CHAIN           723..1074
FT                   /note="Non-structural protein 1"
FT                   /evidence="ECO:0000250|UniProtKB:P06935"
FT                   /id="PRO_0000037873"
FT   CHAIN           1075..1301
FT                   /note="Non-structural protein 2A"
FT                   /evidence="ECO:0000250|UniProtKB:P06935"
FT                   /id="PRO_0000037874"
FT   CHAIN           1302..1432
FT                   /note="Serine protease subunit NS2B"
FT                   /evidence="ECO:0000250|UniProtKB:P06935"
FT                   /id="PRO_0000037875"
FT   CHAIN           1433..>1440
FT                   /note="Serine protease NS3"
FT                   /evidence="ECO:0000250|UniProtKB:P06935"
FT                   /id="PRO_0000037876"
FT   TRANSMEM        36..56
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        57..180
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        181..201
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        202..207
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        208..222
FT                   /note="Helical"
FT                   /evidence="ECO:0000305"
FT   TOPO_DOM        223..674
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        675..695
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        696..701
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        702..722
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        723..1147
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1148..1168
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1169..1178
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1179..1199
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1200
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1201..1221
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1222..1237
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1238..1258
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1259..1269
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1270..1290
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1291..1302
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1303..1323
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1324..1326
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1327..1347
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1348..1404
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   INTRAMEM        1405..1425
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1426..>1440
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          320..333
FT                   /note="Fusion peptide"
FT                   /evidence="ECO:0000250|UniProtKB:P14336"
FT   REGION          1355..1394
FT                   /note="Interacts with and activates NS3 protease"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00859"
FT   SITE            31..32
FT                   /note="Cleavage; by viral protease NS3"
FT                   /evidence="ECO:0000250|UniProtKB:P06935"
FT   SITE            53..54
FT                   /note="Cleavage; by host signal peptidase"
FT                   /evidence="ECO:0000250|UniProtKB:P06935"
FT   SITE            146..147
FT                   /note="Cleavage; by host furin"
FT                   /evidence="ECO:0000250|UniProtKB:P06935"
FT   SITE            222..223
FT                   /note="Cleavage; by host signal peptidase"
FT                   /evidence="ECO:0000250|UniProtKB:P06935"
FT   SITE            722..723
FT                   /note="Cleavage; by host signal peptidase"
FT                   /evidence="ECO:0000250|UniProtKB:P06935"
FT   SITE            1074..1075
FT                   /note="Cleavage; by host"
FT                   /evidence="ECO:0000250|UniProtKB:P06935"
FT   SITE            1301..1302
FT                   /note="Cleavage; by viral protease NS3"
FT                   /evidence="ECO:0000250|UniProtKB:P06935"
FT   SITE            1432..1433
FT                   /note="Cleavage; by autolysis"
FT                   /evidence="ECO:0000250|UniProtKB:P06935"
FT   CARBOHYD        68
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000250|UniProtKB:P14335"
FT   CARBOHYD        376
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        852
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Q6P4"
FT   CARBOHYD        929
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Q6P4"
FT   DISULFID        225..252
FT                   /evidence="ECO:0000250|UniProtKB:Q9Q6P4"
FT   DISULFID        282..343
FT                   /evidence="ECO:0000250|UniProtKB:Q9Q6P4"
FT   DISULFID        282..338
FT                   /evidence="ECO:0000250|UniProtKB:P06935"
FT   DISULFID        296..327
FT                   /evidence="ECO:0000250|UniProtKB:Q9Q6P4"
FT   DISULFID        314..343
FT                   /evidence="ECO:0000250|UniProtKB:P06935"
FT   DISULFID        314..338
FT                   /evidence="ECO:0000250|UniProtKB:Q9Q6P4"
FT   DISULFID        412..509
FT                   /evidence="ECO:0000250|UniProtKB:Q9Q6P4"
FT   DISULFID        526..557
FT                   /evidence="ECO:0000250|UniProtKB:Q9Q6P4"
FT   DISULFID        726..737
FT                   /evidence="ECO:0000250|UniProtKB:Q9Q6P4"
FT   DISULFID        777..865
FT                   /evidence="ECO:0000250|UniProtKB:Q9Q6P4"
FT   DISULFID        901..945
FT                   /evidence="ECO:0000250|UniProtKB:Q9Q6P4"
FT   DISULFID        1002..1051
FT                   /evidence="ECO:0000250|UniProtKB:Q9Q6P4"
FT   DISULFID        1013..1034
FT                   /evidence="ECO:0000250|UniProtKB:Q9Q6P4"
FT   DISULFID        1035..1038
FT                   /evidence="ECO:0000250|UniProtKB:Q9Q6P4"
FT   NON_TER         1
FT   NON_TER         1440
FT   STRAND          1352..1359
FT                   /evidence="ECO:0007829|PDB:4R8T"
FT   HELIX           1365..1368
FT                   /evidence="ECO:0007829|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
//