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 27-NOV-2024, entry version 151. 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; Orthoflavivirus; Orthoflavivirus japonicum. 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 + phosphate + H(+); 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 + phosphate + H(+); 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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:0052170; P:symbiont-mediated suppression of host innate immune response; IEA:UniProtKB-KW. DR GO; GO:0039563; P:symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT1 activity; IEA:UniProtKB-KW. DR GO; GO:0039564; P:symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT2 activity; IEA:UniProtKB-KW. DR GO; GO:0039502; P:symbiont-mediated suppression 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 GO; GO:0019049; P:virus-mediated perturbation of host defense response; IEA:UniProtKB-KW. DR CDD; cd12149; Flavi_E_C; 1. DR CDD; cd17038; Flavi_M; 1. DR FunFam; 1.20.1280.260:FF:000001; Envelope glycoprotein; 1. DR FunFam; 2.60.40.350:FF:000001; Envelope glycoprotein; 1. DR FunFam; 2.60.260.50:FF:000001; Genome polyprotein; 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; IPR011998; Flavi_Glycoprot_E_cen/dimer. 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; 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 NCBIfam; TIGR04240; flavi_E_stem; 1. DR Pfam; PF01003; Flavi_capsid; 1. DR Pfam; PF21659; Flavi_E_stem; 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 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 Interferon antiviral system evasion; Membrane; Multifunctional enzyme; KW Nucleotide-binding; Protease; Secreted; Serine protease; KW Suppressor of RNA silencing; Transmembrane; Transmembrane helix; KW Viral attachment to host cell; Viral envelope protein; Viral immunoevasion; KW Viral penetration into host cytoplasm; Virion; Virus endocytosis by host; KW 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 //