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-APR-2018, entry version 123. 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 particle 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}. 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 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; 1.10.8.970; -; 1. DR Gene3D; 1.20.1280.260; -; 1. DR Gene3D; 2.60.260.50; -; 1. DR Gene3D; 2.60.40.350; -; 1. DR Gene3D; 2.60.98.10; -; 3. DR Gene3D; 3.30.387.10; -; 2. DR Gene3D; 3.30.67.10; -; 4. 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; 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; 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 //