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 21-SEP-2011, entry version 88. DE RecName: Full=Genome polyprotein; DE Contains: DE RecName: Full=Capsid protein C; DE AltName: Full=Core protein; DE Contains: DE RecName: Full=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 positive-strand viruses, no DNA stage; Flaviviridae; OC 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 MEDLINE=87236200; 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 self-assembles to form an icosahedral CC capsid about 30 nm in diameter. The capsid encapsulates the CC genomic RNA (By similarity). CC -!- FUNCTION: prM acts as a chaperone for envelope protein E during CC intracellular virion assembly by masking and inactivating envelope CC protein E fusion peptide. prM is matured in the last step of CC virion assembly, presumably to avoid catastrophic activation of CC the viral fusion peptide induced by the acidic pH of the trans- CC Golgi network. After cleavage by host furin, the pr peptide is CC released in the extracellular medium and small envelope protein M CC and envelope protein E homodimers are dissociated (By similarity). CC -!- FUNCTION: Envelope protein E binding to host cell surface receptor CC is followed by virus internalization through clathrin-mediated CC endocytosis. Envelope protein E is subsequently involved in CC membrane fusion between virion and host late endosomes. CC Synthesized as an homodimer with prM which acts as a chaperone for CC envelope protein E. After cleavage of prM, envelope protein E CC dissociate from small envelope protein M and homodimerizes (By CC similarity). CC -!- FUNCTION: Non-structural protein 1 is involved in virus CC replication and regulation of the innate immune response (By CC similarity). CC -!- FUNCTION: Non-structural protein 2A may be involved viral RNA CC replication and capsid assembly (Potential). CC -!- FUNCTION: Non-structural protein 2B is a required cofactor for the CC serine protease function of NS3 (By similarity). 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, CC NS2B-NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds CC RNA and unwinds dsRNA in the 3' to 5' direction (By similarity). 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 -!- SUBUNIT: Capsid protein C forms homodimers. prM and envelope CC protein E form heterodimers in the endoplasmic reticulum and CC Golgi. In immature particles, there are 60 icosaedrally organized CC trimeric spikes on the surface. Each spike consists of three CC heterodimers of envelope protein M precursor (prM) and envelope CC protein E. NS1 forms homodimers as well as homohexamers when CC secreted. NS1 may interact with NS4A. NS3 and NS2B form a CC heterodimer. NS3 is the catalytic subunit, whereas NS2B strongly CC stimulates the latter, acting as a cofactor. In the absence of the CC NS2B, NS3 protease is unfolded and inactive (By similarity). CC -!- SUBCELLULAR LOCATION: Capsid protein C: Virion (Potential). CC -!- SUBCELLULAR LOCATION: Peptide pr: Secreted (By similarity). CC -!- SUBCELLULAR LOCATION: Small envelope protein M: Virion membrane; CC Multi-pass membrane protein (By similarity). Host endoplasmic CC reticulum membrane; Multi-pass membrane protein (By similarity). CC -!- SUBCELLULAR LOCATION: Envelope protein E: Virion membrane; Multi- CC pass membrane protein (By similarity). Host endoplasmic reticulum CC membrane; Multi-pass membrane protein (By similarity). CC -!- SUBCELLULAR LOCATION: Non-structural protein 1: Secreted. Host CC endoplasmic reticulum membrane; Peripheral membrane protein; CC Lumenal side (By similarity). CC -!- SUBCELLULAR LOCATION: Non-structural protein 2A: Host endoplasmic CC reticulum membrane; Multi-pass membrane protein (Potential). CC -!- SUBCELLULAR LOCATION: Serine protease subunit NS2B: Host CC endoplasmic reticulum membrane; Multi-pass membrane protein CC (Potential). CC -!- SUBCELLULAR LOCATION: Serine protease NS3: Host endoplasmic CC reticulum membrane; Peripheral membrane protein; Cytoplasmic side CC (By similarity). Note=Remains non-covalently associated to NS3 CC protease (By similarity). CC -!- PTM: Specific enzymatic cleavages in vivo by the viral protease CC NS3 and host cell enzymes yield mature proteins. The nascent CC protein C contains a C-terminal hydrophobic domain that act as a CC signal sequence for translocation of prM into the lumen of the ER. CC Mature soluble protein C is released after cleavage by NS3 CC protease at a site upstream of this hydrophobic domain. prM is CC cleaved in post-Golgi vesicles by a host furin, releasing the CC mature small envelope protein M, and peptide pr (By similarity). 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 ProteinModelPortal; P14403; -. DR SMR; P14403; 223-621, 1351-1393. DR GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. DR GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW. DR GO; GO:0019031; C:viral envelope; IEA:InterPro. 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:0004252; F:serine-type endopeptidase activity; IEA:InterPro. DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro. DR GO; GO:0044419; P:interspecies interaction between organisms; IEA:UniProtKB-KW. DR GO; GO:0019058; P:viral infectious cycle; IEA:InterPro. DR InterPro; IPR000069; Env_glycoprot_M_flavivir. DR InterPro; IPR013755; Flav_glyE_cen_dom_subdom1. DR InterPro; IPR013756; Flav_glyE_cen_dom_subdom2. DR InterPro; IPR013754; Flav_glyE_dim. DR InterPro; IPR001122; Flavi_capsidC. DR InterPro; IPR001157; Flavi_NS1. DR InterPro; IPR000752; Flavi_NS2A. DR InterPro; IPR000487; Flavi_NS2B. DR InterPro; IPR002535; Flavi_propep. DR InterPro; IPR000336; Flv_glyE_Ig-like. DR InterPro; IPR011999; GlycoprotE_cen/dimer_Flavivir. DR InterPro; IPR011998; GlycoprotE_cen/dimer_vir. DR InterPro; IPR014756; Ig_E-set. DR Gene3D; G3DSA:3.30.387.10; Flav_glyE_cen_1; 1. DR Gene3D; G3DSA:3.30.67.10; Flav_glyE_cen_2; 1. DR Gene3D; G3DSA:2.60.98.10; Flav_glyE_dim; 1. DR Gene3D; G3DSA:2.60.40.350; Flv_glyE_Ig-like; 1. 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; Flavi_glycoprotE; 1. DR SUPFAM; SSF81296; Ig_E-set; 1. DR PROSITE; PS51527; FLAVIVIRUS_NS2B; 1. PE 3: Inferred from homology; KW 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 endoplasmic reticulum; Host membrane; Host-virus interaction; KW Hydrolase; Initiation of viral infection; Membrane; KW Multifunctional enzyme; Nucleotide-binding; Protease; Secreted; KW Serine protease; Transmembrane; Transmembrane helix; KW Viral attachment to host cell; Viral envelope protein; KW Viral penetration into host cytoplasm; Virion; KW Virus endocytosis by host. FT CHAIN <1 >1440 Genome polyprotein. FT /FTId=PRO_0000405200. FT CHAIN <1 31 Capsid protein C (By similarity). FT /FTId=PRO_0000037869. FT PROPEP 32 53 ER anchor for the protein C, removed in FT mature form by serine protease NS3 (By FT similarity). FT /FTId=PRO_0000405201. FT CHAIN 54 222 prM (By similarity). FT /FTId=PRO_0000405202. FT CHAIN 54 146 Peptide pr (By similarity). FT /FTId=PRO_0000037870. FT CHAIN 147 222 Small envelope protein M (By similarity). FT /FTId=PRO_0000037871. FT CHAIN 223 722 Envelope protein E (By similarity). FT /FTId=PRO_0000037872. FT CHAIN 723 1074 Non-structural protein 1 (By similarity). FT /FTId=PRO_0000037873. FT CHAIN 1075 1301 Non-structural protein 2A (By FT similarity). FT /FTId=PRO_0000037874. FT CHAIN 1302 1432 Serine protease subunit NS2B (By FT similarity). FT /FTId=PRO_0000037875. FT CHAIN 1433 >1440 Serine protease NS3 (By similarity). FT /FTId=PRO_0000037876. FT TRANSMEM 36 56 Helical; (Potential). FT TOPO_DOM 57 180 Extracellular (Potential). FT TRANSMEM 181 201 Helical; (Potential). FT TOPO_DOM 202 207 Cytoplasmic (Potential). FT TRANSMEM 208 222 Helical; (Potential). FT TOPO_DOM 223 674 Extracellular (Potential). FT INTRAMEM 675 695 Helical; (Potential). FT TOPO_DOM 696 701 Extracellular (Potential). FT INTRAMEM 702 722 Helical; (Potential). FT TOPO_DOM 723 1073 Extracellular (Potential). FT TRANSMEM 1074 1094 Helical; (Potential). FT TOPO_DOM 1095 1105 Cytoplasmic (Potential). FT TRANSMEM 1106 1126 Helical; (Potential). FT TOPO_DOM 1127 1147 Lumenal (Potential). FT TRANSMEM 1148 1168 Helical; (Potential). FT TOPO_DOM 1169 1178 Cytoplasmic (Potential). FT TRANSMEM 1179 1199 Helical; (Potential). FT TOPO_DOM 1200 1200 Lumenal (Potential). FT TRANSMEM 1201 1221 Helical; (Potential). FT TOPO_DOM 1222 1302 Cytoplasmic (Potential). FT TRANSMEM 1303 1323 Helical; (Potential). FT TOPO_DOM 1324 1326 Lumenal (Potential). FT TRANSMEM 1327 1347 Helical; (Potential). FT TOPO_DOM 1348 1404 Cytoplasmic (Potential). FT INTRAMEM 1405 1425 Helical; (Potential). FT TOPO_DOM 1426 >1440 Cytoplasmic (Potential). FT REGION 1355 1394 Interacts with and activates NS3 protease FT (By similarity). FT SITE 31 32 Cleavage; by viral protease NS3 FT (Potential). FT SITE 53 54 Cleavage; by host signal peptidase (By FT similarity). FT SITE 146 147 Cleavage; by host furin (By similarity). FT SITE 222 223 Cleavage; by host signal peptidase FT (Potential). FT SITE 722 723 Cleavage; by host signal peptidase FT (Potential). FT SITE 1074 1075 Cleavage; by host (By similarity). FT SITE 1301 1302 Cleavage; by viral protease NS3 FT (Potential). FT SITE 1432 1433 Cleavage; by autolysis (Potential). FT CARBOHYD 68 68 N-linked (GlcNAc...); by host FT (Potential). FT CARBOHYD 376 376 N-linked (GlcNAc...); by host FT (Potential). FT CARBOHYD 852 852 N-linked (GlcNAc...); by host FT (Potential). FT CARBOHYD 929 929 N-linked (GlcNAc...); by host FT (Potential). FT DISULFID 225 252 By similarity. FT DISULFID 282 338 By similarity. FT DISULFID 296 327 By similarity. FT DISULFID 314 343 By similarity. FT DISULFID 412 509 By similarity. FT DISULFID 526 557 By similarity. FT NON_TER 1 1 FT NON_TER 1440 1440 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 //