##gff-version 3 P26664 UniProtKB Initiator methionine 1 1 . . . Note=Removed%3B by host;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7491770;Dbxref=PMID:7491770 P26664 UniProtKB Chain 2 3011 . . . ID=PRO_0000450851;Note=Genome polyprotein P26664 UniProtKB Chain 2 191 . . . ID=PRO_0000037517;Note=Core protein precursor P26664 UniProtKB Chain 2 177 . . . ID=PRO_0000037518;Note=Mature core protein P26664 UniProtKB Propeptide 178 191 . . . ID=PRO_0000037519;Note=ER anchor for the core protein%2C removed in mature form by host signal peptidase;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7491770;Dbxref=PMID:7491770 P26664 UniProtKB Chain 192 383 . . . ID=PRO_0000037520;Note=Envelope glycoprotein E1 P26664 UniProtKB Chain 384 746 . . . ID=PRO_0000037521;Note=Envelope glycoprotein E2 P26664 UniProtKB Chain 747 809 . . . ID=PRO_0000037522;Note=Viroporin p7 P26664 UniProtKB Chain 810 1026 . . . ID=PRO_0000037523;Note=Protease NS2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01030 P26664 UniProtKB Chain 1027 1657 . . . ID=PRO_0000037524;Note=Serine protease/helicase NS3 P26664 UniProtKB Chain 1658 1711 . . . ID=PRO_0000037525;Note=Non-structural protein 4A P26664 UniProtKB Chain 1712 1972 . . . ID=PRO_0000037526;Note=Non-structural protein 4B P26664 UniProtKB Chain 1973 2420 . . . ID=PRO_0000037527;Note=Non-structural protein 5A P26664 UniProtKB Chain 2421 3011 . . . ID=PRO_0000037528;Note=RNA-directed RNA polymerase P26664 UniProtKB Topological domain 2 168 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 P26664 UniProtKB Transmembrane 169 189 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 P26664 UniProtKB Topological domain 190 358 . . . Note=Lumenal;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 P26664 UniProtKB Transmembrane 359 379 . . . Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 P26664 UniProtKB Topological domain 380 725 . . . Note=Lumenal;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 P26664 UniProtKB Transmembrane 726 746 . . . Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 P26664 UniProtKB Topological domain 747 757 . . . Note=Lumenal;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 P26664 UniProtKB Transmembrane 758 778 . . . Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 P26664 UniProtKB Topological domain 779 781 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 P26664 UniProtKB Transmembrane 782 803 . . . Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 P26664 UniProtKB Topological domain 804 813 . . . Note=Lumenal;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12082096;Dbxref=PMID:12082096 P26664 UniProtKB Transmembrane 814 834 . . . Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9WMX2 P26664 UniProtKB Topological domain 835 838 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9WMX2 P26664 UniProtKB Transmembrane 839 859 . . . Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9WMX2 P26664 UniProtKB Topological domain 860 881 . . . Note=Lumenal;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9WMX2 P26664 UniProtKB Transmembrane 882 902 . . . Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9WMX2 P26664 UniProtKB Topological domain 903 1657 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9WMX2 P26664 UniProtKB Transmembrane 1658 1678 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 P26664 UniProtKB Topological domain 1679 1805 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 P26664 UniProtKB Transmembrane 1806 1826 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 P26664 UniProtKB Topological domain 1827 1828 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 P26664 UniProtKB Transmembrane 1829 1849 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 P26664 UniProtKB Topological domain 1850 1850 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 P26664 UniProtKB Transmembrane 1851 1871 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 P26664 UniProtKB Topological domain 1872 1881 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 P26664 UniProtKB Transmembrane 1882 1902 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 P26664 UniProtKB Topological domain 1903 1972 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 P26664 UniProtKB Intramembrane 1973 2003 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 P26664 UniProtKB Topological domain 2004 2990 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 P26664 UniProtKB Transmembrane 2991 3011 . . . Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 P26664 UniProtKB Domain 899 1026 . . . Note=Peptidase C18;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01030 P26664 UniProtKB Domain 1027 1208 . . . Note=Peptidase S29;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01166 P26664 UniProtKB Domain 1217 1369 . . . Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 P26664 UniProtKB Domain 2634 2752 . . . Note=RdRp catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00539 P26664 UniProtKB Region 2 75 . . . Note=Disordered;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 P26664 UniProtKB Region 2 59 . . . Note=Interaction with DDX3X;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5EG65 P26664 UniProtKB Region 2 58 . . . Note=Interaction with EIF2AK2/PKR;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26662 P26664 UniProtKB Region 2 23 . . . Note=Interaction with STAT1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26662 P26664 UniProtKB Region 112 152 . . . Note=Important for endoplasmic reticulum and mitochondrial localization;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26662 P26664 UniProtKB Region 122 173 . . . Note=Interaction with APOA2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P29846 P26664 UniProtKB Region 164 167 . . . Note=Important for lipid droplets localization;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 P26664 UniProtKB Region 265 296 . . . Note=Important for fusion;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 P26664 UniProtKB Region 385 411 . . . Note=HVR1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 P26664 UniProtKB Region 474 480 . . . Note=HVR2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 P26664 UniProtKB Region 481 493 . . . Note=CD81-binding 1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26663 P26664 UniProtKB Region 543 551 . . . Note=CD81-binding 2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26663 P26664 UniProtKB Region 660 671 . . . Note=EIF2AK2/eIF2-alpha phosphorylation homology domain (PePHD) P26664 UniProtKB Region 904 1206 . . . Note=Protease NS2-3;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26663 P26664 UniProtKB Region 929 949 . . . Note=Interaction with host SCPS1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99IB8 P26664 UniProtKB Region 1486 1497 . . . Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26663 P26664 UniProtKB Region 1679 1690 . . . Note=NS3-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 P26664 UniProtKB Region 1833 1861 . . . Note=Glycine zipper;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99IB8 P26664 UniProtKB Region 1978 1998 . . . Note=Membrane-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 P26664 UniProtKB Region 2005 2221 . . . Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 P26664 UniProtKB Region 2120 2332 . . . Note=Transcriptional activation;Ontology_term=ECO:0000255;evidence=ECO:0000255 P26664 UniProtKB Region 2120 2208 . . . Note=FKBP8-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26662 P26664 UniProtKB Region 2135 2139 . . . Note=Interaction with non-structural protein 4A;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26662 P26664 UniProtKB Region 2189 2441 . . . Note=Interaction with host SKP2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 P26664 UniProtKB Region 2206 2245 . . . Note=ISDR;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26662 P26664 UniProtKB Region 2210 2275 . . . Note=EIF2AK2/PKR-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255 P26664 UniProtKB Region 2249 2306 . . . Note=NS4B-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255 P26664 UniProtKB Region 2312 2334 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P26664 UniProtKB Region 2332 2441 . . . Note=Interaction with host IFI27;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 P26664 UniProtKB Region 2351 2408 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P26664 UniProtKB Region 2354 2377 . . . Note=V3;Ontology_term=ECO:0000250;evidence=ECO:0000250 P26664 UniProtKB Motif 5 13 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99IB8 P26664 UniProtKB Motif 38 43 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99IB8 P26664 UniProtKB Motif 58 64 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99IB8 P26664 UniProtKB Motif 66 71 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99IB8 P26664 UniProtKB Motif 1316 1319 . . . Note=DECH box;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99IB8 P26664 UniProtKB Motif 2322 2325 . . . Note=SH3-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255 P26664 UniProtKB Motif 2326 2334 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26662 P26664 UniProtKB Compositional bias 47 69 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P26664 UniProtKB Compositional bias 2312 2329 . . . Note=Pro residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P26664 UniProtKB Compositional bias 2351 2374 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P26664 UniProtKB Active site 952 952 . . . Note=For protease NS2 activity%3B shared with dimeric partner;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01030 P26664 UniProtKB Active site 972 972 . . . Note=For protease NS2 activity%3B shared with dimeric partner;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01030 P26664 UniProtKB Active site 993 993 . . . Note=For protease NS2 activity%3B shared with dimeric partner;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01030 P26664 UniProtKB Active site 1083 1083 . . . Note=Charge relay system%3B for serine protease NS3 activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01166 P26664 UniProtKB Active site 1107 1107 . . . Note=Charge relay system%3B for serine protease NS3 activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01166 P26664 UniProtKB Active site 1165 1165 . . . Note=Charge relay system%3B for serine protease NS3 activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01166 P26664 UniProtKB Binding site 1123 1123 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01166 P26664 UniProtKB Binding site 1125 1125 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01166 P26664 UniProtKB Binding site 1171 1171 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01166 P26664 UniProtKB Binding site 1175 1175 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01166 P26664 UniProtKB Binding site 1230 1237 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 P26664 UniProtKB Binding site 1237 1237 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9WMX2 P26664 UniProtKB Binding site 1317 1317 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9WMX2 P26664 UniProtKB Binding site 2011 2011 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9WMX2 P26664 UniProtKB Binding site 2029 2029 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9WMX2 P26664 UniProtKB Binding site 2031 2031 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9WMX2 P26664 UniProtKB Binding site 2052 2052 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9WMX2 P26664 UniProtKB Binding site 2640 2640 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26663 P26664 UniProtKB Binding site 2738 2738 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26663 P26664 UniProtKB Binding site 2739 2739 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26663 P26664 UniProtKB Site 177 178 . . . Note=Cleavage%3B by host signal peptide peptidase;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:7491770;Dbxref=PMID:7491770 P26664 UniProtKB Site 191 192 . . . Note=Cleavage%3B by host signal peptidase;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26662 P26664 UniProtKB Site 383 384 . . . Note=Cleavage%3B by host signal peptidase;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26662 P26664 UniProtKB Site 746 747 . . . Note=Cleavage%3B by host signal peptidase;Ontology_term=ECO:0000250;evidence=ECO:0000250 P26664 UniProtKB Site 809 810 . . . Note=Cleavage%3B by host signal peptidase;Ontology_term=ECO:0000250;evidence=ECO:0000250 P26664 UniProtKB Site 1026 1027 . . . Note=Cleavage%3B by protease NS2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01030 P26664 UniProtKB Site 1657 1658 . . . Note=Cleavage%3B by serine protease/helicase NS3;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 P26664 UniProtKB Site 1711 1712 . . . Note=Cleavage%3B by serine protease/helicase NS3;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 P26664 UniProtKB Site 1972 1973 . . . Note=Cleavage%3B by serine protease/helicase NS3;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 P26664 UniProtKB Site 2420 2421 . . . Note=Cleavage%3B by serine protease/helicase NS3;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 P26664 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q913V3 P26664 UniProtKB Modified residue 53 53 . . . Note=Phosphoserine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q01403 P26664 UniProtKB Modified residue 99 99 . . . Note=Phosphoserine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q01403 P26664 UniProtKB Modified residue 116 116 . . . Note=Phosphoserine%3B by host PKA;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q01403 P26664 UniProtKB Modified residue 2194 2194 . . . Note=Phosphoserine%3B by host%3B in p56;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26662 P26664 UniProtKB Modified residue 2197 2197 . . . Note=Phosphoserine%3B by host%3B in p58;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26662 P26664 UniProtKB Modified residue 2201 2201 . . . Note=Phosphoserine%3B by host%3B in p58;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26662 P26664 UniProtKB Modified residue 2204 2204 . . . Note=Phosphoserine%3B by host%3B in p58;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26662 P26664 UniProtKB Modified residue 2207 2207 . . . Note=Phosphoserine%3B by host%3B in p58;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99IB8 P26664 UniProtKB Modified residue 2210 2210 . . . Note=Phosphoserine%3B by host%3B in p58;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99IB8 P26664 UniProtKB Modified residue 2321 2321 . . . Note=Phosphoserine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 P26664 UniProtKB Modified residue 2449 2449 . . . Note=Phosphoserine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26662 P26664 UniProtKB Modified residue 2462 2462 . . . Note=Phosphoserine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26662 P26664 UniProtKB Lipidation 922 922 . . . Note=S-palmitoyl cysteine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 P26664 UniProtKB Lipidation 1968 1968 . . . Note=S-palmitoyl cysteine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 P26664 UniProtKB Lipidation 1972 1972 . . . Note=S-palmitoyl cysteine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 P26664 UniProtKB Glycosylation 196 196 . . . Note=N-linked (GlcNAc...) asparagine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 P26664 UniProtKB Glycosylation 209 209 . . . Note=N-linked (GlcNAc...) asparagine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 P26664 UniProtKB Glycosylation 234 234 . . . Note=N-linked (GlcNAc...) asparagine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 P26664 UniProtKB Glycosylation 305 305 . . . Note=N-linked (GlcNAc...) asparagine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 P26664 UniProtKB Glycosylation 417 417 . . . Note=N-linked (GlcNAc...) (high mannose) asparagine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 P26664 UniProtKB Glycosylation 423 423 . . . Note=N-linked (GlcNAc...) (high mannose) asparagine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 P26664 UniProtKB Glycosylation 430 430 . . . Note=N-linked (GlcNAc...) (high mannose) asparagine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 P26664 UniProtKB Glycosylation 448 448 . . . Note=N-linked (GlcNAc...) (high mannose) asparagine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 P26664 UniProtKB Glycosylation 476 476 . . . Note=N-linked (GlcNAc...) asparagine%3B by host;Ontology_term=ECO:0000255;evidence=ECO:0000255 P26664 UniProtKB Glycosylation 532 532 . . . Note=N-linked (GlcNAc...) (high mannose) asparagine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 P26664 UniProtKB Glycosylation 556 556 . . . Note=N-linked (GlcNAc...) (high mannose) asparagine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 P26664 UniProtKB Glycosylation 576 576 . . . Note=N-linked (GlcNAc...) (high mannose) asparagine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 P26664 UniProtKB Glycosylation 623 623 . . . Note=N-linked (GlcNAc...) (high mannose) asparagine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 P26664 UniProtKB Glycosylation 645 645 . . . Note=N-linked (GlcNAc...) (high mannose) asparagine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 P26664 UniProtKB Disulfide bond 429 552 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 P26664 UniProtKB Disulfide bond 452 459 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 P26664 UniProtKB Disulfide bond 486 494 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 P26664 UniProtKB Disulfide bond 503 508 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 P26664 UniProtKB Disulfide bond 564 569 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 P26664 UniProtKB Disulfide bond 581 585 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 P26664 UniProtKB Disulfide bond 597 620 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 P26664 UniProtKB Disulfide bond 607 644 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 P26664 UniProtKB Disulfide bond 652 677 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 P26664 UniProtKB Natural variant 9 11 . . . Note=In infectious clone pHCV-1/SF. KKN->RKT P26664 UniProtKB Natural variant 399 399 . . . Note=In strain: Isolate infectious clone pHCV-1/SF. F->S P26664 UniProtKB Natural variant 402 402 . . . Note=In strain: Isolate infectious clone pHCV-1/SF. L->F P26664 UniProtKB Natural variant 929 929 . . . Note=In strain: Isolate infectious clone pHCV-1/SF. I->A P26664 UniProtKB Natural variant 1703 1703 . . . Note=In strain: Isolate infectious clone pHCV-1/SF. R->Q P26664 UniProtKB Natural variant 2021 2021 . . . Note=In strain: Isolate infectious clone pHCV-1/SF. V->G P26664 UniProtKB Natural variant 2349 2350 . . . Note=In strain: Isolate infectious clone pHCV-1/SF. TR->IK P26664 UniProtKB Natural variant 2378 2378 . . . Note=In strain: Isolate infectious clone pHCV-1/SF. P->R P26664 UniProtKB Natural variant 2413 2413 . . . Note=In strain: Isolate infectious clone pHCV-1/SF. N->S P26664 UniProtKB Natural variant 2992 2992 . . . Note=In strain: Isolate infectious clone pHCV-1/SF. I->F P26664 UniProtKB Mutagenesis 2001 2004 . . . Note=No effect on binding to Src-family kinases. PQLP->AQLA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14993658;Dbxref=PMID:14993658 P26664 UniProtKB Mutagenesis 2315 2318 . . . Note=No effect on binding to Src-family kinases. PLPP->ALAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14993658;Dbxref=PMID:14993658 P26664 UniProtKB Mutagenesis 2322 2326 . . . Note=Complete loss of binding to GRB2 and Src-family kinases. PPVPP->APVAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14993658;Dbxref=PMID:14993658 P26664 UniProtKB Beta strand 1019 1025 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3SU4 P26664 UniProtKB Beta strand 1027 1030 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3SU4 P26664 UniProtKB Beta strand 1032 1035 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7MME P26664 UniProtKB Helix 1039 1048 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7MME P26664 UniProtKB Beta strand 1057 1063 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7MME P26664 UniProtKB Beta strand 1068 1074 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7MME P26664 UniProtKB Beta strand 1077 1081 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7MME P26664 UniProtKB Helix 1082 1085 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7MME P26664 UniProtKB Beta strand 1090 1092 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3EYD P26664 UniProtKB Beta strand 1095 1097 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3EYD P26664 UniProtKB Beta strand 1100 1103 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7MME P26664 UniProtKB Helix 1104 1106 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7MME P26664 UniProtKB Beta strand 1108 1112 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7MME P26664 UniProtKB Beta strand 1129 1133 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7MME P26664 UniProtKB Beta strand 1139 1144 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7MME P26664 UniProtKB Beta strand 1146 1157 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7MME P26664 UniProtKB Helix 1158 1160 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7MME P26664 UniProtKB Turn 1161 1163 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7MME P26664 UniProtKB Beta strand 1168 1170 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7MME P26664 UniProtKB Turn 1172 1174 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2GVF P26664 UniProtKB Beta strand 1176 1186 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7MME P26664 UniProtKB Beta strand 1189 1197 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7MME P26664 UniProtKB Helix 1198 1204 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7MME P26664 UniProtKB Beta strand 1680 1689 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3EYD P26664 UniProtKB Beta strand 2422 2426 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3HKW P26664 UniProtKB Helix 2445 2450 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3HKW P26664 UniProtKB Helix 2454 2456 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3HKW P26664 UniProtKB Beta strand 2457 2459 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3HKW P26664 UniProtKB Helix 2462 2464 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3HKW P26664 UniProtKB Helix 2465 2472 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3HKW P26664 UniProtKB Helix 2482 2495 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3HKW P26664 UniProtKB Helix 2505 2510 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3HKW P26664 UniProtKB Beta strand 2520 2522 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6MVO P26664 UniProtKB Helix 2525 2529 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3HKW P26664 UniProtKB Helix 2533 2548 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3HKW P26664 UniProtKB Beta strand 2550 2552 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3HKW P26664 UniProtKB Beta strand 2556 2560 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3HKW P26664 UniProtKB Beta strand 2564 2566 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3HKW P26664 UniProtKB Helix 2569 2571 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6MVO P26664 UniProtKB Beta strand 2579 2582 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3HKW P26664 UniProtKB Helix 2585 2607 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3HKW P26664 UniProtKB Helix 2608 2610 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3HKW P26664 UniProtKB Helix 2612 2614 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3HKW P26664 UniProtKB Helix 2617 2630 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3HKW P26664 UniProtKB Beta strand 2631 2639 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3HKW P26664 UniProtKB Helix 2644 2647 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3HKW P26664 UniProtKB Helix 2650 2660 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3HKW P26664 UniProtKB Helix 2667 2679 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3HKW P26664 UniProtKB Turn 2680 2682 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3HKW P26664 UniProtKB Beta strand 2684 2687 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3HKW P26664 UniProtKB Beta strand 2693 2697 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3HKW P26664 UniProtKB Helix 2707 2725 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3HKW P26664 UniProtKB Beta strand 2729 2736 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3HKW P26664 UniProtKB Beta strand 2739 2745 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3HKW P26664 UniProtKB Helix 2749 2765 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3HKW P26664 UniProtKB Beta strand 2770 2772 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3HKW P26664 UniProtKB Beta strand 2777 2779 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3HKW P26664 UniProtKB Helix 2780 2782 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3HKW P26664 UniProtKB Beta strand 2788 2794 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3HKW P26664 UniProtKB Beta strand 2800 2806 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3HKW P26664 UniProtKB Helix 2809 2820 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3HKW P26664 UniProtKB Helix 2827 2835 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3HKW P26664 UniProtKB Helix 2839 2843 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3HKW P26664 UniProtKB Helix 2845 2855 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3HKW P26664 UniProtKB Beta strand 2863 2867 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3HKW P26664 UniProtKB Beta strand 2870 2874 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3HKW P26664 UniProtKB Helix 2876 2878 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3HKW P26664 UniProtKB Helix 2879 2887 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3HKW P26664 UniProtKB Helix 2889 2892 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3HKW P26664 UniProtKB Helix 2899 2912 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3HKW P26664 UniProtKB Helix 2917 2933 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3HKW P26664 UniProtKB Helix 2936 2945 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3HKW P26664 UniProtKB Helix 2947 2949 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3HKW P26664 UniProtKB Helix 2960 2964 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3HKW P26664 UniProtKB Turn 2968 2971 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3HKW P26664 UniProtKB Beta strand 2972 2975 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3QGI