##gff-version 3 O39927 UniProtKB Initiator methionine 1 1 . . . Note=Removed%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26664 O39927 UniProtKB Chain 2 3018 . . . ID=PRO_0000450901;Note=Genome polyprotein O39927 UniProtKB Chain 2 191 . . . ID=PRO_0000045544;Note=Core protein precursor;Ontology_term=ECO:0000255;evidence=ECO:0000255 O39927 UniProtKB Chain 2 177 . . . ID=PRO_0000045545;Note=Mature core protein O39927 UniProtKB Propeptide 178 191 . . . ID=PRO_0000045546;Note=ER anchor for the core protein%2C removed in mature form by host signal peptidase O39927 UniProtKB Chain 192 383 . . . ID=PRO_0000045547;Note=Envelope glycoprotein E1 O39927 UniProtKB Chain 384 750 . . . ID=PRO_0000045548;Note=Envelope glycoprotein E2 O39927 UniProtKB Chain 751 813 . . . ID=PRO_0000045549;Note=Viroporin p7 O39927 UniProtKB Chain 814 1030 . . . ID=PRO_0000045550;Note=Protease NS2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01030 O39927 UniProtKB Chain 1031 1661 . . . ID=PRO_0000045551;Note=Serine protease/helicase NS3 O39927 UniProtKB Chain 1662 1715 . . . ID=PRO_0000045552;Note=Non-structural protein 4A O39927 UniProtKB Chain 1716 1976 . . . ID=PRO_0000045553;Note=Non-structural protein 4B O39927 UniProtKB Chain 1977 2427 . . . ID=PRO_0000045554;Note=Non-structural protein 5A O39927 UniProtKB Chain 2428 3018 . . . ID=PRO_0000045555;Note=RNA-directed RNA polymerase O39927 UniProtKB Topological domain 2 168 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 O39927 UniProtKB Transmembrane 169 189 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 O39927 UniProtKB Topological domain 190 358 . . . Note=Lumenal;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O39927 UniProtKB Transmembrane 359 379 . . . Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O39927 UniProtKB Topological domain 380 729 . . . Note=Lumenal;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O39927 UniProtKB Transmembrane 730 750 . . . Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O39927 UniProtKB Topological domain 751 761 . . . Note=Lumenal;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O39927 UniProtKB Transmembrane 762 782 . . . Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O39927 UniProtKB Topological domain 783 786 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O39927 UniProtKB Transmembrane 787 807 . . . Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O39927 UniProtKB Topological domain 808 817 . . . Note=Lumenal;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O39927 UniProtKB Transmembrane 818 838 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 O39927 UniProtKB Topological domain 839 885 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9WMX2 O39927 UniProtKB Transmembrane 886 906 . . . Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9WMX2 O39927 UniProtKB Topological domain 907 932 . . . Note=Lumenal;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9WMX2 O39927 UniProtKB Transmembrane 933 953 . . . Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9WMX2 O39927 UniProtKB Topological domain 954 1661 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9WMX2 O39927 UniProtKB Transmembrane 1662 1682 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 O39927 UniProtKB Topological domain 1683 1809 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 O39927 UniProtKB Transmembrane 1810 1830 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 O39927 UniProtKB Topological domain 1831 1832 . . . Note=Lumenal;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O39927 UniProtKB Transmembrane 1833 1853 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 O39927 UniProtKB Topological domain 1854 1854 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 O39927 UniProtKB Transmembrane 1855 1875 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 O39927 UniProtKB Topological domain 1876 1885 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 O39927 UniProtKB Transmembrane 1886 1906 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 O39927 UniProtKB Topological domain 1907 1976 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 O39927 UniProtKB Intramembrane 1977 2006 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O39927 UniProtKB Topological domain 2007 2997 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O39927 UniProtKB Transmembrane 2998 3018 . . . Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O39927 UniProtKB Domain 907 1030 . . . Note=Peptidase C18;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01030 O39927 UniProtKB Domain 1031 1212 . . . Note=Peptidase S29;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01166 O39927 UniProtKB Domain 2641 2759 . . . Note=RdRp catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00539 O39927 UniProtKB Region 2 75 . . . Note=Disordered;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O39927 UniProtKB Region 2 59 . . . Note=Interaction with DDX3X;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5EG65 O39927 UniProtKB Region 2 58 . . . Note=Interaction with EIF2AK2/PKR;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26662 O39927 UniProtKB Region 2 23 . . . Note=Interaction with STAT1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26662 O39927 UniProtKB Region 112 152 . . . Note=Important for endoplasmic reticulum and mitochondrial localization;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26662 O39927 UniProtKB Region 122 173 . . . Note=Interaction with APOA2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P29846 O39927 UniProtKB Region 164 167 . . . Note=Important for lipid droplets localization;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O39927 UniProtKB Region 265 296 . . . Note=Important for fusion;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O39927 UniProtKB Region 385 411 . . . Note=HVR1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O39927 UniProtKB Region 474 478 . . . Note=HVR2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O39927 UniProtKB Region 480 493 . . . Note=CD81-binding 1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26663 O39927 UniProtKB Region 544 551 . . . Note=CD81-binding 2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26663 O39927 UniProtKB Region 664 675 . . . Note=PKR/eIF2-alpha phosphorylation homology domain (PePHD) O39927 UniProtKB Region 908 1210 . . . Note=Protease NS2-3;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26663 O39927 UniProtKB Region 933 953 . . . Note=Interaction with host SCPS1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99IB8 O39927 UniProtKB Region 1490 1502 . . . Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26663 O39927 UniProtKB Region 1683 1694 . . . Note=NS3-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O39927 UniProtKB Region 2124 2337 . . . Note=Transcriptional activation;Ontology_term=ECO:0000255;evidence=ECO:0000255 O39927 UniProtKB Region 2124 2212 . . . Note=FKBP8-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26662 O39927 UniProtKB Region 2139 2143 . . . Note=Interaction with non-structural protein 4A;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26662 O39927 UniProtKB Region 2192 2215 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite O39927 UniProtKB Region 2193 2445 . . . Note=Interaction with host SKP2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O39927 UniProtKB Region 2214 2279 . . . Note=Interaction with EIF2AK2/PKR;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26663 O39927 UniProtKB Region 2214 2253 . . . Note=ISDR;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26662 O39927 UniProtKB Region 2253 2311 . . . Note=NS4B-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255 O39927 UniProtKB Region 2304 2382 . . . Note=V3 O39927 UniProtKB Region 2359 2417 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite O39927 UniProtKB Motif 5 13 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99IB8 O39927 UniProtKB Motif 38 43 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99IB8 O39927 UniProtKB Motif 58 64 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99IB8 O39927 UniProtKB Motif 66 71 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99IB8 O39927 UniProtKB Motif 1320 1323 . . . Note=DECH box;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99IB8 O39927 UniProtKB Motif 2327 2330 . . . Note=SH3-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255 O39927 UniProtKB Motif 2332 2340 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26662 O39927 UniProtKB Compositional bias 47 61 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite O39927 UniProtKB Compositional bias 2199 2215 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite O39927 UniProtKB Compositional bias 2361 2377 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite O39927 UniProtKB Active site 956 956 . . . Note=For protease NS2 activity%3B shared with dimeric partner;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01030 O39927 UniProtKB Active site 976 976 . . . Note=For protease NS2 activity%3B shared with dimeric partner;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01030 O39927 UniProtKB Active site 997 997 . . . Note=For protease NS2 activity%3B shared with dimeric partner;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01030 O39927 UniProtKB Active site 1087 1087 . . . Note=Charge relay system%3B for serine protease NS3 activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01166 O39927 UniProtKB Active site 1111 1111 . . . Note=Charge relay system%3B for serine protease NS3 activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01166 O39927 UniProtKB Active site 1169 1169 . . . Note=Charge relay system%3B for serine protease NS3 activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01166 O39927 UniProtKB Binding site 1127 1127 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01166 O39927 UniProtKB Binding site 1129 1129 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01166 O39927 UniProtKB Binding site 1175 1175 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01166 O39927 UniProtKB Binding site 1179 1179 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01166 O39927 UniProtKB Binding site 1234 1241 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 O39927 UniProtKB Binding site 1241 1241 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9WMX2 O39927 UniProtKB Binding site 1321 1321 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9WMX2 O39927 UniProtKB Binding site 2015 2015 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9WMX2 O39927 UniProtKB Binding site 2033 2033 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9WMX2 O39927 UniProtKB Binding site 2035 2035 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9WMX2 O39927 UniProtKB Binding site 2056 2056 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9WMX2 O39927 UniProtKB Binding site 2647 2647 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26663 O39927 UniProtKB Binding site 2745 2745 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26663 O39927 UniProtKB Binding site 2746 2746 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26663 O39927 UniProtKB Site 177 178 . . . Note=Cleavage%3B by host signal peptide peptidase;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26662 O39927 UniProtKB Site 191 192 . . . Note=Cleavage%3B by host signal peptidase;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26662 O39927 UniProtKB Site 383 384 . . . Note=Cleavage%3B by host signal peptidase;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26662 O39927 UniProtKB Site 750 751 . . . Note=Cleavage%3B by host signal peptidase O39927 UniProtKB Site 813 814 . . . Note=Cleavage%3B by host signal peptidase O39927 UniProtKB Site 1030 1031 . . . Note=Cleavage%3B by protease NS2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01030 O39927 UniProtKB Site 1661 1662 . . . Note=Cleavage%3B by serine protease NS3;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O39927 UniProtKB Site 1715 1716 . . . Note=Cleavage%3B by serine protease NS3;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O39927 UniProtKB Site 1976 1977 . . . Note=Cleavage%3B by serine protease NS3;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O39927 UniProtKB Site 2427 2428 . . . Note=Cleavage%3B by serine protease NS3;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O39927 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q913V3 O39927 UniProtKB Modified residue 53 53 . . . Note=Phosphoserine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q01403 O39927 UniProtKB Modified residue 99 99 . . . Note=Phosphoserine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q01403 O39927 UniProtKB Modified residue 116 116 . . . Note=Phosphoserine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q01403 O39927 UniProtKB Modified residue 2198 2198 . . . Note=Phosphoserine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9WMX2 O39927 UniProtKB Modified residue 2201 2201 . . . Note=Phosphoserine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9WMX2 O39927 UniProtKB Modified residue 2205 2205 . . . Note=Phosphoserine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9WMX2 O39927 UniProtKB Modified residue 2211 2211 . . . Note=Phosphoserine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99IB8 O39927 UniProtKB Modified residue 2214 2214 . . . Note=Phosphoserine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99IB8 O39927 UniProtKB Modified residue 2456 2456 . . . Note=Phosphoserine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26662 O39927 UniProtKB Modified residue 2469 2469 . . . Note=Phosphoserine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26662 O39927 UniProtKB Lipidation 926 926 . . . Note=S-palmitoyl cysteine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O39927 UniProtKB Lipidation 1976 1976 . . . Note=S-palmitoyl cysteine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O39927 UniProtKB Glycosylation 196 196 . . . Note=N-linked (GlcNAc...) asparagine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O39927 UniProtKB Glycosylation 209 209 . . . Note=N-linked (GlcNAc...) asparagine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O39927 UniProtKB Glycosylation 234 234 . . . Note=N-linked (GlcNAc...) asparagine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O39927 UniProtKB Glycosylation 250 250 . . . Note=N-linked (GlcNAc...) asparagine%3B by host;Ontology_term=ECO:0000255;evidence=ECO:0000255 O39927 UniProtKB Glycosylation 305 305 . . . Note=N-linked (GlcNAc...) asparagine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O39927 UniProtKB Glycosylation 416 416 . . . Note=N-linked (GlcNAc...) (high mannose) asparagine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O39927 UniProtKB Glycosylation 422 422 . . . Note=N-linked (GlcNAc...) (high mannose) asparagine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O39927 UniProtKB Glycosylation 429 429 . . . Note=N-linked (GlcNAc...) (high mannose) asparagine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O39927 UniProtKB Glycosylation 447 447 . . . Note=N-linked (GlcNAc...) asparagine%3B by host;Ontology_term=ECO:0000255;evidence=ECO:0000255 O39927 UniProtKB Glycosylation 475 475 . . . Note=N-linked (GlcNAc...) asparagine%3B by host;Ontology_term=ECO:0000255;evidence=ECO:0000255 O39927 UniProtKB Glycosylation 532 532 . . . Note=N-linked (GlcNAc...) asparagine%3B by host;Ontology_term=ECO:0000255;evidence=ECO:0000255 O39927 UniProtKB Glycosylation 556 556 . . . Note=N-linked (GlcNAc...) asparagine%3B by host;Ontology_term=ECO:0000255;evidence=ECO:0000255 O39927 UniProtKB Glycosylation 577 577 . . . Note=N-linked (GlcNAc...) asparagine%3B by host;Ontology_term=ECO:0000255;evidence=ECO:0000255 O39927 UniProtKB Glycosylation 627 627 . . . Note=N-linked (GlcNAc...) (high mannose) asparagine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O39927 UniProtKB Glycosylation 649 649 . . . Note=N-linked (GlcNAc...) (high mannose) asparagine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O39927 UniProtKB Disulfide bond 428 552 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O39927 UniProtKB Disulfide bond 451 458 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O39927 UniProtKB Disulfide bond 486 494 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O39927 UniProtKB Disulfide bond 503 508 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O39927 UniProtKB Disulfide bond 564 569 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O39927 UniProtKB Disulfide bond 585 589 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O39927 UniProtKB Disulfide bond 601 624 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O39927 UniProtKB Disulfide bond 611 648 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O39927 UniProtKB Disulfide bond 656 681 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O39927 UniProtKB Cross-link 2355 2355 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958