##gff-version 3 Q83887 UniProtKB Signal peptide 1 17 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 Q83887 UniProtKB Chain 18 1140 . . . ID=PRO_0000235995;Note=Envelopment polyprotein Q83887 UniProtKB Chain 18 652 . . . ID=PRO_0000235996;Note=Glycoprotein N;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q83887 UniProtKB Chain 653 1140 . . . ID=PRO_0000235997;Note=Glycoprotein C;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q83887 UniProtKB Topological domain 18 489 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q83887 UniProtKB Transmembrane 490 510 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q83887 UniProtKB Topological domain 511 631 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q83887 UniProtKB Transmembrane 632 652 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q83887 UniProtKB Topological domain 653 1108 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q83887 UniProtKB Transmembrane 1109 1129 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q83887 UniProtKB Topological domain 1130 1140 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q83887 UniProtKB Domain 615 638 . . . Note=ITAM;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00379 Q83887 UniProtKB Zinc finger 549 569 . . . Note=CCHC-type 1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9E006 Q83887 UniProtKB Zinc finger 574 595 . . . Note=CCHC-type 2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9E006 Q83887 UniProtKB Region 520 537 . . . Note=Binding to the ribonucleoprotein;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9E006 Q83887 UniProtKB Region 592 609 . . . Note=Binding to the ribonucleoprotein;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27312 Q83887 UniProtKB Region 596 607 . . . Note=Binding to the ribonucleoprotein;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9E006 Q83887 UniProtKB Region 611 638 . . . Note=Interaction with host TRAF3;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24390324;Dbxref=PMID:24390324 Q83887 UniProtKB Region 615 629 . . . Note=Binding to the ribonucleoprotein;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27312 Q83887 UniProtKB Region 761 781 . . . Note=Fusion loop;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P41266 Q83887 UniProtKB Region 1125 1140 . . . Note=Binding to the ribonucleoprotein;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27312 Q83887 UniProtKB Motif 619 622 . . . Note=YxxL;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08668 Q83887 UniProtKB Site 652 653 . . . Note=Cleavage%3B by host signal peptidase;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08668 Q83887 UniProtKB Modified residue 619 619 . . . Note=Phosphotyrosine%3B by host;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00379 Q83887 UniProtKB Modified residue 632 632 . . . Note=Phosphotyrosine%3B by host;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00379 Q83887 UniProtKB Glycosylation 138 138 . . . Note=N-linked (GlcNAc...) asparagine%3B by host;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q83887 UniProtKB Glycosylation 351 351 . . . Note=N-linked (GlcNAc...) asparagine%3B by host;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q83887 UniProtKB Glycosylation 403 403 . . . Note=N-linked (GlcNAc...) asparagine%3B by host;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q83887 UniProtKB Glycosylation 931 931 . . . Note=N-linked (GlcNAc...) asparagine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08668 Q83887 UniProtKB Disulfide bond 30 155 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9E006 Q83887 UniProtKB Disulfide bond 64 161 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9E006 Q83887 UniProtKB Disulfide bond 113 132 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9E006 Q83887 UniProtKB Disulfide bond 137 142 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9E006 Q83887 UniProtKB Disulfide bond 179 189 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9E006 Q83887 UniProtKB Disulfide bond 214 251 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9E006 Q83887 UniProtKB Disulfide bond 380 439 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9E006 Q83887 UniProtKB Disulfide bond 384 393 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9E006 Q83887 UniProtKB Disulfide bond 409 428 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9E006 Q83887 UniProtKB Disulfide bond 456 479 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9E006 Q83887 UniProtKB Disulfide bond 739 774 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08668 Q83887 UniProtKB Disulfide bond 743 781 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08668 Q83887 UniProtKB Disulfide bond 755 888 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08668 Q83887 UniProtKB Disulfide bond 769 899 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08668 Q83887 UniProtKB Disulfide bond 784 907 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08668 Q83887 UniProtKB Disulfide bond 810 819 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08668 Q83887 UniProtKB Disulfide bond 827 836 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08668 Q83887 UniProtKB Disulfide bond 867 871 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08668 Q83887 UniProtKB Disulfide bond 973 1003 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08668 Q83887 UniProtKB Disulfide bond 996 1048 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08668 Q83887 UniProtKB Disulfide bond 1013 1018 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08668 Q83887 UniProtKB Disulfide bond 1049 1054 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08668 Q83887 UniProtKB Disulfide bond 1088 1092 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9E006 Q83887 UniProtKB Natural variant 4 4 . . . Note=In strain: Isolate New York-2. W->F Q83887 UniProtKB Natural variant 8 8 . . . Note=In strain: Isolate New York-2 and Isolate Rhode Island-1. S->F Q83887 UniProtKB Natural variant 46 46 . . . Note=In strain: Isolate New York-2. E->G Q83887 UniProtKB Natural variant 141 141 . . . Note=In strain: Isolate Rhode Island-1. H->Y Q83887 UniProtKB Natural variant 238 238 . . . Note=In strain: Isolate New York-2. S->G Q83887 UniProtKB Natural variant 261 261 . . . Note=In strain: Isolate Rhode Island-1. F->S Q83887 UniProtKB Natural variant 314 314 . . . Note=In strain: Isolate New York-2. T->A Q83887 UniProtKB Natural variant 325 325 . . . Note=In strain: Isolate Rhode Island-1. M->T Q83887 UniProtKB Natural variant 359 359 . . . Note=In strain: Isolate Rhode Island-1. T->A Q83887 UniProtKB Natural variant 394 394 . . . Note=In strain: Isolate Rhode Island-1. E->K Q83887 UniProtKB Natural variant 452 452 . . . Note=In strain: Isolate Rhode Island-1. V->I Q83887 UniProtKB Natural variant 489 489 . . . Note=In strain: Isolate Rhode Island-1. T->A Q83887 UniProtKB Natural variant 551 551 . . . Note=In strain: Isolate Rhode Island-1. V->A Q83887 UniProtKB Natural variant 589 589 . . . Note=In strain: Isolate Rhode Island-1. Q->L Q83887 UniProtKB Natural variant 618 618 . . . Note=In strain: Isolate Rhode Island-1. C->R Q83887 UniProtKB Natural variant 697 697 . . . Note=In strain: Isolate New York-2. N->D Q83887 UniProtKB Natural variant 794 794 . . . Note=In strain: Isolate Rhode Island-1. V->G Q83887 UniProtKB Natural variant 1043 1043 . . . Note=In strain: Isolate Rhode Island-1. G->S Q83887 UniProtKB Mutagenesis 619 619 . . . Note=No effect on the regulation of RIG-I-directed IRF3 activation. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24390324;Dbxref=PMID:24390324 Q83887 UniProtKB Mutagenesis 627 627 . . . Note=Complete loss of Gn-dependent regulation of RIG-I-directed IRF3 activation. Y->A%2CF%2CS;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24390324;Dbxref=PMID:24390324 Q83887 UniProtKB Mutagenesis 629 629 . . . Note=No effect on the regulation of RIG-I-directed IRF3 activation. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24390324;Dbxref=PMID:24390324 Q83887 UniProtKB Mutagenesis 630 630 . . . Note=No effect on the regulation of RIG-I-directed IRF3 activation. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24390324;Dbxref=PMID:24390324 Q83887 UniProtKB Mutagenesis 632 632 . . . Note=No effect on the regulation of RIG-I-directed IRF3 activation. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24390324;Dbxref=PMID:24390324