##gff-version 3 Q810U3 UniProtKB Signal peptide 1 24 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 Q810U3 UniProtKB Chain 25 1240 . . . ID=PRO_0000015050;Note=Neurofascin Q810U3 UniProtKB Topological domain 25 1110 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q810U3 UniProtKB Transmembrane 1111 1131 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q810U3 UniProtKB Topological domain 1132 1240 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q810U3 UniProtKB Domain 41 137 . . . Note=Ig-like C2-type 1 Q810U3 UniProtKB Domain 143 230 . . . Note=Ig-like C2-type 2 Q810U3 UniProtKB Domain 244 332 . . . Note=Ig-like C2-type 3 Q810U3 UniProtKB Domain 337 424 . . . Note=Ig-like C2-type 4 Q810U3 UniProtKB Domain 430 517 . . . Note=Ig-like C2-type 5 Q810U3 UniProtKB Domain 521 603 . . . Note=Ig-like C2-type 6 Q810U3 UniProtKB Domain 630 725 . . . Note=Fibronectin type-III 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00316 Q810U3 UniProtKB Domain 727 823 . . . Note=Fibronectin type-III 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00316 Q810U3 UniProtKB Domain 827 923 . . . Note=Fibronectin type-III 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00316 Q810U3 UniProtKB Domain 1007 1099 . . . Note=Fibronectin type-III 4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00316 Q810U3 UniProtKB Region 710 740 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q810U3 UniProtKB Region 902 942 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q810U3 UniProtKB Region 1141 1240 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q810U3 UniProtKB Compositional bias 710 729 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q810U3 UniProtKB Compositional bias 1141 1165 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q810U3 UniProtKB Compositional bias 1167 1188 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q810U3 UniProtKB Compositional bias 1211 1225 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q810U3 UniProtKB Compositional bias 1226 1240 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q810U3 UniProtKB Modified residue 481 481 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O94856 Q810U3 UniProtKB Modified residue 485 485 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O94856 Q810U3 UniProtKB Modified residue 1160 1160 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079 Q810U3 UniProtKB Modified residue 1174 1174 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P97685 Q810U3 UniProtKB Modified residue 1187 1187 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P97685 Q810U3 UniProtKB Modified residue 1190 1190 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P97685 Q810U3 UniProtKB Modified residue 1226 1226 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079 Q810U3 UniProtKB Modified residue 1227 1227 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079 Q810U3 UniProtKB Modified residue 1231 1231 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079 Q810U3 UniProtKB Glycosylation 305 305 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q810U3 UniProtKB Glycosylation 409 409 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q810U3 UniProtKB Glycosylation 446 446 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q810U3 UniProtKB Glycosylation 483 483 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q810U3 UniProtKB Glycosylation 752 752 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q810U3 UniProtKB Glycosylation 778 778 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q810U3 UniProtKB Glycosylation 866 866 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q810U3 UniProtKB Glycosylation 881 881 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q810U3 UniProtKB Disulfide bond 63 118 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00114 Q810U3 UniProtKB Disulfide bond 162 213 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00114 Q810U3 UniProtKB Disulfide bond 268 316 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00114 Q810U3 UniProtKB Disulfide bond 358 408 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00114 Q810U3 UniProtKB Disulfide bond 452 501 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00114 Q810U3 UniProtKB Disulfide bond 543 592 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00114