##gff-version 3 P16056 UniProtKB Signal peptide 1 24 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 P16056 UniProtKB Chain 25 1379 . . . ID=PRO_0000024441;Note=Hepatocyte growth factor receptor P16056 UniProtKB Topological domain 25 931 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 P16056 UniProtKB Transmembrane 932 954 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 P16056 UniProtKB Topological domain 955 1379 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 P16056 UniProtKB Domain 27 514 . . . Note=Sema;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00352 P16056 UniProtKB Domain 562 654 . . . Note=IPT/TIG 1 P16056 UniProtKB Domain 656 738 . . . Note=IPT/TIG 2 P16056 UniProtKB Domain 741 835 . . . Note=IPT/TIG 3 P16056 UniProtKB Domain 1076 1343 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 P16056 UniProtKB Region 1210 1379 . . . Note=Interaction with RANBP9;Ontology_term=ECO:0000250;evidence=ECO:0000250 P16056 UniProtKB Region 1318 1357 . . . Note=Interaction with MUC20;Ontology_term=ECO:0000250;evidence=ECO:0000250 P16056 UniProtKB Active site 1202 1202 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10028 P16056 UniProtKB Binding site 1082 1090 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 P16056 UniProtKB Binding site 1108 1108 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 P16056 UniProtKB Site 306 307 . . . Note=Cleavage;Ontology_term=ECO:0000255;evidence=ECO:0000255 P16056 UniProtKB Site 1001 1001 . . . Note=Required for ligand-induced CBL-mediated ubiquitination;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08581 P16056 UniProtKB Modified residue 964 964 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08581 P16056 UniProtKB Modified residue 975 975 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08581 P16056 UniProtKB Modified residue 988 988 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08581 P16056 UniProtKB Modified residue 995 995 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08581 P16056 UniProtKB Modified residue 998 998 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08581 P16056 UniProtKB Modified residue 1001 1001 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08581 P16056 UniProtKB Modified residue 1228 1228 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08581 P16056 UniProtKB Modified residue 1232 1232 . . . Note=Phosphotyrosine%3B by autocatalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08581 P16056 UniProtKB Modified residue 1233 1233 . . . Note=Phosphotyrosine%3B by autocatalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08581 P16056 UniProtKB Modified residue 1287 1287 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08581 P16056 UniProtKB Modified residue 1347 1347 . . . Note=Phosphotyrosine%3B by autocatalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08581 P16056 UniProtKB Modified residue 1354 1354 . . . Note=Phosphotyrosine%3B by autocatalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08581 P16056 UniProtKB Modified residue 1363 1363 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08581 P16056 UniProtKB Glycosylation 45 45 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 P16056 UniProtKB Glycosylation 106 106 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 P16056 UniProtKB Glycosylation 201 201 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 P16056 UniProtKB Glycosylation 357 357 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 P16056 UniProtKB Glycosylation 398 398 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 P16056 UniProtKB Glycosylation 404 404 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 P16056 UniProtKB Glycosylation 581 581 . . . Note=O-linked (Man) threonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08581 P16056 UniProtKB Glycosylation 606 606 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 P16056 UniProtKB Glycosylation 634 634 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 P16056 UniProtKB Glycosylation 675 675 . . . Note=O-linked (Man) threonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08581 P16056 UniProtKB Glycosylation 760 760 . . . Note=O-linked (Man) threonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08581 P16056 UniProtKB Glycosylation 784 784 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 P16056 UniProtKB Glycosylation 878 878 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 P16056 UniProtKB Disulfide bond 95 101 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00352 P16056 UniProtKB Disulfide bond 98 160 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00352 P16056 UniProtKB Disulfide bond 133 141 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00352 P16056 UniProtKB Disulfide bond 171 174 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00352 P16056 UniProtKB Disulfide bond 297 362 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00352 P16056 UniProtKB Disulfide bond 384 396 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00352 P16056 UniProtKB Disulfide bond 519 537 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00352 P16056 UniProtKB Disulfide bond 525 560 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00352 P16056 UniProtKB Disulfide bond 528 544 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00352 P16056 UniProtKB Disulfide bond 540 550 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00352 P16056 UniProtKB Mutagenesis 1232 1232 . . . Note=Mice heterozygous for the mutation show reduced number of myofibers in appendicular and axial muscles%2C defective migration of muscle progenitor cells and impaired proliferation of secondary myoblasts. Y->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30777867;Dbxref=PMID:30777867 P16056 UniProtKB Sequence conflict 1199 1199 . . . Note=V->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 P16056 UniProtKB Sequence conflict 1255 1255 . . . Note=T->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 P16056 UniProtKB Sequence conflict 1261 1261 . . . Note=K->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 P16056 UniProtKB Sequence conflict 1269 1270 . . . Note=VL->IP;Ontology_term=ECO:0000305;evidence=ECO:0000305