##gff-version 3
P35546	UniProtKB	Signal peptide	1	28	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
P35546	UniProtKB	Chain	29	1115	.	.	.	ID=PRO_0000024451;Note=Proto-oncogene tyrosine-protein kinase receptor Ret	
P35546	UniProtKB	Chain	29	708	.	.	.	ID=PRO_0000415294;Note=Extracellular cell-membrane anchored RET cadherin 120 kDa fragment;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P35546	UniProtKB	Chain	709	1018	.	.	.	ID=PRO_0000415295;Note=Soluble RET kinase fragment;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P35546	UniProtKB	Topological domain	29	637	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P35546	UniProtKB	Transmembrane	638	659	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P35546	UniProtKB	Topological domain	660	1115	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P35546	UniProtKB	Domain	168	273	.	.	.	Note=Cadherin;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00043	
P35546	UniProtKB	Domain	725	1017	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
P35546	UniProtKB	Active site	875	875	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10028	
P35546	UniProtKB	Binding site	731	739	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
P35546	UniProtKB	Binding site	759	759	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
P35546	UniProtKB	Site	708	709	.	.	.	Note=Cleavage%3B by caspase-3;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P35546	UniProtKB	Site	1018	1019	.	.	.	Note=Cleavage%3B by caspase-3;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P35546	UniProtKB	Modified residue	697	697	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07949	
P35546	UniProtKB	Modified residue	807	807	.	.	.	Note=Phosphotyrosine%3B by autocatalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07949	
P35546	UniProtKB	Modified residue	810	810	.	.	.	Note=Phosphotyrosine%3B by autocatalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07949	
P35546	UniProtKB	Modified residue	901	901	.	.	.	Note=Phosphotyrosine%3B by autocatalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07949	
P35546	UniProtKB	Modified residue	906	906	.	.	.	Note=Phosphotyrosine%3B by autocatalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07949	
P35546	UniProtKB	Modified residue	982	982	.	.	.	Note=Phosphotyrosine%3B by autocatalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07949	
P35546	UniProtKB	Modified residue	1016	1016	.	.	.	Note=Phosphotyrosine%3B by autocatalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07949	
P35546	UniProtKB	Modified residue	1063	1063	.	.	.	Note=Phosphotyrosine%3B by autocatalysis;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14607833;Dbxref=PMID:14607833	
P35546	UniProtKB	Modified residue	1091	1091	.	.	.	Note=Phosphotyrosine%3B by autocatalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07949	
P35546	UniProtKB	Modified residue	1097	1097	.	.	.	Note=Phosphotyrosine%3B by autocatalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07949	
P35546	UniProtKB	Glycosylation	89	89	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P35546	UniProtKB	Glycosylation	98	98	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P35546	UniProtKB	Glycosylation	151	151	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P35546	UniProtKB	Glycosylation	156	156	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P35546	UniProtKB	Glycosylation	199	199	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P35546	UniProtKB	Glycosylation	345	345	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P35546	UniProtKB	Glycosylation	360	360	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P35546	UniProtKB	Glycosylation	378	378	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P35546	UniProtKB	Glycosylation	396	396	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P35546	UniProtKB	Glycosylation	450	450	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P35546	UniProtKB	Glycosylation	470	470	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P35546	UniProtKB	Glycosylation	556	556	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P35546	UniProtKB	Glycosylation	689	689	.	.	.	Note=O-linked (GlcNAc) serine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07949	
P35546	UniProtKB	Disulfide bond	137	142	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
P35546	UniProtKB	Alternative sequence	1065	1115	.	.	.	ID=VSP_011304;Note=In isoform 2. MSDPNWPGESPVPLTRADGTSTGFPRYANDSVYANWMVSPSAAKLMDTFDS->RISHAFTRF;Ontology_term=ECO:0000303,ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:15489334,ECO:0000303|PubMed:16141072,ECO:0000303|Ref.3;Dbxref=PMID:15489334,PMID:16141072	
P35546	UniProtKB	Mutagenesis	1063	1063	.	.	.	Note=Abolishes interaction with DOK proteins. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11470823;Dbxref=PMID:11470823	
P35546	UniProtKB	Sequence conflict	174	174	.	.	.	Note=F->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P35546	UniProtKB	Beta strand	1057	1059	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1UEF	
P35546	UniProtKB	Turn	1061	1064	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1UEF