##gff-version 3
Q62371	UniProtKB	Signal peptide	1	21	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q62371	UniProtKB	Chain	22	854	.	.	.	ID=PRO_0000016747;Note=Discoidin domain-containing receptor 2	
Q62371	UniProtKB	Topological domain	22	399	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q62371	UniProtKB	Transmembrane	400	421	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q62371	UniProtKB	Topological domain	422	854	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q62371	UniProtKB	Domain	30	185	.	.	.	Note=F5/8 type C;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00081	
Q62371	UniProtKB	Domain	563	848	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
Q62371	UniProtKB	Region	452	471	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q62371	UniProtKB	Active site	709	709	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10028	
Q62371	UniProtKB	Binding site	569	577	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
Q62371	UniProtKB	Binding site	608	608	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
Q62371	UniProtKB	Modified residue	471	471	.	.	.	Note=Phosphotyrosine%3B by SRC and autocatalysis;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11884411;Dbxref=PMID:11884411	
Q62371	UniProtKB	Modified residue	735	735	.	.	.	Note=Phosphotyrosine%3B by SRC and autocatalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16832	
Q62371	UniProtKB	Modified residue	739	739	.	.	.	Note=Phosphotyrosine%3B by SRC and autocatalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16832	
Q62371	UniProtKB	Modified residue	740	740	.	.	.	Note=Phosphotyrosine%3B by SRC and autocatalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16832	
Q62371	UniProtKB	Glycosylation	121	121	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q62371	UniProtKB	Glycosylation	213	213	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q62371	UniProtKB	Glycosylation	261	261	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q62371	UniProtKB	Glycosylation	280	280	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q62371	UniProtKB	Glycosylation	372	372	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q62371	UniProtKB	Disulfide bond	30	185	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00081	
Q62371	UniProtKB	Disulfide bond	73	177	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00081	
Q62371	UniProtKB	Mutagenesis	471	471	.	.	.	Note=Reduces tyrosine phosphorylation by 90%25%3B when associated with E-608. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11884411;Dbxref=PMID:11884411	
Q62371	UniProtKB	Mutagenesis	608	608	.	.	.	Note=Abolishes kinase activity. Reduces tyrosine phosphorylation by 90%25%3B when associated with F-471. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11884411;Dbxref=PMID:11884411