##gff-version 3
P35917	UniProtKB	Signal peptide	1	24	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
P35917	UniProtKB	Chain	25	1363	.	.	.	ID=PRO_0000016777;Note=Vascular endothelial growth factor receptor 3	
P35917	UniProtKB	Topological domain	25	775	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P35917	UniProtKB	Transmembrane	776	796	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P35917	UniProtKB	Topological domain	797	1363	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P35917	UniProtKB	Domain	44	118	.	.	.	Note=Ig-like C2-type 1	
P35917	UniProtKB	Domain	151	213	.	.	.	Note=Ig-like C2-type 2	
P35917	UniProtKB	Domain	230	326	.	.	.	Note=Ig-like C2-type 3	
P35917	UniProtKB	Domain	331	415	.	.	.	Note=Ig-like C2-type 4	
P35917	UniProtKB	Domain	422	552	.	.	.	Note=Ig-like C2-type 5	
P35917	UniProtKB	Domain	555	671	.	.	.	Note=Ig-like C2-type 6	
P35917	UniProtKB	Domain	678	764	.	.	.	Note=Ig-like C2-type 7	
P35917	UniProtKB	Domain	845	1173	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
P35917	UniProtKB	Region	1288	1330	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P35917	UniProtKB	Active site	1037	1037	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10028	
P35917	UniProtKB	Binding site	851	859	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
P35917	UniProtKB	Binding site	879	879	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
P35917	UniProtKB	Modified residue	830	830	.	.	.	Note=Phosphotyrosine%3B by SRC;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P35916	
P35917	UniProtKB	Modified residue	833	833	.	.	.	Note=Phosphotyrosine%3B by SRC;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P35916	
P35917	UniProtKB	Modified residue	1063	1063	.	.	.	Note=Phosphotyrosine%3B by autocatalysis and SRC;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P35916	
P35917	UniProtKB	Modified residue	1068	1068	.	.	.	Note=Phosphotyrosine%3B by autocatalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P35916	
P35917	UniProtKB	Modified residue	1230	1230	.	.	.	Note=Phosphotyrosine%3B by autocatalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P35916	
P35917	UniProtKB	Modified residue	1231	1231	.	.	.	Note=Phosphotyrosine%3B by autocatalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P35916	
P35917	UniProtKB	Modified residue	1265	1265	.	.	.	Note=Phosphotyrosine%3B by autocatalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P35916	
P35917	UniProtKB	Modified residue	1333	1333	.	.	.	Note=Phosphotyrosine%3B by autocatalysis and SRC;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P35916	
P35917	UniProtKB	Modified residue	1337	1337	.	.	.	Note=Phosphotyrosine%3B by autocatalysis and SRC;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P35916	
P35917	UniProtKB	Modified residue	1363	1363	.	.	.	Note=Phosphotyrosine%3B by autocatalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P35916	
P35917	UniProtKB	Glycosylation	33	33	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P35917	UniProtKB	Glycosylation	104	104	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P35917	UniProtKB	Glycosylation	166	166	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P35917	UniProtKB	Glycosylation	251	251	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P35917	UniProtKB	Glycosylation	299	299	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P35917	UniProtKB	Glycosylation	411	411	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P35917	UniProtKB	Glycosylation	515	515	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P35917	UniProtKB	Glycosylation	527	527	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P35917	UniProtKB	Glycosylation	582	582	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16944957;Dbxref=PMID:16944957	
P35917	UniProtKB	Glycosylation	594	594	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P35917	UniProtKB	Glycosylation	683	683	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P35917	UniProtKB	Glycosylation	690	690	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P35917	UniProtKB	Glycosylation	758	758	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P35917	UniProtKB	Disulfide bond	51	111	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00114	
P35917	UniProtKB	Disulfide bond	158	206	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00114	
P35917	UniProtKB	Disulfide bond	252	310	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00114	
P35917	UniProtKB	Disulfide bond	445	534	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00114	
P35917	UniProtKB	Disulfide bond	466	486	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P35916	
P35917	UniProtKB	Disulfide bond	578	653	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00114	
P35917	UniProtKB	Disulfide bond	699	751	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00114