##gff-version 3
Q8QHL3	UniProtKB	Signal peptide	1	24	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q8QHL3	UniProtKB	Chain	25	1327	.	.	.	ID=PRO_0000249462;Note=Vascular endothelial growth factor receptor 1	
Q8QHL3	UniProtKB	Topological domain	25	749	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q8QHL3	UniProtKB	Transmembrane	750	770	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q8QHL3	UniProtKB	Topological domain	771	1327	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q8QHL3	UniProtKB	Domain	30	121	.	.	.	Note=Ig-like C2-type 1	
Q8QHL3	UniProtKB	Domain	120	222	.	.	.	Note=Ig-like C2-type 2	
Q8QHL3	UniProtKB	Domain	227	323	.	.	.	Note=Ig-like C2-type 3	
Q8QHL3	UniProtKB	Domain	331	417	.	.	.	Note=Ig-like C2-type 4	
Q8QHL3	UniProtKB	Domain	424	545	.	.	.	Note=Ig-like C2-type 5	
Q8QHL3	UniProtKB	Domain	552	644	.	.	.	Note=Ig-like C2-type 6	
Q8QHL3	UniProtKB	Domain	651	737	.	.	.	Note=Ig-like C2-type 7	
Q8QHL3	UniProtKB	Domain	819	1151	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
Q8QHL3	UniProtKB	Region	950	971	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q8QHL3	UniProtKB	Compositional bias	950	966	.	.	.	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q8QHL3	UniProtKB	Active site	1015	1015	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10028	
Q8QHL3	UniProtKB	Binding site	825	833	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
Q8QHL3	UniProtKB	Binding site	853	853	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
Q8QHL3	UniProtKB	Modified residue	1046	1046	.	.	.	Note=Phosphotyrosine%3B by autocatalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q8QHL3	UniProtKB	Modified residue	1162	1162	.	.	.	Note=Phosphotyrosine%3B by autocatalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q8QHL3	UniProtKB	Modified residue	1202	1202	.	.	.	Note=Phosphotyrosine%3B by autocatalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q8QHL3	UniProtKB	Modified residue	1231	1231	.	.	.	Note=Phosphotyrosine%3B by autocatalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q8QHL3	UniProtKB	Modified residue	1316	1316	.	.	.	Note=Phosphotyrosine%3B by autocatalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q8QHL3	UniProtKB	Modified residue	1322	1322	.	.	.	Note=Phosphotyrosine%3B by autocatalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q8QHL3	UniProtKB	Glycosylation	48	48	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q8QHL3	UniProtKB	Glycosylation	73	73	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q8QHL3	UniProtKB	Glycosylation	82	82	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q8QHL3	UniProtKB	Glycosylation	98	98	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q8QHL3	UniProtKB	Glycosylation	125	125	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q8QHL3	UniProtKB	Glycosylation	247	247	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q8QHL3	UniProtKB	Glycosylation	319	319	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q8QHL3	UniProtKB	Glycosylation	383	383	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q8QHL3	UniProtKB	Glycosylation	398	398	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q8QHL3	UniProtKB	Glycosylation	409	409	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q8QHL3	UniProtKB	Glycosylation	413	413	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q8QHL3	UniProtKB	Glycosylation	470	470	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q8QHL3	UniProtKB	Glycosylation	512	512	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q8QHL3	UniProtKB	Glycosylation	543	543	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q8QHL3	UniProtKB	Glycosylation	593	593	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q8QHL3	UniProtKB	Glycosylation	615	615	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q8QHL3	UniProtKB	Glycosylation	663	663	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q8QHL3	UniProtKB	Disulfide bond	51	105	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00114	
Q8QHL3	UniProtKB	Disulfide bond	154	203	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00114	
Q8QHL3	UniProtKB	Disulfide bond	248	307	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00114	
Q8QHL3	UniProtKB	Disulfide bond	450	531	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00114	
Q8QHL3	UniProtKB	Disulfide bond	573	626	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00114	
Q8QHL3	UniProtKB	Disulfide bond	672	721	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00114	
Q8QHL3	UniProtKB	Alternative sequence	647	677	.	.	.	ID=VSP_020427;Note=In isoform 2. AQEAPALLRQLMDQTVNTSNSAMLECQVHGI->GEHCNKKAVYSRILKYKNTRNDCTTQSNVKH;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:11855824;Dbxref=PMID:11855824	
Q8QHL3	UniProtKB	Alternative sequence	678	1327	.	.	.	ID=VSP_027160;Note=In isoform 2. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:11855824;Dbxref=PMID:11855824