##gff-version 3
P26618	UniProtKB	Signal peptide	1	24	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
P26618	UniProtKB	Chain	25	1089	.	.	.	ID=PRO_0000016761;Note=Platelet-derived growth factor receptor alpha	
P26618	UniProtKB	Topological domain	25	528	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P26618	UniProtKB	Transmembrane	529	549	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P26618	UniProtKB	Topological domain	550	1089	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P26618	UniProtKB	Domain	25	113	.	.	.	Note=Ig-like C2-type 1	
P26618	UniProtKB	Domain	117	201	.	.	.	Note=Ig-like C2-type 2	
P26618	UniProtKB	Domain	202	306	.	.	.	Note=Ig-like C2-type 3	
P26618	UniProtKB	Domain	319	410	.	.	.	Note=Ig-like C2-type 4	
P26618	UniProtKB	Domain	414	517	.	.	.	Note=Ig-like C2-type 5	
P26618	UniProtKB	Domain	593	954	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
P26618	UniProtKB	Region	1018	1089	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P26618	UniProtKB	Compositional bias	1029	1044	.	.	.	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P26618	UniProtKB	Compositional bias	1045	1060	.	.	.	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P26618	UniProtKB	Active site	818	818	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10028	
P26618	UniProtKB	Binding site	599	607	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
P26618	UniProtKB	Binding site	627	627	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
P26618	UniProtKB	Modified residue	572	572	.	.	.	Note=Phosphotyrosine%3B by autocatalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P16234	
P26618	UniProtKB	Modified residue	574	574	.	.	.	Note=Phosphotyrosine%3B by autocatalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P16234	
P26618	UniProtKB	Modified residue	720	720	.	.	.	Note=Phosphotyrosine%3B by autocatalysis;Ontology_term=ECO:0000250,ECO:0000305;evidence=ECO:0000250|UniProtKB:P16234,ECO:0000305	
P26618	UniProtKB	Modified residue	731	731	.	.	.	Note=Phosphotyrosine%3B by autocatalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P16234	
P26618	UniProtKB	Modified residue	742	742	.	.	.	Note=Phosphotyrosine%3B by autocatalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P16234	
P26618	UniProtKB	Modified residue	754	754	.	.	.	Note=Phosphotyrosine%3B by autocatalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P16234	
P26618	UniProtKB	Modified residue	762	762	.	.	.	Note=Phosphotyrosine%3B by autocatalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P16234	
P26618	UniProtKB	Modified residue	768	768	.	.	.	Note=Phosphotyrosine%3B by autocatalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P16234	
P26618	UniProtKB	Modified residue	849	849	.	.	.	Note=Phosphotyrosine%3B by autocatalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P26618	UniProtKB	Modified residue	988	988	.	.	.	Note=Phosphotyrosine%3B by autocatalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P16234	
P26618	UniProtKB	Modified residue	1018	1018	.	.	.	Note=Phosphotyrosine%3B by autocatalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P16234	
P26618	UniProtKB	Glycosylation	42	42	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P26618	UniProtKB	Glycosylation	76	76	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P26618	UniProtKB	Glycosylation	89	89	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P26618	UniProtKB	Glycosylation	103	103	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P26618	UniProtKB	Glycosylation	179	179	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P26618	UniProtKB	Glycosylation	353	353	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P26618	UniProtKB	Glycosylation	359	359	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P26618	UniProtKB	Glycosylation	458	458	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P26618	UniProtKB	Glycosylation	468	468	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P26618	UniProtKB	Glycosylation	506	506	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P26618	UniProtKB	Disulfide bond	49	100	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00114	
P26618	UniProtKB	Disulfide bond	150	189	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00114	
P26618	UniProtKB	Disulfide bond	235	290	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00114	
P26618	UniProtKB	Disulfide bond	435	501	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00114	
P26618	UniProtKB	Alternative sequence	775	790	.	.	.	ID=VSP_031877;Note=In isoform 2. DSEVKNLLSDDDSEGL->GKSAHAHSGKYDLSVV;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:16141072;Dbxref=PMID:16141072	
P26618	UniProtKB	Alternative sequence	791	1089	.	.	.	ID=VSP_031878;Note=In isoform 2. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:16141072;Dbxref=PMID:16141072	
P26618	UniProtKB	Sequence conflict	65	65	.	.	.	Note=D->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P26618	UniProtKB	Sequence conflict	192	192	.	.	.	Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P26618	UniProtKB	Sequence conflict	202	202	.	.	.	Note=E->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P26618	UniProtKB	Sequence conflict	252	252	.	.	.	Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P26618	UniProtKB	Sequence conflict	271	271	.	.	.	Note=L->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P26618	UniProtKB	Sequence conflict	322	322	.	.	.	Note=G->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P26618	UniProtKB	Sequence conflict	326	326	.	.	.	Note=A->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P26618	UniProtKB	Sequence conflict	439	440	.	.	.	Note=GT->EG;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P26618	UniProtKB	Sequence conflict	472	472	.	.	.	Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P26618	UniProtKB	Sequence conflict	529	529	.	.	.	Note=A->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P26618	UniProtKB	Sequence conflict	737	737	.	.	.	Note=A->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P26618	UniProtKB	Sequence conflict	849	849	.	.	.	Note=Y->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P26618	UniProtKB	Sequence conflict	936	936	.	.	.	Note=E->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P26618	UniProtKB	Sequence conflict	950	950	.	.	.	Note=V->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P26618	UniProtKB	Sequence conflict	1005	1005	.	.	.	Note=G->S;Ontology_term=ECO:0000305;evidence=ECO:0000305