##gff-version 3
P21803	UniProtKB	Signal peptide	1	21	.	.	.	.	
P21803	UniProtKB	Chain	22	821	.	.	.	ID=PRO_0000016784;Note=Fibroblast growth factor receptor 2	
P21803	UniProtKB	Topological domain	22	377	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P21803	UniProtKB	Transmembrane	378	398	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P21803	UniProtKB	Topological domain	399	821	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P21803	UniProtKB	Domain	25	125	.	.	.	Note=Ig-like C2-type 1	
P21803	UniProtKB	Domain	154	247	.	.	.	Note=Ig-like C2-type 2	
P21803	UniProtKB	Domain	256	358	.	.	.	Note=Ig-like C2-type 3	
P21803	UniProtKB	Domain	481	770	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
P21803	UniProtKB	Region	129	151	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P21803	UniProtKB	Region	161	178	.	.	.	Note=Heparin-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P21803	UniProtKB	Active site	626	626	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10028	
P21803	UniProtKB	Binding site	487	495	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
P21803	UniProtKB	Binding site	517	517	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
P21803	UniProtKB	Binding site	565	567	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
P21803	UniProtKB	Binding site	571	571	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
P21803	UniProtKB	Modified residue	466	466	.	.	.	Note=Phosphotyrosine%3B by autocatalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P21802	
P21803	UniProtKB	Modified residue	586	586	.	.	.	Note=Phosphotyrosine%3B by autocatalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P21802	
P21803	UniProtKB	Modified residue	588	588	.	.	.	Note=Phosphotyrosine%3B by autocatalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P21802	
P21803	UniProtKB	Modified residue	656	656	.	.	.	Note=Phosphotyrosine%3B by autocatalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P21802	
P21803	UniProtKB	Modified residue	657	657	.	.	.	Note=Phosphotyrosine%3B by autocatalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P21802	
P21803	UniProtKB	Modified residue	769	769	.	.	.	Note=Phosphotyrosine%3B by autocatalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P21802	
P21803	UniProtKB	Modified residue	780	780	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P21802	
P21803	UniProtKB	Glycosylation	83	83	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P21803	UniProtKB	Glycosylation	123	123	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P21803	UniProtKB	Glycosylation	147	147	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P21803	UniProtKB	Glycosylation	228	228	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P21803	UniProtKB	Glycosylation	241	241	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P21803	UniProtKB	Glycosylation	265	265	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P21803	UniProtKB	Glycosylation	297	297	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P21803	UniProtKB	Glycosylation	318	318	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P21803	UniProtKB	Glycosylation	331	331	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P21803	UniProtKB	Disulfide bond	62	107	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00114	
P21803	UniProtKB	Disulfide bond	179	231	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00114	
P21803	UniProtKB	Disulfide bond	278	342	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00114	
P21803	UniProtKB	Alternative sequence	37	37	.	.	.	ID=VSP_002985;Note=In isoform Short. E->G;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:1846048;Dbxref=PMID:1846048	
P21803	UniProtKB	Alternative sequence	38	152	.	.	.	ID=VSP_002986;Note=In isoform Short. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:1846048;Dbxref=PMID:1846048	
P21803	UniProtKB	Alternative sequence	314	361	.	.	.	ID=VSP_002987;Note=In isoform Short. AAGVNTTDKEIEVLYIRNVTFEDAGEYTCLAGNSIGISFHSAWLTVLP->HSGINSSNAEVLALFNVTEMDAGEYICKVSNYIGQANQSAWLTVLPKQQ;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:1846048;Dbxref=PMID:1846048	
P21803	UniProtKB	Mutagenesis	769	769	.	.	.	Note=Abolishes phosphorylation of FRS2 and activation of MAP kinases. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15629145;Dbxref=PMID:15629145	
P21803	UniProtKB	Sequence conflict	53	53	.	.	.	Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P21803	UniProtKB	Sequence conflict	55	56	.	.	.	Note=GE->RG;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P21803	UniProtKB	Sequence conflict	90	90	.	.	.	Note=E->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P21803	UniProtKB	Sequence conflict	119	119	.	.	.	Note=I->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P21803	UniProtKB	Sequence conflict	142	143	.	.	.	Note=DV->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P21803	UniProtKB	Sequence conflict	169	169	.	.	.	Note=C->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P21803	UniProtKB	Sequence conflict	187	187	.	.	.	Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P21803	UniProtKB	Sequence conflict	214	214	.	.	.	Note=W->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P21803	UniProtKB	Sequence conflict	229	229	.	.	.	Note=Y->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P21803	UniProtKB	Sequence conflict	275	275	.	.	.	Note=E->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P21803	UniProtKB	Sequence conflict	301	301	.	.	.	Note=N->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P21803	UniProtKB	Beta strand	48	52	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4HWU	
P21803	UniProtKB	Beta strand	58	61	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4HWU	
P21803	UniProtKB	Beta strand	69	74	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4HWU	
P21803	UniProtKB	Beta strand	77	79	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4HWU	
P21803	UniProtKB	Beta strand	83	88	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4HWU	
P21803	UniProtKB	Beta strand	91	94	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4HWU	
P21803	UniProtKB	Helix	99	101	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4HWU	
P21803	UniProtKB	Beta strand	103	110	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4HWU	
P21803	UniProtKB	Beta strand	115	124	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4HWU