##gff-version 3
Q00342	UniProtKB	Signal peptide	1	27	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q00342	UniProtKB	Chain	28	1000	.	.	.	ID=PRO_0000016779;Note=Receptor-type tyrosine-protein kinase FLT3	
Q00342	UniProtKB	Topological domain	28	544	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q00342	UniProtKB	Transmembrane	545	564	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q00342	UniProtKB	Topological domain	565	992	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q00342	UniProtKB	Domain	254	344	.	.	.	Note=Ig-like C2-type	
Q00342	UniProtKB	Domain	611	946	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
Q00342	UniProtKB	Region	45	67	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q00342	UniProtKB	Region	592	598	.	.	.	Note=Important for normal regulation of the kinase activity and for maintaining the kinase in an inactive state in the absence of ligand binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q00342	UniProtKB	Region	968	1000	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q00342	UniProtKB	Active site	814	814	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10028	
Q00342	UniProtKB	Binding site	617	625	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
Q00342	UniProtKB	Binding site	645	645	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
Q00342	UniProtKB	Modified residue	573	573	.	.	.	Note=Phosphotyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P36888	
Q00342	UniProtKB	Modified residue	575	575	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P36888	
Q00342	UniProtKB	Modified residue	590	590	.	.	.	Note=Phosphotyrosine%3B by autocatalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P36888	
Q00342	UniProtKB	Modified residue	592	592	.	.	.	Note=Phosphotyrosine%3B by autocatalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P36888	
Q00342	UniProtKB	Modified residue	600	600	.	.	.	Note=Phosphotyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P36888	
Q00342	UniProtKB	Modified residue	727	727	.	.	.	Note=Phosphotyrosine%3B by autocatalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P36888	
Q00342	UniProtKB	Modified residue	760	760	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P36888	
Q00342	UniProtKB	Modified residue	769	769	.	.	.	Note=Phosphotyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P36888	
Q00342	UniProtKB	Modified residue	796	796	.	.	.	Note=Phosphotyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P36888	
Q00342	UniProtKB	Modified residue	845	845	.	.	.	Note=Phosphotyrosine%3B by autocatalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P36888	
Q00342	UniProtKB	Modified residue	958	958	.	.	.	Note=Phosphotyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P36888	
Q00342	UniProtKB	Modified residue	972	972	.	.	.	Note=Phosphotyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P36888	
Q00342	UniProtKB	Modified residue	1000	1000	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P36888	
Q00342	UniProtKB	Glycosylation	44	44	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q00342	UniProtKB	Glycosylation	133	133	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q00342	UniProtKB	Glycosylation	152	152	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q00342	UniProtKB	Glycosylation	307	307	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q00342	UniProtKB	Glycosylation	324	324	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q00342	UniProtKB	Glycosylation	352	352	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q00342	UniProtKB	Glycosylation	445	445	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q00342	UniProtKB	Glycosylation	474	474	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q00342	UniProtKB	Glycosylation	503	503	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q00342	UniProtKB	Glycosylation	542	542	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q00342	UniProtKB	Disulfide bond	36	66	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00114	
Q00342	UniProtKB	Disulfide bond	104	115	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00114	
Q00342	UniProtKB	Disulfide bond	200	207	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00114	
Q00342	UniProtKB	Disulfide bond	273	331	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00114	
Q00342	UniProtKB	Disulfide bond	369	408	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00114	
Q00342	UniProtKB	Disulfide bond	382	393	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00114	
Q00342	UniProtKB	Mutagenesis	645	645	.	.	.	Note=Loss of kinase activity%3B no effect on FIZ1-binding. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10409713;Dbxref=PMID:10409713	
Q00342	UniProtKB	Sequence conflict	150	150	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
Q00342	UniProtKB	Sequence conflict	242	242	.	.	.	Note=S->C;Ontology_term=ECO:0000305;evidence=ECO:0000305	
Q00342	UniProtKB	Sequence conflict	726	726	.	.	.	Note=F->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
Q00342	UniProtKB	Sequence conflict	957	991	.	.	.	Note=MYQNMGGNVPEHPSIYQNRRPLSREAGSEPPSPQA->CIRTSIHLPKQAAPQQRGGLRAQSPQR;Ontology_term=ECO:0000305;evidence=ECO:0000305