##gff-version 3
P80204	UniProtKB	Signal peptide	1	29	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
P80204	UniProtKB	Chain	30	501	.	.	.	ID=PRO_0000024425;Note=TGF-beta receptor type-1	
P80204	UniProtKB	Topological domain	30	124	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P80204	UniProtKB	Transmembrane	125	145	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P80204	UniProtKB	Topological domain	146	501	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P80204	UniProtKB	Domain	173	202	.	.	.	Note=GS;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00585	
P80204	UniProtKB	Domain	203	493	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
P80204	UniProtKB	Motif	191	192	.	.	.	Note=FKBP1A-binding	
P80204	UniProtKB	Active site	331	331	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
P80204	UniProtKB	Binding site	209	217	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
P80204	UniProtKB	Binding site	230	230	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
P80204	UniProtKB	Modified residue	163	163	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P36897	
P80204	UniProtKB	Modified residue	183	183	.	.	.	Note=Phosphothreonine%3B by TGFBR2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P36897	
P80204	UniProtKB	Modified residue	184	184	.	.	.	Note=Phosphothreonine%3B by TGFBR2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P36897	
P80204	UniProtKB	Modified residue	185	185	.	.	.	Note=Phosphoserine%3B by TGFBR2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P36897	
P80204	UniProtKB	Modified residue	187	187	.	.	.	Note=Phosphoserine%3B by TGFBR2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P36897	
P80204	UniProtKB	Modified residue	189	189	.	.	.	Note=Phosphoserine%3B by TGFBR2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P36897	
P80204	UniProtKB	Glycosylation	41	41	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P80204	UniProtKB	Disulfide bond	32	50	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P36897	
P80204	UniProtKB	Disulfide bond	34	37	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P36897	
P80204	UniProtKB	Disulfide bond	44	67	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P36897	
P80204	UniProtKB	Disulfide bond	82	94	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P36897	
P80204	UniProtKB	Disulfide bond	95	100	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P36897	
P80204	UniProtKB	Cross-link	389	389	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)