##gff-version 3
Q6P4Z2	UniProtKB	Signal peptide	1	26	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q6P4Z2	UniProtKB	Propeptide	27	186	.	.	.	ID=PRO_0000286181;Note=N-terminal propeptide;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q6P4Z2	UniProtKB	Chain	187	1246	.	.	.	ID=PRO_0000286182;Note=Collagen alpha-1(II) chain	
Q6P4Z2	UniProtKB	Propeptide	1247	1492	.	.	.	ID=PRO_0000286183;Note=C-terminal propeptide;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q6P4Z2	UniProtKB	Domain	36	94	.	.	.	Note=VWFC;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00220	
Q6P4Z2	UniProtKB	Domain	1258	1492	.	.	.	Note=Fibrillar collagen NC1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00793	
Q6P4Z2	UniProtKB	Region	98	1255	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q6P4Z2	UniProtKB	Region	206	1219	.	.	.	Note=Triple-helical region	
Q6P4Z2	UniProtKB	Region	1220	1246	.	.	.	Note=Nonhelical region (C-terminal)	
Q6P4Z2	UniProtKB	Compositional bias	138	154	.	.	.	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q6P4Z2	UniProtKB	Compositional bias	164	179	.	.	.	Note=Pro residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q6P4Z2	UniProtKB	Compositional bias	356	370	.	.	.	Note=Pro residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q6P4Z2	UniProtKB	Compositional bias	437	451	.	.	.	Note=Pro residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q6P4Z2	UniProtKB	Compositional bias	1205	1222	.	.	.	Note=Pro residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q6P4Z2	UniProtKB	Binding site	1306	1306	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q6P4Z2	UniProtKB	Binding site	1308	1308	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q6P4Z2	UniProtKB	Binding site	1309	1309	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q6P4Z2	UniProtKB	Binding site	1311	1311	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q6P4Z2	UniProtKB	Binding site	1314	1314	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q6P4Z2	UniProtKB	Site	186	187	.	.	.	Note=Cleavage%3B by procollagen N-endopeptidase;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q6P4Z2	UniProtKB	Site	1246	1247	.	.	.	Note=Cleavage%3B by procollagen C-endopeptidase;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q6P4Z2	UniProtKB	Modified residue	664	664	.	.	.	Note=4-hydroxyproline;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05539	
Q6P4Z2	UniProtKB	Modified residue	673	673	.	.	.	Note=4-hydroxyproline;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05539	
Q6P4Z2	UniProtKB	Modified residue	675	675	.	.	.	Note=3-hydroxyproline;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05539	
Q6P4Z2	UniProtKB	Modified residue	676	676	.	.	.	Note=4-hydroxyproline;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05539	
Q6P4Z2	UniProtKB	Modified residue	679	679	.	.	.	Note=4-hydroxyproline;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05539	
Q6P4Z2	UniProtKB	Modified residue	912	912	.	.	.	Note=3-hydroxyproline;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05539	
Q6P4Z2	UniProtKB	Modified residue	913	913	.	.	.	Note=4-hydroxyproline;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05539	
Q6P4Z2	UniProtKB	Modified residue	919	919	.	.	.	Note=4-hydroxyproline;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05539	
Q6P4Z2	UniProtKB	Modified residue	925	925	.	.	.	Note=4-hydroxyproline;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05539	
Q6P4Z2	UniProtKB	Modified residue	1149	1149	.	.	.	Note=3-hydroxyproline;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05539	
Q6P4Z2	UniProtKB	Modified residue	1186	1186	.	.	.	Note=4-hydroxyproline;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05539	
Q6P4Z2	UniProtKB	Modified residue	1191	1191	.	.	.	Note=3-hydroxyproline;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05539	
Q6P4Z2	UniProtKB	Modified residue	1192	1192	.	.	.	Note=4-hydroxyproline;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05539	
Q6P4Z2	UniProtKB	Modified residue	1206	1206	.	.	.	Note=3-hydroxyproline;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05539	
Q6P4Z2	UniProtKB	Modified residue	1207	1207	.	.	.	Note=4-hydroxyproline;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05539	
Q6P4Z2	UniProtKB	Modified residue	1210	1210	.	.	.	Note=4-hydroxyproline;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05539	
Q6P4Z2	UniProtKB	Modified residue	1212	1212	.	.	.	Note=3-hydroxyproline;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05539	
Q6P4Z2	UniProtKB	Modified residue	1213	1213	.	.	.	Note=4-hydroxyproline;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05539	
Q6P4Z2	UniProtKB	Modified residue	1216	1216	.	.	.	Note=4-hydroxyproline;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05539	
Q6P4Z2	UniProtKB	Modified residue	1218	1218	.	.	.	Note=3-hydroxyproline;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05539	
Q6P4Z2	UniProtKB	Modified residue	1219	1219	.	.	.	Note=4-hydroxyproline;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05539	
Q6P4Z2	UniProtKB	Glycosylation	1393	1393	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q6P4Z2	UniProtKB	Disulfide bond	1288	1320	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00793	
Q6P4Z2	UniProtKB	Disulfide bond	1294	1294	.	.	.	Note=Interchain (with C-1311);Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00793	
Q6P4Z2	UniProtKB	Disulfide bond	1311	1311	.	.	.	Note=Interchain (with C-1294);Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00793	
Q6P4Z2	UniProtKB	Disulfide bond	1328	1490	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00793	
Q6P4Z2	UniProtKB	Disulfide bond	1398	1443	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00793