##gff-version 3
Q9R0T4	UniProtKB	Signal peptide	1	23	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9R0T4	UniProtKB	Propeptide	24	158	.	.	.	ID=PRO_0000003719;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9R0T4	UniProtKB	Chain	159	886	.	.	.	ID=PRO_0000003720;Note=Cadherin-1	
Q9R0T4	UniProtKB	Chain	705	886	.	.	.	ID=PRO_0000236073;Note=E-Cad/CTF1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9R0T4	UniProtKB	Chain	736	886	.	.	.	ID=PRO_0000236074;Note=E-Cad/CTF2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9R0T4	UniProtKB	Chain	755	886	.	.	.	ID=PRO_0000236075;Note=E-Cad/CTF3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9R0T4	UniProtKB	Topological domain	24	713	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9R0T4	UniProtKB	Transmembrane	714	734	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9R0T4	UniProtKB	Topological domain	735	886	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9R0T4	UniProtKB	Domain	159	266	.	.	.	Note=Cadherin 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00043	
Q9R0T4	UniProtKB	Domain	267	379	.	.	.	Note=Cadherin 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00043	
Q9R0T4	UniProtKB	Domain	380	490	.	.	.	Note=Cadherin 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00043	
Q9R0T4	UniProtKB	Domain	491	597	.	.	.	Note=Cadherin 4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00043	
Q9R0T4	UniProtKB	Domain	598	701	.	.	.	Note=Cadherin 5;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00043	
Q9R0T4	UniProtKB	Region	751	771	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q9R0T4	UniProtKB	Region	762	773	.	.	.	Note=Required for binding CTNND1 and PSEN1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q9R0T4	UniProtKB	Region	815	886	.	.	.	Note=Required for binding alpha%2C beta and;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q9R0T4	UniProtKB	Binding site	261	261	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q9R0T4	UniProtKB	Binding site	261	261	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q9R0T4	UniProtKB	Binding site	292	292	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q9R0T4	UniProtKB	Site	704	705	.	.	.	Note=Cleavage%3B by a metalloproteinase;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q9R0T4	UniProtKB	Site	735	736	.	.	.	Note=Cleavage%3B by gamma-secretase/PS1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q9R0T4	UniProtKB	Site	754	755	.	.	.	Note=Cleavage%3B by caspase-3;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q9R0T4	UniProtKB	Modified residue	757	757	.	.	.	Note=Phosphotyrosine%3B by SRC;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P12830	
Q9R0T4	UniProtKB	Modified residue	758	758	.	.	.	Note=Phosphotyrosine%3B by SRC;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P12830	
Q9R0T4	UniProtKB	Modified residue	759	759	.	.	.	Note=Phosphotyrosine%3B by SRC;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P12830	
Q9R0T4	UniProtKB	Modified residue	774	774	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P12830	
Q9R0T4	UniProtKB	Modified residue	797	797	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P12830	
Q9R0T4	UniProtKB	Modified residue	842	842	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P09803	
Q9R0T4	UniProtKB	Modified residue	844	844	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P09803	
Q9R0T4	UniProtKB	Modified residue	850	850	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P09803	
Q9R0T4	UniProtKB	Glycosylation	284	284	.	.	.	Note=O-linked (Man...) serine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P09803	
Q9R0T4	UniProtKB	Glycosylation	289	289	.	.	.	Note=O-linked (Man...) serine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P09803	
Q9R0T4	UniProtKB	Glycosylation	362	362	.	.	.	Note=O-linked (Man...) threonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P09803	
Q9R0T4	UniProtKB	Glycosylation	474	474	.	.	.	Note=O-linked (Man...) threonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P09803	
Q9R0T4	UniProtKB	Glycosylation	476	476	.	.	.	Note=O-linked (Man...) threonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P09803	
Q9R0T4	UniProtKB	Glycosylation	513	513	.	.	.	Note=O-linked (Man...) threonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P09803	
Q9R0T4	UniProtKB	Glycosylation	562	562	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9R0T4	UniProtKB	Glycosylation	580	580	.	.	.	Note=O-linked (Man...) threonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P09803	
Q9R0T4	UniProtKB	Glycosylation	582	582	.	.	.	Note=O-linked (Man...) threonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P09803	
Q9R0T4	UniProtKB	Glycosylation	584	584	.	.	.	Note=O-linked (Man...) threonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P09803	
Q9R0T4	UniProtKB	Glycosylation	641	641	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255