##gff-version 3
Q9R069	UniProtKB	Signal peptide	1	25	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9R069	UniProtKB	Chain	26	622	.	.	.	ID=PRO_0000383338;Note=Basal cell adhesion molecule	
Q9R069	UniProtKB	Topological domain	26	541	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9R069	UniProtKB	Transmembrane	542	562	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9R069	UniProtKB	Topological domain	563	622	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9R069	UniProtKB	Domain	26	135	.	.	.	Note=Ig-like V-type 1	
Q9R069	UniProtKB	Domain	140	250	.	.	.	Note=Ig-like V-type 2	
Q9R069	UniProtKB	Domain	267	342	.	.	.	Note=Ig-like C2-type 1	
Q9R069	UniProtKB	Domain	356	435	.	.	.	Note=Ig-like C2-type 2	
Q9R069	UniProtKB	Domain	442	532	.	.	.	Note=Ig-like C2-type 3	
Q9R069	UniProtKB	Region	574	622	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q9R069	UniProtKB	Compositional bias	579	595	.	.	.	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q9R069	UniProtKB	Modified residue	590	590	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P50895	
Q9R069	UniProtKB	Modified residue	592	592	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P50895	
Q9R069	UniProtKB	Modified residue	594	594	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P50895	
Q9R069	UniProtKB	Modified residue	615	615	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P50895	
Q9R069	UniProtKB	Glycosylation	314	314	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9R069	UniProtKB	Glycosylation	323	323	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9R069	UniProtKB	Glycosylation	370	370	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9R069	UniProtKB	Glycosylation	377	377	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9R069	UniProtKB	Disulfide bond	47	118	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00114	
Q9R069	UniProtKB	Disulfide bond	165	230	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00114	
Q9R069	UniProtKB	Disulfide bond	284	330	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00114	
Q9R069	UniProtKB	Disulfide bond	378	418	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00114	
Q9R069	UniProtKB	Disulfide bond	467	516	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00114	
Q9R069	UniProtKB	Sequence conflict	227	227	.	.	.	Note=N->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
Q9R069	UniProtKB	Sequence conflict	319	319	.	.	.	Note=R->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
Q9R069	UniProtKB	Sequence conflict	361	361	.	.	.	Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
Q9R069	UniProtKB	Sequence conflict	388	388	.	.	.	Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305