##gff-version 3
Q8NFZ8	UniProtKB	Signal peptide	1	20	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q8NFZ8	UniProtKB	Chain	21	388	.	.	.	ID=PRO_0000291980;Note=Cell adhesion molecule 4	
Q8NFZ8	UniProtKB	Topological domain	21	324	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q8NFZ8	UniProtKB	Transmembrane	325	345	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q8NFZ8	UniProtKB	Topological domain	346	388	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q8NFZ8	UniProtKB	Domain	21	119	.	.	.	Note=Ig-like V-type	
Q8NFZ8	UniProtKB	Domain	124	219	.	.	.	Note=Ig-like C2-type 1	
Q8NFZ8	UniProtKB	Domain	224	307	.	.	.	Note=Ig-like C2-type 2	
Q8NFZ8	UniProtKB	Modified residue	361	361	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8R464	
Q8NFZ8	UniProtKB	Glycosylation	31	31	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q8NFZ8	UniProtKB	Glycosylation	67	67	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q8NFZ8	UniProtKB	Glycosylation	286	286	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q8NFZ8	UniProtKB	Disulfide bond	44	104	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00114	
Q8NFZ8	UniProtKB	Disulfide bond	145	199	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00114	
Q8NFZ8	UniProtKB	Disulfide bond	245	291	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00114	
Q8NFZ8	UniProtKB	Natural variant	225	225	.	.	.	ID=VAR_032906;Note=T->A;Dbxref=dbSNP:rs34246023