##gff-version 3
Q08481	UniProtKB	Signal peptide	1	17	.	.	.	Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1415479;Dbxref=PMID:1415479	
Q08481	UniProtKB	Chain	18	727	.	.	.	ID=PRO_0000014896;Note=Platelet endothelial cell adhesion molecule	
Q08481	UniProtKB	Topological domain	18	590	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q08481	UniProtKB	Transmembrane	591	609	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q08481	UniProtKB	Topological domain	610	727	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q08481	UniProtKB	Domain	40	126	.	.	.	Note=Ig-like C2-type 1	
Q08481	UniProtKB	Domain	135	213	.	.	.	Note=Ig-like C2-type 2	
Q08481	UniProtKB	Domain	225	309	.	.	.	Note=Ig-like C2-type 3	
Q08481	UniProtKB	Domain	315	391	.	.	.	Note=Ig-like C2-type 4	
Q08481	UniProtKB	Domain	413	472	.	.	.	Note=Ig-like C2-type 5	
Q08481	UniProtKB	Domain	488	578	.	.	.	Note=Ig-like C2-type 6	
Q08481	UniProtKB	Region	642	672	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q08481	UniProtKB	Region	698	718	.	.	.	Note=Membrane-bound segment which detaches upon phosphorylation;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P16284	
Q08481	UniProtKB	Region	710	727	.	.	.	Note=May play a role in cytoprotective signaling;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q08481	UniProtKB	Motif	677	682	.	.	.	Note=ITIM motif 1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P16284	
Q08481	UniProtKB	Motif	700	705	.	.	.	Note=ITIM motif 2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P16284	
Q08481	UniProtKB	Modified residue	679	679	.	.	.	Note=Phosphotyrosine%3B by FER;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16731527;Dbxref=PMID:16731527	
Q08481	UniProtKB	Modified residue	702	702	.	.	.	Note=Phosphotyrosine%3B by FER;Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:16731527,ECO:0007744|PubMed:17947660;Dbxref=PMID:16731527,PMID:17947660	
Q08481	UniProtKB	Modified residue	718	718	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P16284	
Q08481	UniProtKB	Modified residue	723	723	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P16284	
Q08481	UniProtKB	Lipidation	611	611	.	.	.	Note=S-palmitoyl cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q08481	UniProtKB	Glycosylation	74	74	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19349973;Dbxref=PMID:19349973	
Q08481	UniProtKB	Glycosylation	141	141	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19349973;Dbxref=PMID:19349973	
Q08481	UniProtKB	Glycosylation	309	309	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q08481	UniProtKB	Glycosylation	345	345	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q08481	UniProtKB	Glycosylation	360	360	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19349973;Dbxref=PMID:19349973	
Q08481	UniProtKB	Glycosylation	424	424	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19349973;Dbxref=PMID:19349973	
Q08481	UniProtKB	Glycosylation	540	540	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19349973;Dbxref=PMID:19349973	
Q08481	UniProtKB	Disulfide bond	47	99	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00114	
Q08481	UniProtKB	Disulfide bond	142	195	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00114	
Q08481	UniProtKB	Disulfide bond	245	293	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00114	
Q08481	UniProtKB	Disulfide bond	336	375	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00114	
Q08481	UniProtKB	Disulfide bond	420	465	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00114	
Q08481	UniProtKB	Disulfide bond	512	561	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00114	
Q08481	UniProtKB	Alternative sequence	119	219	.	.	.	ID=VSP_038723;Note=In isoform 4. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:16141072;Dbxref=PMID:16141072	
Q08481	UniProtKB	Alternative sequence	692	727	.	.	.	ID=VSP_038724;Note=In isoform 2. ALGTRATETVYSEIRKVDPNLMENRYSRTEGSLNGT->ENGRLP;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:15489334;Dbxref=PMID:15489334	
Q08481	UniProtKB	Alternative sequence	711	727	.	.	.	ID=VSP_038725;Note=In isoform 3. NLMENRYSRTEGSLNGT->KNGRLP;Ontology_term=ECO:0000305;evidence=ECO:0000305	
Q08481	UniProtKB	Mutagenesis	679	679	.	.	.	Note=Reduces tyrosine phosphorylation by FER by about 60%25. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16731527;Dbxref=PMID:16731527	
Q08481	UniProtKB	Mutagenesis	702	702	.	.	.	Note=Reduces tyrosine phosphorylation by FER by about 60%25. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16731527;Dbxref=PMID:16731527	
Q08481	UniProtKB	Mutagenesis	717	717	.	.	.	Note=No significant effect on phosphorylation by FER. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16731527;Dbxref=PMID:16731527	
Q08481	UniProtKB	Sequence conflict	18	18	.	.	.	Note=E->T;Ontology_term=ECO:0000305;evidence=ECO:0000305