##gff-version 3
Q62170	UniProtKB	Signal peptide	1	17	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q62170	UniProtKB	Propeptide	18	41	.	.	.	ID=PRO_0000022304;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q62170	UniProtKB	Chain	42	397	.	.	.	ID=PRO_0000022305;Note=P-selectin glycoprotein ligand 1	
Q62170	UniProtKB	Topological domain	18	307	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q62170	UniProtKB	Transmembrane	308	328	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q62170	UniProtKB	Topological domain	329	397	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q62170	UniProtKB	Repeat	126	135	.	.	.	Note=1	
Q62170	UniProtKB	Repeat	136	145	.	.	.	Note=2	
Q62170	UniProtKB	Repeat	146	155	.	.	.	Note=3	
Q62170	UniProtKB	Repeat	156	165	.	.	.	Note=4	
Q62170	UniProtKB	Repeat	166	175	.	.	.	Note=5	
Q62170	UniProtKB	Repeat	176	185	.	.	.	Note=6	
Q62170	UniProtKB	Repeat	186	195	.	.	.	Note=7	
Q62170	UniProtKB	Repeat	196	205	.	.	.	Note=8	
Q62170	UniProtKB	Repeat	206	215	.	.	.	Note=9	
Q62170	UniProtKB	Repeat	216	225	.	.	.	Note=10	
Q62170	UniProtKB	Region	89	261	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q62170	UniProtKB	Region	126	225	.	.	.	Note=10 X 10 AA tandem repeats	
Q62170	UniProtKB	Region	364	390	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q62170	UniProtKB	Modified residue	54	54	.	.	.	Note=Sulfotyrosine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:12393631;Dbxref=PMID:12393631	
Q62170	UniProtKB	Modified residue	391	391	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q14242	
Q62170	UniProtKB	Modified residue	394	394	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q14242	
Q62170	UniProtKB	Glycosylation	58	58	.	.	.	Note=O-linked (GalNAc...) threonine;Ontology_term=ECO:0000305;evidence=ECO:0000305	
Q62170	UniProtKB	Glycosylation	66	66	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q62170	UniProtKB	Glycosylation	261	261	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q62170	UniProtKB	Disulfide bond	307	307	.	.	.	Note=Interchain;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q62170	UniProtKB	Mutagenesis	54	54	.	.	.	Note=Greatly decreased P-selectin binding and tethering and rolling of cells. No further reduction of P-selectin binding%3B when associated with Y-56. Binding of P-selectin completely abolished%3B when associated with A-55%3B Y-56 and A-58. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12393631;Dbxref=PMID:12393631	
Q62170	UniProtKB	Mutagenesis	55	55	.	.	.	Note=No effect on P-selectin binding. Greatly reduced P-selectin binding and tethering and rolling of cells%3B when associated with A-58. Binding of P-selectin completely abolished%3B when associated with Y-54%3B Y-56 and A-58. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12393631;Dbxref=PMID:12393631	
Q62170	UniProtKB	Mutagenesis	56	56	.	.	.	Note=No effect on P-selectin binding. Greatly decreased P-selectin binding and tethering and rolling of cells%3B when associated with Y-54. Binding of P-selectin completely abolished%3B when associated with Y-54%3B A-55 and A-58. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12393631;Dbxref=PMID:12393631	
Q62170	UniProtKB	Mutagenesis	58	58	.	.	.	Note=Greatly decreased P-selectin binding and tethering and rolling of cells. No further reduction in P-selectin binding when associated with A-55. Binding of P-selectin completely abolished%3B when associated with Y-54%3B A-55%3B and Y-56. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12393631;Dbxref=PMID:12393631	
Q62170	UniProtKB	Mutagenesis	66	66	.	.	.	Note=No effect on P-selectin binding%3B when associated with A-261. N->T	
Q62170	UniProtKB	Mutagenesis	261	261	.	.	.	Note=No effect on P-selectin binding%3B when associated with T-66. N->A	
Q62170	UniProtKB	Sequence conflict	173	173	.	.	.	Note=E->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
Q62170	UniProtKB	Sequence conflict	176	176	.	.	.	Note=Q->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
Q62170	UniProtKB	Sequence conflict	180	180	.	.	.	Note=M->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
Q62170	UniProtKB	Sequence conflict	183	183	.	.	.	Note=D->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
Q62170	UniProtKB	Sequence conflict	186	186	.	.	.	Note=Q->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
Q62170	UniProtKB	Sequence conflict	190	190	.	.	.	Note=M->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
Q62170	UniProtKB	Beta strand	337	342	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2EMT