##gff-version 3
P54290	UniProtKB	Signal peptide	1	24	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
P54290	UniProtKB	Chain	25	1091	.	.	.	ID=PRO_0000304635;Note=Voltage-dependent calcium channel subunit alpha-2/delta-1	
P54290	UniProtKB	Chain	25	944	.	.	.	ID=PRO_0000005005;Note=Voltage-dependent calcium channel subunit alpha-2-1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P54290	UniProtKB	Chain	945	1091	.	.	.	ID=PRO_0000005006;Note=Voltage-dependent calcium channel subunit delta-1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P54290	UniProtKB	Topological domain	25	1061	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P54290	UniProtKB	Transmembrane	1062	1082	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P54290	UniProtKB	Topological domain	1083	1091	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P54290	UniProtKB	Domain	252	429	.	.	.	Note=VWFA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00219	
P54290	UniProtKB	Domain	445	536	.	.	.	Note=Cache	
P54290	UniProtKB	Motif	258	262	.	.	.	Note=MIDAS-like motif	
P54290	UniProtKB	Binding site	258	258	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
P54290	UniProtKB	Binding site	260	260	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
P54290	UniProtKB	Binding site	262	262	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
P54290	UniProtKB	Modified residue	119	119	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:22673903;Dbxref=PMID:22673903	
P54290	UniProtKB	Glycosylation	92	92	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P54290	UniProtKB	Glycosylation	136	136	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P54290	UniProtKB	Glycosylation	184	184	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P54290	UniProtKB	Glycosylation	323	323	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:24090084;Dbxref=PMID:24090084	
P54290	UniProtKB	Glycosylation	347	347	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P54290	UniProtKB	Glycosylation	593	593	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P54290	UniProtKB	Glycosylation	769	769	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P54290	UniProtKB	Glycosylation	876	876	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P54290	UniProtKB	Glycosylation	973	973	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:24090084;Dbxref=PMID:24090084	
P54290	UniProtKB	Disulfide bond	403	1047	.	.	.	Note=Interchain (between alpha-2-1 and delta-1 chains);Ontology_term=ECO:0000250;evidence=ECO:0000250