##gff-version 3
P32301	UniProtKB	Signal peptide	1	21	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
P32301	UniProtKB	Chain	22	463	.	.	.	ID=PRO_0000012837;Note=Glucagon-like peptide 1 receptor	
P32301	UniProtKB	Topological domain	22	139	.	.	.	Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P32301	UniProtKB	Transmembrane	140	164	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P43220	
P32301	UniProtKB	Topological domain	165	175	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P32301	UniProtKB	Transmembrane	176	201	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P43220	
P32301	UniProtKB	Topological domain	202	227	.	.	.	Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P32301	UniProtKB	Transmembrane	228	251	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P43220	
P32301	UniProtKB	Topological domain	252	265	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P32301	UniProtKB	Transmembrane	266	290	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P43220	
P32301	UniProtKB	Topological domain	291	305	.	.	.	Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P32301	UniProtKB	Transmembrane	306	328	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P43220	
P32301	UniProtKB	Topological domain	329	348	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P32301	UniProtKB	Transmembrane	349	370	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P43220	
P32301	UniProtKB	Topological domain	371	383	.	.	.	Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P32301	UniProtKB	Transmembrane	384	404	.	.	.	Note=Helical%3B Name%3D7;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P43220	
P32301	UniProtKB	Topological domain	405	463	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P32301	UniProtKB	Region	352	355	.	.	.	Note=Important for allosteric inhibitor binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P43220	
P32301	UniProtKB	Site	121	121	.	.	.	Note=Interaction with the endogenous ligand GLP-1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P43220	
P32301	UniProtKB	Site	128	128	.	.	.	Note=Interaction with the endogenous ligand GLP-1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P43220	
P32301	UniProtKB	Modified residue	341	341	.	.	.	Note=ADP-ribosylcysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P43220	
P32301	UniProtKB	Modified residue	348	348	.	.	.	Note=ADP-ribosylarginine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P43220	
P32301	UniProtKB	Glycosylation	63	63	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P32301	UniProtKB	Glycosylation	82	82	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P32301	UniProtKB	Glycosylation	115	115	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P32301	UniProtKB	Disulfide bond	46	71	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P43220	
P32301	UniProtKB	Disulfide bond	62	104	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P43220	
P32301	UniProtKB	Disulfide bond	85	126	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P43220	
P32301	UniProtKB	Disulfide bond	226	296	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P43220	
P32301	UniProtKB	Sequence conflict	323	323	.	.	.	Note=V->I;Ontology_term=ECO:0000305;evidence=ECO:0000305