##gff-version 3
Q61606	UniProtKB	Signal peptide	1	26	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q61606	UniProtKB	Chain	27	485	.	.	.	ID=PRO_0000012833;Note=Glucagon receptor	
Q61606	UniProtKB	Topological domain	27	137	.	.	.	Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P47871	
Q61606	UniProtKB	Transmembrane	138	162	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P47871	
Q61606	UniProtKB	Topological domain	163	174	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P47871	
Q61606	UniProtKB	Transmembrane	175	199	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P47871	
Q61606	UniProtKB	Topological domain	200	226	.	.	.	Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P47871	
Q61606	UniProtKB	Transmembrane	227	250	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P47871	
Q61606	UniProtKB	Topological domain	251	264	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P47871	
Q61606	UniProtKB	Transmembrane	265	286	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P47871	
Q61606	UniProtKB	Topological domain	287	304	.	.	.	Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P47871	
Q61606	UniProtKB	Transmembrane	305	327	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P47871	
Q61606	UniProtKB	Topological domain	328	351	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P47871	
Q61606	UniProtKB	Transmembrane	352	370	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P47871	
Q61606	UniProtKB	Topological domain	371	382	.	.	.	Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P47871	
Q61606	UniProtKB	Transmembrane	383	403	.	.	.	Note=Helical%3B Name%3D7;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P47871	
Q61606	UniProtKB	Topological domain	404	485	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P47871	
Q61606	UniProtKB	Region	351	354	.	.	.	Note=Important for allosteric inhibitor binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P47871	
Q61606	UniProtKB	Region	457	485	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q61606	UniProtKB	Modified residue	460	460	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P47871	
Q61606	UniProtKB	Modified residue	476	476	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P30082	
Q61606	UniProtKB	Glycosylation	47	47	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q61606	UniProtKB	Glycosylation	60	60	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q61606	UniProtKB	Glycosylation	75	75	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q61606	UniProtKB	Glycosylation	79	79	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q61606	UniProtKB	Glycosylation	118	118	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q61606	UniProtKB	Disulfide bond	44	68	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P47871	
Q61606	UniProtKB	Disulfide bond	59	101	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P47871	
Q61606	UniProtKB	Disulfide bond	82	122	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P47871	
Q61606	UniProtKB	Disulfide bond	225	295	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P47871	
Q61606	UniProtKB	Mutagenesis	369	369	.	.	.	Note=Results in impaired glucagon binding and glucagon-mediated signaling. Homozygous mice show hyperglucagonemia with alpha-cell hyperplasia and enlargement of the pancreas. V->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:32677665;Dbxref=PMID:32677665	
Q61606	UniProtKB	Sequence conflict	65	65	.	.	.	Note=K->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
Q61606	UniProtKB	Sequence conflict	89	89	.	.	.	Note=Y->C;Ontology_term=ECO:0000305;evidence=ECO:0000305	
Q61606	UniProtKB	Sequence conflict	238	238	.	.	.	Note=A->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
Q61606	UniProtKB	Sequence conflict	325	325	.	.	.	Note=H->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
Q61606	UniProtKB	Sequence conflict	328	328	.	.	.	Note=H->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305