##gff-version 3
P41968	UniProtKB	Chain	1	323	.	.	.	ID=PRO_0000069718;Note=Melanocortin receptor 3	
P41968	UniProtKB	Topological domain	1	37	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P41968	UniProtKB	Transmembrane	38	63	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P41968	UniProtKB	Topological domain	64	75	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P41968	UniProtKB	Transmembrane	76	100	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P41968	UniProtKB	Topological domain	101	118	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P41968	UniProtKB	Transmembrane	119	140	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P41968	UniProtKB	Topological domain	141	160	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P41968	UniProtKB	Transmembrane	161	181	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P41968	UniProtKB	Topological domain	182	186	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P41968	UniProtKB	Transmembrane	187	210	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P41968	UniProtKB	Topological domain	211	245	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P41968	UniProtKB	Transmembrane	246	268	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P41968	UniProtKB	Topological domain	269	277	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P41968	UniProtKB	Transmembrane	278	301	.	.	.	Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P41968	UniProtKB	Topological domain	302	323	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P41968	UniProtKB	Lipidation	315	315	.	.	.	Note=S-palmitoyl cysteine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P41968	UniProtKB	Glycosylation	2	2	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P41968	UniProtKB	Glycosylation	16	16	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P41968	UniProtKB	Glycosylation	28	28	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P41968	UniProtKB	Natural variant	44	44	.	.	.	ID=VAR_020070;Note=Have ligand binding and signaling properties similar to wild-type. V->I;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15292330,ECO:0000269|PubMed:8463333;Dbxref=dbSNP:rs3827103,PMID:15292330,PMID:8463333	
P41968	UniProtKB	Natural variant	146	146	.	.	.	ID=VAR_055000;Note=Risk factor for obesity%3B completely lacks signaling in response to agonist stimulation%3B coexpression of the wild-type and the mutant receptor shows that it does not exert dominant-negative activity on wild-type. I->N;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11889220,ECO:0000269|PubMed:15292330;Dbxref=dbSNP:rs74315393,PMID:11889220,PMID:15292330	
P41968	UniProtKB	Natural variant	298	298	.	.	.	ID=VAR_055001;Note=Risk factor for obesity%3B in vitro expression studies demonstrate that the mutation causes complete loss of function%3B transfected cells show diffuse cytoplasmic staining indicating intracellular retention of the receptor. I->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18231126;Dbxref=dbSNP:rs121913556,PMID:18231126