##gff-version 3 P51810 UniProtKB Chain 1 404 . . . ID=PRO_0000195086;Note=G-protein coupled receptor 143 P51810 UniProtKB Topological domain 1 28 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 P51810 UniProtKB Transmembrane 29 49 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 P51810 UniProtKB Topological domain 50 78 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 P51810 UniProtKB Transmembrane 79 99 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 P51810 UniProtKB Topological domain 100 124 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 P51810 UniProtKB Transmembrane 125 145 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 P51810 UniProtKB Topological domain 146 149 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 P51810 UniProtKB Transmembrane 150 170 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255 P51810 UniProtKB Topological domain 171 191 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 P51810 UniProtKB Transmembrane 192 212 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255 P51810 UniProtKB Topological domain 213 248 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 P51810 UniProtKB Transmembrane 249 269 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255 P51810 UniProtKB Topological domain 270 292 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 P51810 UniProtKB Transmembrane 293 313 . . . Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255 P51810 UniProtKB Topological domain 314 404 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 P51810 UniProtKB Region 221 238 . . . Note=Necessary for its G protein-activation ability and normal distribution of melanosomes P51810 UniProtKB Region 338 404 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P51810 UniProtKB Motif 222 231 . . . Note=Lysosomal/melanosomal membrane localization signal P51810 UniProtKB Motif 329 330 . . . Note=Lysosomal/melanosomal membrane localization signal P51810 UniProtKB Compositional bias 355 393 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P51810 UniProtKB Glycosylation 106 106 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 P51810 UniProtKB Natural variant 5 5 . . . ID=VAR_018130;Note=In OA1%3B results in altered glycosylation pattern and subcellular localization consistent with protein retention in the endoplasmic reticulum%3B lacks G protein-activation abilities. R->C;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11115845,ECO:0000269|PubMed:11214907;Dbxref=dbSNP:rs62635289,PMID:11115845,PMID:11214907 P51810 UniProtKB Natural variant 35 35 . . . ID=VAR_005507;Note=In OA1%3B results in altered glycosylation pattern and subcellular localization consistent with protein retention in the endoplasmic reticulum. G->D;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11115845,ECO:0000269|PubMed:8634705,ECO:0000269|PubMed:9887374;Dbxref=dbSNP:rs62635018,PMID:11115845,PMID:8634705,PMID:9887374 P51810 UniProtKB Natural variant 39 39 . . . ID=VAR_018131;Note=In OA1. L->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9887374;Dbxref=dbSNP:rs62635019,PMID:9887374 P51810 UniProtKB Natural variant 78 78 . . . ID=VAR_018132;Note=In OA1%3B results in altered glycosylation pattern and subcellular localization consistent with protein retention in the endoplasmic reticulum. D->N;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11115845,ECO:0000269|PubMed:11214907;Dbxref=dbSNP:rs62635024,PMID:11115845,PMID:11214907 P51810 UniProtKB Natural variant 78 78 . . . ID=VAR_018133;Note=In OA1. D->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9887374;Dbxref=dbSNP:rs62635025,PMID:9887374 P51810 UniProtKB Natural variant 80 80 . . . ID=VAR_063264;Note=In OA1. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18978956;Dbxref=PMID:18978956 P51810 UniProtKB Natural variant 81 81 . . . ID=VAR_063265;Note=In OA1. G->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16646960;Dbxref=PMID:16646960 P51810 UniProtKB Natural variant 84 84 . . . ID=VAR_005508;Note=In OA1%3B results in altered glycosylation pattern and subcellular localization consistent with protein retention in the endoplasmic reticulum. G->D;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11115845,ECO:0000269|PubMed:8634705;Dbxref=dbSNP:rs62635027,PMID:11115845,PMID:8634705 P51810 UniProtKB Natural variant 84 84 . . . ID=VAR_005509;Note=In OA1. G->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9529334;Dbxref=dbSNP:rs62635026,PMID:9529334 P51810 UniProtKB Natural variant 89 89 . . . ID=VAR_063266;Note=In NYS6. S->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17516023;Dbxref=dbSNP:rs137852298,PMID:17516023 P51810 UniProtKB Natural variant 116 116 . . . ID=VAR_063267;Note=In OA1. C->G;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16524428,ECO:0000269|PubMed:17960122;Dbxref=PMID:16524428,PMID:17960122 P51810 UniProtKB Natural variant 116 116 . . . ID=VAR_005510;Note=In OA1. C->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9529334;Dbxref=dbSNP:rs62635030,PMID:9529334 P51810 UniProtKB Natural variant 116 116 . . . ID=VAR_018134;Note=In OA1%3B results in altered glycosylation pattern and subcellular localization consistent with protein retention in the endoplasmic reticulum. C->S;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11115845,ECO:0000269|PubMed:11214907;Dbxref=dbSNP:rs62635029,PMID:11115845,PMID:11214907 P51810 UniProtKB Natural variant 116 116 . . . ID=VAR_063268;Note=In OA1. C->W;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16646960;Dbxref=PMID:16646960 P51810 UniProtKB Natural variant 118 118 . . . ID=VAR_005511;Note=In OA1%3B results in altered glycosylation pattern and subcellular localization consistent with protein retention in the endoplasmic reticulum. G->E;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11115845,ECO:0000269|PubMed:11214907,ECO:0000269|PubMed:18978956,ECO:0000269|PubMed:9529334;Dbxref=dbSNP:rs62635031,PMID:11115845,PMID:11214907,PMID:18978956,PMID:9529334 P51810 UniProtKB Natural variant 124 124 . . . ID=VAR_018135;Note=In OA1. Q->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11214907;Dbxref=dbSNP:rs62635032,PMID:11214907 P51810 UniProtKB Natural variant 132 132 . . . ID=VAR_063269;Note=In OA1. W->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17822861;Dbxref=PMID:17822861 P51810 UniProtKB Natural variant 133 133 . . . ID=VAR_005513;Note=In OA1%3B results in altered glycosylation pattern and subcellular localization consistent with protein retention in the endoplasmic reticulum. W->R;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11115845,ECO:0000269|PubMed:9529334,ECO:0000269|PubMed:9887374;Dbxref=dbSNP:rs137852296,PMID:11115845,PMID:9529334,PMID:9887374 P51810 UniProtKB Natural variant 134 134 . . . ID=VAR_063270;Note=In OA1. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16646960;Dbxref=PMID:16646960 P51810 UniProtKB Natural variant 138 138 . . . ID=VAR_005514;Note=In OA1. A->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9529334;Dbxref=dbSNP:rs62635762,PMID:9529334 P51810 UniProtKB Natural variant 152 152 . . . ID=VAR_005515;Note=In OA1. S->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9529334;Dbxref=dbSNP:rs58933950,PMID:9529334 P51810 UniProtKB Natural variant 166 166 . . . ID=VAR_063271;Note=In OA1. T->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16646960;Dbxref=PMID:16646960 P51810 UniProtKB Natural variant 173 173 . . . ID=VAR_005516;Note=In OA1%3B results in altered glycosylation pattern and subcellular localization consistent with protein retention in the endoplasmic reticulum. A->D;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11115845,ECO:0000269|PubMed:8634705;Dbxref=dbSNP:rs62635035,PMID:11115845,PMID:8634705 P51810 UniProtKB Natural variant 185 185 . . . ID=VAR_063272;Note=In OA1. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17822861;Dbxref=PMID:17822861 P51810 UniProtKB Natural variant 186 186 . . . ID=VAR_063273;Note=In OA1. R->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17822861;Dbxref=PMID:17822861 P51810 UniProtKB Natural variant 186 186 . . . ID=VAR_063274;Note=In OA1. R->W;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17822861;Dbxref=dbSNP:rs199899645,PMID:17822861 P51810 UniProtKB Natural variant 229 229 . . . ID=VAR_018136;Note=In OA1%3B not delivered at the cell surface of melanocytic and non-melanocytic cells. G->V;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11214907,ECO:0000269|PubMed:16621890;Dbxref=dbSNP:rs62635037,PMID:11214907,PMID:16621890 P51810 UniProtKB Natural variant 232 232 . . . ID=VAR_005517;Note=In OA1%3B abnormal distribution of melanosomes%3B Not delivered at the cell surface of melanocytic and non-melanocytic cells. T->K;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16621890,ECO:0000269|PubMed:18697795,ECO:0000269|PubMed:9529334;Dbxref=dbSNP:rs137852297,PMID:16621890,PMID:18697795,PMID:9529334 P51810 UniProtKB Natural variant 233 233 . . . ID=VAR_018137;Note=In OA1. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9887374;Dbxref=dbSNP:rs62635038,PMID:9887374 P51810 UniProtKB Natural variant 235 235 . . . ID=VAR_005518;Note=In OA1%3B not delivered at the cell surface of melanocytic and non-melanocytic cells. E->K;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16621890,ECO:0000269|PubMed:9529334;Dbxref=PMID:16621890,PMID:9529334 P51810 UniProtKB Natural variant 244 244 . . . ID=VAR_018138;Note=In OA1%3B not delivered at the cell surface of melanocytic and non-melanocytic cells. I->V;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11214907,ECO:0000269|PubMed:16621890;Dbxref=dbSNP:rs62635040,PMID:11214907,PMID:16621890 P51810 UniProtKB Natural variant 261 261 . . . ID=VAR_018139;Note=In OA1%3B results in altered glycosylation pattern and subcellular localization consistent with protein retention in the endoplasmic reticulum. I->N;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11115845,ECO:0000269|PubMed:11214907;Dbxref=PMID:11115845,PMID:11214907 P51810 UniProtKB Natural variant 271 271 . . . ID=VAR_018140;Note=In OA1. E->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11214907;Dbxref=dbSNP:rs62635043,PMID:11214907 P51810 UniProtKB Natural variant 290 290 . . . ID=VAR_005519;Note=In OA1%3B results in altered glycosylation pattern and subcellular localization consistent with protein retention in the endoplasmic reticulum. Missing;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11115845,ECO:0000269|PubMed:8634705;Dbxref=dbSNP:rs62635044,PMID:11115845,PMID:8634705 P51810 UniProtKB Natural variant 292 292 . . . ID=VAR_018141;Note=In OA1. W->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11214907;Dbxref=dbSNP:rs62635046,PMID:11214907 P51810 UniProtKB Natural variant 292 292 . . . ID=VAR_005520;Note=In OA1%3B results in altered glycosylation pattern and subcellular localization consistent with protein retention in the endoplasmic reticulum. W->G;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11115845,ECO:0000269|PubMed:8634705;Dbxref=dbSNP:rs62635045,PMID:11115845,PMID:8634705 P51810 UniProtKB Mutagenesis 223 224 . . . Note=Delivered to both at the cell surface and in vesicles of melanocytic and non-melanocytic cells. Strongly delivered at the cell surface of melanocytic and non-melanocytic cells%3B when associated with 329-A-A-330. LL->AA P51810 UniProtKB Mutagenesis 329 330 . . . Note=Mostly delivered at the cell surface of melanocytic and non-melanocytic cells. Strongly delivered at the cell surface of melanocytic and non-melanocytic cells%3B when associated with 224-A-A-225. WE->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16621890;Dbxref=PMID:16621890