##gff-version 3 P40967 UniProtKB Signal peptide 1 24 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8179825;Dbxref=PMID:8179825 P40967 UniProtKB Chain 25 661 . . . ID=PRO_0000024712;Note=Melanocyte protein PMEL P40967 UniProtKB Chain 25 467 . . . ID=PRO_0000292263;Note=M-alpha P40967 UniProtKB Chain 470 661 . . . ID=PRO_0000386648;Note=M-beta P40967 UniProtKB Topological domain 470 595 . . . Note=Lumenal;Ontology_term=ECO:0000305;evidence=ECO:0000305 P40967 UniProtKB Transmembrane 596 616 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 P40967 UniProtKB Topological domain 617 661 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305 P40967 UniProtKB Domain 255 292 . . . Note=PKD;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00151 P40967 UniProtKB Repeat 302 314 . . . Note=1;Ontology_term=ECO:0000255;evidence=ECO:0000255 P40967 UniProtKB Repeat 315 327 . . . Note=2;Ontology_term=ECO:0000255;evidence=ECO:0000255 P40967 UniProtKB Repeat 328 340 . . . Note=3;Ontology_term=ECO:0000255;evidence=ECO:0000255 P40967 UniProtKB Repeat 341 353 . . . Note=4;Ontology_term=ECO:0000255;evidence=ECO:0000255 P40967 UniProtKB Repeat 354 366 . . . Note=5;Ontology_term=ECO:0000255;evidence=ECO:0000255 P40967 UniProtKB Repeat 367 379 . . . Note=6;Ontology_term=ECO:0000255;evidence=ECO:0000255 P40967 UniProtKB Repeat 380 392 . . . Note=7;Ontology_term=ECO:0000255;evidence=ECO:0000255 P40967 UniProtKB Repeat 393 405 . . . Note=8;Ontology_term=ECO:0000255;evidence=ECO:0000255 P40967 UniProtKB Repeat 406 418 . . . Note=9;Ontology_term=ECO:0000255;evidence=ECO:0000255 P40967 UniProtKB Repeat 419 431 . . . Note=10;Ontology_term=ECO:0000255;evidence=ECO:0000255 P40967 UniProtKB Repeat 432 444 . . . Note=11;Ontology_term=ECO:0000255;evidence=ECO:0000255 P40967 UniProtKB Repeat 445 457 . . . Note=12;Ontology_term=ECO:0000255;evidence=ECO:0000255 P40967 UniProtKB Region 148 223 . . . Note=Amyloidogenic unit;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28272432;Dbxref=PMID:28272432 P40967 UniProtKB Region 154 162 . . . Note=Antigenic peptide%3B presented by A*02:01;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7706734;Dbxref=PMID:7706734 P40967 UniProtKB Region 209 217 . . . Note=Antigenic peptide%3B presented by A*02:01;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7706734;Dbxref=PMID:7706734 P40967 UniProtKB Region 280 288 . . . Note=Antigenic peptide%3B presented by A*02:01;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7706734;Dbxref=PMID:7706734 P40967 UniProtKB Region 302 457 . . . Note=12 X 13 AA approximate tandem repeats%2C RPT domain;Ontology_term=ECO:0000255,ECO:0000305;evidence=ECO:0000255,ECO:0000305|PubMed:30988362;Dbxref=PMID:30988362 P40967 UniProtKB Region 302 353 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P40967 UniProtKB Region 516 566 . . . Note=Kringle-like fold;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:26694611;Dbxref=PMID:26694611 P40967 UniProtKB Site 151 151 . . . Note=Essential for fibril formation;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28272432;Dbxref=PMID:28272432 P40967 UniProtKB Site 160 160 . . . Note=Essential for fibril formation;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28272432;Dbxref=PMID:28272432 P40967 UniProtKB Site 469 470 . . . Note=Cleavage%3B by furin-like proprotein convertase;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12732614;Dbxref=PMID:12732614 P40967 UniProtKB Site 583 584 . . . Note=Cleavage%3B by ADAM metalloproteinases;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19047044;Dbxref=PMID:19047044 P40967 UniProtKB Site 655 656 . . . Note=Endocytosis signal;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16760433;Dbxref=PMID:16760433 P40967 UniProtKB Site 661 661 . . . Note=ER exit signal;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16760433;Dbxref=PMID:16760433 P40967 UniProtKB Glycosylation 81 81 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 P40967 UniProtKB Glycosylation 106 106 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 P40967 UniProtKB Glycosylation 111 111 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 P40967 UniProtKB Glycosylation 321 321 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 P40967 UniProtKB Glycosylation 568 568 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 P40967 UniProtKB Alternative sequence 26 111 . . . ID=VSP_038266;Note=In isoform 3. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:14702039;Dbxref=PMID:14702039 P40967 UniProtKB Alternative sequence 373 414 . . . ID=VSP_038267;Note=In isoform 4 and isoform 5. Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 P40967 UniProtKB Alternative sequence 587 587 . . . ID=VSP_038268;Note=In isoform 2 and isoform 5. P->PVPGILLT;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:1924386;Dbxref=PMID:1924386 P40967 UniProtKB Natural variant 320 320 . . . ID=VAR_050606;Note=P->H;Dbxref=dbSNP:rs2071024 P40967 UniProtKB Natural variant 370 370 . . . ID=VAR_050607;Note=E->D;Dbxref=dbSNP:rs17118154 P40967 UniProtKB Mutagenesis 60 60 . . . Note=Does not affect dimer formation. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26694611;Dbxref=PMID:26694611 P40967 UniProtKB Mutagenesis 130 130 . . . Note=Does not affect dimer formation. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26694611;Dbxref=PMID:26694611 P40967 UniProtKB Mutagenesis 138 138 . . . Note=Does not affect dimer formation. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26694611;Dbxref=PMID:26694611 P40967 UniProtKB Mutagenesis 149 149 . . . Note=Loss-of-function. Retained in the endoplasmic reticulum likely due to misfolding. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28272432;Dbxref=PMID:28272432 P40967 UniProtKB Mutagenesis 149 149 . . . Note=Reduces fibril formation. F->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28272432;Dbxref=PMID:28272432 P40967 UniProtKB Mutagenesis 151 151 . . . Note=Loss-of-function. Abolishes fibril formation. Does not exert dominant negative effect%3B when associated with A-211. Y->A%2CL;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28272432;Dbxref=PMID:28272432 P40967 UniProtKB Mutagenesis 151 151 . . . Note=Has normal fibril formation. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28272432;Dbxref=PMID:28272432 P40967 UniProtKB Mutagenesis 152 152 . . . Note=Markedly reduces fibril formation. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28272432;Dbxref=PMID:28272432 P40967 UniProtKB Mutagenesis 153 153 . . . Note=Loss-of-function. Abolishes fibrillar amyloid formation. Does not exert dominant negative effect and retains the amyloidogenic potential%3B when associated with A-211. W->A%2CF;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28272432;Dbxref=PMID:28272432 P40967 UniProtKB Mutagenesis 154 154 . . . Note=Reduces fibril formation. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28272432;Dbxref=PMID:28272432 P40967 UniProtKB Mutagenesis 155 155 . . . Note=Reduces fibril formation. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28272432;Dbxref=PMID:28272432 P40967 UniProtKB Mutagenesis 156 156 . . . Note=Reduces fibril formation. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28272432;Dbxref=PMID:28272432 P40967 UniProtKB Mutagenesis 157 157 . . . Note=Reduces fibril formation. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28272432;Dbxref=PMID:28272432 P40967 UniProtKB Mutagenesis 158 158 . . . Note=Reduces fibril formation. Q->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28272432;Dbxref=PMID:28272432 P40967 UniProtKB Mutagenesis 159 159 . . . Note=Reduces fibril formation. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28272432;Dbxref=PMID:28272432 P40967 UniProtKB Mutagenesis 160 160 . . . Note=Loss-of-function. Abolishes fibril formation. Does not exert dominant negative effect%3B when associated with A-211. W->A%2CF;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28272432;Dbxref=PMID:28272432 P40967 UniProtKB Mutagenesis 161 161 . . . Note=Reduces fibril formation. Q->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28272432;Dbxref=PMID:28272432 P40967 UniProtKB Mutagenesis 162 162 . . . Note=Reduces fibril formation. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28272432;Dbxref=PMID:28272432 P40967 UniProtKB Mutagenesis 165 165 . . . Note=Reduces fibril formation. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28272432;Dbxref=PMID:28272432 P40967 UniProtKB Mutagenesis 170 170 . . . Note=Loss-of-function. Abolishes fibrillar amyloid formation. Does not exert dominant negative effect and retains the amyloidogenic potential%3B when associated with A-211. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28272432;Dbxref=PMID:28272432 P40967 UniProtKB Mutagenesis 172 172 . . . Note=Loss-of-function. Likely misfolded and rapidly degraded. I->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28272432;Dbxref=PMID:28272432 P40967 UniProtKB Mutagenesis 174 174 . . . Note=Markedly reduces fibril formation. Does not exert dominant negative effect%3B when associated with A-211. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28272432;Dbxref=PMID:28272432 P40967 UniProtKB Mutagenesis 180 180 . . . Note=Reduces fibril formation. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28272432;Dbxref=PMID:28272432 P40967 UniProtKB Mutagenesis 189 189 . . . Note=Loss-of-function. Abolishes fibrillar amyloid formation. Does not exert dominant negative effect and retains the amyloidogenic potential%3B when associated with A-211. Y->A%2CL;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28272432;Dbxref=PMID:28272432 P40967 UniProtKB Mutagenesis 189 189 . . . Note=Has normal fibril formation. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28272432;Dbxref=PMID:28272432 P40967 UniProtKB Mutagenesis 191 191 . . . Note=Reduces fibril formation. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28272432;Dbxref=PMID:28272432 P40967 UniProtKB Mutagenesis 192 192 . . . Note=Reduces fibril formation. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28272432;Dbxref=PMID:28272432 P40967 UniProtKB Mutagenesis 200 200 . . . Note=Reduces fibril formation. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28272432;Dbxref=PMID:28272432 P40967 UniProtKB Mutagenesis 207 207 . . . Note=Loss-of-function. Abolishes fibrillar amyloid formation. Does not exert dominant negative effect and retains the amyloidogenic potential%3B when associated with A-211. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28272432;Dbxref=PMID:28272432 P40967 UniProtKB Mutagenesis 207 207 . . . Note=Has normal fibril formation. Reduces fibril formation%3B when associated with L-215. F->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28272432;Dbxref=PMID:28272432 P40967 UniProtKB Mutagenesis 209 209 . . . Note=Loss-of-function. Abolishes fibrillar amyloid formation. Does not exert dominant negative effect and retains the amyloidogenic potential%3B when associated with A-211. I->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28272432;Dbxref=PMID:28272432 P40967 UniProtKB Mutagenesis 210 210 . . . Note=Reduces fibril formation. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28272432;Dbxref=PMID:28272432 P40967 UniProtKB Mutagenesis 211 211 . . . Note=Forms fibrils at normal levels. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28272432;Dbxref=PMID:28272432 P40967 UniProtKB Mutagenesis 213 213 . . . Note=Reduces fibril formation. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28272432;Dbxref=PMID:28272432 P40967 UniProtKB Mutagenesis 214 214 . . . Note=Reduces fibril formation. P->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28272432;Dbxref=PMID:28272432 P40967 UniProtKB Mutagenesis 215 215 . . . Note=Reduces fibril formation. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28272432;Dbxref=PMID:28272432 P40967 UniProtKB Mutagenesis 215 215 . . . Note=Has normal fibril formation. Reduces fibril formation%3B when associated with L-207. F->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28272432;Dbxref=PMID:28272432 P40967 UniProtKB Mutagenesis 301 301 . . . Note=Abolishes interchain and intrachain disulfide linkage formation. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26694611;Dbxref=PMID:26694611 P40967 UniProtKB Mutagenesis 468 469 . . . Note=Loss of proteolytic cleavage. KR->QQ;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12732614;Dbxref=PMID:12732614 P40967 UniProtKB Mutagenesis 475 475 . . . Note=Does not affect dimer formation. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26694611;Dbxref=PMID:26694611 P40967 UniProtKB Mutagenesis 516 516 . . . Note=Abolishes disulfide linkage rearrangement that converts dimer to monomer. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26694611;Dbxref=PMID:26694611 P40967 UniProtKB Mutagenesis 525 525 . . . Note=Abolishes disulfide linkage rearrangement that converts dimer to monomer. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26694611;Dbxref=PMID:26694611 P40967 UniProtKB Mutagenesis 533 533 . . . Note=Abolishes disulfide linkage rearrangement that converts dimer to monomer. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26694611;Dbxref=PMID:26694611 P40967 UniProtKB Mutagenesis 541 541 . . . Note=Abolishes disulfide linkage rearrangement that converts dimer to monomer. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26694611;Dbxref=PMID:26694611 P40967 UniProtKB Mutagenesis 550 550 . . . Note=Abolishes disulfide linkage rearrangement that converts dimer to monomer. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26694611;Dbxref=PMID:26694611 P40967 UniProtKB Mutagenesis 566 566 . . . Note=Abolishes disulfide linkage rearrangement that converts dimer to monomer. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26694611;Dbxref=PMID:26694611 P40967 UniProtKB Mutagenesis 582 585 . . . Note=Impairs the cleavage of the C-terminal fragment. TQLI->DDDD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19047044;Dbxref=PMID:19047044 P40967 UniProtKB Mutagenesis 582 585 . . . Note=Impairs the cleavage of the C-terminal fragment. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19047044;Dbxref=PMID:19047044 P40967 UniProtKB Mutagenesis 583 584 . . . Note=Impairs the cleavage of the C-terminal fragment. QL->DD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19047044;Dbxref=PMID:19047044 P40967 UniProtKB Mutagenesis 637 661 . . . Note=Leads to inefficient ER exit%2C endocytic trafficking and protein maturation. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16760433;Dbxref=PMID:16760433 P40967 UniProtKB Mutagenesis 655 656 . . . Note=Leads to inefficient endocytic trafficking. LL->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16760433;Dbxref=PMID:16760433 P40967 UniProtKB Mutagenesis 661 661 . . . Note=Leads to inefficient ER exit. V->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16760433;Dbxref=PMID:16760433 P40967 UniProtKB Sequence conflict 162 162 . . . Note=V->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 P40967 UniProtKB Sequence conflict 274 274 . . . Note=L->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 P40967 UniProtKB Sequence conflict 373 373 . . . Note=G->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 P40967 UniProtKB Sequence conflict 592 592 . . . Note=G->GG;Ontology_term=ECO:0000305;evidence=ECO:0000305 P40967 UniProtKB Sequence conflict 597 597 . . . Note=P->R;Ontology_term=ECO:0000305;evidence=ECO:0000305