##gff-version 3 Q9GZU1 UniProtKB Chain 1 580 . . . ID=PRO_0000215362;Note=Mucolipin-1 Q9GZU1 UniProtKB Topological domain 1 65 . . . Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29019983;Dbxref=PMID:29019983 Q9GZU1 UniProtKB Transmembrane 66 86 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29019983;Dbxref=PMID:29019983 Q9GZU1 UniProtKB Topological domain 87 298 . . . Note=Extracellular;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29019983;Dbxref=PMID:29019983 Q9GZU1 UniProtKB Transmembrane 299 321 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29019983;Dbxref=PMID:29019983 Q9GZU1 UniProtKB Topological domain 322 350 . . . Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29019983;Dbxref=PMID:29019983 Q9GZU1 UniProtKB Transmembrane 351 371 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29019983;Dbxref=PMID:29019983 Q9GZU1 UniProtKB Topological domain 372 382 . . . Note=Extracellular;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29019983;Dbxref=PMID:29019983 Q9GZU1 UniProtKB Transmembrane 383 405 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29019983;Dbxref=PMID:29019983 Q9GZU1 UniProtKB Topological domain 406 427 . . . Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29019983;Dbxref=PMID:29019983 Q9GZU1 UniProtKB Transmembrane 428 448 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29019983;Dbxref=PMID:29019983 Q9GZU1 UniProtKB Topological domain 449 456 . . . Note=Extracellular;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29019983;Dbxref=PMID:29019983 Q9GZU1 UniProtKB Intramembrane 457 477 . . . Note=Pore-forming;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29019983;Dbxref=PMID:29019983 Q9GZU1 UniProtKB Topological domain 478 491 . . . Note=Extracellular;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29019983;Dbxref=PMID:29019983 Q9GZU1 UniProtKB Transmembrane 492 513 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29019983;Dbxref=PMID:29019983 Q9GZU1 UniProtKB Topological domain 514 580 . . . Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29019983;Dbxref=PMID:29019983 Q9GZU1 UniProtKB Region 1 38 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9GZU1 UniProtKB Region 42 62 . . . Note=Interaction with phosphoinositides;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22733759;Dbxref=PMID:22733759 Q9GZU1 UniProtKB Region 107 121 . . . Note=Extracellular/lumenal pore loop;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:28112729;Dbxref=PMID:28112729 Q9GZU1 UniProtKB Region 565 567 . . . Note=Required for palmitoylation and association with membranes;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16497227;Dbxref=PMID:16497227 Q9GZU1 UniProtKB Motif 11 16 . . . Note=Dileucine motif%3B mediates targeting to lysosomes;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16497227;Dbxref=PMID:16497227 Q9GZU1 UniProtKB Motif 469 474 . . . Note=Selectivity filter;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:29019983;Dbxref=PMID:29019983 Q9GZU1 UniProtKB Motif 573 578 . . . Note=Dileucine internalization motif%3B mediates AP2 complex-dependent internalization;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16497227;Dbxref=PMID:16497227 Q9GZU1 UniProtKB Modified residue 10 10 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99J21 Q9GZU1 UniProtKB Modified residue 557 557 . . . Note=Phosphoserine%3B by PAK;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17988215;Dbxref=PMID:17988215 Q9GZU1 UniProtKB Modified residue 559 559 . . . Note=Phosphoserine%3B by PAK;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17988215;Dbxref=PMID:17988215 Q9GZU1 UniProtKB Glycosylation 230 230 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19159218;Dbxref=PMID:19159218 Q9GZU1 UniProtKB Disulfide bond 166 192 . . . Ontology_term=ECO:0000269,ECO:0000269,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0000269|PubMed:28112729,ECO:0000269|PubMed:29019983,ECO:0007744|PDB:5TJA,ECO:0007744|PDB:5TJB,ECO:0007744|PDB:5TJC,ECO:0007744|PDB:5WJ5,ECO:0007744|PDB:5WJ9;Dbxref=PMID:28112729,PMID:29019983 Q9GZU1 UniProtKB Disulfide bond 253 284 . . . Ontology_term=ECO:0000269,ECO:0000269,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0000269|PubMed:28112729,ECO:0000269|PubMed:29019983,ECO:0007744|PDB:5TJA,ECO:0007744|PDB:5TJB,ECO:0007744|PDB:5TJC,ECO:0007744|PDB:5WJ5,ECO:0007744|PDB:5WJ9;Dbxref=PMID:28112729,PMID:29019983 Q9GZU1 UniProtKB Natural variant 106 106 . . . ID=VAR_019369;Note=In ML4%3B decreases formation and extrusion of tubulo-vesicular structures when overexpressed%3B disrupts tetrameric assembly%3B abolishes lysosomal localization. L->P;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12182165,ECO:0000269|PubMed:21256127,ECO:0000269|PubMed:28112729;Dbxref=dbSNP:rs797044825,PMID:12182165,PMID:21256127,PMID:28112729 Q9GZU1 UniProtKB Natural variant 232 232 . . . ID=VAR_019370;Note=In ML4%3B fails to localize to late endosomes%3B abolishes Fe(2+) permeability%3B disrupts tetrameric assembly%3B abolishes lysosomal localization. T->P;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11317355,ECO:0000269|PubMed:15178326,ECO:0000269|PubMed:18794901,ECO:0000269|PubMed:28112729;Dbxref=dbSNP:rs767122713,PMID:11317355,PMID:15178326,PMID:18794901,PMID:28112729 Q9GZU1 UniProtKB Natural variant 331 331 . . . ID=VAR_036453;Note=In a breast cancer sample%3B somatic mutation. V->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16959974;Dbxref=PMID:16959974 Q9GZU1 UniProtKB Natural variant 362 362 . . . ID=VAR_019371;Note=In ML4%3B affects channel activity%3B abolishes Fe(2+) permeability. D->Y;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11030752,ECO:0000269|PubMed:12182165,ECO:0000269|PubMed:14749347,ECO:0000269|PubMed:18794901;Dbxref=dbSNP:rs121908372,PMID:11030752,PMID:12182165,PMID:14749347,PMID:18794901 Q9GZU1 UniProtKB Natural variant 403 403 . . . ID=VAR_038380;Note=In ML4%3B impairs Fe(2+) permeability. R->C;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15523648,ECO:0000269|PubMed:18794901;Dbxref=dbSNP:rs121908374,PMID:15523648,PMID:18794901 Q9GZU1 UniProtKB Natural variant 408 408 . . . ID=VAR_019372;Note=In ML4%3B mild psychomotor involvement%3B does not affect channel activity%3B affects channel inhibition by low pH%3B still localizes to late endosomes. Missing;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11030752,ECO:0000269|PubMed:11317355,ECO:0000269|PubMed:12182165,ECO:0000269|PubMed:14749347,ECO:0000269|PubMed:15178326;Dbxref=dbSNP:rs797044817,PMID:11030752,PMID:11317355,PMID:12182165,PMID:14749347,PMID:15178326 Q9GZU1 UniProtKB Natural variant 446 446 . . . ID=VAR_019373;Note=In ML4%3B does not affect channel activity%3B affects channel inhibition by low pH%3B impairs Fe(2+) permeability. V->L;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11030752,ECO:0000269|PubMed:14749347,ECO:0000269|PubMed:18794901;Dbxref=dbSNP:rs754097561,PMID:11030752,PMID:14749347,PMID:18794901 Q9GZU1 UniProtKB Natural variant 447 447 . . . ID=VAR_019374;Note=In ML4. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12182165;Dbxref=dbSNP:rs797044827,PMID:12182165 Q9GZU1 UniProtKB Natural variant 465 465 . . . ID=VAR_019375;Note=In ML4%3B still localizes to late endosomes%3B fails to rescue defect of lactosylceramide traffic through the late endocytic pathway in ML4 patient cells%3B minor effect on formation and extrusion of tubulo-vesicular structures when overexpressed. F->L;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11317355,ECO:0000269|PubMed:15178326,ECO:0000269|PubMed:16978393,ECO:0000269|PubMed:21256127;Dbxref=dbSNP:rs797044828,PMID:11317355,PMID:15178326,PMID:16978393,PMID:21256127 Q9GZU1 UniProtKB Mutagenesis 15 16 . . . Note=No effect on localization to lysosomes. LL->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16497227;Dbxref=PMID:16497227 Q9GZU1 UniProtKB Mutagenesis 15 15 . . . Note=Abolishes localization to lysosomes and leads to expression at the cell membrane%3B when associated with A-577. L->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16497227,ECO:0000269|PubMed:29019983;Dbxref=PMID:16497227,PMID:29019983 Q9GZU1 UniProtKB Mutagenesis 42 44 . . . Note=Reduces PtdIns(4%2C5)P2 sensitivity. RRR->AAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22733759;Dbxref=PMID:22733759 Q9GZU1 UniProtKB Mutagenesis 44 46 . . . Note=Abolishes interaction with PDCD6 and decreases formation of aberrant endosomes upon overexpression. RLK->AAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19864416;Dbxref=PMID:19864416 Q9GZU1 UniProtKB Mutagenesis 44 44 . . . Note=Abolishes interaction with PDCD6. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19864416;Dbxref=PMID:19864416 Q9GZU1 UniProtKB Mutagenesis 45 45 . . . Note=Abolishes interaction with PDCD6. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19864416;Dbxref=PMID:19864416 Q9GZU1 UniProtKB Mutagenesis 47 49 . . . Note=Abolishes interaction with PDCD6. YFF->AAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19864416;Dbxref=PMID:19864416 Q9GZU1 UniProtKB Mutagenesis 61 62 . . . Note=Reduces PtdIns(3%2C5)P2 sensitivity. RK->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22733759;Dbxref=PMID:22733759 Q9GZU1 UniProtKB Mutagenesis 109 109 . . . Note=Abolishes formation and extrusion of tubulo-vesicular structures and decreases lysosomal exocytosis when overexpressed. Y->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21256127;Dbxref=PMID:21256127 Q9GZU1 UniProtKB Mutagenesis 110 110 . . . Note=Modulates ion conduction%3B when associoated with C-112 and C-113. S->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28112729;Dbxref=PMID:28112729 Q9GZU1 UniProtKB Mutagenesis 111 111 . . . Note=Modulates inhibition by Ca(2+) at different pH levels but does not abolish channel inward rectification%3B when associated with Q-114 and Q-115. D->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28112729;Dbxref=PMID:28112729 Q9GZU1 UniProtKB Mutagenesis 112 112 . . . Note=Modulates ion conduction%3B when associoated with C-110 and C-113. G->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28112729;Dbxref=PMID:28112729 Q9GZU1 UniProtKB Mutagenesis 113 113 . . . Note=Modulates ion conduction%3B when associoated with C-110 and C-112. A->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28112729;Dbxref=PMID:28112729 Q9GZU1 UniProtKB Mutagenesis 114 114 . . . Note=Modulates inhibition by Ca(2+) at different pH levels but does not abolish channel inward rectification%3B when associated with Q-111 and Q-115. D->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28112729;Dbxref=PMID:28112729 Q9GZU1 UniProtKB Mutagenesis 115 115 . . . Note=Modulates inhibition by Ca(2+) at different pH levels but does not abolish channel inward rectification%3B when associated with Q-111 and Q-114. D->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28112729;Dbxref=PMID:28112729 Q9GZU1 UniProtKB Mutagenesis 144 144 . . . Note=Disrupts tetrameric assembly and abolishes lysosomal localization%3B when associated with S-146. L->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28112729;Dbxref=PMID:28112729 Q9GZU1 UniProtKB Mutagenesis 146 146 . . . Note=Disrupts tetrameric assembly and abolishes lysosomal localization%3B when associated with K-144. R->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28112729;Dbxref=PMID:28112729 Q9GZU1 UniProtKB Mutagenesis 200 200 . . . Note=Does not prevent proteolytic cleavage but changes cleavage pattern. R->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16257972;Dbxref=PMID:16257972 Q9GZU1 UniProtKB Mutagenesis 432 432 . . . Note=Mediates localization to the plasma membrane and strong inwardly rectifying current. V->P;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18794901,ECO:0000269|PubMed:28112729;Dbxref=PMID:18794901,PMID:28112729 Q9GZU1 UniProtKB Mutagenesis 471 471 . . . Note=Fails to rescue defect of lactosylceramide traffic through the late endocytic pathway in ML4 patient cells. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16978393;Dbxref=PMID:16978393 Q9GZU1 UniProtKB Mutagenesis 565 567 . . . Note=Abolishes association with membranes. CCC->AAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16497227;Dbxref=PMID:16497227 Q9GZU1 UniProtKB Mutagenesis 577 578 . . . Note=No effect on localization to lysosomes. LL->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16497227;Dbxref=PMID:16497227 Q9GZU1 UniProtKB Mutagenesis 577 577 . . . Note=Abolishes localization to lysosomes and leads to expression at the cell membrane%3B when associated with A-15. L->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16497227,ECO:0000269|PubMed:29019983;Dbxref=PMID:16497227,PMID:29019983 Q9GZU1 UniProtKB Sequence conflict 164 191 . . . Note=ALCQRYYHRGHVDPANDTFDIDPMVVTD->LSASGTTTEATWTRPTTHLTLIRWWLLVN;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9GZU1 UniProtKB Sequence conflict 203 203 . . . Note=P->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9GZU1 UniProtKB Helix 41 49 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7MGL Q9GZU1 UniProtKB Helix 52 58 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7MGL Q9GZU1 UniProtKB Helix 84 105 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5TJA Q9GZU1 UniProtKB Turn 114 116 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5TJA Q9GZU1 UniProtKB Helix 122 137 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5TJA Q9GZU1 UniProtKB Helix 139 142 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5TJA Q9GZU1 UniProtKB Beta strand 143 145 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5WJ9 Q9GZU1 UniProtKB Beta strand 148 151 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5TJB Q9GZU1 UniProtKB Beta strand 154 156 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5TJA Q9GZU1 UniProtKB Beta strand 162 176 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5TJA Q9GZU1 UniProtKB Helix 177 179 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5TJA Q9GZU1 UniProtKB Beta strand 181 195 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5TJA Q9GZU1 UniProtKB Helix 218 220 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5WJ9 Q9GZU1 UniProtKB Helix 225 227 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5TJA Q9GZU1 UniProtKB Beta strand 228 241 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5TJA Q9GZU1 UniProtKB Helix 242 247 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5TJA Q9GZU1 UniProtKB Beta strand 252 263 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5TJA Q9GZU1 UniProtKB Beta strand 271 282 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5TJA Q9GZU1 UniProtKB Helix 291 293 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7MGL Q9GZU1 UniProtKB Helix 295 337 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7MGL Q9GZU1 UniProtKB Helix 346 349 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7MGL Q9GZU1 UniProtKB Helix 353 377 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7MGL Q9GZU1 UniProtKB Helix 383 399 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7MGL Q9GZU1 UniProtKB Helix 402 405 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7MGL Q9GZU1 UniProtKB Helix 409 447 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7MGL Q9GZU1 UniProtKB Turn 448 450 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7MGL Q9GZU1 UniProtKB Helix 452 454 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7MGL Q9GZU1 UniProtKB Helix 457 467 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7MGL Q9GZU1 UniProtKB Turn 468 470 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7MGL Q9GZU1 UniProtKB Helix 473 481 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7MGL Q9GZU1 UniProtKB Turn 482 486 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7MGL Q9GZU1 UniProtKB Helix 488 507 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7MGL Q9GZU1 UniProtKB Helix 510 524 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7MGL