##gff-version 3 P57757 UniProtKB Signal peptide 1 22 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O60931 P57757 UniProtKB Chain 23 367 . . . ID=PRO_0000205515;Note=Cystinosin P57757 UniProtKB Topological domain 23 125 . . . Note=Lumenal;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O60931 P57757 UniProtKB Transmembrane 126 150 . . . Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O60931 P57757 UniProtKB Topological domain 151 159 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O60931 P57757 UniProtKB Transmembrane 160 179 . . . Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O60931 P57757 UniProtKB Topological domain 180 202 . . . Note=Lumenal;Ontology_term=ECO:0000250,ECO:0000305;evidence=ECO:0000250|UniProtKB:O60931,ECO:0000305 P57757 UniProtKB Transmembrane 203 225 . . . Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O60931 P57757 UniProtKB Topological domain 226 234 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O60931 P57757 UniProtKB Transmembrane 235 257 . . . Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O60931 P57757 UniProtKB Topological domain 258 263 . . . Note=Lumenal;Ontology_term=ECO:0000250,ECO:0000305;evidence=ECO:0000250|UniProtKB:O60931,ECO:0000305 P57757 UniProtKB Transmembrane 264 289 . . . Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O60931 P57757 UniProtKB Topological domain 290 298 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O60931 P57757 UniProtKB Transmembrane 299 308 . . . Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O60931 P57757 UniProtKB Topological domain 309 331 . . . Note=Lumenal;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O60931 P57757 UniProtKB Transmembrane 332 354 . . . Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O60931 P57757 UniProtKB Topological domain 355 367 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O60931 P57757 UniProtKB Domain 123 189 . . . Note=PQ-loop 1 P57757 UniProtKB Domain 263 328 . . . Note=PQ-loop 2 P57757 UniProtKB Motif 362 366 . . . Note=Lysosomal targeting motif;Ontology_term=ECO:0000255;evidence=ECO:0000255 P57757 UniProtKB Binding site 166 166 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O60931 P57757 UniProtKB Binding site 205 205 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O60931 P57757 UniProtKB Binding site 273 273 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O60931 P57757 UniProtKB Binding site 280 280 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O60931 P57757 UniProtKB Binding site 281 281 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O60931 P57757 UniProtKB Binding site 305 305 . . . Note=Protonated residue following cystine-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O60931 P57757 UniProtKB Binding site 305 305 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O60931 P57757 UniProtKB Binding site 346 346 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O60931 P57757 UniProtKB Glycosylation 36 36 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 P57757 UniProtKB Glycosylation 51 51 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 P57757 UniProtKB Glycosylation 66 66 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19349973;Dbxref=PMID:19349973 P57757 UniProtKB Glycosylation 84 84 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 P57757 UniProtKB Glycosylation 104 104 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 P57757 UniProtKB Glycosylation 107 107 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 P57757 UniProtKB Mutagenesis 280 280 . . . Note=Abolished cystine transport. Abolished interaction with components of the v-ATPase and Ragulator complexes. Does not affect ability to lysosomal localization of LAMP2A. K->R;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:26449607,ECO:0000269|PubMed:28465352;Dbxref=PMID:26449607,PMID:28465352