##gff-version 3 Q68CP4 UniProtKB Chain 1 663 . . . ID=PRO_0000273153;Note=Heparan-alpha-glucosaminide N-acetyltransferase Q68CP4 UniProtKB Topological domain 1 190 . . . Note=Lumenal%2C vesicle;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q68CP4 UniProtKB Transmembrane 191 211 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q68CP4 UniProtKB Topological domain 212 275 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q68CP4 UniProtKB Transmembrane 276 296 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q68CP4 UniProtKB Topological domain 297 302 . . . Note=Lumenal%2C vesicle;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q68CP4 UniProtKB Transmembrane 303 323 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q68CP4 UniProtKB Topological domain 324 345 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q68CP4 UniProtKB Transmembrane 346 366 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q68CP4 UniProtKB Topological domain 367 374 . . . Note=Lumenal%2C vesicle;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q68CP4 UniProtKB Transmembrane 375 395 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q68CP4 UniProtKB Topological domain 396 420 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q68CP4 UniProtKB Transmembrane 421 441 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q68CP4 UniProtKB Topological domain 442 500 . . . Note=Lumenal%2C vesicle;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q68CP4 UniProtKB Transmembrane 501 521 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q68CP4 UniProtKB Topological domain 522 529 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q68CP4 UniProtKB Transmembrane 530 550 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q68CP4 UniProtKB Topological domain 551 564 . . . Note=Lumenal%2C vesicle;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q68CP4 UniProtKB Transmembrane 565 585 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q68CP4 UniProtKB Topological domain 586 592 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q68CP4 UniProtKB Transmembrane 593 613 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q68CP4 UniProtKB Topological domain 614 634 . . . Note=Lumenal%2C vesicle;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q68CP4 UniProtKB Transmembrane 635 655 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q68CP4 UniProtKB Topological domain 656 663 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q68CP4 UniProtKB Region 1 24 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q68CP4 UniProtKB Region 624 635 . . . Note=Lysosomal targeting region Q68CP4 UniProtKB Active site 297 297 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20650889;Dbxref=PMID:20650889 Q68CP4 UniProtKB Modified residue 243 243 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 Q68CP4 UniProtKB Modified residue 245 245 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:20068231,ECO:0007744|PubMed:23186163;Dbxref=PMID:20068231,PMID:23186163 Q68CP4 UniProtKB Glycosylation 94 94 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q68CP4 UniProtKB Glycosylation 142 142 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19159218;Dbxref=PMID:19159218 Q68CP4 UniProtKB Glycosylation 162 162 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q68CP4 UniProtKB Disulfide bond 151 462 . . . Ontology_term=ECO:0000305;evidence=ECO:0000305 Q68CP4 UniProtKB Alternative sequence 1 28 . . . ID=VSP_040504;Note=In isoform 2. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:14702039;Dbxref=PMID:14702039 Q68CP4 UniProtKB Natural variant 82 82 . . . ID=VAR_075812;Note=In MPS3C%3B shows practically no enzyme activity. A->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20825431;Dbxref=PMID:20825431 Q68CP4 UniProtKB Natural variant 104 104 . . . ID=VAR_063983;Note=In MPS3C%3B results in a negligible amount of protein synthesis%3B very low enzyme activity%3B retained in the endoplasmic reticulum%3B loss of intralysosomal proteolytic cleavage. C->F;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17033958,ECO:0000269|PubMed:19823584,ECO:0000269|PubMed:20583299,ECO:0000269|PubMed:20650889;Dbxref=PMID:17033958,PMID:19823584,PMID:20583299,PMID:20650889 Q68CP4 UniProtKB Natural variant 141 141 . . . ID=VAR_075813;Note=In MPS3C%3B shows practically no enzyme activity. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20825431;Dbxref=PMID:20825431 Q68CP4 UniProtKB Natural variant 152 152 . . . ID=VAR_075814;Note=In RP73. R->W;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25859010;Dbxref=PMID:25859010 Q68CP4 UniProtKB Natural variant 161 161 . . . ID=VAR_075815;Note=In RP73. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25859010;Dbxref=PMID:25859010 Q68CP4 UniProtKB Natural variant 165 165 . . . ID=VAR_063984;Note=In MPS3C%3B results in a negligible amount of protein synthesis%3B very low enzyme activity%3B retained in the endoplasmic reticulum. L->P;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17397050,ECO:0000269|PubMed:18024218,ECO:0000269|PubMed:19479962,ECO:0000269|PubMed:19823584,ECO:0000269|PubMed:20583299;Dbxref=PMID:17397050,PMID:18024218,PMID:19479962,PMID:19823584,PMID:20583299 Q68CP4 UniProtKB Natural variant 265 265 . . . ID=VAR_063985;Note=In MPS3C%3B likely benign%3B does not influence stability%3B does not influence activity%3B does not influence cellular localization of the enzyme. P->Q;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17033958,ECO:0000269|PubMed:17397050,ECO:0000269|PubMed:18024218,ECO:0000269|PubMed:19479962,ECO:0000269|PubMed:19823584,ECO:0000269|PubMed:20583299,ECO:0000269|PubMed:20825431;Dbxref=PMID:17033958,PMID:17397050,PMID:18024218,PMID:19479962,PMID:19823584,PMID:20583299,PMID:20825431 Q68CP4 UniProtKB Natural variant 280 280 . . . ID=VAR_063986;Note=In MPS3C. I->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18024218;Dbxref=PMID:18024218 Q68CP4 UniProtKB Natural variant 290 290 . . . ID=VAR_063987;Note=In MPS3C%3B results in a negligible amount of protein synthesis%3B very low enzyme activity%3B retained in the endoplasmic reticulum. G->R;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18024218,ECO:0000269|PubMed:19823584,ECO:0000269|PubMed:20583299;Dbxref=PMID:18024218,PMID:19823584,PMID:20583299 Q68CP4 UniProtKB Natural variant 301 301 . . . ID=VAR_063988;Note=In MPS3C%3B retained in the endoplasmic reticulum%3B loss of enzymatic activity. N->K;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18024218,ECO:0000269|PubMed:19823584;Dbxref=PMID:18024218,PMID:19823584 Q68CP4 UniProtKB Natural variant 311 311 . . . ID=VAR_030083;Note=In MPS3C%3B results in a negligible amount of protein synthesis%3B very low enzyme activity%3B retained in the endoplasmic reticulum. P->L;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17033958,ECO:0000269|PubMed:19479962,ECO:0000269|PubMed:19823584,ECO:0000269|PubMed:20583299;Dbxref=PMID:17033958,PMID:19479962,PMID:19823584,PMID:20583299 Q68CP4 UniProtKB Natural variant 372 372 . . . ID=VAR_030084;Note=In MPS3C%3B results in a negligible amount of protein synthesis%3B very low enzyme activity%3B retained in the endoplasmic reticulum. R->C;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17033958,ECO:0000269|PubMed:18024218,ECO:0000269|PubMed:19479962,ECO:0000269|PubMed:20583299;Dbxref=PMID:17033958,PMID:18024218,PMID:19479962,PMID:20583299 Q68CP4 UniProtKB Natural variant 372 372 . . . ID=VAR_063989;Note=In MPS3C%3B retained in the endoplasmic reticulum%3B loss of enzymatic activity. R->H;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17033958,ECO:0000269|PubMed:19823584;Dbxref=PMID:17033958,PMID:19823584 Q68CP4 UniProtKB Natural variant 431 431 . . . ID=VAR_063990;Note=In MPS3C%3B results in a negligible amount of protein synthesis%3B very low enzyme activity%3B retained in the endoplasmic reticulum. W->C;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17033958,ECO:0000269|PubMed:19479962,ECO:0000269|PubMed:19823584,ECO:0000269|PubMed:20583299;Dbxref=PMID:17033958,PMID:19479962,PMID:19823584,PMID:20583299 Q68CP4 UniProtKB Natural variant 452 452 . . . ID=VAR_030085;Note=In MPS3C%3B results in a negligible amount of protein synthesis%3B very low enzyme activity%3B retained in the endoplasmic reticulum. G->S;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17033958,ECO:0000269|PubMed:19823584,ECO:0000269|PubMed:20583299;Dbxref=PMID:17033958,PMID:19823584,PMID:20583299 Q68CP4 UniProtKB Natural variant 452 452 . . . ID=VAR_075816;Note=In MPS3C%3B shows practically no enzyme activity. G->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20825431;Dbxref=PMID:20825431 Q68CP4 UniProtKB Natural variant 473 473 . . . ID=VAR_075817;Note=In MPS3C%3B shows practically no enzyme activity. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20825431;Dbxref=PMID:20825431 Q68CP4 UniProtKB Natural variant 499 499 . . . ID=VAR_030086;Note=In MPS3C%3B results in a negligible amount of protein synthesis%3B very low enzyme activity%3B retained in the endoplasmic reticulum. E->K;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17033958,ECO:0000269|PubMed:18024218,ECO:0000269|PubMed:19479962,ECO:0000269|PubMed:19823584,ECO:0000269|PubMed:20583299;Dbxref=PMID:17033958,PMID:18024218,PMID:19479962,PMID:19823584,PMID:20583299 Q68CP4 UniProtKB Natural variant 509 509 . . . ID=VAR_063991;Note=In MPS3C%3B likely benign%3B no loss of enzymatic activity. V->L;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:19479962,ECO:0000269|PubMed:19823584,ECO:0000269|PubMed:20583299;Dbxref=PMID:19479962,PMID:19823584,PMID:20583299 Q68CP4 UniProtKB Natural variant 510 510 . . . ID=VAR_030087;Note=In MPS3C%3B results in a negligible amount of protein synthesis%3B very low enzyme activity%3B retained in the endoplasmic reticulum. M->K;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17033958,ECO:0000269|PubMed:19823584,ECO:0000269|PubMed:20583299;Dbxref=PMID:17033958,PMID:19823584,PMID:20583299 Q68CP4 UniProtKB Natural variant 514 514 . . . ID=VAR_063992;Note=In MPS3C%3B results in a negligible amount of protein synthesis%3B very low enzyme activity%3B retained in the endoplasmic reticulum. G->E;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:19479962,ECO:0000269|PubMed:20583299;Dbxref=PMID:19479962,PMID:20583299 Q68CP4 UniProtKB Natural variant 517 517 . . . ID=VAR_063993;Note=In MPS3C%3B results in a negligible amount of protein synthesis%3B very low enzyme activity%3B retained in the endoplasmic reticulum. A->E;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:19479962,ECO:0000269|PubMed:19823584,ECO:0000269|PubMed:20583299;Dbxref=PMID:19479962,PMID:19823584,PMID:20583299 Q68CP4 UniProtKB Natural variant 546 546 . . . ID=VAR_063994;Note=In MPS3C%3B results in a negligible amount of protein synthesis%3B very low enzyme activity%3B retained in the endoplasmic reticulum. S->F;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17397050,ECO:0000269|PubMed:18024218,ECO:0000269|PubMed:19479962,ECO:0000269|PubMed:19823584,ECO:0000269|PubMed:20583299,ECO:0000269|PubMed:20825431;Dbxref=PMID:17397050,PMID:18024218,PMID:19479962,PMID:19823584,PMID:20583299,PMID:20825431 Q68CP4 UniProtKB Natural variant 551 551 . . . ID=VAR_063995;Note=In MPS3C%3B likely benign%3B no loss of enzymatic activity. K->Q;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17033958,ECO:0000269|PubMed:19479962,ECO:0000269|PubMed:19823584,ECO:0000269|PubMed:20583299;Dbxref=dbSNP:rs73569592,PMID:17033958,PMID:19479962,PMID:19823584,PMID:20583299 Q68CP4 UniProtKB Natural variant 567 567 . . . ID=VAR_063996;Note=In MPS3C%3B results in a negligible amount of protein synthesis%3B very low enzyme activity%3B retained in the endoplasmic reticulum. S->C;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18024218,ECO:0000269|PubMed:19823584,ECO:0000269|PubMed:20583299;Dbxref=PMID:18024218,PMID:19823584,PMID:20583299 Q68CP4 UniProtKB Natural variant 569 569 . . . ID=VAR_030088;Note=In MPS3C%3B results in a negligible amount of protein synthesis%3B very low enzyme activity. S->L;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17033958,ECO:0000269|PubMed:19479962,ECO:0000269|PubMed:19823584,ECO:0000269|PubMed:20583299;Dbxref=PMID:17033958,PMID:19479962,PMID:19823584,PMID:20583299 Q68CP4 UniProtKB Natural variant 590 590 . . . ID=VAR_030089;Note=In MPS3C%3B results in a negligible amount of protein synthesis%3B very low enzyme activity. D->V;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17033958,ECO:0000269|PubMed:19823584,ECO:0000269|PubMed:20583299;Dbxref=PMID:17033958,PMID:19823584,PMID:20583299 Q68CP4 UniProtKB Natural variant 599 599 . . . ID=VAR_030090;Note=In MPS3C%3B results in a negligible amount of protein synthesis%3B very low enzyme activity. P->L;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17033958,ECO:0000269|PubMed:19823584,ECO:0000269|PubMed:20583299;Dbxref=PMID:17033958,PMID:19823584,PMID:20583299 Q68CP4 UniProtKB Natural variant 643 643 . . . ID=VAR_063997;Note=In RP73 and MPS3C%3B uncertain significance%3B may act as a modifier of disease severity in patients with retinitis pigmentosa%3B has a negligible effect on the enzyme expression%3B moderately reduced enzyme activity. A->T;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17033958,ECO:0000269|PubMed:19479962,ECO:0000269|PubMed:19823584,ECO:0000269|PubMed:20583299,ECO:0000269|PubMed:25859010;Dbxref=dbSNP:rs112029032,PMID:17033958,PMID:19479962,PMID:19823584,PMID:20583299,PMID:25859010 Q68CP4 UniProtKB Mutagenesis 107 107 . . . Note=Loss of intralysosomal proteolytic cleavage and enzymatic activity. Reduced oligomer formation. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20650889;Dbxref=PMID:20650889 Q68CP4 UniProtKB Mutagenesis 151 151 . . . Note=Loss of intralysosomal proteolytic cleavage and enzymatic activity. Reduced oligomer formation. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20650889;Dbxref=PMID:20650889 Q68CP4 UniProtKB Mutagenesis 179 179 . . . Note=Loss of intralysosomal proteolytic cleavage and enzymatic activity. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20650889;Dbxref=PMID:20650889 Q68CP4 UniProtKB Mutagenesis 236 236 . . . Note=Displayed both lysosomal and plasma membrane localization%2C reduced intralysosomal proteolytic cleavage and enzymatic activity%3B when associated with A-209. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20650889;Dbxref=PMID:20650889 Q68CP4 UniProtKB Mutagenesis 237 237 . . . Note=Displayed both lysosomal and plasma membrane localization%2C reduced intralysosomal proteolytic cleavage and enzymatic activity%3B when associated with A-208. I->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20650889;Dbxref=PMID:20650889 Q68CP4 UniProtKB Mutagenesis 297 297 . . . Note=Loss of enzymatic activity%2C but correctly targeted and processed. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20650889;Dbxref=PMID:20650889 Q68CP4 UniProtKB Mutagenesis 333 333 . . . Note=No loss of intralysosomal proteolytic cleavage and enzymatic activity. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20650889;Dbxref=PMID:20650889 Q68CP4 UniProtKB Mutagenesis 402 402 . . . Note=No loss of intralysosomal proteolytic cleavage and enzymatic activity. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20650889;Dbxref=PMID:20650889 Q68CP4 UniProtKB Mutagenesis 462 462 . . . Note=Complete loss of intralysosomal proteolytic cleavage and enzymatic activity. Reduced oligomer formation. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20650889;Dbxref=PMID:20650889 Q68CP4 UniProtKB Mutagenesis 479 479 . . . Note=Loss of intralysosomal proteolytic cleavage and enzymatic activity%2C retained in the endoplasmic reticulum. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20650889;Dbxref=PMID:20650889 Q68CP4 UniProtKB Mutagenesis 633 633 . . . Note=Loss of intralysosomal proteolytic cleavage and enzymatic activity%2C retained in the endoplasmic reticulum. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20650889;Dbxref=PMID:20650889 Q68CP4 UniProtKB Mutagenesis 652 663 . . . Note=Loss of intralysosomal proteolytic cleavage and enzymatic activity. Localized in the plasma membrane. Missing