##gff-version 3 Q9R0E0 UniProtKB Chain 1 394 . . . ID=PRO_0000059178;Note=Ceramide glucosyltransferase Q9R0E0 UniProtKB Topological domain 1 10 . . . Note=Lumenal;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:10393098;Dbxref=PMID:10393098 Q9R0E0 UniProtKB Transmembrane 11 32 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q9R0E0 UniProtKB Topological domain 33 195 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:10393098;Dbxref=PMID:10393098 Q9R0E0 UniProtKB Transmembrane 196 215 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q9R0E0 UniProtKB Topological domain 216 287 . . . Note=Lumenal;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:10393098;Dbxref=PMID:10393098 Q9R0E0 UniProtKB Transmembrane 288 304 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q9R0E0 UniProtKB Topological domain 305 309 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:10393098;Dbxref=PMID:10393098 Q9R0E0 UniProtKB Transmembrane 310 328 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q9R0E0 UniProtKB Topological domain 329 348 . . . Note=Lumenal;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:10393098;Dbxref=PMID:10393098 Q9R0E0 UniProtKB Transmembrane 349 369 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q9R0E0 UniProtKB Topological domain 370 394 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:10393098;Dbxref=PMID:10393098 Q9R0E0 UniProtKB Motif 92 92 . . . Note=D1;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9R0E0 UniProtKB Motif 144 144 . . . Note=D2;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9R0E0 UniProtKB Motif 236 236 . . . Note=D3;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9R0E0 UniProtKB Motif 272 276 . . . Note=(Q/R)XXRW;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9R0E0 UniProtKB Active site 236 236 . . . Note=Proton acceptor;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:11337504;Dbxref=PMID:11337504 Q9R0E0 UniProtKB Site 193 193 . . . Note=May play an important role in binding to the inhibitors DEPC and PDMP;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10393098;Dbxref=PMID:10393098 Q9R0E0 UniProtKB Modified residue 117 117 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O88693 Q9R0E0 UniProtKB Natural variant 8 8 . . . Note=In strain: Wistar. Q->L Q9R0E0 UniProtKB Natural variant 89 89 . . . Note=In strain: Wistar. D->G Q9R0E0 UniProtKB Natural variant 153 153 . . . Note=In strain: Wistar. T->S Q9R0E0 UniProtKB Natural variant 179 179 . . . Note=In strain: Wistar. G->A Q9R0E0 UniProtKB Natural variant 387 387 . . . Note=In strain: Wistar. T->I Q9R0E0 UniProtKB Mutagenesis 26 26 . . . Note=Inhibits activity to less than 6%25. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10393098;Dbxref=PMID:10393098 Q9R0E0 UniProtKB Mutagenesis 26 26 . . . Note=Inhibits activity to about 10%25. H->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10393098;Dbxref=PMID:10393098 Q9R0E0 UniProtKB Mutagenesis 26 26 . . . Note=Inhibits activity to about 50%25. H->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10393098;Dbxref=PMID:10393098 Q9R0E0 UniProtKB Mutagenesis 26 26 . . . Note=No effect on activity. Decreased sensitivity to the inhibitor PDMP. H->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10393098;Dbxref=PMID:10393098 Q9R0E0 UniProtKB Mutagenesis 36 36 . . . Note=No effect on activity. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10393098;Dbxref=PMID:10393098 Q9R0E0 UniProtKB Mutagenesis 90 90 . . . Note=No effect on activity. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10393098;Dbxref=PMID:10393098 Q9R0E0 UniProtKB Mutagenesis 92 92 . . . Note=Inhibits activity to about 20%25. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11337504;Dbxref=PMID:11337504 Q9R0E0 UniProtKB Mutagenesis 124 124 . . . Note=Completely abolishes catalytic activity. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11337504;Dbxref=PMID:11337504 Q9R0E0 UniProtKB Mutagenesis 144 144 . . . Note=Completely abolishes catalytic activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11337504;Dbxref=PMID:11337504 Q9R0E0 UniProtKB Mutagenesis 169 169 . . . Note=Inhibits activity to about 30%25. Decreased sensitivity to PDMP. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10393098;Dbxref=PMID:10393098 Q9R0E0 UniProtKB Mutagenesis 193 193 . . . Note=Inhibits activity to about 30%25. Insensitive to the inhibitors DEPC and PDMP. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10393098;Dbxref=PMID:10393098 Q9R0E0 UniProtKB Mutagenesis 193 193 . . . Note=Abolishes activity. H->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10393098;Dbxref=PMID:10393098 Q9R0E0 UniProtKB Mutagenesis 193 193 . . . Note=Inhibits activity to about 20%25. Insensitive to the inhibitors DEPC and PDMP. H->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10393098;Dbxref=PMID:10393098 Q9R0E0 UniProtKB Mutagenesis 193 193 . . . Note=Abolishes activity. H->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10393098;Dbxref=PMID:10393098 Q9R0E0 UniProtKB Mutagenesis 224 224 . . . Note=Completely abolishes catalytic activity. G->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11337504;Dbxref=PMID:11337504 Q9R0E0 UniProtKB Mutagenesis 225 225 . . . Note=Completely abolishes catalytic activity. G->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11337504;Dbxref=PMID:11337504 Q9R0E0 UniProtKB Mutagenesis 235 235 . . . Note=Inhibits activity to less than 1.5%25. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11337504;Dbxref=PMID:11337504 Q9R0E0 UniProtKB Mutagenesis 236 236 . . . Note=Completely abolishes catalytic activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11337504;Dbxref=PMID:11337504 Q9R0E0 UniProtKB Mutagenesis 247 247 . . . Note=Leads to near complete loss of activity. G->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11337504;Dbxref=PMID:11337504 Q9R0E0 UniProtKB Mutagenesis 272 272 . . . Note=Completely abolishes catalytic activity. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11337504;Dbxref=PMID:11337504 Q9R0E0 UniProtKB Mutagenesis 275 275 . . . Note=Completely abolishes catalytic activity. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11337504;Dbxref=PMID:11337504 Q9R0E0 UniProtKB Mutagenesis 276 276 . . . Note=Completely abolishes catalytic activity. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11337504;Dbxref=PMID:11337504 Q9R0E0 UniProtKB Mutagenesis 308 309 . . . Note=Inhibits activity to about 10%25. HH->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10393098;Dbxref=PMID:10393098 Q9R0E0 UniProtKB Mutagenesis 308 308 . . . Note=Inhibits activity to about 35%25. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10393098;Dbxref=PMID:10393098 Q9R0E0 UniProtKB Mutagenesis 309 309 . . . Note=Inhibits activity to about 70%25. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10393098;Dbxref=PMID:10393098 Q9R0E0 UniProtKB Mutagenesis 322 322 . . . Note=Inhibits activity to less than 6%25. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10393098;Dbxref=PMID:10393098 Q9R0E0 UniProtKB Mutagenesis 322 322 . . . Note=Inhibits activity to less than 6%25. H->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10393098;Dbxref=PMID:10393098 Q9R0E0 UniProtKB Mutagenesis 322 322 . . . Note=Inhibits activity to about 50%25. H->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10393098;Dbxref=PMID:10393098 Q9R0E0 UniProtKB Mutagenesis 322 322 . . . Note=Abolishes activity. H->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10393098;Dbxref=PMID:10393098