##gff-version 3 E9Q876 UniProtKB Chain 1 2595 . . . ID=PRO_0000452550;Note=Glucosylceramide transporter ABCA12 E9Q876 UniProtKB Transmembrane 23 43 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 E9Q876 UniProtKB Transmembrane 1062 1082 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 E9Q876 UniProtKB Transmembrane 1109 1129 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 E9Q876 UniProtKB Transmembrane 1142 1162 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 E9Q876 UniProtKB Transmembrane 1171 1191 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 E9Q876 UniProtKB Transmembrane 1197 1217 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 E9Q876 UniProtKB Transmembrane 1247 1267 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 E9Q876 UniProtKB Transmembrane 1747 1767 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 E9Q876 UniProtKB Transmembrane 1979 1999 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 E9Q876 UniProtKB Transmembrane 2035 2055 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 E9Q876 UniProtKB Transmembrane 2072 2092 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 E9Q876 UniProtKB Transmembrane 2103 2123 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 E9Q876 UniProtKB Transmembrane 2143 2163 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 E9Q876 UniProtKB Transmembrane 2187 2207 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 E9Q876 UniProtKB Transmembrane 2270 2290 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 E9Q876 UniProtKB Domain 1346 1577 . . . Note=ABC transporter 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 E9Q876 UniProtKB Domain 2254 2489 . . . Note=ABC transporter 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 E9Q876 UniProtKB Region 109 143 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite E9Q876 UniProtKB Region 1672 1703 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite E9Q876 UniProtKB Region 2575 2595 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite E9Q876 UniProtKB Compositional bias 115 139 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite E9Q876 UniProtKB Binding site 1378 1385 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 E9Q876 UniProtKB Binding site 2290 2297 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 E9Q876 UniProtKB Glycosylation 120 120 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 E9Q876 UniProtKB Glycosylation 156 156 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 E9Q876 UniProtKB Glycosylation 174 174 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 E9Q876 UniProtKB Glycosylation 214 214 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 E9Q876 UniProtKB Glycosylation 275 275 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 E9Q876 UniProtKB Glycosylation 331 331 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 E9Q876 UniProtKB Glycosylation 365 365 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 E9Q876 UniProtKB Glycosylation 381 381 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 E9Q876 UniProtKB Glycosylation 410 410 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 E9Q876 UniProtKB Glycosylation 433 433 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 E9Q876 UniProtKB Glycosylation 455 455 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 E9Q876 UniProtKB Glycosylation 526 526 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 E9Q876 UniProtKB Glycosylation 541 541 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 E9Q876 UniProtKB Glycosylation 574 574 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 E9Q876 UniProtKB Glycosylation 605 605 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 E9Q876 UniProtKB Glycosylation 645 645 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 E9Q876 UniProtKB Glycosylation 749 749 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 E9Q876 UniProtKB Glycosylation 773 773 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 E9Q876 UniProtKB Glycosylation 812 812 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 E9Q876 UniProtKB Glycosylation 823 823 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 E9Q876 UniProtKB Glycosylation 854 854 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 E9Q876 UniProtKB Glycosylation 917 917 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 E9Q876 UniProtKB Glycosylation 960 960 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 E9Q876 UniProtKB Glycosylation 1167 1167 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 E9Q876 UniProtKB Glycosylation 1319 1319 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 E9Q876 UniProtKB Glycosylation 1524 1524 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 E9Q876 UniProtKB Glycosylation 1663 1663 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 E9Q876 UniProtKB Glycosylation 1673 1673 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 E9Q876 UniProtKB Glycosylation 1686 1686 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 E9Q876 UniProtKB Glycosylation 1690 1690 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 E9Q876 UniProtKB Glycosylation 1704 1704 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 E9Q876 UniProtKB Glycosylation 1819 1819 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 E9Q876 UniProtKB Glycosylation 1835 1835 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 E9Q876 UniProtKB Glycosylation 1876 1876 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 E9Q876 UniProtKB Glycosylation 1921 1921 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 E9Q876 UniProtKB Glycosylation 1952 1952 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 E9Q876 UniProtKB Glycosylation 2318 2318 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 E9Q876 UniProtKB Glycosylation 2542 2542 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 E9Q876 UniProtKB Glycosylation 2547 2547 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 E9Q876 UniProtKB Mutagenesis 1388 1461 . . . Note=In a mouse model for harlequin ichthyosis (HI)%2C smooth skin (smsk) mutant mice show a pronounced perinatal lethal skin phenotype in 25%25 of the offspring and newborn mutant pups die within a few hours after birth%2C and appear severely dehydrated with dry cracking skin. Smsk homozygous mutants embryos show a normal appearance at 14.5 dpc%2C but at 16.5 dpc develop a partial absence of normal skin folds around the trunk and limbs%2C and by 18.5 dpc develop a taut%2C thick skin and limb contractures. ISMLTGLFGATAGTIFVYGKDIKTDLNTVRKNMGVCMQHDVLFSYLTTKEHLLLYGSIKVPHWTKTQLHEEVKR->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27551807;Dbxref=PMID:27551807 E9Q876 UniProtKB Mutagenesis 1996 1996 . . . Note=In a mouse model for harlequin ichthyosis (HI)%2C homozygous mice are embryonic lethal but occasionally pups are found in the first few hours after birth but die and are severely dehydrated and fail to suckle normally. Homozygous pups show hallmarks of HI desease including hyperkeratosis%2C abnormal extracellular lipid lamellae and defects in cornified envelope processing. At 14.5 dpc and 15.5 dpc homozygous embryos appear normal%3B however from 16.5 dpc onwards they are characterized by an absence of normal skin folds around the trunk and limbs. As development progressed%2C embryos develop a taut%2C thick epidermis and multiple contractures affecting the limbs. Late stage embryos are smaller. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18802465;Dbxref=PMID:18802465