##gff-version 3 Q99J27 UniProtKB Chain 1 550 . . . ID=PRO_0000076166;Note=Acetyl-coenzyme A transporter 1 Q99J27 UniProtKB Topological domain 1 74 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q99J27 UniProtKB Transmembrane 75 95 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q99J27 UniProtKB Topological domain 96 113 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q99J27 UniProtKB Transmembrane 114 134 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q99J27 UniProtKB Topological domain 135 141 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q99J27 UniProtKB Transmembrane 142 162 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q99J27 UniProtKB Topological domain 163 175 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q99J27 UniProtKB Transmembrane 176 196 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q99J27 UniProtKB Topological domain 197 217 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q99J27 UniProtKB Transmembrane 218 238 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q99J27 UniProtKB Topological domain 239 256 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q99J27 UniProtKB Transmembrane 257 277 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q99J27 UniProtKB Topological domain 278 300 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q99J27 UniProtKB Transmembrane 301 321 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q99J27 UniProtKB Topological domain 322 344 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q99J27 UniProtKB Transmembrane 345 365 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q99J27 UniProtKB Topological domain 366 375 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q99J27 UniProtKB Transmembrane 376 396 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q99J27 UniProtKB Topological domain 397 405 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q99J27 UniProtKB Transmembrane 406 426 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q99J27 UniProtKB Topological domain 427 509 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q99J27 UniProtKB Transmembrane 510 530 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q99J27 UniProtKB Topological domain 531 550 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q99J27 UniProtKB Region 1 58 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q99J27 UniProtKB Modified residue 42 42 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:17208939,ECO:0007744|PubMed:17242355,ECO:0007744|PubMed:21183079;Dbxref=PMID:17208939,PMID:17242355,PMID:21183079 Q99J27 UniProtKB Glycosylation 103 103 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q99J27 UniProtKB Mutagenesis 113 113 . . . Note=Mice homozygous for the mutation display early developmental arrest. Heterozygous animals display a deregulated form of autophagy. S->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24828632;Dbxref=PMID:24828632 Q99J27 UniProtKB Sequence conflict 255 257 . . . Note=VTL->GNP;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q99J27 UniProtKB Sequence conflict 274 275 . . . Note=LV->SL;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q99J27 UniProtKB Sequence conflict 293 293 . . . Note=Q->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q99J27 UniProtKB Sequence conflict 337 337 . . . Note=V->E;Ontology_term=ECO:0000305;evidence=ECO:0000305