##gff-version 3 P17809 UniProtKB Chain 1 492 . . . ID=PRO_0000050339;Note=Solute carrier family 2%2C facilitated glucose transporter member 1 P17809 UniProtKB Topological domain 1 11 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11166 P17809 UniProtKB Transmembrane 12 33 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11166 P17809 UniProtKB Topological domain 34 66 . . . Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11166 P17809 UniProtKB Transmembrane 67 87 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11166 P17809 UniProtKB Topological domain 88 90 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11166 P17809 UniProtKB Transmembrane 91 112 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11166 P17809 UniProtKB Topological domain 113 120 . . . Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11166 P17809 UniProtKB Transmembrane 121 144 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11166 P17809 UniProtKB Topological domain 145 155 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11166 P17809 UniProtKB Transmembrane 156 176 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11166 P17809 UniProtKB Topological domain 177 185 . . . Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11166 P17809 UniProtKB Transmembrane 186 206 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11166 P17809 UniProtKB Topological domain 207 271 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11166 P17809 UniProtKB Transmembrane 272 293 . . . Note=Helical%3B Name%3D7;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11166 P17809 UniProtKB Topological domain 294 306 . . . Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11166 P17809 UniProtKB Transmembrane 307 328 . . . Note=Helical%3B Name%3D8;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11166 P17809 UniProtKB Topological domain 329 334 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11166 P17809 UniProtKB Transmembrane 335 355 . . . Note=Helical%3B Name%3D9;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11166 P17809 UniProtKB Topological domain 356 365 . . . Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11166 P17809 UniProtKB Transmembrane 366 388 . . . Note=Helical%3B Name%3D10;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11166 P17809 UniProtKB Topological domain 389 401 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11166 P17809 UniProtKB Transmembrane 402 422 . . . Note=Helical%3B Name%3D11;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11166 P17809 UniProtKB Topological domain 423 429 . . . Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11166 P17809 UniProtKB Transmembrane 430 450 . . . Note=Helical%3B Name%3D12;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11166 P17809 UniProtKB Topological domain 451 492 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11166 P17809 UniProtKB Region 468 492 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P17809 UniProtKB Binding site 161 161 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11169 P17809 UniProtKB Binding site 282 283 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11169 P17809 UniProtKB Binding site 288 288 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11169 P17809 UniProtKB Binding site 317 317 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11169 P17809 UniProtKB Binding site 380 380 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11169 P17809 UniProtKB Binding site 388 388 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11169 P17809 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11166 P17809 UniProtKB Modified residue 226 226 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11166 P17809 UniProtKB Modified residue 465 465 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11166 P17809 UniProtKB Modified residue 478 478 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11166 P17809 UniProtKB Modified residue 490 490 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11166 P17809 UniProtKB Glycosylation 45 45 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:19349973,ECO:0000269|PubMed:19656770;Dbxref=PMID:19349973,PMID:19656770 P17809 UniProtKB Mutagenesis 485 485 . . . Note=Lethality immediately after birth in knockin mice%3B caused by creation of a dileucine internalization motif that promotes mislocalization of the protein. P->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30197081;Dbxref=PMID:30197081 P17809 UniProtKB Sequence conflict 52 52 . . . Note=Y->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 P17809 UniProtKB Sequence conflict 193 195 . . . Note=IFI->VFV;Ontology_term=ECO:0000305;evidence=ECO:0000305 P17809 UniProtKB Sequence conflict 357 360 . . . Note=LLER->MQEQ;Ontology_term=ECO:0000305;evidence=ECO:0000305 P17809 UniProtKB Sequence conflict 403 403 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305