##gff-version 3 P19357 UniProtKB Chain 1 509 . . . ID=PRO_0000050366;Note=Solute carrier family 2%2C facilitated glucose transporter member 4 P19357 UniProtKB Topological domain 1 24 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 P19357 UniProtKB Transmembrane 25 45 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 P19357 UniProtKB Topological domain 46 81 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 P19357 UniProtKB Transmembrane 82 102 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 P19357 UniProtKB Topological domain 103 111 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 P19357 UniProtKB Transmembrane 112 132 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 P19357 UniProtKB Topological domain 133 142 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 P19357 UniProtKB Transmembrane 143 163 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255 P19357 UniProtKB Topological domain 164 171 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 P19357 UniProtKB Transmembrane 172 192 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255 P19357 UniProtKB Topological domain 193 201 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 P19357 UniProtKB Transmembrane 202 222 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255 P19357 UniProtKB Topological domain 223 287 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 P19357 UniProtKB Transmembrane 288 308 . . . Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255 P19357 UniProtKB Topological domain 309 323 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 P19357 UniProtKB Transmembrane 324 344 . . . Note=Helical%3B Name%3D8;Ontology_term=ECO:0000255;evidence=ECO:0000255 P19357 UniProtKB Topological domain 345 353 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 P19357 UniProtKB Transmembrane 354 374 . . . Note=Helical%3B Name%3D9;Ontology_term=ECO:0000255;evidence=ECO:0000255 P19357 UniProtKB Topological domain 375 384 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 P19357 UniProtKB Transmembrane 385 405 . . . Note=Helical%3B Name%3D10;Ontology_term=ECO:0000255;evidence=ECO:0000255 P19357 UniProtKB Topological domain 406 417 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 P19357 UniProtKB Transmembrane 418 438 . . . Note=Helical%3B Name%3D11;Ontology_term=ECO:0000255;evidence=ECO:0000255 P19357 UniProtKB Topological domain 439 445 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 P19357 UniProtKB Transmembrane 446 466 . . . Note=Helical%3B Name%3D12;Ontology_term=ECO:0000255;evidence=ECO:0000255 P19357 UniProtKB Topological domain 467 509 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 P19357 UniProtKB Region 7 13 . . . Note=Interaction with SRFBP1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P14672 P19357 UniProtKB Motif 489 490 . . . Note=Dileucine internalization motif;Ontology_term=ECO:0000255;evidence=ECO:0000255 P19357 UniProtKB Binding site 177 177 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11169 P19357 UniProtKB Binding site 298 299 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11169 P19357 UniProtKB Binding site 304 304 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11169 P19357 UniProtKB Binding site 333 333 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11169 P19357 UniProtKB Binding site 396 396 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11169 P19357 UniProtKB Binding site 404 404 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11169 P19357 UniProtKB Modified residue 10 10 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:22673903;Dbxref=PMID:22673903 P19357 UniProtKB Modified residue 274 274 . . . Note=Phosphoserine%3B by SGK1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P14672 P19357 UniProtKB Modified residue 486 486 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P14142 P19357 UniProtKB Modified residue 488 488 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:22673903;Dbxref=PMID:22673903 P19357 UniProtKB Lipidation 223 223 . . . Note=S-palmitoyl cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P14672 P19357 UniProtKB Glycosylation 57 57 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 P19357 UniProtKB Sequence conflict 349 349 . . . Note=R->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305