##gff-version 3 A2VE31 UniProtKB Chain 1 506 . . . ID=PRO_0000311368;Note=Sodium-coupled neutral amino acid symporter 2 A2VE31 UniProtKB Topological domain 1 76 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250|UniProtKB:Q9JHE5,ECO:0000255 A2VE31 UniProtKB Transmembrane 77 96 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 A2VE31 UniProtKB Topological domain 97 102 . . . Note=Extracellular;Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250|UniProtKB:Q9JHE5,ECO:0000255 A2VE31 UniProtKB Transmembrane 103 123 . . . Note=Helical;Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250|UniProtKB:Q9JHE5,ECO:0000255 A2VE31 UniProtKB Topological domain 124 158 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250|UniProtKB:Q9JHE5,ECO:0000255 A2VE31 UniProtKB Transmembrane 159 177 . . . Note=Helical;Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250|UniProtKB:Q9JHE5,ECO:0000255 A2VE31 UniProtKB Topological domain 178 188 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 A2VE31 UniProtKB Transmembrane 189 209 . . . Note=Helical;Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250|UniProtKB:Q9JHE5,ECO:0000255 A2VE31 UniProtKB Topological domain 210 217 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250|UniProtKB:Q9JHE5,ECO:0000255 A2VE31 UniProtKB Transmembrane 218 238 . . . Note=Helical;Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250|UniProtKB:Q9JHE5,ECO:0000255 A2VE31 UniProtKB Topological domain 239 292 . . . Note=Extracellular;Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250|UniProtKB:Q9JHE5,ECO:0000255 A2VE31 UniProtKB Transmembrane 293 313 . . . Note=Helical;Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250|UniProtKB:Q9JHE5,ECO:0000255 A2VE31 UniProtKB Topological domain 314 329 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250|UniProtKB:Q9JHE5,ECO:0000255 A2VE31 UniProtKB Transmembrane 330 350 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 A2VE31 UniProtKB Topological domain 351 371 . . . Note=Extracellular;Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250|UniProtKB:Q9JHE5,ECO:0000255 A2VE31 UniProtKB Transmembrane 372 392 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 A2VE31 UniProtKB Topological domain 393 413 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250|UniProtKB:Q9JHE5,ECO:0000255 A2VE31 UniProtKB Transmembrane 414 434 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 A2VE31 UniProtKB Topological domain 435 436 . . . Note=Extracellular;Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250|UniProtKB:Q9JHE5,ECO:0000255 A2VE31 UniProtKB Transmembrane 437 457 . . . Note=Helical;Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250|UniProtKB:Q9JHE5,ECO:0000255 A2VE31 UniProtKB Topological domain 458 472 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 A2VE31 UniProtKB Transmembrane 473 495 . . . Note=Helical;Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250|UniProtKB:Q9JHE5,ECO:0000255 A2VE31 UniProtKB Topological domain 496 506 . . . Note=Extracellular;Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250|UniProtKB:Q9JHE5,ECO:0000255 A2VE31 UniProtKB Region 1 96 . . . Note=Regulates protein turnover upon amino acid deprivation;Ontology_term=ECO:0000250;evidence=ECO:0000250 A2VE31 UniProtKB Region 1 23 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite A2VE31 UniProtKB Binding site 82 82 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9JHE5 A2VE31 UniProtKB Binding site 386 386 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9JHE5 A2VE31 UniProtKB Modified residue 12 12 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q96QD8 A2VE31 UniProtKB Modified residue 21 21 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8CFE6 A2VE31 UniProtKB Modified residue 22 22 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q96QD8 A2VE31 UniProtKB Modified residue 55 55 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q96QD8 A2VE31 UniProtKB Glycosylation 258 258 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 A2VE31 UniProtKB Glycosylation 274 274 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 A2VE31 UniProtKB Disulfide bond 245 281 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00114 A2VE31 UniProtKB Sequence conflict 409 409 . . . Note=S->N;Ontology_term=ECO:0000305;evidence=ECO:0000305