##gff-version 3
P43007	UniProtKB	Chain	1	532	.	.	.	ID=PRO_0000202079;Note=Neutral amino acid transporter A	
P43007	UniProtKB	Topological domain	1	41	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P43007	UniProtKB	Transmembrane	42	62	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P43007	UniProtKB	Transmembrane	88	108	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P43007	UniProtKB	Transmembrane	119	139	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P43007	UniProtKB	Topological domain	140	216	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P43007	UniProtKB	Transmembrane	217	237	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P43007	UniProtKB	Transmembrane	257	277	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P43007	UniProtKB	Transmembrane	298	318	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P43007	UniProtKB	Transmembrane	328	348	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P43007	UniProtKB	Transmembrane	373	393	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P43007	UniProtKB	Transmembrane	418	438	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P43007	UniProtKB	Region	1	25	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P43007	UniProtKB	Region	500	532	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P43007	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:22814378;Dbxref=PMID:22814378	
P43007	UniProtKB	Modified residue	507	507	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:18669648;Dbxref=PMID:18669648	
P43007	UniProtKB	Modified residue	527	527	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O35874	
P43007	UniProtKB	Modified residue	530	530	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O35874	
P43007	UniProtKB	Glycosylation	201	201	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19349973;Dbxref=PMID:19349973	
P43007	UniProtKB	Glycosylation	206	206	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19349973;Dbxref=PMID:19349973	
P43007	UniProtKB	Alternative sequence	1	220	.	.	.	ID=VSP_042880;Note=In isoform 2. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:14702039;Dbxref=PMID:14702039	
P43007	UniProtKB	Alternative sequence	267	345	.	.	.	ID=VSP_042881;Note=In isoform 2. WYVPVGIMFLVGSKIVEMKDIIVLVTSLGKYIFASILGHVIHGGIVLPLIYFVFTRKNPFRFLLGLLAPFATAFATCSS->C;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:14702039;Dbxref=PMID:14702039	
P43007	UniProtKB	Natural variant	37	37	.	.	.	ID=VAR_011878;Note=G->R;Dbxref=dbSNP:rs1064512	
P43007	UniProtKB	Natural variant	256	256	.	.	.	ID=VAR_075085;Note=In SPATCCM%3B does not affect localization at the cell surface%3B decreased uptake of L-serine and L-alanine%3B Vmax is decreased by at least 50%25 for both substrates%3B 3-fold increase of affinity for L-serine%3B 2-fold increase of affinity for L-alanine. E->K;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:25930971,ECO:0000269|PubMed:26041762,ECO:0000269|PubMed:26138499;Dbxref=dbSNP:rs201278558,PMID:25930971,PMID:26041762,PMID:26138499	
P43007	UniProtKB	Natural variant	399	399	.	.	.	ID=VAR_011879;Note=V->I;Dbxref=dbSNP:rs759458	
P43007	UniProtKB	Natural variant	457	457	.	.	.	ID=VAR_075086;Note=In SPATCCM%3B does not affect localization at the cell surface%3B loss of uptake of L-serine and L-alanine. R->W;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26041762;Dbxref=dbSNP:rs761533681,PMID:26041762	
P43007	UniProtKB	Sequence conflict	117	117	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P43007	UniProtKB	Sequence conflict	127	127	.	.	.	Note=S->T;Ontology_term=ECO:0000305;evidence=ECO:0000305