##gff-version 3 Q9Y487 UniProtKB Chain 1 856 . . . ID=PRO_0000119216;Note=V-type proton ATPase 116 kDa subunit a 2 Q9Y487 UniProtKB Topological domain 1 393 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q9Y487 UniProtKB Transmembrane 394 412 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q9Y487 UniProtKB Topological domain 413 414 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q9Y487 UniProtKB Transmembrane 415 431 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q9Y487 UniProtKB Topological domain 432 445 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q9Y487 UniProtKB Transmembrane 446 475 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q9Y487 UniProtKB Topological domain 476 549 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q9Y487 UniProtKB Transmembrane 550 569 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q9Y487 UniProtKB Topological domain 570 587 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q9Y487 UniProtKB Transmembrane 588 608 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q9Y487 UniProtKB Topological domain 609 651 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q9Y487 UniProtKB Transmembrane 652 671 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q9Y487 UniProtKB Topological domain 672 739 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q9Y487 UniProtKB Transmembrane 740 764 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q9Y487 UniProtKB Topological domain 765 785 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q9Y487 UniProtKB Transmembrane 786 824 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q9Y487 UniProtKB Topological domain 825 856 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q9Y487 UniProtKB Modified residue 695 695 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:17525332,ECO:0007744|PubMed:23186163;Dbxref=PMID:17525332,PMID:23186163 Q9Y487 UniProtKB Modified residue 700 700 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P15920 Q9Y487 UniProtKB Glycosylation 484 484 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q9Y487 UniProtKB Glycosylation 505 505 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q9Y487 UniProtKB Natural variant 685 685 . . . ID=VAR_042730;Note=R->Q;Dbxref=dbSNP:rs7969410 Q9Y487 UniProtKB Natural variant 813 813 . . . ID=VAR_042731;Note=A->V;Dbxref=dbSNP:rs17883456 Q9Y487 UniProtKB Sequence conflict 428 428 . . . Note=L->W;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9Y487 UniProtKB Sequence conflict 669 669 . . . Note=L->P;Ontology_term=ECO:0000305;evidence=ECO:0000305