VPP1_YEAST
ID VPP1_YEAST Reviewed; 840 AA.
AC P32563; D6W2X0;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 213.
DE RecName: Full=V-type proton ATPase subunit a, vacuolar isoform;
DE Short=V-ATPase a 1 subunit;
DE AltName: Full=V-ATPase 95 kDa subunit;
DE AltName: Full=Vacuolar pH protein 1;
DE AltName: Full=Vacuolar proton pump a subunit;
DE AltName: Full=Vacuolar proton translocating ATPase subunit a 1;
GN Name=VPH1 {ECO:0000303|PubMed:1385813}; OrderedLocusNames=YOR270C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1385813; DOI=10.1016/s0021-9258(19)49711-1;
RA Manolson M.F., Proteau D., Preston R.A., Stenbit A., Roberts B.T.,
RA Hoyt M.A., Preuss D., Mulholland J., Botstein D., Jones E.W.;
RT "The VPH1 gene encodes a 95-kDa integral membrane polypeptide required for
RT in vivo assembly and activity of the yeast vacuolar H(+)-ATPase.";
RL J. Biol. Chem. 267:14294-14303(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8896271;
RX DOI=10.1002/(sici)1097-0061(199609)12:10b%3c1059::aid-yea994%3e3.0.co;2-7;
RA Cheret G., Bernardi A., Sor F.J.;
RT "DNA sequence analysis of the VPH1-SNF2 region on chromosome XV of
RT Saccharomyces cerevisiae.";
RL Yeast 12:1059-1064(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=9153759;
RX DOI=10.1002/(sici)1097-0061(199704)13:5<483::aid-yea105>3.0.co;2-u;
RA Poirey R., Jauniaux J.-C.;
RT "Sequencing analysis of a 36.8 kb fragment of yeast chromosome XV reveals
RT 26 open reading frames including SEC63, CDC31, SUG2, GCD1, RBL2, PNT1, PAC1
RT and VPH1.";
RL Yeast 13:483-487(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [6]
RP PROTEIN SEQUENCE OF 2-10, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT
RP ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RA Bienvenut W.V., Peters C.;
RL Submitted (JUN-2005) to UniProtKB.
RN [7]
RP FUNCTION, AND SUBUNIT.
RX PubMed=1491220; DOI=10.1242/jeb.172.1.105;
RA Manolson M.F., Proteau D., Jones E.W.;
RT "Evidence for a conserved 95-120 kDa subunit associated with and essential
RT for activity of V-ATPases.";
RL J. Exp. Biol. 172:105-112(1992).
RN [8]
RP FUNCTION, AND MUTAGENESIS OF ASP-425; LYS-538; LYS-593; GLN-634; ARG-735;
RP HIS-743 AND GLU-789.
RX PubMed=8798414; DOI=10.1074/jbc.271.37.22487;
RA Leng X.-H., Manolson M.F., Liu Q., Forgac M.;
RT "Site-directed mutagenesis of the 100-kDa subunit (Vph1p) of the yeast
RT vacuolar (H+)-ATPase.";
RL J. Biol. Chem. 271:22487-22493(1996).
RN [9]
RP ERRATUM OF PUBMED:8798414.
RA Leng X.-H., Manolson M.F., Liu Q., Forgac M.;
RL J. Biol. Chem. 271:28725-28725(1996).
RN [10]
RP MUTAGENESIS OF HIS-729; LEU-739; HIS-743; LEU-746; LEU-780; GLU-789;
RP LEU-800; TRP-802; VAL-803; PHE-809 AND GLY-814.
RX PubMed=9506970; DOI=10.1074/jbc.273.12.6717;
RA Leng X.-H., Manolson M.F., Forgac M.;
RT "Function of the COOH-terminal domain of Vph1p in activity and assembly of
RT the yeast V-ATPase.";
RL J. Biol. Chem. 273:6717-6723(1998).
RN [11]
RP TOPOLOGY.
RX PubMed=10329659; DOI=10.1074/jbc.274.21.14655;
RA Leng X.-H., Nishi T., Forgac M.;
RT "Transmembrane topography of the 100-kDa a subunit (Vph1p) of the yeast
RT vacuolar proton-translocating ATPase.";
RL J. Biol. Chem. 274:14655-14661(1999).
RN [12]
RP TOPOLOGY.
RX PubMed=10473553; DOI=10.1074/jbc.274.37.26057;
RA Landolt-Marticorena C., Kahr W.H., Zawarinski P., Correa J., Manolson M.F.;
RT "Substrate- and inhibitor-induced conformational changes in the yeast V-
RT ATPase provide evidence for communication between the catalytic and proton-
RT translocating sectors.";
RL J. Biol. Chem. 274:26057-26064(1999).
RN [13]
RP FUNCTION.
RX PubMed=11278748; DOI=10.1074/jbc.m010790200;
RA Kawasaki-Nishi S., Nishi T., Forgac M.;
RT "Yeast V-ATPase complexes containing different isoforms of the 100-kDa a-
RT subunit differ in coupling efficiency and in vivo dissociation.";
RL J. Biol. Chem. 276:17941-17948(2001).
RN [14]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [15]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [16]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA Kim H., Melen K., Oesterberg M., von Heijne G.;
RT "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [18]
RP TOPOLOGY.
RX PubMed=21832060; DOI=10.1074/jbc.m111.273409;
RA Toei M., Toei S., Forgac M.;
RT "Definition of membrane topology and identification of residues important
RT for transport in subunit a of the vacuolar ATPase.";
RL J. Biol. Chem. 286:35176-35186(2011).
RN [19]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [20] {ECO:0007744|PDB:3J9T, ECO:0007744|PDB:3J9U, ECO:0007744|PDB:3J9V}
RP STRUCTURE BY ELECTRON MICROSCOPY (6.90 ANGSTROMS), AND IDENTIFICATION IN
RP THE V-ATPASE COMPLEX.
RX PubMed=25971514; DOI=10.1038/nature14365;
RA Zhao J., Benlekbir S., Rubinstein J.L.;
RT "Electron cryomicroscopy observation of rotational states in a eukaryotic
RT V-ATPase.";
RL Nature 521:241-245(2015).
RN [21] {ECO:0007744|PDB:5TJ5}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.90 ANGSTROMS) OF 400-829, AND
RP IDENTIFICATION IN THE V-ATPASE COMPLEX.
RX PubMed=27776355; DOI=10.1038/nature19828;
RA Mazhab-Jafari M.T., Rohou A., Schmidt C., Bueler S.A., Benlekbir S.,
RA Robinson C.V., Rubinstein J.L.;
RT "Atomic model for the membrane-embedded VO motor of a eukaryotic V-
RT ATPase.";
RL Nature 539:118-122(2016).
RN [22] {ECO:0007744|PDB:6C6L}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS), AND IDENTIFICATION IN
RP THE V-ATPASE COMPLEX.
RX PubMed=29526695; DOI=10.1016/j.molcel.2018.02.006;
RA Roh S.H., Stam N.J., Hryc C.F., Couoh-Cardel S., Pintilie G., Chiu W.,
RA Wilkens S.;
RT "The 3.5-A CryoEM Structure of Nanodisc-Reconstituted Yeast Vacuolar ATPase
RT Vo Proton Channel.";
RL Mol. Cell 69:993-1004.e3(2018).
CC -!- FUNCTION: Subunit of the V0 complex of vacuolar(H+)-ATPase (V-ATPase),
CC a multisubunit enzyme composed of a peripheral complex (V1) that
CC hydrolyzes ATP and a membrane integral complex (V0) that translocates
CC protons (PubMed:1491220, PubMed:8798414, PubMed:11278748). V-ATPase is
CC responsible for acidifying and maintaining the pH of intracellular
CC compartments (PubMed:1491220, PubMed:11278748). Is present only in
CC vacuolar V-ATPase complexes; enzymes containing this subunit have a 4-
CC fold higher ratio of proton transport to ATP hydrolysis than complexes
CC containing the Golgi/endosomal isoform and undergo reversible
CC dissociation of V1 and V0 in response to glucose depletion
CC (PubMed:8798414, PubMed:11278748). {ECO:0000269|PubMed:11278748,
CC ECO:0000269|PubMed:1491220, ECO:0000269|PubMed:8798414}.
CC -!- SUBUNIT: V-ATPase is a heteromultimeric enzyme composed of a peripheral
CC catalytic V1 complex (components A to H) attached to an integral
CC membrane V0 proton pore complex (components: a, c, c', c'', d, e, f and
CC VOA1). {ECO:0000269|PubMed:1491220, ECO:0000269|PubMed:25971514,
CC ECO:0000269|PubMed:27776355, ECO:0000269|PubMed:29526695}.
CC -!- INTERACTION:
CC P32563; P41807: VMA13; NbExp=3; IntAct=EBI-20455, EBI-20281;
CC P32563; P32366: VMA6; NbExp=12; IntAct=EBI-20455, EBI-20201;
CC P32563; P39111: VMA7; NbExp=5; IntAct=EBI-20455, EBI-20272;
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:14562095};
CC Multi-pass membrane protein {ECO:0000269|PubMed:14562095}.
CC -!- PTM: Glycosylated.
CC -!- MISCELLANEOUS: Present with 55714 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the V-ATPase 116 kDa subunit family.
CC {ECO:0000305}.
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DR EMBL; M89778; AAA35211.1; -; Genomic_DNA.
DR EMBL; X89633; CAA61776.1; -; Genomic_DNA.
DR EMBL; Z75178; CAA99494.1; -; Genomic_DNA.
DR EMBL; Z75179; CAA99496.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA11036.1; -; Genomic_DNA.
DR PIR; A42970; A42970.
DR RefSeq; NP_014913.3; NM_001183689.3.
DR PDB; 2JTW; NMR; -; A=728-748.
DR PDB; 2NVJ; NMR; -; A=721-745.
DR PDB; 2RPW; NMR; -; X=728-748.
DR PDB; 3J9T; EM; 6.90 A; b=1-840.
DR PDB; 3J9U; EM; 7.60 A; b=1-840.
DR PDB; 3J9V; EM; 8.30 A; b=1-840.
DR PDB; 5I1M; EM; 7.00 A; V=383-840.
DR PDB; 5TJ5; EM; 3.90 A; A=400-829.
DR PDB; 5VOX; EM; 6.80 A; b=1-840.
DR PDB; 5VOY; EM; 7.90 A; b=1-840.
DR PDB; 5VOZ; EM; 7.60 A; b=1-840.
DR PDB; 6C6L; EM; 3.50 A; A=1-840.
DR PDB; 6HH0; NMR; -; A=728-748.
DR PDB; 6M0R; EM; 2.70 A; A=3-827.
DR PDB; 6M0S; EM; 3.60 A; A=3-827.
DR PDB; 6O7T; EM; 3.20 A; a=1-840.
DR PDB; 6PE4; EM; 3.10 A; A=1-840.
DR PDB; 6PE5; EM; 3.20 A; A=1-840.
DR PDB; 7FDA; EM; 4.20 A; Q=1-840.
DR PDB; 7FDB; EM; 4.80 A; Q=1-840.
DR PDB; 7FDC; EM; 6.60 A; Q=1-840.
DR PDB; 7TAO; EM; 3.20 A; A=1-840.
DR PDB; 7TAP; EM; 2.80 A; A=1-840.
DR PDB; 7TMR; EM; 3.50 A; a=1-840.
DR PDB; 7TMS; EM; 3.80 A; a=1-840.
DR PDBsum; 2JTW; -.
DR PDBsum; 2NVJ; -.
DR PDBsum; 2RPW; -.
DR PDBsum; 3J9T; -.
DR PDBsum; 3J9U; -.
DR PDBsum; 3J9V; -.
DR PDBsum; 5I1M; -.
DR PDBsum; 5TJ5; -.
DR PDBsum; 5VOX; -.
DR PDBsum; 5VOY; -.
DR PDBsum; 5VOZ; -.
DR PDBsum; 6C6L; -.
DR PDBsum; 6HH0; -.
DR PDBsum; 6M0R; -.
DR PDBsum; 6M0S; -.
DR PDBsum; 6O7T; -.
DR PDBsum; 6PE4; -.
DR PDBsum; 6PE5; -.
DR PDBsum; 7FDA; -.
DR PDBsum; 7FDB; -.
DR PDBsum; 7FDC; -.
DR PDBsum; 7TAO; -.
DR PDBsum; 7TAP; -.
DR PDBsum; 7TMR; -.
DR PDBsum; 7TMS; -.
DR AlphaFoldDB; P32563; -.
DR BMRB; P32563; -.
DR SMR; P32563; -.
DR BioGRID; 34659; 371.
DR ComplexPortal; CPX-1193; Vacuolar proton translocating ATPase complex, vacuole variant.
DR DIP; DIP-2960N; -.
DR IntAct; P32563; 35.
DR MINT; P32563; -.
DR STRING; 4932.YOR270C; -.
DR TCDB; 3.A.2.2.3; the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
DR iPTMnet; P32563; -.
DR MaxQB; P32563; -.
DR PaxDb; P32563; -.
DR PRIDE; P32563; -.
DR EnsemblFungi; YOR270C_mRNA; YOR270C; YOR270C.
DR GeneID; 854444; -.
DR KEGG; sce:YOR270C; -.
DR SGD; S000005796; VPH1.
DR VEuPathDB; FungiDB:YOR270C; -.
DR eggNOG; KOG2189; Eukaryota.
DR GeneTree; ENSGT00950000182881; -.
DR HOGENOM; CLU_005230_0_2_1; -.
DR InParanoid; P32563; -.
DR OMA; FSYDRAR; -.
DR BioCyc; YEAST:G3O-33760-MON; -.
DR Reactome; R-SCE-1222556; ROS and RNS production in phagocytes.
DR Reactome; R-SCE-6798695; Neutrophil degranulation.
DR Reactome; R-SCE-77387; Insulin receptor recycling.
DR Reactome; R-SCE-917977; Transferrin endocytosis and recycling.
DR Reactome; R-SCE-9639288; Amino acids regulate mTORC1.
DR EvolutionaryTrace; P32563; -.
DR PRO; PR:P32563; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P32563; protein.
DR GO; GO:0000324; C:fungal-type vacuole; IDA:SGD.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:ComplexPortal.
DR GO; GO:0016471; C:vacuolar proton-transporting V-type ATPase complex; IPI:ComplexPortal.
DR GO; GO:0000220; C:vacuolar proton-transporting V-type ATPase, V0 domain; IDA:UniProtKB.
DR GO; GO:0051117; F:ATPase binding; IBA:GO_Central.
DR GO; GO:0080025; F:phosphatidylinositol-3,5-bisphosphate binding; IDA:SGD.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IMP:UniProtKB.
DR GO; GO:0071474; P:cellular hyperosmotic response; IGI:SGD.
DR GO; GO:0071469; P:cellular response to alkaline pH; IGI:UniProtKB.
DR GO; GO:0006797; P:polyphosphate metabolic process; IMP:SGD.
DR GO; GO:0065003; P:protein-containing complex assembly; IMP:SGD.
DR GO; GO:1902600; P:proton transmembrane transport; IDA:FlyBase.
DR GO; GO:0007035; P:vacuolar acidification; IMP:SGD.
DR InterPro; IPR002490; V-ATPase_116kDa_su.
DR InterPro; IPR026028; V-type_ATPase_116kDa_su_euka.
DR PANTHER; PTHR11629; PTHR11629; 1.
DR Pfam; PF01496; V_ATPase_I; 1.
DR PIRSF; PIRSF001293; ATP6V0A1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Coiled coil; Direct protein sequencing;
KW Glycoprotein; Hydrogen ion transport; Ion transport; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport; Vacuole.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.6, ECO:0007744|PubMed:22814378"
FT CHAIN 2..840
FT /note="V-type proton ATPase subunit a, vacuolar isoform"
FT /id="PRO_0000119224"
FT TOPO_DOM 2..404
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 405..423
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 424..425
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 426..442
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 443..456
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 457..486
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 487..534
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 535..554
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 555..572
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 573..593
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 594..636
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 637..656
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 657..719
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 720..744
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 745..765
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 766..804
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 805..840
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT COILED 117..145
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.6, ECO:0007744|PubMed:22814378"
FT MUTAGEN 425
FT /note="D->N: Reduces assembly of V-ATPase complexes and
FT reduces ATPase activity of the assembled complexes."
FT /evidence="ECO:0000269|PubMed:8798414"
FT MUTAGEN 538
FT /note="K->A: Reduces assembly of V-ATPase complexes."
FT /evidence="ECO:0000269|PubMed:8798414"
FT MUTAGEN 593
FT /note="K->A: Reduces ATPase activity."
FT /evidence="ECO:0000269|PubMed:8798414"
FT MUTAGEN 634
FT /note="Q->L: Reduces subunit stability."
FT /evidence="ECO:0000269|PubMed:8798414"
FT MUTAGEN 729
FT /note="H->R: Reduces ATPase activity."
FT /evidence="ECO:0000269|PubMed:9506970"
FT MUTAGEN 735
FT /note="R->L: Reduces subunit stability."
FT /evidence="ECO:0000269|PubMed:8798414"
FT MUTAGEN 739
FT /note="L->S: Reduces ATPase activity."
FT /evidence="ECO:0000269|PubMed:9506970"
FT MUTAGEN 743
FT /note="H->A,E,Y: Reduces ATPase activity."
FT /evidence="ECO:0000269|PubMed:8798414,
FT ECO:0000269|PubMed:9506970"
FT MUTAGEN 746
FT /note="L->S: Reduces ATPase activity."
FT /evidence="ECO:0000269|PubMed:9506970"
FT MUTAGEN 780
FT /note="L->S: Reduces assembly of V-ATPase complexes."
FT /evidence="ECO:0000269|PubMed:9506970"
FT MUTAGEN 789
FT /note="E->A,D,H,Q: Abolishes ATPase activity and proton
FT transport, but does not affect complex assembly."
FT /evidence="ECO:0000269|PubMed:8798414,
FT ECO:0000269|PubMed:9506970"
FT MUTAGEN 800
FT /note="L->S: Reduces assembly of V-ATPase complexes."
FT /evidence="ECO:0000269|PubMed:9506970"
FT MUTAGEN 802
FT /note="W->R: Reduces assembly of V-ATPase complexes."
FT /evidence="ECO:0000269|PubMed:9506970"
FT MUTAGEN 803
FT /note="V->D: Reduces ATPase activity."
FT /evidence="ECO:0000269|PubMed:9506970"
FT MUTAGEN 803
FT /note="V->F: Reduces assembly of V-ATPase complexes."
FT /evidence="ECO:0000269|PubMed:9506970"
FT MUTAGEN 809
FT /note="F->L: Reduces assembly of V-ATPase complexes."
FT /evidence="ECO:0000269|PubMed:9506970"
FT MUTAGEN 814
FT /note="G->D: Reduces assembly of V-ATPase complexes."
FT /evidence="ECO:0000269|PubMed:9506970"
FT STRAND 8..10
FT /evidence="ECO:0007829|PDB:6M0R"
FT STRAND 14..21
FT /evidence="ECO:0007829|PDB:6M0R"
FT STRAND 23..25
FT /evidence="ECO:0007829|PDB:6M0R"
FT HELIX 26..36
FT /evidence="ECO:0007829|PDB:6M0R"
FT STRAND 39..41
FT /evidence="ECO:0007829|PDB:6PE5"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:6O7T"
FT TURN 50..52
FT /evidence="ECO:0007829|PDB:6M0R"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:6PE4"
FT HELIX 56..78
FT /evidence="ECO:0007829|PDB:6M0R"
FT STRAND 91..94
FT /evidence="ECO:0007829|PDB:6PE4"
FT STRAND 95..98
FT /evidence="ECO:0007829|PDB:6O7T"
FT HELIX 104..146
FT /evidence="ECO:0007829|PDB:6M0R"
FT HELIX 150..152
FT /evidence="ECO:0007829|PDB:6M0R"
FT STRAND 186..192
FT /evidence="ECO:0007829|PDB:6M0R"
FT HELIX 193..195
FT /evidence="ECO:0007829|PDB:6M0R"
FT HELIX 196..206
FT /evidence="ECO:0007829|PDB:6M0R"
FT TURN 207..209
FT /evidence="ECO:0007829|PDB:6M0R"
FT STRAND 213..217
FT /evidence="ECO:0007829|PDB:6M0R"
FT STRAND 225..227
FT /evidence="ECO:0007829|PDB:6M0R"
FT STRAND 233..239
FT /evidence="ECO:0007829|PDB:6M0R"
FT HELIX 243..255
FT /evidence="ECO:0007829|PDB:6M0R"
FT STRAND 259..261
FT /evidence="ECO:0007829|PDB:6PE4"
FT HELIX 267..302
FT /evidence="ECO:0007829|PDB:6M0R"
FT TURN 304..307
FT /evidence="ECO:0007829|PDB:6O7T"
FT HELIX 309..324
FT /evidence="ECO:0007829|PDB:6M0R"
FT STRAND 326..328
FT /evidence="ECO:0007829|PDB:6M0R"
FT STRAND 330..333
FT /evidence="ECO:0007829|PDB:6M0R"
FT STRAND 335..342
FT /evidence="ECO:0007829|PDB:6M0R"
FT HELIX 343..345
FT /evidence="ECO:0007829|PDB:6M0R"
FT HELIX 347..360
FT /evidence="ECO:0007829|PDB:6M0R"
FT STRAND 368..371
FT /evidence="ECO:0007829|PDB:6M0R"
FT TURN 385..387
FT /evidence="ECO:0007829|PDB:6M0R"
FT HELIX 388..397
FT /evidence="ECO:0007829|PDB:6M0R"
FT TURN 408..410
FT /evidence="ECO:0007829|PDB:6M0R"
FT HELIX 411..423
FT /evidence="ECO:0007829|PDB:6M0R"
FT HELIX 426..441
FT /evidence="ECO:0007829|PDB:6M0R"
FT HELIX 443..448
FT /evidence="ECO:0007829|PDB:6M0R"
FT HELIX 454..460
FT /evidence="ECO:0007829|PDB:6M0R"
FT TURN 461..463
FT /evidence="ECO:0007829|PDB:6M0R"
FT HELIX 464..479
FT /evidence="ECO:0007829|PDB:6M0R"
FT STRAND 482..484
FT /evidence="ECO:0007829|PDB:6C6L"
FT STRAND 493..495
FT /evidence="ECO:0007829|PDB:6M0R"
FT STRAND 515..518
FT /evidence="ECO:0007829|PDB:6M0R"
FT HELIX 520..522
FT /evidence="ECO:0007829|PDB:6M0R"
FT TURN 525..527
FT /evidence="ECO:0007829|PDB:6PE4"
FT HELIX 528..562
FT /evidence="ECO:0007829|PDB:6M0R"
FT HELIX 565..570
FT /evidence="ECO:0007829|PDB:6M0R"
FT HELIX 572..594
FT /evidence="ECO:0007829|PDB:6M0R"
FT HELIX 598..601
FT /evidence="ECO:0007829|PDB:6M0R"
FT HELIX 608..617
FT /evidence="ECO:0007829|PDB:6M0R"
FT STRAND 618..620
FT /evidence="ECO:0007829|PDB:6C6L"
FT STRAND 626..629
FT /evidence="ECO:0007829|PDB:6O7T"
FT HELIX 630..658
FT /evidence="ECO:0007829|PDB:6M0R"
FT HELIX 707..732
FT /evidence="ECO:0007829|PDB:6M0R"
FT HELIX 735..758
FT /evidence="ECO:0007829|PDB:6M0R"
FT HELIX 764..784
FT /evidence="ECO:0007829|PDB:6M0R"
FT HELIX 787..802
FT /evidence="ECO:0007829|PDB:6M0R"
FT TURN 803..805
FT /evidence="ECO:0007829|PDB:6M0R"
FT HELIX 806..808
FT /evidence="ECO:0007829|PDB:6M0R"
FT HELIX 828..831
FT /evidence="ECO:0007829|PDB:6PE4"
FT TURN 832..834
FT /evidence="ECO:0007829|PDB:6PE4"
SQ SEQUENCE 840 AA; 95529 MW; 77709A914410CD4D CRC64;
MAEKEEAIFR SAEMALVQFY IPQEISRDSA YTLGQLGLVQ FRDLNSKVRA FQRTFVNEIR
RLDNVERQYR YFYSLLKKHD IKLYEGDTDK YLDGSGELYV PPSGSVIDDY VRNASYLEER
LIQMEDATDQ IEVQKNDLEQ YRFILQSGDE FFLKGDNTDS TSYMDEDMID ANGENIAAAI
GASVNYVTGV IARDKVATLE QILWRVLRGN LFFKTVEIEQ PVYDVKTREY KHKNAFIVFS
HGDLIIKRIR KIAESLDANL YDVDSSNEGR SQQLAKVNKN LSDLYTVLKT TSTTLESELY
AIAKELDSWF QDVTREKAIF EILNKSNYDT NRKILIAEGW IPRDELATLQ ARLGEMIARL
GIDVPSIIQV LDTNHTPPTF HRTNKFTAGF QSICDCYGIA QYREINAGLP TIVTFPFMFA
IMFGDMGHGF LMTLAALSLV LNEKKINKMK RGEIFDMAFT GRYIILLMGV FSMYTGFLYN
DIFSKTMTIF KSGWKWPDHW KKGESITATS VGTYPIGLDW AWHGTENALL FSNSYKMKLS
ILMGFIHMTY SYFFSLANHL YFNSMIDIIG NFIPGLLFMQ GIFGYLSVCI VYKWAVDWVK
DGKPAPGLLN MLINMFLSPG TIDDELYPHQ AKVQVFLLLM ALVCIPWLLL VKPLHFKFTH
KKKSHEPLPS TEADASSEDL EAQQLISAMD ADDAEEEEVG SGSHGEDFGD IMIHQVIHTI
EFCLNCVSHT ASYLRLWALS LAHAQLSSVL WTMTIQIAFG FRGFVGVFMT VALFAMWFAL
TCAVLVLMEG TSAMLHSLRL HWVESMSKFF VGEGLPYEPF AFEYKDMEVA VASASSSASS
