AVP1_ARATH
ID AVP1_ARATH Reviewed; 770 AA.
AC P31414; O80390; Q41919; Q41920; Q56WP6; Q8RY20; Q8VZE3;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Pyrophosphate-energized vacuolar membrane proton pump 1;
DE EC=7.1.3.1;
DE AltName: Full=Pyrophosphate-energized inorganic pyrophosphatase 1;
DE Short=H(+)-PPase 1;
DE AltName: Full=Vacuolar proton pyrophosphatase 1;
DE AltName: Full=Vacuolar proton pyrophosphatase 3;
GN Name=AVP1; Synonyms=AVP, AVP-3, AVP3; OrderedLocusNames=At1g15690;
GN ORFNames=F7H2.3;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=1311852; DOI=10.1073/pnas.89.5.1775;
RA Sarafian V., Kim Y., Poole R.J., Rea P.A.;
RT "Molecular cloning and sequence of cDNA encoding the pyrophosphate-
RT energized vacuolar membrane proton pump of Arabidopsis thaliana.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:1775-1779(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, INDUCTION, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=cv. Columbia; TISSUE=Leaf;
RX PubMed=11442058; DOI=10.1023/a:1010681129557;
RA Mitsuda N., Takeyasu K., Sato M.H.;
RT "Pollen-specific regulation of vacuolar H(+)-PPase expression by multiple
RT cis-acting elements.";
RL Plant Mol. Biol. 46:185-192(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 554-671 AND 716-770.
RC STRAIN=cv. Columbia; TISSUE=Green siliques;
RX PubMed=8281187; DOI=10.1046/j.1365-313x.1993.04061051.x;
RA Hoefte H., Desprez T., Amselem J., Chiapello H., Rouze P., Caboche M.,
RA Moisan A., Jourjon M.-F., Charpenteau J.-L., Berthomieu P., Guerrier D.,
RA Giraudat J., Quigley F., Thomas F., Yu D.-Y., Mache R., Raynal M.,
RA Cooke R., Grellet F., Delseny M., Parmentier Y., de Marcillac G., Gigot C.,
RA Fleck J., Philipps G., Axelos M., Bardet C., Tremousaygue D., Lescure B.;
RT "An inventory of 1152 expressed sequence tags obtained by partial
RT sequencing of cDNAs from Arabidopsis thaliana.";
RL Plant J. 4:1051-1061(1993).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 595-770.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP PROTEIN SEQUENCE OF 625-640, AND ACTIVITY REGULATION.
RX PubMed=8083239; DOI=10.1016/s0021-9258(17)31659-9;
RA Zhen R.-G., Kim E.J., Rea P.A.;
RT "Localization of cytosolically oriented maleimide-reactive domain of
RT vacuolar H(+)-pyrophosphatase.";
RL J. Biol. Chem. 269:23342-23350(1994).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND ACTIVITY REGULATION.
RX PubMed=8016125; DOI=10.1073/pnas.91.13.6128;
RA Kim E.J., Zhen R.-G., Rea P.A.;
RT "Heterologous expression of plant vacuolar pyrophosphatase in yeast
RT demonstrates sufficiency of the substrate-binding subunit for proton
RT transport.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:6128-6132(1994).
RN [10]
RP MUTAGENESIS OF CYS-634, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=7852329; DOI=10.1074/jbc.270.6.2630;
RA Kim E.J., Zhen R.-G., Rea P.A.;
RT "Site-directed mutagenesis of vacuolar H(+)-pyrophosphatase. Necessity of
RT Cys634 for inhibition by maleimides but not catalysis.";
RL J. Biol. Chem. 270:2630-2635(1995).
RN [11]
RP ACTIVITY REGULATION, AND MUTAGENESIS OF GLU-119; GLU-229; GLU-305; GLU-427;
RP ASP-504; ASP-573; GLU-667 AND GLU-751.
RX PubMed=9268385; DOI=10.1074/jbc.272.35.22340;
RA Zhen R.-G., Kim E.J., Rea P.A.;
RT "Acidic residues necessary for pyrophosphate-energized pumping and
RT inhibition of the vacuolar H(+)-pyrophosphatase by N,N'-
RT dicyclohexylcarbodiimide.";
RL J. Biol. Chem. 272:22340-22348(1997).
RN [12]
RP ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=cv. Columbia;
RX PubMed=10806252; DOI=10.1104/pp.123.1.353;
RA Drozdowicz Y.M., Kissinger J.C., Rea P.A.;
RT "AVP2, a sequence-divergent, K(+)-insensitive H(+)-translocating inorganic
RT pyrophosphatase from Arabidopsis.";
RL Plant Physiol. 123:353-362(2000).
RN [13]
RP FUNCTION.
RX PubMed=11572991; DOI=10.1073/pnas.191389398;
RA Gaxiola R.A., Li J., Undurraga S., Dang L.M., Allen G.J., Alper S.L.,
RA Fink G.R.;
RT "Drought- and salt-tolerant plants result from overexpression of the AVP1
RT H(+)-pump.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:11444-11449(2001).
RN [14]
RP INDUCTION.
RX PubMed=14581622; DOI=10.1093/pcp/pcg137;
RA Mitsuda N., Isono T., Sato M.H.;
RT "Arabidopsis CAMTA family proteins enhance V-PPase expression in pollen.";
RL Plant Cell Physiol. 44:975-981(2003).
RN [15]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=16210544; DOI=10.1126/science.1115711;
RA Li J., Yang H., Peer W.A., Richter G., Blakeslee J., Bandyopadhyay A.,
RA Titapiwantakun B., Undurraga S., Khodakovskaya M., Richards E.L.,
RA Krizek B., Murphy A.S., Gilroy S., Gaxiola R.;
RT "Arabidopsis H(+)-PPase AVP1 regulates auxin-mediated organ development.";
RL Science 310:121-125(2005).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=17151019; DOI=10.1074/mcp.m600250-mcp200;
RA Jaquinod M., Villiers F., Kieffer-Jaquinod S., Hugouvieux V., Bruley C.,
RA Garin J., Bourguignon J.;
RT "A proteomics dissection of Arabidopsis thaliana vacuoles isolated from
RT cell culture.";
RL Mol. Cell. Proteomics 6:394-412(2007).
CC -!- FUNCTION: Contributes to the transtonoplast (from cytosol to vacuole
CC lumen) H(+)-electrochemical potential difference. It establishes a
CC proton gradient of similar and often greater magnitude than the H(+)-
CC ATPase on the same membrane. In addition, facilitates auxin transport
CC by modulating apoplastic pH and regulates auxin-mediated developmental
CC processes. Confers tolerance to NaCl and to drought by increasing ion
CC retention. {ECO:0000269|PubMed:11572991, ECO:0000269|PubMed:16210544,
CC ECO:0000269|PubMed:8016125}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=diphosphate + H(+)(in) + H2O = 2 H(+)(out) + 2 phosphate;
CC Xref=Rhea:RHEA:13973, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:43474; EC=7.1.3.1;
CC -!- ACTIVITY REGULATION: Activated by K(+) and Mg(2+). Inhibited by Ca(2+),
CC N,N'-dicyclohexylcarbodiimide (DCCD), N-ethylmaleimide (NEM) and
CC aminomethylenediphosphonate (AMDP), and, to a lower extent, by fluoride
CC (KF). {ECO:0000269|PubMed:10806252, ECO:0000269|PubMed:8016125,
CC ECO:0000269|PubMed:8083239, ECO:0000269|PubMed:9268385}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=110 uM for PPi (at pH 8 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:10806252, ECO:0000269|PubMed:7852329};
CC Vmax=0.5 umol/min/mg enzyme (at pH 8 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:10806252, ECO:0000269|PubMed:7852329};
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:17151019};
CC Multi-pass membrane protein {ECO:0000255}. Endosome membrane; Multi-
CC pass membrane protein. Cell membrane; Multi-pass membrane protein.
CC Note=Mostly vacuolar, tonoplast. Also present in endosomes and plasma
CC membrane.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=P31414-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Ubiquitous (at protein level). Mostly expressed in
CC vascular tissues, meristems and root pericycle.
CC {ECO:0000269|PubMed:11442058, ECO:0000269|PubMed:16210544}.
CC -!- DEVELOPMENTAL STAGE: Increase of expression in pollen during flower
CC development. Expressed in developing leaves, sepals, petals, stamens
CC and carpels. {ECO:0000269|PubMed:11442058,
CC ECO:0000269|PubMed:16210544}.
CC -!- INDUCTION: Repressed by light. Induced by CAMTA1 and/or CAMTA5 in
CC pollen. {ECO:0000269|PubMed:11442058, ECO:0000269|PubMed:14581622}.
CC -!- DOMAIN: Has 16 transmembrane helices and a cytoplasmic domain that
CC contains the active site. {ECO:0000250}.
CC -!- MISCELLANEOUS: Has few direct interactions with pyrophosphate.
CC Interacts with the substrate via divalent metal cations, such as
CC magnesium ions, that are bound to the pyrophosphate (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the H(+)-translocating pyrophosphatase (TC
CC 3.A.10) family. K(+)-stimulated subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD94555.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA79039.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; M81892; AAA32754.1; -; mRNA.
DR EMBL; AB015138; BAA32210.1; -; Genomic_DNA.
DR EMBL; AC034256; AAF82139.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29349.1; -; Genomic_DNA.
DR EMBL; AY065016; AAL57660.1; -; mRNA.
DR EMBL; AY078953; AAL84953.1; -; mRNA.
DR EMBL; BT002481; AAO00841.1; -; mRNA.
DR EMBL; Z17694; CAA79038.1; -; mRNA.
DR EMBL; Z17695; CAA79039.1; ALT_FRAME; mRNA.
DR EMBL; AK221989; BAD94555.1; ALT_INIT; mRNA.
DR PIR; A38230; A38230.
DR RefSeq; NP_173021.1; NM_101437.5. [P31414-1]
DR AlphaFoldDB; P31414; -.
DR SMR; P31414; -.
DR BioGRID; 23378; 13.
DR IntAct; P31414; 10.
DR STRING; 3702.AT1G15690.1; -.
DR TCDB; 3.A.10.1.1; the h(+), na(+)-translocating pyrophosphatase (m(+)-ppase) family.
DR iPTMnet; P31414; -.
DR SwissPalm; P31414; -.
DR PaxDb; P31414; -.
DR PRIDE; P31414; -.
DR ProteomicsDB; 241153; -. [P31414-1]
DR EnsemblPlants; AT1G15690.1; AT1G15690.1; AT1G15690. [P31414-1]
DR GeneID; 838138; -.
DR Gramene; AT1G15690.1; AT1G15690.1; AT1G15690. [P31414-1]
DR KEGG; ath:AT1G15690; -.
DR Araport; AT1G15690; -.
DR TAIR; locus:2036134; AT1G15690.
DR eggNOG; ENOG502QPJC; Eukaryota.
DR HOGENOM; CLU_008743_3_0_1; -.
DR InParanoid; P31414; -.
DR OMA; DITRMCK; -.
DR PhylomeDB; P31414; -.
DR BioCyc; ARA:AT1G15690-MON; -.
DR BioCyc; MetaCyc:AT1G15690-MON; -.
DR BRENDA; 7.1.3.1; 399.
DR SABIO-RK; P31414; -.
DR PRO; PR:P31414; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; P31414; baseline and differential.
DR Genevisible; P31414; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0010008; C:endosome membrane; IDA:TAIR.
DR GO; GO:0005576; C:extracellular region; HDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0009705; C:plant-type vacuole membrane; IDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0005774; C:vacuolar membrane; HDA:TAIR.
DR GO; GO:0005773; C:vacuole; HDA:TAIR.
DR GO; GO:0004427; F:inorganic diphosphatase activity; IDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0009678; F:pyrophosphate hydrolysis-driven proton transmembrane transporter activity; IDA:TAIR.
DR GO; GO:0009926; P:auxin polar transport; IGI:TAIR.
DR GO; GO:0052546; P:cell wall pectin metabolic process; IMP:TAIR.
DR GO; GO:0010248; P:establishment or maintenance of transmembrane electrochemical gradient; TAS:TAIR.
DR GO; GO:0048366; P:leaf development; IMP:TAIR.
DR GO; GO:2000904; P:regulation of starch metabolic process; IMP:TAIR.
DR GO; GO:0009651; P:response to salt stress; IMP:TAIR.
DR GO; GO:0009414; P:response to water deprivation; IMP:TAIR.
DR GO; GO:0005985; P:sucrose metabolic process; IDA:TAIR.
DR HAMAP; MF_01129; PPase_energized_pump; 1.
DR InterPro; IPR004131; PPase-energised_H-pump.
DR PANTHER; PTHR31998; PTHR31998; 1.
DR Pfam; PF03030; H_PPase; 1.
DR PIRSF; PIRSF001265; H+-PPase; 1.
DR TIGRFAMs; TIGR01104; V_PPase; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Direct protein sequencing;
KW Disulfide bond; Endosome; Hydrogen ion transport; Ion transport; Magnesium;
KW Membrane; Metal-binding; Reference proteome; Translocase; Transmembrane;
KW Transmembrane helix; Transport; Vacuole.
FT CHAIN 1..770
FT /note="Pyrophosphate-energized vacuolar membrane proton
FT pump 1"
FT /id="PRO_0000217039"
FT TOPO_DOM 1..9
FT /note="Intravacuolar"
FT /evidence="ECO:0000250"
FT TRANSMEM 10..36
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 37..88
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 89..118
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 119..139
FT /note="Intravacuolar"
FT /evidence="ECO:0000250"
FT TRANSMEM 140..167
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 168..190
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 191..220
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 221..223
FT /note="Intravacuolar"
FT /evidence="ECO:0000250"
FT TRANSMEM 224..252
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 253..290
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 291..316
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 317..324
FT /note="Intravacuolar"
FT /evidence="ECO:0000250"
FT TRANSMEM 325..350
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 351..358
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 359..386
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 387..405
FT /note="Intravacuolar"
FT /evidence="ECO:0000250"
FT TRANSMEM 406..429
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 430..451
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 452..476
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 477..482
FT /note="Intravacuolar"
FT /evidence="ECO:0000250"
FT TRANSMEM 483..509
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 510..538
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 539..567
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 568..577
FT /note="Intravacuolar"
FT /evidence="ECO:0000250"
FT TRANSMEM 578..606
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 607..635
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 636..664
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 665
FT /note="Intravacuolar"
FT /evidence="ECO:0000250"
FT TRANSMEM 666..693
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 694..736
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 737..762
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 763..770
FT /note="Intravacuolar"
FT /evidence="ECO:0000250"
FT BINDING 254
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 257
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 257
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 261
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 287
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 511
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 538
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 695
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 731
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 734
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 246
FT /note="Important for proton transport"
FT /evidence="ECO:0000250"
FT SITE 291
FT /note="Important for proton transport"
FT /evidence="ECO:0000250"
FT SITE 298
FT /note="Important for proton transport"
FT /evidence="ECO:0000250"
FT SITE 305
FT /note="Important for proton transport"
FT /evidence="ECO:0000250"
FT SITE 735
FT /note="Important for proton transport"
FT /evidence="ECO:0000250"
FT SITE 746
FT /note="Important for proton transport"
FT /evidence="ECO:0000250"
FT DISULFID 128..136
FT /evidence="ECO:0000250"
FT MUTAGEN 119
FT /note="E->Q: Slight reduction of PPi hydrolysis and H(+)
FT translocation."
FT /evidence="ECO:0000269|PubMed:9268385"
FT MUTAGEN 229
FT /note="E->D: Slight increased PPi hydrolysis and H(+)
FT translocation."
FT /evidence="ECO:0000269|PubMed:9268385"
FT MUTAGEN 229
FT /note="E->Q: Slight reduction of PPi hydrolysis and H(+)
FT translocation."
FT /evidence="ECO:0000269|PubMed:9268385"
FT MUTAGEN 305
FT /note="E->D: Abolishes H(+) translocation and strong
FT reduction of PPi hydrolysis."
FT /evidence="ECO:0000269|PubMed:9268385"
FT MUTAGEN 305
FT /note="E->Q: Abolishes H(+) translocation and strong
FT reduction of PPi hydrolysis, reduced sensitivity to DCCD."
FT /evidence="ECO:0000269|PubMed:9268385"
FT MUTAGEN 427
FT /note="E->D: Increases H(+) translocation, normal PPi
FT hydrolysis."
FT /evidence="ECO:0000269|PubMed:9268385"
FT MUTAGEN 427
FT /note="E->Q: Strong reduction of PPi hydrolysis and H(+)
FT translocation."
FT /evidence="ECO:0000269|PubMed:9268385"
FT MUTAGEN 504
FT /note="D->E: Abolishes H(+) translocation and strong
FT reduction of PPi hydrolysis."
FT /evidence="ECO:0000269|PubMed:9268385"
FT MUTAGEN 504
FT /note="D->N: Abolishes H(+) translocation and strong
FT reduction of PPi hydrolysis, reduced sensitivity to DCCD."
FT /evidence="ECO:0000269|PubMed:9268385"
FT MUTAGEN 573
FT /note="D->N: Increases H(+) translocation, normal PPi
FT hydrolysis."
FT /evidence="ECO:0000269|PubMed:9268385"
FT MUTAGEN 634
FT /note="C->A,S: Reduced sensitivity to NEM."
FT /evidence="ECO:0000269|PubMed:7852329"
FT MUTAGEN 667
FT /note="E->Q: Slight reduction of PPi hydrolysis and H(+)
FT translocation."
FT /evidence="ECO:0000269|PubMed:9268385"
FT MUTAGEN 751
FT /note="E->Q: Slight reduction of PPi hydrolysis and H(+)
FT translocation."
FT /evidence="ECO:0000269|PubMed:9268385"
FT CONFLICT 8
FT /note="P -> L (in Ref. 2; BAA32210)"
FT /evidence="ECO:0000305"
FT CONFLICT 576
FT /note="T -> A (in Ref. 6; CAA79038)"
FT /evidence="ECO:0000305"
FT CONFLICT 584
FT /note="L -> P (in Ref. 6; CAA79038)"
FT /evidence="ECO:0000305"
FT CONFLICT 624
FT /note="E -> K (in Ref. 5; AAL57660)"
FT /evidence="ECO:0000305"
FT CONFLICT 685
FT /note="I -> T (in Ref. 5; AAL84953)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 770 AA; 80820 MW; CE7132B42B299860 CRC64;
MVAPALLPEL WTEILVPICA VIGIAFSLFQ WYVVSRVKLT SDLGASSSGG ANNGKNGYGD
YLIEEEEGVN DQSVVAKCAE IQTAISEGAT SFLFTEYKYV GVFMIFFAAV IFVFLGSVEG
FSTDNKPCTY DTTRTCKPAL ATAAFSTIAF VLGAVTSVLS GFLGMKIATY ANARTTLEAR
KGVGKAFIVA FRSGAVMGFL LAASGLLVLY ITINVFKIYY GDDWEGLFEA ITGYGLGGSS
MALFGRVGGG IYTKAADVGA DLVGKIERNI PEDDPRNPAV IADNVGDNVG DIAGMGSDLF
GSYAEASCAA LVVASISSFG INHDFTAMCY PLLISSMGIL VCLITTLFAT DFFEIKLVKE
IEPALKNQLI ISTVIMTVGI AIVSWVGLPT SFTIFNFGTQ KVVKNWQLFL CVCVGLWAGL
IIGFVTEYYT SNAYSPVQDV ADSCRTGAAT NVIFGLALGY KSVIIPIFAI AISIFVSFSF
AAMYGVAVAA LGMLSTIATG LAIDAYGPIS DNAGGIAEMA GMSHRIRERT DALDAAGNTT
AAIGKGFAIG SAALVSLALF GAFVSRAGIH TVDVLTPKVI IGLLVGAMLP YWFSAMTMKS
VGSAALKMVE EVRRQFNTIP GLMEGTAKPD YATCVKISTD ASIKEMIPPG CLVMLTPLIV
GFFFGVETLS GVLAGSLVSG VQIAISASNT GGAWDNAKKY IEAGVSEHAK SLGPKGSEPH
KAAVIGDTIG DPLKDTSGPS LNILIKLMAV ESLVFAPFFA THGGILFKYF
