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Pyrophosphate-energized vacuolar membrane proton pump 1 (EC 3.6.1.1) (Pyrophosphate-energized inorganic pyrophosphatase 1) (H( )-PPase 1) (Vacuolar proton pyrophosphatase 1) (Vacuolar proton pyrophosphatase 3)

 AVP1_ARATH              Reviewed;         770 AA.
P31414; O80390; Q41919; Q41920; Q56WP6; Q8RY20; Q8VZE3;
01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
01-JUL-1993, sequence version 1.
23-MAY-2018, entry version 146.
RecName: Full=Pyrophosphate-energized vacuolar membrane proton pump 1;
EC=3.6.1.1;
AltName: Full=Pyrophosphate-energized inorganic pyrophosphatase 1;
Short=H(+)-PPase 1;
AltName: Full=Vacuolar proton pyrophosphatase 1;
AltName: Full=Vacuolar proton pyrophosphatase 3;
Name=AVP1; Synonyms=AVP, AVP-3, AVP3; OrderedLocusNames=At1g15690;
ORFNames=F7H2.3;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Columbia;
PubMed=1311852; DOI=10.1073/pnas.89.5.1775;
Sarafian V., Kim Y., Poole R.J., Rea P.A.;
"Molecular cloning and sequence of cDNA encoding the pyrophosphate-
energized vacuolar membrane proton pump of Arabidopsis thaliana.";
Proc. Natl. Acad. Sci. U.S.A. 89:1775-1779(1992).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, INDUCTION, AND
DEVELOPMENTAL STAGE.
STRAIN=cv. Columbia; TISSUE=Leaf;
PubMed=11442058; DOI=10.1023/A:1010681129557;
Mitsuda N., Takeyasu K., Sato M.H.;
"Pollen-specific regulation of vacuolar H(+)-PPase expression by
multiple cis-acting elements.";
Plant Mol. Biol. 46:185-192(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130712; DOI=10.1038/35048500;
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S.,
White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M.,
Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
"Sequence and analysis of chromosome 1 of the plant Arabidopsis
thaliana.";
Nature 408:816-820(2000).
[4]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 554-671 AND 716-770.
STRAIN=cv. Columbia; TISSUE=Green siliques;
PubMed=8281187; DOI=10.1046/j.1365-313X.1993.04061051.x;
Hoefte H., Desprez T., Amselem J., Chiapello H., Rouze P., Caboche M.,
Moisan A., Jourjon M.-F., Charpenteau J.-L., Berthomieu P.,
Guerrier D., Giraudat J., Quigley F., Thomas F., Yu D.-Y., Mache R.,
Raynal M., Cooke R., Grellet F., Delseny M., Parmentier Y.,
de Marcillac G., Gigot C., Fleck J., Philipps G., Axelos M.,
Bardet C., Tremousaygue D., Lescure B.;
"An inventory of 1152 expressed sequence tags obtained by partial
sequencing of cDNAs from Arabidopsis thaliana.";
Plant J. 4:1051-1061(1993).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 595-770.
STRAIN=cv. Columbia;
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J.,
Hayashizaki Y., Shinozaki K.;
"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[8]
PROTEIN SEQUENCE OF 625-640, AND ENZYME REGULATION.
PubMed=8083239;
Zhen R.-G., Kim E.J., Rea P.A.;
"Localization of cytosolically oriented maleimide-reactive domain of
vacuolar H(+)-pyrophosphatase.";
J. Biol. Chem. 269:23342-23350(1994).
[9]
FUNCTION, SUBCELLULAR LOCATION, AND ENZYME REGULATION.
PubMed=8016125; DOI=10.1073/pnas.91.13.6128;
Kim E.J., Zhen R.-G., Rea P.A.;
"Heterologous expression of plant vacuolar pyrophosphatase in yeast
demonstrates sufficiency of the substrate-binding subunit for proton
transport.";
Proc. Natl. Acad. Sci. U.S.A. 91:6128-6132(1994).
[10]
MUTAGENESIS OF CYS-634, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=7852329; DOI=10.1074/jbc.270.6.2630;
Kim E.J., Zhen R.-G., Rea P.A.;
"Site-directed mutagenesis of vacuolar H(+)-pyrophosphatase. Necessity
of Cys634 for inhibition by maleimides but not catalysis.";
J. Biol. Chem. 270:2630-2635(1995).
[11]
ENZYME REGULATION, AND MUTAGENESIS OF GLU-119; GLU-229; GLU-305;
GLU-427; ASP-504; ASP-573; GLU-667 AND GLU-751.
PubMed=9268385; DOI=10.1074/jbc.272.35.22340;
Zhen R.-G., Kim E.J., Rea P.A.;
"Acidic residues necessary for pyrophosphate-energized pumping and
inhibition of the vacuolar H(+)-pyrophosphatase by N,N'-
dicyclohexylcarbodiimide.";
J. Biol. Chem. 272:22340-22348(1997).
[12]
ENZYME REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
STRAIN=cv. Columbia;
PubMed=10806252; DOI=10.1104/pp.123.1.353;
Drozdowicz Y.M., Kissinger J.C., Rea P.A.;
"AVP2, a sequence-divergent, K(+)-insensitive H(+)-translocating
inorganic pyrophosphatase from Arabidopsis.";
Plant Physiol. 123:353-362(2000).
[13]
FUNCTION.
PubMed=11572991; DOI=10.1073/pnas.191389398;
Gaxiola R.A., Li J., Undurraga S., Dang L.M., Allen G.J., Alper S.L.,
Fink G.R.;
"Drought- and salt-tolerant plants result from overexpression of the
AVP1 H(+)-pump.";
Proc. Natl. Acad. Sci. U.S.A. 98:11444-11449(2001).
[14]
INDUCTION.
PubMed=14581622; DOI=10.1093/pcp/pcg137;
Mitsuda N., Isono T., Sato M.H.;
"Arabidopsis CAMTA family proteins enhance V-PPase expression in
pollen.";
Plant Cell Physiol. 44:975-981(2003).
[15]
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
STAGE.
PubMed=16210544; DOI=10.1126/science.1115711;
Li J., Yang H., Peer W.A., Richter G., Blakeslee J., Bandyopadhyay A.,
Titapiwantakun B., Undurraga S., Khodakovskaya M., Richards E.L.,
Krizek B., Murphy A.S., Gilroy S., Gaxiola R.;
"Arabidopsis H(+)-PPase AVP1 regulates auxin-mediated organ
development.";
Science 310:121-125(2005).
[16]
IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE
SCALE ANALYSIS].
PubMed=17151019; DOI=10.1074/mcp.M600250-MCP200;
Jaquinod M., Villiers F., Kieffer-Jaquinod S., Hugouvieux V.,
Bruley C., Garin J., Bourguignon J.;
"A proteomics dissection of Arabidopsis thaliana vacuoles isolated
from cell culture.";
Mol. Cell. Proteomics 6:394-412(2007).
-!- FUNCTION: Contributes to the transtonoplast (from cytosol to
vacuole lumen) H(+)-electrochemical potential difference. It
establishes a proton gradient of similar and often greater
magnitude than the H(+)-ATPase on the same membrane. In addition,
facilitates auxin transport by modulating apoplastic pH and
regulates auxin-mediated developmental processes. Confers
tolerance to NaCl and to drought by increasing ion retention.
{ECO:0000269|PubMed:11572991, ECO:0000269|PubMed:16210544,
ECO:0000269|PubMed:8016125}.
-!- CATALYTIC ACTIVITY: Diphosphate + H(2)O = 2 phosphate.
-!- ENZYME REGULATION: Activated by K(+) and Mg(2+). Inhibited by
Ca(2+), N,N'-dicyclohexylcarbodiimide (DCCD), N-ethylmaleimide
(NEM) and aminomethylenediphosphonate (AMDP), and, to a lower
extent, by fluoride (KF). {ECO:0000269|PubMed:10806252,
ECO:0000269|PubMed:8016125, ECO:0000269|PubMed:8083239,
ECO:0000269|PubMed:9268385}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=110 uM for PPi (at pH 8 and 37 degrees Celsius)
{ECO:0000269|PubMed:10806252, ECO:0000269|PubMed:7852329};
Vmax=0.5 umol/min/mg enzyme (at pH 8 and 37 degrees Celsius)
{ECO:0000269|PubMed:10806252, ECO:0000269|PubMed:7852329};
-!- SUBUNIT: Monomer.
-!- SUBCELLULAR LOCATION: Vacuole membrane
{ECO:0000269|PubMed:17151019}; Multi-pass membrane protein
{ECO:0000255}. Endosome membrane; Multi-pass membrane protein.
Cell membrane; Multi-pass membrane protein. Note=Mostly vacuolar,
tonoplast. Also present in endosomes and plasma membrane.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=1;
Comment=A number of isoforms are produced. According to EST
sequences.;
Name=1;
IsoId=P31414-1; Sequence=Displayed;
-!- TISSUE SPECIFICITY: Ubiquitous (at protein level). Mostly
expressed in vascular tissues, meristems and root pericycle.
{ECO:0000269|PubMed:11442058, ECO:0000269|PubMed:16210544}.
-!- DEVELOPMENTAL STAGE: Increase of expression in pollen during
flower development. Expressed in developing leaves, sepals,
petals, stamens and carpels. {ECO:0000269|PubMed:11442058,
ECO:0000269|PubMed:16210544}.
-!- INDUCTION: Repressed by light. Induced by CAMTA1 and/or CAMTA5 in
pollen. {ECO:0000269|PubMed:11442058,
ECO:0000269|PubMed:14581622}.
-!- DOMAIN: Has 16 transmembrane helices and a cytoplasmic domain that
contains the active site. {ECO:0000250}.
-!- MISCELLANEOUS: Has few direct interactions with pyrophosphate.
Interacts with the substrate via divalent metal cations, such as
magnesium ions, that are bound to the pyrophosphate (By
similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the H(+)-translocating pyrophosphatase (TC
3.A.10) family. K(+)-stimulated subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAD94555.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=CAA79039.1; Type=Frameshift; Positions=718; Evidence={ECO:0000305};
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EMBL; M81892; AAA32754.1; -; mRNA.
EMBL; AB015138; BAA32210.1; -; Genomic_DNA.
EMBL; AC034256; AAF82139.1; -; Genomic_DNA.
EMBL; CP002684; AEE29349.1; -; Genomic_DNA.
EMBL; AY065016; AAL57660.1; -; mRNA.
EMBL; AY078953; AAL84953.1; -; mRNA.
EMBL; BT002481; AAO00841.1; -; mRNA.
EMBL; Z17694; CAA79038.1; -; mRNA.
EMBL; Z17695; CAA79039.1; ALT_FRAME; mRNA.
EMBL; AK221989; BAD94555.1; ALT_INIT; mRNA.
PIR; A38230; A38230.
RefSeq; NP_173021.1; NM_101437.5. [P31414-1]
UniGene; At.21942; -.
UniGene; At.66944; -.
UniGene; At.67102; -.
UniGene; At.74973; -.
ProteinModelPortal; P31414; -.
SMR; P31414; -.
BioGrid; 23378; 13.
STRING; 3702.AT1G15690.1; -.
TCDB; 3.A.10.1.1; the h(+), na(+)-translocating pyrophosphatase (m(+)-ppase) family.
iPTMnet; P31414; -.
SwissPalm; P31414; -.
PaxDb; P31414; -.
PRIDE; P31414; -.
EnsemblPlants; AT1G15690.1; AT1G15690.1; AT1G15690. [P31414-1]
GeneID; 838138; -.
Gramene; AT1G15690.1; AT1G15690.1; AT1G15690. [P31414-1]
KEGG; ath:AT1G15690; -.
Araport; AT1G15690; -.
TAIR; locus:2036134; AT1G15690.
eggNOG; ENOG410IFIU; Eukaryota.
eggNOG; COG3808; LUCA.
InParanoid; P31414; -.
KO; K01507; -.
OMA; LMEGHAR; -.
OrthoDB; EOG093603U6; -.
PhylomeDB; P31414; -.
BioCyc; ARA:AT1G15690-MONOMER; -.
BRENDA; 3.6.1.1; 399.
PRO; PR:P31414; -.
Proteomes; UP000006548; Chromosome 1.
ExpressionAtlas; P31414; baseline and differential.
Genevisible; P31414; AT.
GO; GO:0009507; C:chloroplast; IDA:TAIR.
GO; GO:0009941; C:chloroplast envelope; IDA:TAIR.
GO; GO:0010008; C:endosome membrane; IDA:TAIR.
GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0016020; C:membrane; IDA:TAIR.
GO; GO:0005739; C:mitochondrion; IDA:TAIR.
GO; GO:0000325; C:plant-type vacuole; IDA:TAIR.
GO; GO:0009705; C:plant-type vacuole membrane; IDA:TAIR.
GO; GO:0005886; C:plasma membrane; IDA:TAIR.
GO; GO:0005774; C:vacuolar membrane; IDA:TAIR.
GO; GO:0005773; C:vacuole; IDA:TAIR.
GO; GO:0009678; F:hydrogen-translocating pyrophosphatase activity; IDA:TAIR.
GO; GO:0004427; F:inorganic diphosphatase activity; IEA:UniProtKB-EC.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0009926; P:auxin polar transport; IGI:TAIR.
GO; GO:0010248; P:establishment or maintenance of transmembrane electrochemical gradient; TAS:TAIR.
GO; GO:0048366; P:leaf development; IMP:TAIR.
GO; GO:1902600; P:proton transmembrane transport; IEA:InterPro.
GO; GO:0009651; P:response to salt stress; IMP:TAIR.
GO; GO:0009414; P:response to water deprivation; IMP:TAIR.
HAMAP; MF_01129; PPase_energized_pump; 1.
InterPro; IPR004131; PPase-energised_H-pump.
PANTHER; PTHR31998; PTHR31998; 1.
Pfam; PF03030; H_PPase; 1.
PIRSF; PIRSF001265; H+-PPase; 1.
TIGRFAMs; TIGR01104; V_PPase; 1.
1: Evidence at protein level;
Alternative splicing; Cell membrane; Complete proteome;
Direct protein sequencing; Disulfide bond; Endosome;
Hydrogen ion transport; Hydrolase; Ion transport; Magnesium; Membrane;
Metal-binding; Reference proteome; Transmembrane; Transmembrane helix;
Transport; Vacuole.
CHAIN 1 770 Pyrophosphate-energized vacuolar membrane
proton pump 1.
/FTId=PRO_0000217039.
TOPO_DOM 1 9 Intravacuolar. {ECO:0000250}.
TRANSMEM 10 36 Helical. {ECO:0000250}.
TOPO_DOM 37 88 Cytoplasmic. {ECO:0000250}.
TRANSMEM 89 118 Helical. {ECO:0000250}.
TOPO_DOM 119 139 Intravacuolar. {ECO:0000250}.
TRANSMEM 140 167 Helical. {ECO:0000250}.
TOPO_DOM 168 190 Cytoplasmic. {ECO:0000250}.
TRANSMEM 191 220 Helical. {ECO:0000250}.
TOPO_DOM 221 223 Intravacuolar. {ECO:0000250}.
TRANSMEM 224 252 Helical. {ECO:0000250}.
TOPO_DOM 253 290 Cytoplasmic. {ECO:0000250}.
TRANSMEM 291 316 Helical. {ECO:0000250}.
TOPO_DOM 317 324 Intravacuolar. {ECO:0000250}.
TRANSMEM 325 350 Helical. {ECO:0000250}.
TOPO_DOM 351 358 Cytoplasmic. {ECO:0000250}.
TRANSMEM 359 386 Helical. {ECO:0000250}.
TOPO_DOM 387 405 Intravacuolar. {ECO:0000250}.
TRANSMEM 406 429 Helical. {ECO:0000250}.
TOPO_DOM 430 451 Cytoplasmic. {ECO:0000250}.
TRANSMEM 452 476 Helical. {ECO:0000250}.
TOPO_DOM 477 482 Intravacuolar. {ECO:0000250}.
TRANSMEM 483 509 Helical. {ECO:0000250}.
TOPO_DOM 510 538 Cytoplasmic. {ECO:0000250}.
TRANSMEM 539 567 Helical. {ECO:0000250}.
TOPO_DOM 568 577 Intravacuolar. {ECO:0000250}.
TRANSMEM 578 606 Helical. {ECO:0000250}.
TOPO_DOM 607 635 Cytoplasmic. {ECO:0000250}.
TRANSMEM 636 664 Helical. {ECO:0000250}.
TOPO_DOM 665 665 Intravacuolar. {ECO:0000250}.
TRANSMEM 666 693 Helical. {ECO:0000250}.
TOPO_DOM 694 736 Cytoplasmic. {ECO:0000250}.
TRANSMEM 737 762 Helical. {ECO:0000250}.
TOPO_DOM 763 770 Intravacuolar. {ECO:0000250}.
METAL 257 257 Magnesium 1. {ECO:0000250}.
METAL 257 257 Magnesium 2. {ECO:0000250}.
METAL 261 261 Magnesium 1. {ECO:0000250}.
METAL 287 287 Magnesium 3. {ECO:0000250}.
METAL 511 511 Magnesium 3. {ECO:0000250}.
METAL 538 538 Magnesium 4. {ECO:0000250}.
METAL 695 695 Magnesium 4. {ECO:0000250}.
METAL 731 731 Magnesium 2. {ECO:0000250}.
BINDING 254 254 Substrate. {ECO:0000250}.
BINDING 734 734 Substrate. {ECO:0000250}.
SITE 246 246 Important for proton transport.
{ECO:0000250}.
SITE 291 291 Important for proton transport.
{ECO:0000250}.
SITE 298 298 Important for proton transport.
{ECO:0000250}.
SITE 305 305 Important for proton transport.
{ECO:0000250}.
SITE 735 735 Important for proton transport.
{ECO:0000250}.
SITE 746 746 Important for proton transport.
{ECO:0000250}.
DISULFID 128 136 {ECO:0000250}.
MUTAGEN 119 119 E->Q: Slight reduction of PPi hydrolysis
and H(+) translocation.
{ECO:0000269|PubMed:9268385}.
MUTAGEN 229 229 E->D: Slight increased PPi hydrolysis and
H(+) translocation.
{ECO:0000269|PubMed:9268385}.
MUTAGEN 229 229 E->Q: Slight reduction of PPi hydrolysis
and H(+) translocation.
{ECO:0000269|PubMed:9268385}.
MUTAGEN 305 305 E->D: Abolishes H(+) translocation and
strong reduction of PPi hydrolysis.
{ECO:0000269|PubMed:9268385}.
MUTAGEN 305 305 E->Q: Abolishes H(+) translocation and
strong reduction of PPi hydrolysis,
reduced sensitivity to DCCD.
{ECO:0000269|PubMed:9268385}.
MUTAGEN 427 427 E->D: Increases H(+) translocation,
normal PPi hydrolysis.
{ECO:0000269|PubMed:9268385}.
MUTAGEN 427 427 E->Q: Strong reduction of PPi hydrolysis
and H(+) translocation.
{ECO:0000269|PubMed:9268385}.
MUTAGEN 504 504 D->E: Abolishes H(+) translocation and
strong reduction of PPi hydrolysis.
{ECO:0000269|PubMed:9268385}.
MUTAGEN 504 504 D->N: Abolishes H(+) translocation and
strong reduction of PPi hydrolysis,
reduced sensitivity to DCCD.
{ECO:0000269|PubMed:9268385}.
MUTAGEN 573 573 D->N: Increases H(+) translocation,
normal PPi hydrolysis.
{ECO:0000269|PubMed:9268385}.
MUTAGEN 634 634 C->A,S: Reduced sensitivity to NEM.
{ECO:0000269|PubMed:7852329}.
MUTAGEN 667 667 E->Q: Slight reduction of PPi hydrolysis
and H(+) translocation.
{ECO:0000269|PubMed:9268385}.
MUTAGEN 751 751 E->Q: Slight reduction of PPi hydrolysis
and H(+) translocation.
{ECO:0000269|PubMed:9268385}.
CONFLICT 8 8 P -> L (in Ref. 2; BAA32210).
{ECO:0000305}.
CONFLICT 576 576 T -> A (in Ref. 6; CAA79038).
{ECO:0000305}.
CONFLICT 584 584 L -> P (in Ref. 6; CAA79038).
{ECO:0000305}.
CONFLICT 624 624 E -> K (in Ref. 5; AAL57660).
{ECO:0000305}.
CONFLICT 685 685 I -> T (in Ref. 5; AAL84953).
{ECO:0000305}.
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


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