AVP_HORVU
ID AVP_HORVU Reviewed; 762 AA.
AC Q06572;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 14-AUG-2001, sequence version 2.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Pyrophosphate-energized vacuolar membrane proton pump;
DE EC=7.1.3.1;
DE AltName: Full=Pyrophosphate-energized inorganic pyrophosphatase;
DE Short=H(+)-PPase;
OS Hordeum vulgare (Barley).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX NCBI_TaxID=4513;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Kashima; TISSUE=Root;
RX PubMed=8382487; DOI=10.1006/bbrc.1993.1164;
RA Tanaka Y., Chiba K., Maeda M., Maeshima M.;
RT "Molecular cloning of cDNA for vacuolar membrane proton-translocating
RT inorganic pyrophosphatase in Hordeum vulgare.";
RL Biochem. Biophys. Res. Commun. 190:1110-1114(1993).
RN [2]
RP SEQUENCE REVISION TO 41-45.
RA Tanaka Y.;
RL Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
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.
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 -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Vacuole membrane; Multi-pass membrane protein.
CC Note=Tonoplast.
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}.
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DR EMBL; D13472; BAA02717.2; -; mRNA.
DR PIR; JC1466; JC1466.
DR AlphaFoldDB; Q06572; -.
DR SMR; Q06572; -.
DR PRIDE; Q06572; -.
DR EnsemblPlants; HORVU.MOREX.r2.7HG0545990.1; HORVU.MOREX.r2.7HG0545990.1; HORVU.MOREX.r2.7HG0545990.
DR EnsemblPlants; HORVU.MOREX.r2.7HG0545990.1.mrna1; HORVU.MOREX.r2.7HG0545990.1.mrna1; HORVU.MOREX.r2.7HG0545990.1.
DR Gramene; HORVU.MOREX.r2.7HG0545990.1; HORVU.MOREX.r2.7HG0545990.1; HORVU.MOREX.r2.7HG0545990.
DR Gramene; HORVU.MOREX.r2.7HG0545990.1.mrna1; HORVU.MOREX.r2.7HG0545990.1.mrna1; HORVU.MOREX.r2.7HG0545990.1.
DR ExpressionAtlas; Q06572; differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004427; F:inorganic diphosphatase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009678; F:pyrophosphate hydrolysis-driven proton transmembrane transporter activity; IEA:UniProtKB-EC.
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 2: Evidence at transcript level;
KW Disulfide bond; Hydrogen ion transport; Ion transport; Magnesium; Membrane;
KW Metal-binding; Translocase; Transmembrane; Transmembrane helix; Transport;
KW Vacuole.
FT CHAIN 1..762
FT /note="Pyrophosphate-energized vacuolar membrane proton
FT pump"
FT /id="PRO_0000217042"
FT TOPO_DOM 1..6
FT /note="Intravacuolar"
FT /evidence="ECO:0000250"
FT TRANSMEM 7..33
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 34..81
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 82..111
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 112..131
FT /note="Intravacuolar"
FT /evidence="ECO:0000250"
FT TRANSMEM 132..159
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 160..182
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 183..212
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 213..215
FT /note="Intravacuolar"
FT /evidence="ECO:0000250"
FT TRANSMEM 216..244
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 245..282
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 283..308
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 309..316
FT /note="Intravacuolar"
FT /evidence="ECO:0000250"
FT TRANSMEM 317..342
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 343..350
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 351..378
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 379..397
FT /note="Intravacuolar"
FT /evidence="ECO:0000250"
FT TRANSMEM 398..421
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 422..443
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 444..468
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 469..474
FT /note="Intravacuolar"
FT /evidence="ECO:0000250"
FT TRANSMEM 475..501
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 502..530
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 531..559
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 560..569
FT /note="Intravacuolar"
FT /evidence="ECO:0000250"
FT TRANSMEM 570..598
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 599..627
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 628..656
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 657
FT /note="Intravacuolar"
FT /evidence="ECO:0000250"
FT TRANSMEM 658..685
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 686..728
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 729..754
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 755..762
FT /note="Intravacuolar"
FT /evidence="ECO:0000250"
FT BINDING 246
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 249
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 249
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 253
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 279
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 503
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 530
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 687
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 723
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 726
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 238
FT /note="Important for proton transport"
FT /evidence="ECO:0000250"
FT SITE 283
FT /note="Important for proton transport"
FT /evidence="ECO:0000250"
FT SITE 290
FT /note="Important for proton transport"
FT /evidence="ECO:0000250"
FT SITE 297
FT /note="Important for proton transport"
FT /evidence="ECO:0000250"
FT SITE 727
FT /note="Important for proton transport"
FT /evidence="ECO:0000250"
FT SITE 738
FT /note="Important for proton transport"
FT /evidence="ECO:0000250"
FT DISULFID 121..128
FT /evidence="ECO:0000250"
SQ SEQUENCE 762 AA; 79533 MW; 90CA2A2532D2C910 CRC64;
MAILGELGTE ILIPVCGVIG IVFAVAQWFI VSKVKVTPGA ASAAAGAKNG YGDYLIEEEE
GLNDHNVVVK CAEIQTAISE GATSFLFTMY QYVGMFMVVF AAIIFLFLGS IEGFSTKGQP
CTYSKGTCKP ALYTALFSTA SFLLGAITSL VSGFLGMKIA TYANARTTLE ARKGVGKAFI
TAFRSGAVMG FLLSSSGLVV LYITINVFKM YYGDDWEGLF ESITGYGLGG SSMALFGRVG
GGIYTKAADV GADLVGKVER NIPEDDPRNP AVIADNVGDN VGDIAGMGSD LFGSYAESSC
AALVVASISS FGINHDFTAM CYPLLVSSVG IIVCLLTTLF ATDFFEIKAA NEIEPALKKQ
LIISTALMTV GVAVISWLAL PAKFTIFNFG AQKEVSNWGL FFCVAVGLWA GLIIGFVTEY
YTSNAYSPVQ DVADSCRTGA ATNVIFGLAL GYKSVIIPIF AIAVSIYVSF SIAAMYGIAM
AALGMLSTMA TGLAIDAYGP ISDNAGGIAE MAGMSHRIRE RTDALDAAGN TTAAIGKGFA
IGSAALVSLA LFGAFVSRAG VKVVDVLSPK VFIGLIVGAM LPYWFSAMTM KSVGSAALKM
VEEVRRQFNT IPGLMEGTAK PDYATCVKIS TDASIKEMIP PGALVMLTPL IVGTLFGVET
LSGVLAGALV SGVQIAISAS NTGGAWDNAK KYIEAGNSEH ARSLGPKGSD CHKAAVIGDT
IGDPLKDTSG PSLNILIKLM AVESLVFAPF FATYGGLLFK YI
