AVP_VIGRR
ID AVP_VIGRR Reviewed; 766 AA.
AC P21616; O22124; Q41686;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 19-MAR-2014, sequence version 4.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Pyrophosphate-energized vacuolar membrane proton pump;
DE EC=7.1.3.1 {ECO:0000269|PubMed:10477275, ECO:0000269|PubMed:22456709};
DE AltName: Full=Pyrophosphate-energized inorganic pyrophosphatase;
DE Short=H(+)-PPase;
DE AltName: Full=Vacuolar H(+)-pyrophosphatase;
OS Vigna radiata var. radiata (Mung bean) (Phaseolus aureus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX NCBI_TaxID=3916;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=cv. Wilczek; TISSUE=Hypocotyl;
RX PubMed=9489011; DOI=10.1104/pp.116.2.589;
RA Nakanishi Y., Maeshima M.;
RT "Molecular cloning of vacuolar H(+)-pyrophosphatase and its developmental
RT expression in growing hypocotyl of mung bean.";
RL Plant Physiol. 116:589-597(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Hypocotyl;
RA Hung S.-H., Chiu S.-J., Lin L.-Y., Pan R.L.;
RT "Vacuolar H+-pyrophosphatase cDNA from etiolated mung bean seedlings.";
RL (er) Plant Gene Register PGR95-082(1995).
RN [3]
RP PROTEIN SEQUENCE OF 2-31, FUNCTION, ACTIVITY REGULATION, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=cv. Wilczek; TISSUE=Hypocotyl;
RX PubMed=2555340; DOI=10.1016/s0021-9258(19)47219-0;
RA Maeshima M., Yoshida S.;
RT "Purification and properties of vacuolar membrane proton-translocating
RT inorganic pyrophosphatase from mung bean.";
RL J. Biol. Chem. 264:20068-20073(1989).
RN [4]
RP ACTIVITY REGULATION, CATALYTIC ACTIVITY, FUNCTION, SUBCELLULAR LOCATION,
RP AND PROTEIN SEQUENCE OF 277-286.
RX PubMed=10477275; DOI=10.1042/bj3420641;
RA Yang S.J., Jiang S.S., Kuo S.Y., Hung S.H., Tam M.F., Pan R.L.;
RT "Localization of a carboxylic residue possibly involved in the inhibition
RT of vacuolar H+-pyrophosphatase by N,N'-dicyclohexylcarbodi-imide.";
RL Biochem. J. 342:641-646(1999).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) IN COMPLEX WITH PYROPHOSPHATE ANALOG
RP AND MAGNESIUM, TOPOLOGY, SUBCELLULAR LOCATION, SUBUNIT, DOMAIN, MUTAGENESIS
RP OF ASP-294 AND LYS-742, FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=22456709; DOI=10.1038/nature10963;
RA Lin S.M., Tsai J.Y., Hsiao C.D., Huang Y.T., Chiu C.L., Liu M.H.,
RA Tung J.Y., Liu T.H., Pan R.L., Sun Y.J.;
RT "Crystal structure of a membrane-embedded H+-translocating
RT pyrophosphatase.";
RL Nature 484:399-403(2012).
CC -!- FUNCTION: Proton-translocating inorganic pyrophosphatase that
CC contributes to the transtonoplast (from cytosol to vacuole lumen) H(+)-
CC electrochemical potential difference. It establishes a proton gradient
CC of similar and often greater magnitude than the H(+)-ATPase on the same
CC membrane. {ECO:0000269|PubMed:10477275, ECO:0000269|PubMed:22456709,
CC ECO:0000269|PubMed:2555340, ECO:0000269|PubMed:9489011}.
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 Evidence={ECO:0000269|PubMed:10477275, ECO:0000269|PubMed:22456709};
CC -!- ACTIVITY REGULATION: Inhibited by excess pyrophosphate as well as
CC excess Mg(2+). Inhibition by ATP, GTP, and CTP is reversed by
CC increasing the Mg(2+) concentration. This suggests that the substrate
CC is a particular metal complex such as MgPPi(2-). Modification of Asp-
CC 283 with DCCD abolishes pyrophosphatase activity.
CC {ECO:0000269|PubMed:10477275, ECO:0000269|PubMed:2555340}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:22456709}.
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:10477275,
CC ECO:0000269|PubMed:22456709, ECO:0000269|PubMed:2555340,
CC ECO:0000269|PubMed:9489011}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:10477275, ECO:0000269|PubMed:22456709,
CC ECO:0000269|PubMed:2555340, ECO:0000269|PubMed:9489011}. Note=Tonoplast
CC membrane.
CC -!- DEVELOPMENTAL STAGE: Detected in the hypocotyl, with the highest
CC expression in the rapidly expanding segment of the hypocotyl and lower
CC expression in older, less rapidly expanding parts of the hypocotyl.
CC {ECO:0000269|PubMed:9489011}.
CC -!- DOMAIN: Has 16 transmembrane helices and a large cytoplasmic domain
CC that contains the active site. {ECO:0000269|PubMed:22456709}.
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.
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; AB009077; BAA23649.1; -; mRNA.
DR EMBL; U31467; AAC49175.1; -; mRNA.
DR PIR; A34486; A34486.
DR PIR; T07801; T07801.
DR PIR; T10841; T10841.
DR PDB; 4A01; X-ray; 2.35 A; A/B=1-766.
DR PDB; 5GPJ; X-ray; 3.50 A; A/B/C/D=1-766.
DR PDB; 6AFS; X-ray; 2.30 A; A/B=1-766.
DR PDB; 6AFT; X-ray; 2.49 A; A/B=1-766.
DR PDB; 6AFU; X-ray; 2.80 A; A/B=1-766.
DR PDB; 6AFV; X-ray; 2.70 A; A/B=1-766.
DR PDB; 6AFW; X-ray; 2.19 A; A/B=1-766.
DR PDB; 6AFX; X-ray; 2.30 A; A/B=1-766.
DR PDB; 6AFY; X-ray; 2.40 A; A/B=1-766.
DR PDB; 6AFZ; X-ray; 2.48 A; A/B=1-766.
DR PDBsum; 4A01; -.
DR PDBsum; 5GPJ; -.
DR PDBsum; 6AFS; -.
DR PDBsum; 6AFT; -.
DR PDBsum; 6AFU; -.
DR PDBsum; 6AFV; -.
DR PDBsum; 6AFW; -.
DR PDBsum; 6AFX; -.
DR PDBsum; 6AFY; -.
DR PDBsum; 6AFZ; -.
DR AlphaFoldDB; P21616; -.
DR SMR; P21616; -.
DR DIP; DIP-59673N; -.
DR STRING; 3916.P21616; -.
DR TCDB; 3.A.10.1.8; the h(+), na(+)-translocating pyrophosphatase (m(+)-ppase) family.
DR PRIDE; P21616; -.
DR SABIO-RK; P21616; -.
DR Proteomes; UP000087766; Genome assembly.
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 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond;
KW Hydrogen ion transport; Ion transport; Magnesium; Membrane; Metal-binding;
KW Reference proteome; Translocase; Transmembrane; Transmembrane helix;
KW Transport; Vacuole.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2555340"
FT CHAIN 2..766
FT /note="Pyrophosphate-energized vacuolar membrane proton
FT pump"
FT /id="PRO_0000217043"
FT TOPO_DOM 2..8
FT /note="Intravacuolar"
FT /evidence="ECO:0000305|PubMed:22456709"
FT TRANSMEM 9..35
FT /note="Helical"
FT TOPO_DOM 36..84
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:22456709"
FT TRANSMEM 85..114
FT /note="Helical"
FT TOPO_DOM 115..135
FT /note="Intravacuolar"
FT /evidence="ECO:0000305|PubMed:22456709"
FT TRANSMEM 136..163
FT /note="Helical"
FT TOPO_DOM 164..186
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:22456709"
FT TRANSMEM 187..216
FT /note="Helical"
FT TOPO_DOM 217..219
FT /note="Intravacuolar"
FT /evidence="ECO:0000305|PubMed:22456709"
FT TRANSMEM 220..248
FT /note="Helical"
FT TOPO_DOM 249..286
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:22456709"
FT TRANSMEM 287..312
FT /note="Helical"
FT TOPO_DOM 313..320
FT /note="Intravacuolar"
FT /evidence="ECO:0000305|PubMed:22456709"
FT TRANSMEM 321..346
FT /note="Helical"
FT TOPO_DOM 347..354
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:22456709"
FT TRANSMEM 355..382
FT /note="Helical"
FT TOPO_DOM 383..401
FT /note="Intravacuolar"
FT /evidence="ECO:0000305|PubMed:22456709"
FT TRANSMEM 402..425
FT /note="Helical"
FT TOPO_DOM 426..447
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:22456709"
FT TRANSMEM 448..472
FT /note="Helical"
FT TOPO_DOM 473..478
FT /note="Intravacuolar"
FT /evidence="ECO:0000305|PubMed:22456709"
FT TRANSMEM 479..505
FT /note="Helical"
FT TOPO_DOM 506..534
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:22456709"
FT TRANSMEM 535..563
FT /note="Helical"
FT TOPO_DOM 564..573
FT /note="Intravacuolar"
FT /evidence="ECO:0000305|PubMed:22456709"
FT TRANSMEM 574..602
FT /note="Helical"
FT TOPO_DOM 603..631
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:22456709"
FT TRANSMEM 632..660
FT /note="Helical"
FT TOPO_DOM 661
FT /note="Intravacuolar"
FT /evidence="ECO:0000305|PubMed:22456709"
FT TRANSMEM 662..689
FT /note="Helical"
FT TOPO_DOM 690..732
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:22456709"
FT TRANSMEM 733..758
FT /note="Helical"
FT TOPO_DOM 759..765
FT /note="Intravacuolar"
FT /evidence="ECO:0000305|PubMed:22456709"
FT BINDING 250
FT /ligand="substrate"
FT BINDING 253
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:22456709"
FT BINDING 253
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:22456709"
FT BINDING 257
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:22456709"
FT BINDING 283
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:22456709"
FT BINDING 507
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:22456709"
FT BINDING 534
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:22456709"
FT BINDING 691
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:22456709"
FT BINDING 727
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:22456709"
FT BINDING 730
FT /ligand="substrate"
FT SITE 242
FT /note="Important for proton transport"
FT /evidence="ECO:0000305"
FT SITE 287
FT /note="Important for proton transport"
FT /evidence="ECO:0000305"
FT SITE 294
FT /note="Important for proton transport"
FT /evidence="ECO:0000305"
FT SITE 301
FT /note="Important for proton transport"
FT /evidence="ECO:0000305"
FT SITE 731
FT /note="Important for proton transport"
FT /evidence="ECO:0000305"
FT SITE 742
FT /note="Important for proton transport"
FT /evidence="ECO:0000305"
FT DISULFID 124..132
FT MUTAGEN 294
FT /note="D->A,E,G,N,T: Reduces pyrophosphatase activity by
FT over 90%. Abolishes proton transport."
FT /evidence="ECO:0000269|PubMed:22456709"
FT MUTAGEN 742
FT /note="K->A,R,M: Reduces pyrophosphatase activity by over
FT 90%. Abolishes proton transport."
FT /evidence="ECO:0000269|PubMed:22456709"
FT CONFLICT 22
FT /note="G -> W (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 476
FT /note="F -> L (in Ref. 1; BAA23649)"
FT /evidence="ECO:0000305"
FT CONFLICT 687
FT /note="Missing (in Ref. 2; AAC49175)"
FT /evidence="ECO:0000305"
FT HELIX 8..33
FT /evidence="ECO:0007829|PDB:6AFW"
FT HELIX 68..112
FT /evidence="ECO:0007829|PDB:6AFW"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:6AFW"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:6AFW"
FT STRAND 127..132
FT /evidence="ECO:0007829|PDB:6AFW"
FT HELIX 135..174
FT /evidence="ECO:0007829|PDB:6AFW"
FT TURN 175..177
FT /evidence="ECO:0007829|PDB:6AFW"
FT HELIX 179..216
FT /evidence="ECO:0007829|PDB:6AFW"
FT HELIX 220..227
FT /evidence="ECO:0007829|PDB:6AFW"
FT HELIX 229..261
FT /evidence="ECO:0007829|PDB:6AFW"
FT HELIX 276..285
FT /evidence="ECO:0007829|PDB:6AFW"
FT TURN 286..288
FT /evidence="ECO:0007829|PDB:6AFW"
FT HELIX 289..311
FT /evidence="ECO:0007829|PDB:6AFW"
FT HELIX 314..317
FT /evidence="ECO:0007829|PDB:6AFW"
FT HELIX 321..324
FT /evidence="ECO:0007829|PDB:6AFW"
FT HELIX 326..346
FT /evidence="ECO:0007829|PDB:6AFW"
FT HELIX 354..356
FT /evidence="ECO:0007829|PDB:6AFW"
FT HELIX 357..383
FT /evidence="ECO:0007829|PDB:6AFW"
FT STRAND 386..392
FT /evidence="ECO:0007829|PDB:6AFW"
FT STRAND 395..400
FT /evidence="ECO:0007829|PDB:6AFW"
FT HELIX 401..426
FT /evidence="ECO:0007829|PDB:6AFW"
FT HELIX 431..438
FT /evidence="ECO:0007829|PDB:6AFW"
FT HELIX 439..442
FT /evidence="ECO:0007829|PDB:6AFW"
FT HELIX 444..458
FT /evidence="ECO:0007829|PDB:6AFW"
FT HELIX 460..489
FT /evidence="ECO:0007829|PDB:6AFW"
FT TURN 490..492
FT /evidence="ECO:0007829|PDB:6AFW"
FT HELIX 493..515
FT /evidence="ECO:0007829|PDB:6AFW"
FT HELIX 520..562
FT /evidence="ECO:0007829|PDB:6AFW"
FT STRAND 569..572
FT /evidence="ECO:0007829|PDB:4A01"
FT HELIX 573..582
FT /evidence="ECO:0007829|PDB:6AFW"
FT HELIX 585..614
FT /evidence="ECO:0007829|PDB:6AFW"
FT TURN 616..621
FT /evidence="ECO:0007829|PDB:6AFW"
FT HELIX 627..641
FT /evidence="ECO:0007829|PDB:6AFW"
FT HELIX 643..659
FT /evidence="ECO:0007829|PDB:6AFW"
FT HELIX 662..699
FT /evidence="ECO:0007829|PDB:6AFW"
FT HELIX 703..708
FT /evidence="ECO:0007829|PDB:6AFW"
FT HELIX 714..731
FT /evidence="ECO:0007829|PDB:6AFW"
FT HELIX 734..736
FT /evidence="ECO:0007829|PDB:6AFW"
FT HELIX 737..750
FT /evidence="ECO:0007829|PDB:6AFW"
FT HELIX 752..758
FT /evidence="ECO:0007829|PDB:6AFW"
FT HELIX 761..765
FT /evidence="ECO:0007829|PDB:6AFW"
SQ SEQUENCE 766 AA; 80037 MW; D2E37BC5C113D485 CRC64;
MGAAILPDLG TEILIPVCAV IGIAFALFQW LLVSKVKLSA VRDASPNAAA KNGYNDYLIE
EEEGINDHNV VVKCAEIQNA ISEGATSFLF TEYKYVGIFM VAFAILIFLF LGSVEGFSTS
PQACSYDKTK TCKPALATAI FSTVSFLLGG VTSLVSGFLG MKIATYANAR TTLEARKGVG
KAFITAFRSG AVMGFLLAAN GLLVLYIAIN LFKIYYGDDW GGLFEAITGY GLGGSSMALF
GRVGGGIYTK AADVGADLVG KVERNIPEDD PRNPAVIADN VGDNVGDIAG MGSDLFGSYA
ESSCAALVVA SISSFGLNHE LTAMLYPLIV SSVGILVCLL TTLFATDFFE IKAVKEIEPA
LKKQLVISTV LMTIGVAVVS FVALPTSFTI FNFGVQKDVK SWQLFLCVAV GLWAGLIIGF
VTEYYTSNAY SPVQDVADSC RTGAATNVIF GLALGYKSVI IPIFAIAISI FVSFTFAAMY
GIAVAALGML STIATGLAID AYGPISDNAG GIAEMAGMSH RIRERTDALD AAGNTTAAIG
KGFAIGSAAL VSLALFGAFV SRASITTVDV LTPKVFIGLI VGAMLPYWFS AMTMKSVGSA
ALKMVEEVRR QFNTIPGLME GTAKPDYATC VKISTDASIK EMIPPGALVM LTPLVVGILF
GVETLSGVLA GSLVSGVQIA ISASNTGGAW DNAKKYIEAG ASEHARSLGP KGSDCHKAAV
IGDTIGDPLK DTSGPSLNIL IKLMAVESLV FAPFFATHGG LLFKIF
