ID   AVPX_ARATH              Reviewed;         802 AA.
AC   Q9FWR2; F4I4J7;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=Pyrophosphate-energized membrane proton pump 3;
DE            EC=7.1.3.1;
DE   AltName: Full=AVP1-like protein 2;
DE   AltName: Full=Pyrophosphate-energized inorganic pyrophosphatase 3;
DE            Short=H(+)-PPase 3;
GN   Name=AVPL2; OrderedLocusNames=At1g16780; ORFNames=F17F16.2;
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 [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   [2]
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).
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: Golgi apparatus membrane {ECO:0000250}; Multi-
CC       pass membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the H(+)-translocating pyrophosphatase (TC
CC       3.A.10) family. K(+)-insensitive subfamily. {ECO:0000305}.
CC   -!- CAUTION: It is uncertain whether Met-1, Met-2 or Met-3 is the
CC       initiator. {ECO:0000305}.
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DR   EMBL; AC026237; AAG09080.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE29496.2; -; Genomic_DNA.
DR   EMBL; CP002684; ANM60769.1; -; Genomic_DNA.
DR   EMBL; CP002684; ANM60770.1; -; Genomic_DNA.
DR   PIR; C86303; C86303.
DR   RefSeq; NP_001319021.1; NM_001332258.1.
DR   RefSeq; NP_001323031.1; NM_001332259.1.
DR   RefSeq; NP_001323032.1; NM_001332260.1.
DR   AlphaFoldDB; Q9FWR2; -.
DR   SMR; Q9FWR2; -.
DR   BioGRID; 23489; 1.
DR   STRING; 3702.AT1G16780.1; -.
DR   PaxDb; Q9FWR2; -.
DR   PRIDE; Q9FWR2; -.
DR   ProteomicsDB; 240934; -.
DR   EnsemblPlants; AT1G16780.1; AT1G16780.1; AT1G16780.
DR   EnsemblPlants; AT1G16780.2; AT1G16780.2; AT1G16780.
DR   EnsemblPlants; AT1G16780.3; AT1G16780.3; AT1G16780.
DR   GeneID; 838249; -.
DR   Gramene; AT1G16780.1; AT1G16780.1; AT1G16780.
DR   Gramene; AT1G16780.2; AT1G16780.2; AT1G16780.
DR   Gramene; AT1G16780.3; AT1G16780.3; AT1G16780.
DR   KEGG; ath:AT1G16780; -.
DR   Araport; AT1G16780; -.
DR   eggNOG; ENOG502QPJC; Eukaryota.
DR   HOGENOM; CLU_008743_3_1_1; -.
DR   InParanoid; Q9FWR2; -.
DR   OMA; VWISRYY; -.
DR   OrthoDB; 257116at2759; -.
DR   PhylomeDB; Q9FWR2; -.
DR   BioCyc; ARA:AT1G16780-MON; -.
DR   PRO; PR:Q9FWR2; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9FWR2; baseline and differential.
DR   Genevisible; Q9FWR2; AT.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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   3: Inferred from homology;
KW   Golgi apparatus; Hydrogen ion transport; Ion transport; Magnesium;
KW   Membrane; Metal-binding; Reference proteome; Translocase; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..802
FT                   /note="Pyrophosphate-energized membrane proton pump 3"
FT                   /id="PRO_0000217041"
FT   TRANSMEM        41..61
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        66..86
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        118..138
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        160..180
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        206..226
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        246..266
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        348..368
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        386..406
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        421..441
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        468..491
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        511..531
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        577..597
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        615..635
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        686..706
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        716..736
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        782..802
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         273
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         276
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         276
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         280
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         306
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         541
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         568
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000250"
FT   BINDING         743
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000250"
FT   BINDING         773
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         776
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            310
FT                   /note="Important for proton transport"
FT                   /evidence="ECO:0000250"
FT   SITE            317
FT                   /note="Important for proton transport"
FT                   /evidence="ECO:0000250"
FT   SITE            777
FT                   /note="Important for proton transport"
FT                   /evidence="ECO:0000250"
FT   SITE            788
FT                   /note="Important for proton transport"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   802 AA;  85349 MW;  E3CFD70DAF219880 CRC64;
     MMMDEDVEQA TLVSYSDKPR TFPDMRSKTY SPLIIRILRN LNVRALSVLL LLSFGGIFYM
     GARTSPIIVF VFVVCIISFM LSVYLTKWVL AKDEGPPEMV QISDAIRDGA EGFLRTQYGT
     ISKMAFLLAF VILCIYLFRN LTPQQEASGL GRTMSAYITV AAFLLGALCS GIAGYVGMWV
     SVRANVRVSS AARRSAREAL QIAVRAGGFS ALVVVGMAVI GIAILYSTFY VWLDVDSPGS
     MKVTDLPLLL VGYGFGASFV ALFAQLGGGI YTKGADVGAD LVGKVEHGIP EDDPRNPAVI
     ADLVGDNVGD CAARGADLFE SIAAEIISAM ILGGTMAQKC KIEDPSGFIL FPLVVHSFDL
     VISSIGILSI KGTRNASVKS PVEDPMVVLQ KGYSLTIILA VLTFGASTRW LLYTEQAPSA
     WLNFFMCGLV GIITAYVFVW ISRYYTDYKY EPVRTLALAS STGHGTNIIA GVSLGLESTA
     LPVLVISVAI ISAFWLGNTS GLIDEKGNPT GGLFGTAVAT MGMLSTAAYV LTMDMFGPIA
     DNAGGIVEMS QQPESVREIT DVLDAVGNTT KATTKGFAIG SAALASFLLF SAYMDEVSAF
     ANVSFKEVDI AIPEVFIGGL LGAMLIFLFS AWACAAVGRT AQEVVNEVRR QFIERPGIMD
     YKEKPDYGRC VAIVASSALR EMIKPGALAI ISPIAVGFVF RILGYYTGQP LLGAKVVAAM
     LMFATVCGIL MALFLNTAGG AWDNAKKYIE TGALGGKGSD SHKAAVTGDT VGDPFKDTAG
     PSIHVLIKML ATITLVMAPI FL