AVP2_ARATH
ID AVP2_ARATH Reviewed; 802 AA.
AC Q56ZN6; Q9LDJ4; Q9MB70; Q9ZVB1;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Pyrophosphate-energized membrane proton pump 2;
DE EC=7.1.3.1 {ECO:0000305|PubMed:10806252};
DE AltName: Full=AVP1-like protein 1;
DE AltName: Full=Pyrophosphate-energized inorganic pyrophosphatase 2;
DE Short=H(+)-PPase 2;
DE AltName: Full=Vacuolar proton pyrophosphatase 2;
GN Name=AVPL1; Synonyms=AVP2 {ECO:0000303|PubMed:10806252};
GN OrderedLocusNames=At1g78920; ORFNames=F9K20.2;
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 [GENOMIC DNA / MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP ACTIVITY REGULATION, TISSUE SPECIFICITY, 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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Nakanishi Y., Maeshima M.;
RT "Isolation of a cDNA for a H+-pyrophosphatase-like protein from Arabidopsis
RT thaliana and its functional expression in yeast.";
RL (er) Plant Gene Register PGR00-026(2000).
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 502-801.
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 [7]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=11163790; DOI=10.1016/s0014-5793(00)02400-5;
RA Mitsuda N., Enami K., Nakata M., Takeyasu K., Sato M.H.;
RT "Novel type Arabidopsis thaliana H(+)-PPase is localized to the Golgi
RT apparatus.";
RL FEBS Lett. 488:29-33(2001).
CC -!- FUNCTION: Pyrophosphatase active in both inorganic pyrophosphate
CC hydrolysis and H(+) translocation. {ECO:0000269|PubMed:10806252}.
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:0000305|PubMed:10806252};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13974;
CC Evidence={ECO:0000305|PubMed:10806252};
CC -!- ACTIVITY REGULATION: Activated by Mg(+) but not by K(+). Inhibited by
CC Ca(2+). {ECO:0000269|PubMed:10806252}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=90 uM for PPi (at pH 8 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:10806252};
CC Vmax=0.5 umol/min/mg enzyme (at pH 8 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:10806252};
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane; Multi-pass membrane
CC protein.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Mostly expressed in cotyledons, roots
CC and flowers. Especially high levels in trichomes, sepals and stamen
CC filaments. {ECO:0000269|PubMed:10806252, ECO:0000269|PubMed:11163790}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC83018.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAF31163.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAF31164.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAD94402.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF182813; AAF31163.1; ALT_INIT; mRNA.
DR EMBL; AF184917; AAF31164.1; ALT_INIT; Genomic_DNA.
DR EMBL; AB034696; BAA92151.1; -; mRNA.
DR EMBL; AC005679; AAC83018.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE36177.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE36178.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM60408.1; -; Genomic_DNA.
DR EMBL; AY054485; AAK96676.1; -; mRNA.
DR EMBL; BT010353; AAQ56796.1; -; mRNA.
DR EMBL; AK220927; BAD94402.1; ALT_SEQ; mRNA.
DR PIR; H96818; H96818.
DR RefSeq; NP_001117619.1; NM_001124147.1.
DR RefSeq; NP_001322698.1; NM_001334854.1.
DR RefSeq; NP_565195.1; NM_106541.4.
DR AlphaFoldDB; Q56ZN6; -.
DR SMR; Q56ZN6; -.
DR BioGRID; 29450; 29.
DR IntAct; Q56ZN6; 28.
DR STRING; 3702.AT1G78920.2; -.
DR TCDB; 3.A.10.2.3; the h(+), na(+)-translocating pyrophosphatase (m(+)-ppase) family.
DR SwissPalm; Q56ZN6; -.
DR PaxDb; Q56ZN6; -.
DR PRIDE; Q56ZN6; -.
DR ProteomicsDB; 241154; -.
DR EnsemblPlants; AT1G78920.1; AT1G78920.1; AT1G78920.
DR EnsemblPlants; AT1G78920.2; AT1G78920.2; AT1G78920.
DR EnsemblPlants; AT1G78920.3; AT1G78920.3; AT1G78920.
DR GeneID; 844231; -.
DR Gramene; AT1G78920.1; AT1G78920.1; AT1G78920.
DR Gramene; AT1G78920.2; AT1G78920.2; AT1G78920.
DR Gramene; AT1G78920.3; AT1G78920.3; AT1G78920.
DR KEGG; ath:AT1G78920; -.
DR Araport; AT1G78920; -.
DR TAIR; locus:2037543; AT1G78920.
DR eggNOG; ENOG502QPJC; Eukaryota.
DR HOGENOM; CLU_008743_3_1_1; -.
DR InParanoid; Q56ZN6; -.
DR OMA; GWKGILF; -.
DR OrthoDB; 257116at2759; -.
DR PhylomeDB; Q56ZN6; -.
DR BioCyc; ARA:AT1G78920-MON; -.
DR BRENDA; 7.1.3.1; 399.
DR SABIO-RK; Q56ZN6; -.
DR PRO; PR:Q56ZN6; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q56ZN6; baseline and differential.
DR Genevisible; Q56ZN6; AT.
DR GO; GO:0005768; C:endosome; HDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
DR GO; GO:0000137; C:Golgi cis cisterna; HDA:TAIR.
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:0005802; C:trans-Golgi network; HDA:TAIR.
DR GO; GO:0005773; C:vacuole; HDA:TAIR.
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; 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 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 2"
FT /id="PRO_0000217040"
FT TRANSMEM 45..65
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..488
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; 85133 MW; E9C4891A33DD65BD CRC64;
MMMDEDVEQA SLMSFNDRPR AFPNMRSKTY SPLIFRIIRK LNVRVLSIIL LFCFGAIFYM
GASTSPIIVF VFTVCIISFL LSIYLTKWVL AKDEGPPEMV EISDAIRDGA EGFFRTQYST
ISKMAILLAF VILCIYLFRS LTPQQEAAGL GRAMSAYITV AAFLLGALCS GIAGYVGMWV
SVRANVRVSS AARRSAREAL QIAVRAGGFS ALVVVGMAVI GIAILYSTFY VWLGVGSPGS
MNVTDLPLLL VGYGFGASFV ALFAQLGGGI YTKGADVGAD LVGKVEQGIP EDDPRNPAVI
ADLVGDNVGD CAARGADLFE SIAAEIISAM ILGGTMAKKC KIEDPSGFIL FPLVVHSFDL
IISSIGILSI KGTRDASVKS PVEDPMAVLQ KGYSLTIILA VITFGASTRW LLYTEQAPSA
WFNFALCGLV GIITAYIFVW ISKYYTDYKH EPVRTLALAS STGHGTNIIA GVSLGLESTA
LPVLTISVAI ISAYWLGNTS GLVDENGIPT GGLFGTAVAT MGMLSTAAYV LTMDMFGPIA
DNAGGIVEMS QQPESVREIT DLLDAVGNTT KATTKGFAIG SAALASFLLF SAYMDEVSAF
ANVSFKEVDI AIPEVFVGGL LGAMLIFLFS AWACAAVGRT AQEVVNEVRR QFIERPGIME
YKEKPDYSRC VAIVASAALR EMIKPGALAI ASPIVVGLVF RILGYYTGQP LLGAKVVASM
LMFATVCGIL MALFLNTAGG AWDNAKKYIE TGALGGKGSE AHKAAVTGDT VGDPFKDTAG
PSIHVLIKML ATITLVMAPV FL
