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P31414 (AVP1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Pyrophosphate-energized vacuolar membrane proton pump 1

EC=3.6.1.1
Alternative name(s):
Pyrophosphate-energized inorganic pyrophosphatase 1
Short name=H(+)-PPase 1
Vacuolar proton pyrophosphatase 1
Vacuolar proton pyrophosphatase 3
Gene names
Name:AVP1
Synonyms:AVP, AVP-3, AVP3
Ordered Locus Names:At1g15690
ORF Names:F7H2.3
OrganismArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length770 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.9 Ref.13 Ref.16

Catalytic activity

Diphosphate + H2O = 2 phosphate.

Enzyme regulation

Activated by K+ and Mg2+. Inhibited by Ca2+, N,N'-dicyclohexylcarbodiimide (DCCD), N-ethylmaleimide (NEM) and aminomethylenediphosphonate (AMDP), and, to a lower extent, by fluoride (KF). Ref.8 Ref.9 Ref.11 Ref.12

Subunit structure

Monomer.

Subcellular location

Vacuole membrane; Multi-pass membrane protein. Endosome membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein. Note: Mostly vacuolar, tonoplast. Also present in endosomes and plasma membrane. Ref.9 Ref.15 Ref.16

Tissue specificity

Ubiquitous (at protein level). Mostly expressed in vascular tissues, meristems and root pericycle. Ref.2 Ref.16

Developmental stage

Increase of expression in pollen during flower development. Expressed in developing leaves, sepals, petals, stamens and carpels. Ref.2 Ref.16

Induction

Repressed by light. Induced by CAMTA1 and/or CAMTA5 in pollen. Ref.2 Ref.8 Ref.9 Ref.11 Ref.12 Ref.14

Sequence similarities

Belongs to the H(+)-translocating pyrophosphatase (TC 3.A.10) family. K(+)-stimulated subfamily. [View classification]

Biophysicochemical properties

Kinetic parameters:

KM=110 µM for PPi (at pH 8 and 37 degrees Celsius) Ref.10 Ref.12

Vmax=0.5 µmol/min/mg enzyme (at pH 8 and 37 degrees Celsius)

Sequence caution

The sequence BAD94555.1 differs from that shown. Reason: Erroneous initiation.

The sequence CAA79039.1 differs from that shown. Reason: Frameshift at position 718.

Ontologies

Keywords
   Biological processHydrogen ion transport
Ion transport
Transport
   Cellular componentCell membrane
Endosome
Membrane
Vacuole
   Coding sequence diversityAlternative splicing
   DomainTransmembrane
Transmembrane helix
   LigandMagnesium
   Molecular functionHydrolase
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological processauxin polar transport

Inferred from genetic interaction Ref.16. Source: TAIR

establishment or maintenance of transmembrane electrochemical gradient

Traceable author statement Ref.1. Source: TAIR

leaf development

Inferred from mutant phenotype. Source: TAIR

proton transport

Inferred from electronic annotation. Source: UniProtKB-KW

response to salt stress

Inferred from mutant phenotype Ref.13. Source: TAIR

response to water deprivation

Inferred from mutant phenotype Ref.13. Source: TAIR

   Cellular componentchloroplast envelope

Inferred from direct assay. Source: TAIR

endosome membrane

Inferred from direct assay Ref.16. Source: TAIR

integral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

mitochondrion

Inferred from direct assay. Source: TAIR

plant-type vacuole membrane

Inferred from direct assay Ref.1. Source: TAIR

plasma membrane

Inferred from direct assay Ref.16. Source: TAIR

   Molecular functionhydrogen-translocating pyrophosphatase activity

Inferred from direct assay Ref.1. Source: TAIR

inorganic diphosphatase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms are produced. According to EST sequences.
Isoform 1 (identifier: P31414-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 770770Pyrophosphate-energized vacuolar membrane proton pump 1
PRO_0000217039

Regions

Transmembrane14 – 3421Helical; Potential
Transmembrane101 – 12121Helical; Potential
Transmembrane143 – 16321Helical; Potential
Transmembrane196 – 21621Helical; Potential
Transmembrane328 – 34821Helical; Potential
Transmembrane369 – 38921Helical; Potential
Transmembrane406 – 42621Helical; Potential
Transmembrane485 – 50521Helical; Potential
Transmembrane543 – 56321Helical; Potential
Transmembrane574 – 59421Helical; Potential
Transmembrane646 – 66621Helical; Potential
Transmembrane668 – 68821Helical; Potential
Transmembrane747 – 76721Helical; Potential

Experimental info

Mutagenesis1191E → Q: Slight reduction of PPi hydrolysis and H(+) translocation. Ref.11
Mutagenesis2291E → D: Slight increased PPi hydrolysis and H(+) translocation. Ref.11
Mutagenesis2291E → Q: Slight reduction of PPi hydrolysis and H(+) translocation. Ref.11
Mutagenesis3051E → D: Abolishes H(+) translocation and strong reduction of PPi hydrolysis. Ref.11
Mutagenesis3051E → Q: Abolishes H(+) translocation and strong reduction of PPi hydrolysis, reduced sensitivity to DCCD. Ref.11
Mutagenesis4271E → D: Increases H(+) translocation, normal PPi hydrolysis. Ref.11
Mutagenesis4271E → Q: Strong reduction of PPi hydrolysis and H(+) translocation. Ref.11
Mutagenesis5041D → E: Abolishes H(+) translocation and strong reduction of PPi hydrolysis. Ref.11
Mutagenesis5041D → N: Abolishes H(+) translocation and strong reduction of PPi hydrolysis, reduced sensitivity to DCCD. Ref.11
Mutagenesis5731D → N: Increases H(+) translocation, normal PPi hydrolysis. Ref.11
Mutagenesis6341C → A or S: Reduced sensitivity to NEM. Ref.10
Mutagenesis6671E → Q: Slight reduction of PPi hydrolysis and H(+) translocation. Ref.11
Mutagenesis7511E → Q: Slight reduction of PPi hydrolysis and H(+) translocation. Ref.11
Sequence conflict81P → L in BAA32210. Ref.2
Sequence conflict5761T → A in CAA79038. Ref.6
Sequence conflict5841L → P in CAA79038. Ref.6
Sequence conflict6241E → K in AAL57660. Ref.5
Sequence conflict6851I → T in AAL84953. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 1, 1993. Version 1.
Checksum: CE7132B42B299860

FASTA77080,820
        10         20         30         40         50         60 
MVAPALLPEL WTEILVPICA VIGIAFSLFQ WYVVSRVKLT SDLGASSSGG ANNGKNGYGD 

        70         80         90        100        110        120 
YLIEEEEGVN DQSVVAKCAE IQTAISEGAT SFLFTEYKYV GVFMIFFAAV IFVFLGSVEG 

       130        140        150        160        170        180 
FSTDNKPCTY DTTRTCKPAL ATAAFSTIAF VLGAVTSVLS GFLGMKIATY ANARTTLEAR 

       190        200        210        220        230        240 
KGVGKAFIVA FRSGAVMGFL LAASGLLVLY ITINVFKIYY GDDWEGLFEA ITGYGLGGSS 

       250        260        270        280        290        300 
MALFGRVGGG IYTKAADVGA DLVGKIERNI PEDDPRNPAV IADNVGDNVG DIAGMGSDLF 

       310        320        330        340        350        360 
GSYAEASCAA LVVASISSFG INHDFTAMCY PLLISSMGIL VCLITTLFAT DFFEIKLVKE 

       370        380        390        400        410        420 
IEPALKNQLI ISTVIMTVGI AIVSWVGLPT SFTIFNFGTQ KVVKNWQLFL CVCVGLWAGL 

       430        440        450        460        470        480 
IIGFVTEYYT SNAYSPVQDV ADSCRTGAAT NVIFGLALGY KSVIIPIFAI AISIFVSFSF 

       490        500        510        520        530        540 
AAMYGVAVAA LGMLSTIATG LAIDAYGPIS DNAGGIAEMA GMSHRIRERT DALDAAGNTT 

       550        560        570        580        590        600 
AAIGKGFAIG SAALVSLALF GAFVSRAGIH TVDVLTPKVI IGLLVGAMLP YWFSAMTMKS 

       610        620        630        640        650        660 
VGSAALKMVE EVRRQFNTIP GLMEGTAKPD YATCVKISTD ASIKEMIPPG CLVMLTPLIV 

       670        680        690        700        710        720 
GFFFGVETLS GVLAGSLVSG VQIAISASNT GGAWDNAKKY IEAGVSEHAK SLGPKGSEPH 

       730        740        750        760        770 
KAAVIGDTIG DPLKDTSGPS LNILIKLMAV ESLVFAPFFA THGGILFKYF 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning and sequence of cDNA encoding the pyrophosphate-energized vacuolar membrane proton pump of Arabidopsis thaliana."
Sarafian V., Kim Y., Poole R.J., Rea P.A.
Proc. Natl. Acad. Sci. U.S.A. 89:1775-1779(1992) [PubMed: 1311852] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Columbia.
[2]"Pollen-specific regulation of vacuolar H(+)-PPase expression by multiple cis-acting elements."
Mitsuda N., Takeyasu K., Sato M.H.
Plant Mol. Biol. 46:185-192(2001) [PubMed: 11442058] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, INDUCTION, DEVELOPMENTAL STAGE.
Strain: cv. Columbia.
Tissue: Leaf.
[3]"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
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. expand/collapse author list , 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.
Nature 408:816-820(2000) [PubMed: 11130712] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[4]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[5]"Empirical analysis of transcriptional activity in the Arabidopsis genome."
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. expand/collapse author list , 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.
Science 302:842-846(2003) [PubMed: 14593172] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[6]"An inventory of 1152 expressed sequence tags obtained by partial sequencing of cDNAs from Arabidopsis thaliana."
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. expand/collapse author list , Grellet F., Delseny M., Parmentier Y., de Marcillac G., Gigot C., Fleck J., Philipps G., Axelos M., Bardet C., Tremousaygue D., Lescure B.
Plant J. 4:1051-1061(1993) [PubMed: 8281187] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 554-671 AND 716-770.
Strain: cv. Columbia.
Tissue: Green siliques.
[7]"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
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. expand/collapse author list , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 595-770.
Strain: cv. Columbia.
[8]"Localization of cytosolically oriented maleimide-reactive domain of vacuolar H(+)-pyrophosphatase."
Zhen R.-G., Kim E.J., Rea P.A.
J. Biol. Chem. 269:23342-23350(1994) [PubMed: 8083239] [Abstract]
Cited for: PROTEIN SEQUENCE OF 625-640, ENZYME REGULATION.
[9]"Heterologous expression of plant vacuolar pyrophosphatase in yeast demonstrates sufficiency of the substrate-binding subunit for proton transport."
Kim E.J., Zhen R.-G., Rea P.A.
Proc. Natl. Acad. Sci. U.S.A. 91:6128-6132(1994) [PubMed: 8016125] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, ENZYME REGULATION.
[10]"Site-directed mutagenesis of vacuolar H(+)-pyrophosphatase. Necessity of Cys634 for inhibition by maleimides but not catalysis."
Kim E.J., Zhen R.-G., Rea P.A.
J. Biol. Chem. 270:2630-2635(1995) [PubMed: 7852329] [Abstract]
Cited for: MUTAGENESIS OF CYS-634, BIOPHYSICOCHEMICAL PROPERTIES.
[11]"Acidic residues necessary for pyrophosphate-energized pumping and inhibition of the vacuolar H(+)-pyrophosphatase by N,N'-dicyclohexylcarbodiimide."
Zhen R.-G., Kim E.J., Rea P.A.
J. Biol. Chem. 272:22340-22348(1997) [PubMed: 9268385] [Abstract]
Cited for: ENZYME REGULATION, MUTAGENESIS OF GLU-119; GLU-229; GLU-305; GLU-427; ASP-504; ASP-573; GLU-667 AND GLU-751.
[12]"AVP2, a sequence-divergent, K(+)-insensitive H(+)-translocating inorganic pyrophosphatase from Arabidopsis."
Drozdowicz Y.M., Kissinger J.C., Rea P.A.
Plant Physiol. 123:353-362(2000) [PubMed: 10806252] [Abstract]
Cited for: ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
Strain: cv. Columbia.
[13]"Drought- and salt-tolerant plants result from overexpression of the AVP1 H(+)-pump."
Gaxiola R.A., Li J., Undurraga S., Dang L.M., Allen G.J., Alper S.L., Fink G.R.
Proc. Natl. Acad. Sci. U.S.A. 98:11444-11449(2001) [PubMed: 11572991] [Abstract]
Cited for: FUNCTION.
[14]"Arabidopsis CAMTA family proteins enhance V-PPase expression in pollen."
Mitsuda N., Isono T., Sato M.H.
Plant Cell Physiol. 44:975-981(2003) [PubMed: 14581622] [Abstract]
Cited for: INDUCTION.
[15]"Isolation of intact vacuoles and proteomic analysis of tonoplast from suspension-cultured cells of Arabidopsis thaliana."
Shimaoka T., Ohnishi M., Sazuka T., Mitsuhashi N., Hara-Nishimura I., Shimazaki K., Maeshima M., Yokota A., Tomizawa K., Mimura T.
Plant Cell Physiol. 45:672-683(2004) [PubMed: 15215502] [Abstract]
Cited for: SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
[16]"Arabidopsis H(+)-PPase AVP1 regulates auxin-mediated organ development."
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.
Science 310:121-125(2005) [PubMed: 16210544] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M81892 mRNA. Translation: AAA32754.1.
AB015138 Genomic DNA. Translation: BAA32210.1.
AC034256 Genomic DNA. Translation: AAF82139.1.
CP002684 Genomic DNA. Translation: AEE29349.1.
AY065016 mRNA. Translation: AAL57660.1.
AY078953 mRNA. Translation: AAL84953.1.
BT002481 mRNA. Translation: AAO00841.1.
Z17694 mRNA. Translation: CAA79038.1.
Z17695 mRNA. Translation: CAA79039.1. Frameshift.
AK221989 mRNA. Translation: BAD94555.1. Different initiation.
IPIIPI00521876.
PIRA38230.
RefSeqNP_173021.1. NM_101437.4.
UniGeneAt.21942.
At.66944.
At.67102.
At.74973.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGP31414.

Protein family/group databases

TCDB3.A.10.1.1. H+-translocating pyrophosphatase (H+-PPase) family.

Proteomic databases

PRIDEP31414.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT1G15690.1; AT1G15690.1; AT1G15690.
GeneID838138.
GenomeReviewsGene locus AT1G15690 in contig CT485782_GR.
KEGGath:AT1G15690.
NMPDRfig|3702.1.peg.1875.

Organism-specific databases

GeneFarm5159. 491.
TAIRAt1g15690.

Phylogenomic databases

InParanoidP31414.
OMAMAITSIV.
PhylomeDBP31414.
ProtClustDBPLN02255.

Enzyme and pathway databases

BRENDA3.6.1.1. 399.

Gene expression databases

ArrayExpressP31414.
GenevestigatorP31414.
GermOnlineAT1G15690. Arabidopsis thaliana.

Family and domain databases

InterProIPR004131. PPase-energised_H-pump.
[Graphical view]
KOK01507.
PfamPF03030. H_PPase. 1 hit.
[Graphical view]
PIRSFPIRSF001265. H+-PPase. 1 hit.
TIGRFAMsTIGR01104. V_PPase. 1 hit.
ProtoNetSearch...

Entry information

Entry nameAVP1_ARATH
AccessionPrimary (citable) accession number: P31414
Secondary accession number(s): O80390 expand/collapse secondary AC list , Q41919, Q41920, Q56WP6, Q8RY20, Q8VZE3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: December 14, 2011
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

SIMILARITY comments

Index of protein domains and families