P31414 (AVP1_ARATH) Reviewed, UniProtKB/Swiss-Prot
Last modified
December 14, 2011.
Version 98.
History...
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended 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 |
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| Organism | Arabidopsis thaliana (Mouse-ear cress) | ||||||||
| Taxonomic identifier | 3702 [NCBI] | ||||||||
| Taxonomic lineage | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis |
Protein attributes
| Sequence length | 770 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence 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
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 key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 770 | 770 | Pyrophosphate-energized vacuolar membrane proton pump 1 | PRO_0000217039 | |||||
Regions | |||||||||
| Transmembrane | 14 – 34 | 21 | Helical; Potential | ||||||
| Transmembrane | 101 – 121 | 21 | Helical; Potential | ||||||
| Transmembrane | 143 – 163 | 21 | Helical; Potential | ||||||
| Transmembrane | 196 – 216 | 21 | Helical; Potential | ||||||
| Transmembrane | 328 – 348 | 21 | Helical; Potential | ||||||
| Transmembrane | 369 – 389 | 21 | Helical; Potential | ||||||
| Transmembrane | 406 – 426 | 21 | Helical; Potential | ||||||
| Transmembrane | 485 – 505 | 21 | Helical; Potential | ||||||
| Transmembrane | 543 – 563 | 21 | Helical; Potential | ||||||
| Transmembrane | 574 – 594 | 21 | Helical; Potential | ||||||
| Transmembrane | 646 – 666 | 21 | Helical; Potential | ||||||
| Transmembrane | 668 – 688 | 21 | Helical; Potential | ||||||
| Transmembrane | 747 – 767 | 21 | Helical; Potential | ||||||
Experimental info | |||||||||
| Mutagenesis | 119 | 1 | E → Q: Slight reduction of PPi hydrolysis and H(+) translocation. Ref.11 | ||||||
| Mutagenesis | 229 | 1 | E → D: Slight increased PPi hydrolysis and H(+) translocation. Ref.11 | ||||||
| Mutagenesis | 229 | 1 | E → Q: Slight reduction of PPi hydrolysis and H(+) translocation. Ref.11 | ||||||
| Mutagenesis | 305 | 1 | E → D: Abolishes H(+) translocation and strong reduction of PPi hydrolysis. Ref.11 | ||||||
| Mutagenesis | 305 | 1 | E → Q: Abolishes H(+) translocation and strong reduction of PPi hydrolysis, reduced sensitivity to DCCD. Ref.11 | ||||||
| Mutagenesis | 427 | 1 | E → D: Increases H(+) translocation, normal PPi hydrolysis. Ref.11 | ||||||
| Mutagenesis | 427 | 1 | E → Q: Strong reduction of PPi hydrolysis and H(+) translocation. Ref.11 | ||||||
| Mutagenesis | 504 | 1 | D → E: Abolishes H(+) translocation and strong reduction of PPi hydrolysis. Ref.11 | ||||||
| Mutagenesis | 504 | 1 | D → N: Abolishes H(+) translocation and strong reduction of PPi hydrolysis, reduced sensitivity to DCCD. Ref.11 | ||||||
| Mutagenesis | 573 | 1 | D → N: Increases H(+) translocation, normal PPi hydrolysis. Ref.11 | ||||||
| Mutagenesis | 634 | 1 | C → A or S: Reduced sensitivity to NEM. Ref.10 | ||||||
| Mutagenesis | 667 | 1 | E → Q: Slight reduction of PPi hydrolysis and H(+) translocation. Ref.11 | ||||||
| Mutagenesis | 751 | 1 | E → Q: Slight reduction of PPi hydrolysis and H(+) translocation. Ref.11 | ||||||
| Sequence conflict | 8 | 1 | P → L in BAA32210. Ref.2 | ||||||
| Sequence conflict | 576 | 1 | T → A in CAA79038. Ref.6 | ||||||
| Sequence conflict | 584 | 1 | L → P in CAA79038. Ref.6 | ||||||
| Sequence conflict | 624 | 1 | E → K in AAL57660. Ref.5 | ||||||
| Sequence conflict | 685 | 1 | I → T in AAL84953. Ref.5 | ||||||
Sequences
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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. 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. 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. 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. 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. |
| IPI | IPI00521876. |
| PIR | A38230. |
| RefSeq | NP_173021.1. NM_101437.4. |
| UniGene | At.21942. At.66944. At.67102. At.74973. |
3D structure databases | |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | P31414. |
Protein family/group databases | |
| TCDB | 3.A.10.1.1. H+-translocating pyrophosphatase (H+-PPase) family. |
Proteomic databases | |
| PRIDE | P31414. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblPlants | AT1G15690.1; AT1G15690.1; AT1G15690. |
| GeneID | 838138. |
| GenomeReviews | Gene locus AT1G15690 in contig CT485782_GR. |
| KEGG | ath:AT1G15690. |
| NMPDR | fig|3702.1.peg.1875. |
Organism-specific databases | |
| GeneFarm | 5159. 491. |
| TAIR | At1g15690. |
Phylogenomic databases | |
| InParanoid | P31414. |
| OMA | MAITSIV. |
| PhylomeDB | P31414. |
| ProtClustDB | PLN02255. |
Enzyme and pathway databases | |
| BRENDA | 3.6.1.1. 399. |
Gene expression databases | |
| ArrayExpress | P31414. |
| Genevestigator | P31414. |
| GermOnline | AT1G15690. Arabidopsis thaliana. |
Family and domain databases | |
| InterPro | IPR004131. PPase-energised_H-pump. [Graphical view] |
| KO | K01507. |
| Pfam | PF03030. H_PPase. 1 hit. [Graphical view] |
| PIRSF | PIRSF001265. H+-PPase. 1 hit. |
| TIGRFAMs | TIGR01104. V_PPase. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | AVP1_ARATH | ||||||||
| Accession | Primary (citable) accession number: P31414 Secondary accession number(s): O80390 Q8VZE3 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Plant Protein Annotation Program | ||||||||
Relevant documents
| Arabidopsis thaliana Arabidopsis thaliana: entries and gene names |
| SIMILARITY comments Index of protein domains and families |

Clusters with