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Q56ZN6 (AVP2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 56. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Pyrophosphate-energized membrane proton pump 2

EC=3.6.1.1
Alternative name(s):
AVP1-like protein 1
Pyrophosphate-energized inorganic pyrophosphatase 2
Short name=H(+)-PPase 2
Vacuolar proton pyrophosphatase 2
Gene names
Name:AVPL1
Synonyms:AVP2
Ordered Locus Names:At1g78920
ORF Names:F9K20.2
OrganismArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length802 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Diphosphate + H2O = 2 phosphate.

Enzyme regulation

Activated by Mg+ but not by K+. Inhibited by Ca2+. Ref.1

Subunit structure

Monomer.

Subcellular location

Golgi apparatus membrane; Multi-pass membrane protein Ref.7 Ref.8.

Tissue specificity

Ubiquitous. Mostly expressed in cotyledons, roots and flowers. Especially high levels in trichomes, sepals and stamen filaments. Ref.1 Ref.8

Sequence similarities

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

Caution

It is uncertain whether Met-1, Met-2 or Met-3 is the initiator.

Biophysicochemical properties

Kinetic parameters:

KM=90 µM for PPi (at pH 8 and 37 degrees Celsius) Ref.1

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

Sequence caution

The sequence AAC83018.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence AAF31163.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAF31164.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAD94402.1 differs from that shown. Reason: Frameshift at position 301.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 802802Pyrophosphate-energized membrane proton pump 2
PRO_0000217040

Regions

Transmembrane45 – 6521Helical; Potential
Transmembrane66 – 8621Helical; Potential
Transmembrane118 – 13821Helical; Potential
Transmembrane160 – 18021Helical; Potential
Transmembrane206 – 22621Helical; Potential
Transmembrane246 – 26621Helical; Potential
Transmembrane348 – 36821Helical; Potential
Transmembrane386 – 40621Helical; Potential
Transmembrane421 – 44121Helical; Potential
Transmembrane452 – 47423Helical; Potential
Transmembrane479 – 49618Helical; Potential
Transmembrane511 – 53121Helical; Potential
Transmembrane577 – 59721Helical; Potential
Transmembrane615 – 63521Helical; Potential
Transmembrane686 – 70621Helical; Potential
Transmembrane716 – 73621Helical; Potential
Transmembrane782 – 80221Helical; Potential

Sequences

Sequence LengthMass (Da)Tools
Q56ZN6 [UniParc].

Last modified December 6, 2005. Version 2.
Checksum: E9C4891A33DD65BD

FASTA80285,133
        10         20         30         40         50         60 
MMMDEDVEQA SLMSFNDRPR AFPNMRSKTY SPLIFRIIRK LNVRVLSIIL LFCFGAIFYM 

        70         80         90        100        110        120 
GASTSPIIVF VFTVCIISFL LSIYLTKWVL AKDEGPPEMV EISDAIRDGA EGFFRTQYST 

       130        140        150        160        170        180 
ISKMAILLAF VILCIYLFRS LTPQQEAAGL GRAMSAYITV AAFLLGALCS GIAGYVGMWV 

       190        200        210        220        230        240 
SVRANVRVSS AARRSAREAL QIAVRAGGFS ALVVVGMAVI GIAILYSTFY VWLGVGSPGS 

       250        260        270        280        290        300 
MNVTDLPLLL VGYGFGASFV ALFAQLGGGI YTKGADVGAD LVGKVEQGIP EDDPRNPAVI 

       310        320        330        340        350        360 
ADLVGDNVGD CAARGADLFE SIAAEIISAM ILGGTMAKKC KIEDPSGFIL FPLVVHSFDL 

       370        380        390        400        410        420 
IISSIGILSI KGTRDASVKS PVEDPMAVLQ KGYSLTIILA VITFGASTRW LLYTEQAPSA 

       430        440        450        460        470        480 
WFNFALCGLV GIITAYIFVW ISKYYTDYKH EPVRTLALAS STGHGTNIIA GVSLGLESTA 

       490        500        510        520        530        540 
LPVLTISVAI ISAYWLGNTS GLVDENGIPT GGLFGTAVAT MGMLSTAAYV LTMDMFGPIA 

       550        560        570        580        590        600 
DNAGGIVEMS QQPESVREIT DLLDAVGNTT KATTKGFAIG SAALASFLLF SAYMDEVSAF 

       610        620        630        640        650        660 
ANVSFKEVDI AIPEVFVGGL LGAMLIFLFS AWACAAVGRT AQEVVNEVRR QFIERPGIME 

       670        680        690        700        710        720 
YKEKPDYSRC VAIVASAALR EMIKPGALAI ASPIVVGLVF RILGYYTGQP LLGAKVVASM 

       730        740        750        760        770        780 
LMFATVCGIL MALFLNTAGG AWDNAKKYIE TGALGGKGSE AHKAAVTGDT VGDPFKDTAG 

       790        800 
PSIHVLIKML ATITLVMAPV FL 

« Hide

References

« Hide 'large scale' references
[1]"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: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], ENZYME REGULATION, TISSUE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES.
Strain: cv. Columbia.
[2]"Isolation of a cDNA for a H+-pyrophosphatase-like protein from Arabidopsis thaliana and its functional expression in yeast."
Nakanishi Y., Maeshima M.
Plant Gene Register PGR00-026
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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]"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 502-801.
Strain: cv. Columbia.
[7]"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.
[8]"Novel type Arabidopsis thaliana H(+)-PPase is localized to the Golgi apparatus."
Mitsuda N., Enami K., Nakata M., Takeyasu K., Sato M.H.
FEBS Lett. 488:29-33(2001) [PubMed: 11163790] [Abstract]
Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF182813 mRNA. Translation: AAF31163.1. Different initiation.
AF184917 Genomic DNA. Translation: AAF31164.1. Different initiation.
AB034696 mRNA. Translation: BAA92151.1.
AC005679 Genomic DNA. Translation: AAC83018.1. Sequence problems.
CP002684 Genomic DNA. Translation: AEE36177.1.
CP002684 Genomic DNA. Translation: AEE36178.1.
AY054485 mRNA. Translation: AAK96676.1.
BT010353 mRNA. Translation: AAQ56796.1.
AK220927 mRNA. Translation: BAD94402.1. Sequence problems.
IPIIPI00570542.
PIRH96818.
RefSeqNP_001117619.1. NM_001124147.1.
NP_565195.1. NM_106541.3.
UniGeneAt.474.
At.70012.

3D structure databases

ProteinModelPortalQ56ZN6.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ56ZN6.

Protein family/group databases

TCDB3.A.10.2.3. H+-translocating pyrophosphatase (H+-PPase) family.

Proteomic databases

PRIDEQ56ZN6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT1G78920.1; AT1G78920.1; AT1G78920.
AT1G78920.2; AT1G78920.2; AT1G78920.
GeneID844231.
GenomeReviewsGene locus AT1G78920 in contig CT485782_GR.
KEGGath:AT1G78920.
NMPDRfig|3702.1.peg.7451.

Organism-specific databases

GeneFarm5160. 491.
TAIRAt1g78920.

Phylogenomic databases

eggNOGeuNOG15486.
GeneTreeEPGT00070000030400.
HOGENOMHBG593668.
InParanoidQ56ZN6.
OMAAINRGFF.
PhylomeDBQ56ZN6.
ProtClustDBPLN02277.

Enzyme and pathway databases

BRENDA3.6.1.1. 399.

Gene expression databases

GenevestigatorQ56ZN6.
GermOnlineAT1G78920. Arabidopsis thaliana.

Family and domain databases

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

Entry information

Entry nameAVP2_ARATH
AccessionPrimary (citable) accession number: Q56ZN6
Secondary accession number(s): Q9LDJ4, Q9MB70, Q9ZVB1
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: December 6, 2005
Last modified: December 14, 2011
This is version 56 of the entry and version 2 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