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Protein

V-type proton ATPase subunit G2

Gene

VHA-G2

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic subunit of the peripheral V1 complex of vacuolar ATPase (V-ATPase). V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Hydrogen ion transport, Ion transport, Transport

Protein family/group databases

TCDBi3.A.2.2.5. the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.

Names & Taxonomyi

Protein namesi
Recommended name:
V-type proton ATPase subunit G2
Short name:
V-ATPase subunit G2
Alternative name(s):
Vacuolar H(+)-ATPase subunit G isoform 2
Vacuolar proton pump subunit G2
Gene namesi
Name:VHA-G2
Synonyms:VAG2, VATG2
Ordered Locus Names:At4g23710
ORF Names:F9D16.180
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 4

Organism-specific databases

TAIRiAT4G23710.

Subcellular locationi

GO - Cellular componenti

  • Golgi apparatus Source: TAIR
  • vacuolar membrane Source: TAIR
  • vacuolar proton-transporting V-type ATPase complex Source: InterPro
  • vacuole Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Vacuole

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 106106V-type proton ATPase subunit G2PRO_0000192909Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiO82629.
PRIDEiO82629.

PTM databases

iPTMnetiO82629.

Expressioni

Gene expression databases

ExpressionAtlasiO82629. baseline and differential.
GenevisibleiO82629. AT.

Interactioni

Subunit structurei

V-ATPase is a heteromultimeric enzyme composed of a peripheral catalytic V1 complex (components A to H) attached to an integral membrane V0 proton pore complex (components: a, c, c'', d and e).

Protein-protein interaction databases

STRINGi3702.AT4G23710.1.

Structurei

3D structure databases

ProteinModelPortaliO82629.
SMRiO82629. Positions 2-105.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the V-ATPase G subunit family.Curated

Phylogenomic databases

eggNOGiKOG1772. Eukaryota.
ENOG4111XX0. LUCA.
HOGENOMiHOG000186416.
InParanoidiO82629.
KOiK02152.
OMAiRTAKMTR.
PhylomeDBiO82629.

Family and domain databases

InterProiIPR005124. V-ATPase_G.
[Graphical view]
PANTHERiPTHR12713. PTHR12713. 1 hit.
TIGRFAMsiTIGR01147. V_ATP_synt_G. 1 hit.

Sequencei

Sequence statusi: Complete.

O82629-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MESAGIQQLL AAEREAQQIV NAARTAKMTR LKQAKEEAET EVAEHKTSTE
60 70 80 90 100
QGFQRKLEAT SGDSGANVKR LEQETDAKIE QLKNEATRIS KDVVDMLLKN

VTTVNN
Length:106
Mass (Da):11,742
Last modified:January 24, 2001 - v2
Checksum:i78A8677D45BC8AB4
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti15 – 151E → K in CAA06759 (Ref. 1) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ005902 mRNA. Translation: CAA06759.1.
AL035394 Genomic DNA. Translation: CAA23037.1.
AL161560 Genomic DNA. Translation: CAB81289.1.
CP002687 Genomic DNA. Translation: AEE84797.1.
BT003107 mRNA. Translation: AAO24539.1.
PIRiT05603.
T51826.
RefSeqiNP_194102.1. NM_118502.2.
UniGeneiAt.161.

Genome annotation databases

EnsemblPlantsiAT4G23710.1; AT4G23710.1; AT4G23710.
GeneIDi828471.
GrameneiAT4G23710.1; AT4G23710.1; AT4G23710.
KEGGiath:AT4G23710.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ005902 mRNA. Translation: CAA06759.1.
AL035394 Genomic DNA. Translation: CAA23037.1.
AL161560 Genomic DNA. Translation: CAB81289.1.
CP002687 Genomic DNA. Translation: AEE84797.1.
BT003107 mRNA. Translation: AAO24539.1.
PIRiT05603.
T51826.
RefSeqiNP_194102.1. NM_118502.2.
UniGeneiAt.161.

3D structure databases

ProteinModelPortaliO82629.
SMRiO82629. Positions 2-105.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3702.AT4G23710.1.

Protein family/group databases

TCDBi3.A.2.2.5. the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.

PTM databases

iPTMnetiO82629.

Proteomic databases

PaxDbiO82629.
PRIDEiO82629.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G23710.1; AT4G23710.1; AT4G23710.
GeneIDi828471.
GrameneiAT4G23710.1; AT4G23710.1; AT4G23710.
KEGGiath:AT4G23710.

Organism-specific databases

TAIRiAT4G23710.

Phylogenomic databases

eggNOGiKOG1772. Eukaryota.
ENOG4111XX0. LUCA.
HOGENOMiHOG000186416.
InParanoidiO82629.
KOiK02152.
OMAiRTAKMTR.
PhylomeDBiO82629.

Miscellaneous databases

PROiO82629.

Gene expression databases

ExpressionAtlasiO82629. baseline and differential.
GenevisibleiO82629. AT.

Family and domain databases

InterProiIPR005124. V-ATPase_G.
[Graphical view]
PANTHERiPTHR12713. PTHR12713. 1 hit.
TIGRFAMsiTIGR01147. V_ATP_synt_G. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and expression of G subunits of vacuolar-type ATPase from plants."
    Rouquie D., Tournaire-Roux C., Szponarski W., Rossignol M., Doumas P.
    Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: cv. Columbia.
    Tissue: Leaf.
  2. "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
    Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B.
    , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
    Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  4. "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.
    , 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  5. "A simple nomenclature for a complex proton pump: VHA genes encode the vacuolar H(+)-ATPase."
    Sze H., Schumacher K., Mueller M.L., Padmanaban S., Taiz L.
    Trends Plant Sci. 7:157-161(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENE FAMILY, NOMENCLATURE.
  6. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiVATG2_ARATH
AccessioniPrimary (citable) accession number: O82629
Secondary accession number(s): Q9SUQ6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: January 24, 2001
Last modified: June 8, 2016
This is version 113 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.