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Protein

V-type proton ATPase subunit H

Gene

VHA-H

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

Functioni

Subunit of the peripheral V1 complex of vacuolar ATPase. Subunit H activates the ATPase activity of the enzyme and couples ATPase activity to proton flow. Vacuolar ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells, thus providing most of the energy required for transport processes in the vacuolar system (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Hydrogen ion transport, Ion transport, Transport

Enzyme and pathway databases

ReactomeiR-ATH-77387. Insulin receptor recycling.
R-ATH-917977. Transferrin endocytosis and recycling.

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 H
Short name:
V-ATPase subunit H
Alternative name(s):
Vacuolar H(+)-ATPase subunit H
Vacuolar proton pump subunit H
Gene namesi
Name:VHA-H
Ordered Locus Names:At3g42050
ORF Names:F4M19_10
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 3

Organism-specific databases

TAIRiAT3G42050.

Subcellular locationi

GO - Cellular componenti

  • chloroplast Source: TAIR
  • Golgi apparatus Source: TAIR
  • plant-type vacuole Source: TAIR
  • plasma membrane Source: TAIR
  • vacuolar membrane Source: TAIR
  • vacuolar proton-transporting V-type ATPase, V1 domain Source: InterPro
  • vacuole Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Vacuole

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 441441V-type proton ATPase subunit HPRO_0000124200Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiQ9LX65.
PRIDEiQ9LX65.

PTM databases

SwissPalmiQ9LX65.

Expressioni

Gene expression databases

GenevisibleiQ9LX65. 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

BioGridi8496. 2 interactions.
STRINGi3702.AT3G42050.1.

Structurei

3D structure databases

ProteinModelPortaliQ9LX65.
SMRiQ9LX65. Positions 201-430.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the V-ATPase H subunit family.Curated

Phylogenomic databases

eggNOGiKOG2759. Eukaryota.
COG5231. LUCA.
HOGENOMiHOG000012406.
InParanoidiQ9LX65.
KOiK02144.
OMAiDTLQENH.
PhylomeDBiQ9LX65.

Family and domain databases

Gene3Di1.25.10.10. 1 hit.
1.25.40.150. 1 hit.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR004908. ATPase_V1-cplx_hsu.
IPR011987. ATPase_V1-cplx_hsu_C.
[Graphical view]
PfamiPF11698. V-ATPase_H_C. 1 hit.
[Graphical view]
PIRSFiPIRSF032184. ATPase_V1_H. 1 hit.
SUPFAMiSSF48371. SSF48371. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9LX65-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDQAELSIEQ VLKRDIPWET YMNTKLVSAK GLQLLRRYDK KPESARAQLL
60 70 80 90 100
DEDGPAYVHL FVSILRDIFK EETVEYVLAL IYEMLSANPT RARLFHDESL
110 120 130 140 150
ANEDTYEPFL RLLWKGNWFI QEKSCKILAW IISARPKAGN AVIGNGIDDV
160 170 180 190 200
LKGLVEWLCA QLKQPSHPTR GVPIAISCLS SLLKEPVVRS SFVQADGVKL
210 220 230 240 250
LVPLISPAST QQSIQLLYET CLCIWLLSYY EPAIEYLATS RTMQRLTEVV
260 270 280 290 300
KHSTKEKVVR VVILTFRNLL PKGTFGAQMV DLGLPHIIHS LKTQAWSDED
310 320 330 340 350
LLDALNQLEE GLKDKIKKLS SFDKYKQEVL LGHLDWNPMH KETNFWRENV
360 370 380 390 400
TCFEENDFQI LRVLLTILDT SSDPRSLAVA CFDISQFIQY HAAGRVIVAD
410 420 430 440
LKAKERVMKL INHENAEVTK NAILCIQRLL LGAKYASFLQ A
Length:441
Mass (Da):50,284
Last modified:October 1, 2000 - v1
Checksum:iE0D57EB194158528
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL356013 Genomic DNA. Translation: CAB91576.1.
CP002686 Genomic DNA. Translation: AEE77718.1.
AY091685 mRNA. Translation: AAM10284.1.
PIRiT48960.
RefSeqiNP_189791.1. NM_114072.3.
UniGeneiAt.19846.

Genome annotation databases

EnsemblPlantsiAT3G42050.1; AT3G42050.1; AT3G42050.
GeneIDi823170.
GrameneiAT3G42050.1; AT3G42050.1; AT3G42050.
KEGGiath:AT3G42050.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL356013 Genomic DNA. Translation: CAB91576.1.
CP002686 Genomic DNA. Translation: AEE77718.1.
AY091685 mRNA. Translation: AAM10284.1.
PIRiT48960.
RefSeqiNP_189791.1. NM_114072.3.
UniGeneiAt.19846.

3D structure databases

ProteinModelPortaliQ9LX65.
SMRiQ9LX65. Positions 201-430.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi8496. 2 interactions.
STRINGi3702.AT3G42050.1.

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

SwissPalmiQ9LX65.

Proteomic databases

PaxDbiQ9LX65.
PRIDEiQ9LX65.

Protocols and materials databases

DNASUi823170.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT3G42050.1; AT3G42050.1; AT3G42050.
GeneIDi823170.
GrameneiAT3G42050.1; AT3G42050.1; AT3G42050.
KEGGiath:AT3G42050.

Organism-specific databases

TAIRiAT3G42050.

Phylogenomic databases

eggNOGiKOG2759. Eukaryota.
COG5231. LUCA.
HOGENOMiHOG000012406.
InParanoidiQ9LX65.
KOiK02144.
OMAiDTLQENH.
PhylomeDBiQ9LX65.

Enzyme and pathway databases

ReactomeiR-ATH-77387. Insulin receptor recycling.
R-ATH-917977. Transferrin endocytosis and recycling.

Miscellaneous databases

PROiQ9LX65.

Gene expression databases

GenevisibleiQ9LX65. AT.

Family and domain databases

Gene3Di1.25.10.10. 1 hit.
1.25.40.150. 1 hit.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR004908. ATPase_V1-cplx_hsu.
IPR011987. ATPase_V1-cplx_hsu_C.
[Graphical view]
PfamiPF11698. V-ATPase_H_C. 1 hit.
[Graphical view]
PIRSFiPIRSF032184. ATPase_V1_H. 1 hit.
SUPFAMiSSF48371. SSF48371. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."
    Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F.
    , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
    Nature 408:820-822(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  2. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  3. "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.
  4. "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.
  5. "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] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  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 nameiVATH_ARATH
AccessioniPrimary (citable) accession number: Q9LX65
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: October 1, 2000
Last modified: February 17, 2016
This is version 120 of the entry and version 1 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.