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Protein

V-type proton ATPase subunit B2

Gene

VHA-B2

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

Functioni

Non-catalytic subunit of the peripheral V1 complex of vacuolar 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 - Molecular functioni

Hydrolase

Keywords - Biological processi

Hydrogen ion transport, Ion transport, Transport

Enzyme and pathway databases

BioCyciARA:AT4G38510-MONOMER.
ARA:GQT-1527-MONOMER.
ARA:GQT-292-MONOMER.
ARA:GQT-293-MONOMER.
ARA:GQT-294-MONOMER.
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 B2
Short name:
V-ATPase subunit B2
Alternative name(s):
Vacuolar H(+)-ATPase subunit B isoform 2
Vacuolar proton pump subunit B2
Gene namesi
Name:VHA-B2
Ordered Locus Names:At4g38510
ORF Names:F20M13.70
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 4

Organism-specific databases

TAIRiAT4G38510.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane, Vacuole

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 487486V-type proton ATPase subunit B2PRO_0000373816Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylglycineCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiQ9SZN1.
PRIDEiQ9SZN1.

PTM databases

iPTMnetiQ9SZN1.

Expressioni

Gene expression databases

ExpressionAtlasiQ9SZN1. baseline and differential.
GenevisibleiQ9SZN1. 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

BioGridi15288. 2 interactions.
IntActiQ9SZN1. 1 interaction.
MINTiMINT-8061837.
STRINGi3702.AT4G38510.5.

Structurei

3D structure databases

ProteinModelPortaliQ9SZN1.
SMRiQ9SZN1. Positions 22-481.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ATPase alpha/beta chains family.Curated

Phylogenomic databases

eggNOGiKOG1351. Eukaryota.
COG1156. LUCA.
HOGENOMiHOG000165320.
InParanoidiQ9SZN1.
KOiK02147.
PhylomeDBiQ9SZN1.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00310. ATP_synth_B_arch.
InterProiIPR020003. ATPase_a/bsu_AS.
IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
IPR004100. ATPase_F1_a/bsu_N.
IPR005723. ATPase_V1-cplx_bsu.
IPR027417. P-loop_NTPase.
IPR022879. V-ATPase_su_B/beta.
[Graphical view]
PfamiPF00006. ATP-synt_ab. 1 hit.
PF02874. ATP-synt_ab_N. 1 hit.
[Graphical view]
PIRSFiPIRSF039114. V-ATPsynth_beta/V-ATPase_B. 1 hit.
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR01040. V-ATPase_V1_B. 1 hit.
PROSITEiPS00152. ATPASE_ALPHA_BETA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 1 isoform i produced by alternative splicing. AlignAdd to basket

Note: A number of isoforms are produced. According to EST sequences.

Isoform 1 (identifier: Q9SZN1-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MGAAENNLEM EGTLEIGMEY RTVSGVAGPL VILEKVKGPK YQEIVNIRLG
60 70 80 90 100
DGTTRRGQVL EVDGEKAVVQ VFEGTSGIDN KYTTVQFTGE VLKTPVSLDM
110 120 130 140 150
LGRIFNGSGK PIDNGPPILP EAYLDISGSS INPSERTYPE EMIQTGISTI
160 170 180 190 200
DVMNSIARGQ KIPLFSAAGL PHNEIAAQIC RQAGLVKRLE KSDNLLEHQE
210 220 230 240 250
DDNFAIVFAA MGVNMETAQF FKRDFEENGS MERVTLFLNL ANDPTIERII
260 270 280 290 300
TPRIALTTAE YLAYECGKHV LVILTDMSSY ADALREVSAA REEVPGRRGY
310 320 330 340 350
PGYMYTDLAT IYERAGRIEG RKGSITQIPI LTMPNDDITH PTPDLTGYIT
360 370 380 390 400
EGQIYIDRQL HNRQIYPPIN VLPSLSRLMK SAIGEGMTRR DHSDVSNQLY
410 420 430 440 450
ANYAIGKDVQ AMKAVVGEEA LSSEDLLYLE FLDKFERKFV AQGAYDTRNI
460 470 480
FQSLDLAWTL LRIFPRELLH RIPAKTLDQF YSRDTTN
Length:487
Mass (Da):54,305
Last modified:May 1, 2000 - v1
Checksum:i170224B66A22F1F1
GO

Sequence cautioni

The sequence AAK73967.1 differs from that shown. Reason: Frameshift at position 43. Curated
The sequence BAD95251.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti37 – 371K → R in BAH19957 (PubMed:19423640).Curated
Sequence conflicti330 – 3301I → F in BAH19957 (PubMed:19423640).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL035540 Genomic DNA. Translation: CAB37507.1.
AL161593 Genomic DNA. Translation: CAB80515.1.
CP002687 Genomic DNA. Translation: AEE86936.1.
CP002687 Genomic DNA. Translation: AEE86937.1.
CP002687 Genomic DNA. Translation: AEE86938.1.
CP002687 Genomic DNA. Translation: AEE86939.1.
AY039518 mRNA. Translation: AAK62575.1.
AY045609 mRNA. Translation: AAK73967.1. Frameshift.
AY059167 mRNA. Translation: AAL15392.1.
AY090334 mRNA. Translation: AAL90995.1.
AK317281 mRNA. Translation: BAH19957.1.
AK317596 mRNA. Translation: BAH20260.1.
AK222158 mRNA. Translation: BAD95251.1. Different initiation.
PIRiT05679.
RefSeqiNP_001031807.1. NM_001036730.2. [Q9SZN1-1]
NP_001031808.1. NM_001036731.2. [Q9SZN1-1]
NP_195563.1. NM_120012.4. [Q9SZN1-1]
NP_974707.1. NM_202978.2. [Q9SZN1-1]
UniGeneiAt.48961.
At.71095.

Genome annotation databases

EnsemblPlantsiAT4G38510.1; AT4G38510.1; AT4G38510. [Q9SZN1-1]
AT4G38510.2; AT4G38510.2; AT4G38510. [Q9SZN1-1]
AT4G38510.3; AT4G38510.3; AT4G38510. [Q9SZN1-1]
AT4G38510.4; AT4G38510.4; AT4G38510. [Q9SZN1-1]
GeneIDi830008.
KEGGiath:AT4G38510.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL035540 Genomic DNA. Translation: CAB37507.1.
AL161593 Genomic DNA. Translation: CAB80515.1.
CP002687 Genomic DNA. Translation: AEE86936.1.
CP002687 Genomic DNA. Translation: AEE86937.1.
CP002687 Genomic DNA. Translation: AEE86938.1.
CP002687 Genomic DNA. Translation: AEE86939.1.
AY039518 mRNA. Translation: AAK62575.1.
AY045609 mRNA. Translation: AAK73967.1. Frameshift.
AY059167 mRNA. Translation: AAL15392.1.
AY090334 mRNA. Translation: AAL90995.1.
AK317281 mRNA. Translation: BAH19957.1.
AK317596 mRNA. Translation: BAH20260.1.
AK222158 mRNA. Translation: BAD95251.1. Different initiation.
PIRiT05679.
RefSeqiNP_001031807.1. NM_001036730.2. [Q9SZN1-1]
NP_001031808.1. NM_001036731.2. [Q9SZN1-1]
NP_195563.1. NM_120012.4. [Q9SZN1-1]
NP_974707.1. NM_202978.2. [Q9SZN1-1]
UniGeneiAt.48961.
At.71095.

3D structure databases

ProteinModelPortaliQ9SZN1.
SMRiQ9SZN1. Positions 22-481.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi15288. 2 interactions.
IntActiQ9SZN1. 1 interaction.
MINTiMINT-8061837.
STRINGi3702.AT4G38510.5.

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

iPTMnetiQ9SZN1.

Proteomic databases

PaxDbiQ9SZN1.
PRIDEiQ9SZN1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G38510.1; AT4G38510.1; AT4G38510. [Q9SZN1-1]
AT4G38510.2; AT4G38510.2; AT4G38510. [Q9SZN1-1]
AT4G38510.3; AT4G38510.3; AT4G38510. [Q9SZN1-1]
AT4G38510.4; AT4G38510.4; AT4G38510. [Q9SZN1-1]
GeneIDi830008.
KEGGiath:AT4G38510.

Organism-specific databases

TAIRiAT4G38510.

Phylogenomic databases

eggNOGiKOG1351. Eukaryota.
COG1156. LUCA.
HOGENOMiHOG000165320.
InParanoidiQ9SZN1.
KOiK02147.
PhylomeDBiQ9SZN1.

Enzyme and pathway databases

BioCyciARA:AT4G38510-MONOMER.
ARA:GQT-1527-MONOMER.
ARA:GQT-292-MONOMER.
ARA:GQT-293-MONOMER.
ARA:GQT-294-MONOMER.
ReactomeiR-ATH-77387. Insulin receptor recycling.
R-ATH-917977. Transferrin endocytosis and recycling.

Miscellaneous databases

PROiQ9SZN1.

Gene expression databases

ExpressionAtlasiQ9SZN1. baseline and differential.
GenevisibleiQ9SZN1. AT.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00310. ATP_synth_B_arch.
InterProiIPR020003. ATPase_a/bsu_AS.
IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
IPR004100. ATPase_F1_a/bsu_N.
IPR005723. ATPase_V1-cplx_bsu.
IPR027417. P-loop_NTPase.
IPR022879. V-ATPase_su_B/beta.
[Graphical view]
PfamiPF00006. ATP-synt_ab. 1 hit.
PF02874. ATP-synt_ab_N. 1 hit.
[Graphical view]
PIRSFiPIRSF039114. V-ATPsynth_beta/V-ATPase_B. 1 hit.
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR01040. V-ATPase_V1_B. 1 hit.
PROSITEiPS00152. ATPASE_ALPHA_BETA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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.
  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. "Analysis of multiple occurrences of alternative splicing events in Arabidopsis thaliana using novel sequenced full-length cDNAs."
    Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M., Shinozaki K.
    DNA Res. 16:155-164(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  5. "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.
    , 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 198-487.
    Strain: cv. Columbia.
  6. "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.
  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] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  8. "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 GLY-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiVATB2_ARATH
AccessioniPrimary (citable) accession number: Q9SZN1
Secondary accession number(s): B9DGU0
, B9DHP3, Q56W88, Q94AY7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 5, 2009
Last sequence update: May 1, 2000
Last modified: May 11, 2016
This is version 118 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.