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Protein

Probable V-type proton ATPase subunit B

Gene

vha-12

Organism
Caenorhabditis elegans
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Protein inferred from homologyi

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 (By similarity). Required for necrotic cell death and epidermal cell fusion.By similarity2 Publications

GO - Molecular functioni

  • ATP binding Source: InterPro
  • proton-transporting ATPase activity, rotational mechanism Source: UniProtKB

GO - Biological processi

  • ATP hydrolysis coupled proton transport Source: InterPro
  • ATP metabolic process Source: InterPro
  • cell death Source: UniProtKB
  • energy coupled proton transmembrane transport, against electrochemical gradient Source: UniProtKB
  • positive regulation of programmed cell death Source: WormBase
  • proton transport Source: UniProtKB
  • regulation of intracellular pH Source: WormBase
  • regulation of syncytium formation by plasma membrane fusion Source: WormBase
  • response to hypoxia Source: WormBase
  • single organismal cell-cell adhesion Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Hydrogen ion transport, Ion transport, Transport

Enzyme and pathway databases

ReactomeiR-CEL-1222556. ROS, RNS production in response to bacteria.
R-CEL-77387. Insulin receptor recycling.
R-CEL-917977. Transferrin endocytosis and recycling.

Protein family/group databases

TCDBi3.A.2.2.7. the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable V-type proton ATPase subunit B
Short name:
V-ATPase subunit B
Alternative name(s):
Vacuolar proton pump subunit B
Gene namesi
Name:vha-12
ORF Names:F20B6.2
OrganismiCaenorhabditis elegans
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
Proteomesi
  • UP000001940 Componenti: Chromosome X

Organism-specific databases

WormBaseiF20B6.2; CE04424; WBGene00006921; vha-12.

Subcellular locationi

GO - Cellular componenti

  • cell Source: GOC
  • proton-transporting V-type ATPase, V1 domain Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Disruption phenotypei

Suppression of necrotic cell death and hyperfusion of embryonic epidermal cells.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 491491Probable V-type proton ATPase subunit BPRO_0000144631Add
BLAST

Proteomic databases

EPDiQ19626.
PaxDbiQ19626.
PRIDEiQ19626.

2D gel databases

World-2DPAGE0020:Q19626.

Interactioni

Subunit structurei

V-ATPase is a heteromultimeric enzyme composed of a peripheral catalytic V1 complex (main components: subunits A, B, C, D, E, and F) attached to an integral membrane V0 proton pore complex (main component: the proteolipid protein).

Protein-protein interaction databases

BioGridi45627. 1 interaction.
IntActiQ19626. 1 interaction.
STRINGi6239.F20B6.2.2.

Structurei

3D structure databases

ProteinModelPortaliQ19626.
SMRiQ19626. Positions 31-484.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ATPase alpha/beta chains family.Curated

Phylogenomic databases

eggNOGiKOG1351. Eukaryota.
COG1156. LUCA.
GeneTreeiENSGT00550000074724.
HOGENOMiHOG000165320.
InParanoidiQ19626.
KOiK02147.
OMAiDRPHEQT.
OrthoDBiEOG7NW68Q.
PhylomeDBiQ19626.

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.

Q19626-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAVDVNQPI TGHKSAIIRN YNTNPRLIYQ TVCGVNGPLV ILNDVKFPQF
60 70 80 90 100
SEIVKITLPD GSKRSGQVLE ISKNKAVVQV FEGTSGIDAK NTICEFTGDI
110 120 130 140 150
LRTPVSEDML GRIFNGSGKP IDKGPPVLAE DFLDINGQPI NPWSRIYPEE
160 170 180 190 200
MIQTGISAID VMNSIARGQK IPIFSASGLP HNEIAAQIVR QGGLVQLPDR
210 220 230 240 250
PHEQTNFAIV FAAMGVNMET ARFFKQDFEE NGSMENVCLF LNLANDPTIE
260 270 280 290 300
RIITPRIALT SAEFLAYQCK KHVLVVLTDM SSYAEALREV SAAREEVPGR
310 320 330 340 350
RGFPGYMYTD LATIYERAGR VEGRDGSITQ IPILTMPNDD ITHPIPDLTG
360 370 380 390 400
YITEGQIYVD RQLHNRLIYP PINVLPSLSR LMKSAIGEGM TREDHSDVSN
410 420 430 440 450
QLYACYAIGK DVQAMKAVVG EEALSSDDLL YLEFLTKFEK NFITQGHYEN
460 470 480 490
RSVFESLDIG WQLLRIFPRE MLKRIPESTL EKYYPRGGAK E
Length:491
Mass (Da):54,751
Last modified:November 1, 1997 - v1
Checksum:iEDF4D13B3BD34716
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FO081186 Genomic DNA. Translation: CCD69755.1.
PIRiT34226.
RefSeqiNP_508711.1. NM_076310.7.
UniGeneiCel.23532.

Genome annotation databases

EnsemblMetazoaiF20B6.2; F20B6.2; WBGene00006921.
GeneIDi180692.
KEGGicel:CELE_F20B6.2.
UCSCiF20B6.2.2. c. elegans.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FO081186 Genomic DNA. Translation: CCD69755.1.
PIRiT34226.
RefSeqiNP_508711.1. NM_076310.7.
UniGeneiCel.23532.

3D structure databases

ProteinModelPortaliQ19626.
SMRiQ19626. Positions 31-484.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi45627. 1 interaction.
IntActiQ19626. 1 interaction.
STRINGi6239.F20B6.2.2.

Protein family/group databases

TCDBi3.A.2.2.7. the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.

2D gel databases

World-2DPAGE0020:Q19626.

Proteomic databases

EPDiQ19626.
PaxDbiQ19626.
PRIDEiQ19626.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiF20B6.2; F20B6.2; WBGene00006921.
GeneIDi180692.
KEGGicel:CELE_F20B6.2.
UCSCiF20B6.2.2. c. elegans.

Organism-specific databases

CTDi180692.
WormBaseiF20B6.2; CE04424; WBGene00006921; vha-12.

Phylogenomic databases

eggNOGiKOG1351. Eukaryota.
COG1156. LUCA.
GeneTreeiENSGT00550000074724.
HOGENOMiHOG000165320.
InParanoidiQ19626.
KOiK02147.
OMAiDRPHEQT.
OrthoDBiEOG7NW68Q.
PhylomeDBiQ19626.

Enzyme and pathway databases

ReactomeiR-CEL-1222556. ROS, RNS production in response to bacteria.
R-CEL-77387. Insulin receptor recycling.
R-CEL-917977. Transferrin endocytosis and recycling.

Miscellaneous databases

PROiQ19626.

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. "Genome sequence of the nematode C. elegans: a platform for investigating biology."
    The C. elegans sequencing consortium
    Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Bristol N2.
  2. "The vacuolar H+ -ATPase mediates intracellular acidification required for neurodegeneration in C. elegans."
    Syntichaki P., Samara C., Tavernarakis N.
    Curr. Biol. 15:1249-1254(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  3. "Repression of cell-cell fusion by components of the C. elegans vacuolar ATPase complex."
    Kontani K., Moskowitz I.P.G., Rothman J.H.
    Dev. Cell 8:787-794(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiVATB_CAEEL
AccessioniPrimary (citable) accession number: Q19626
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: July 6, 2016
This is version 129 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
  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.