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Protein

V-type proton ATPase 16 kDa proteolipid subunit 2/3

Gene

vha-2

more
Organism
Caenorhabditis elegans
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Proton-conducting pore forming subunit of the membrane integral V0 complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells (By similarity). Involved in necrotic cell death (PubMed:22157748).By similarity1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei145Essential for proton translocationBy similarity1

GO - Molecular functioni

GO - Biological processi

  • ATP hydrolysis coupled proton transport Source: InterPro
  • lysosomal lumen acidification Source: GO_Central
  • positive regulation of necrotic cell death Source: WormBase
  • positive regulation of programmed cell death Source: WormBase
  • proton transport Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Hydrogen ion transport, Ion transport, Necrosis, Transport

Enzyme and pathway databases

ReactomeiR-CEL-1222556. ROS, RNS production in response to bacteria.
R-CEL-6798695. Neutrophil degranulation.
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:
V-type proton ATPase 16 kDa proteolipid subunit 2/3
Short name:
V-ATPase 16 kDa proteolipid subunit 2/3
Alternative name(s):
Vacuolar proton pump 16 kDa proteolipid subunit 2/3
Gene namesi
Name:vha-2
ORF Names:R10E11.2
AND
Name:vha-3
ORF Names:Y38F2AL.4
OrganismiCaenorhabditis elegans
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
Proteomesi
  • UP000001940 Componentsi: Chromosome III, Chromosome IV

Organism-specific databases

WormBaseiR10E11.2; CE06290; WBGene00006911; vha-2.
Y38F2AL.4; CE06290; WBGene00006912; vha-3.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 15LumenalSequence analysisAdd BLAST15
Transmembranei16 – 36HelicalSequence analysisAdd BLAST21
Topological domaini37 – 58CytoplasmicSequence analysisAdd BLAST22
Transmembranei59 – 79HelicalSequence analysisAdd BLAST21
Topological domaini80 – 98LumenalSequence analysisAdd BLAST19
Transmembranei99 – 119HelicalSequence analysisAdd BLAST21
Topological domaini120 – 137CytoplasmicSequence analysisAdd BLAST18
Transmembranei138 – 158HelicalSequence analysisAdd BLAST21
Topological domaini159 – 161LumenalSequence analysis3

GO - Cellular componenti

  • integral component of membrane Source: UniProtKB
  • vacuolar proton-transporting V-type ATPase, V0 domain Source: WormBase
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Vacuole

Pathology & Biotechi

Disruption phenotypei

RNAi-mediated knockdown causes a reduction in the formation of neuron cell corpses in a hyperactive mec-4 mutant background.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000717581 – 161V-type proton ATPase 16 kDa proteolipid subunit 2/3Add BLAST161

Proteomic databases

EPDiP34546.
PaxDbiP34546.
PeptideAtlasiP34546.
PRIDEiP34546.

Expressioni

Tissue specificityi

Expressed ubiquitously. Higher levels of vha-2 are found in adult H-shaped excretory cell and rectum. Higher levels of vha-3 are found in gastrointestinal and hypodermal cells, as well as H-shaped excretory cell.1 Publication

Developmental stagei

High levels during embryogenesis, moderate levels during L1, L4 and adult stages and very low levels during L2 and L3 stages.1 Publication

Gene expression databases

BgeeiWBGene00006911.

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; which is present as a hexamer that forms the proton-conducting pore).

Protein-protein interaction databases

BioGridi52462. 5 interactors.
DIPiDIP-24599N.
MINTiMINT-1055570.
STRINGi6239.Y38F2AL.4.

Structurei

3D structure databases

ProteinModelPortaliP34546.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0232. Eukaryota.
COG0636. LUCA.
GeneTreeiENSGT00550000074873.
HOGENOMiHOG000056520.
InParanoidiP34546.
KOiK02155.
OMAiMSYDLET.
OrthoDBiEOG091G0U1Y.
PhylomeDBiP34546.

Family and domain databases

InterProiIPR002379. ATPase_proteolipid_c-like_dom.
IPR000245. ATPase_proteolipid_csu.
IPR011555. ATPase_proteolipid_su_C_euk.
[Graphical view]
PfamiPF00137. ATP-synt_C. 2 hits.
[Graphical view]
PRINTSiPR00122. VACATPASE.
SUPFAMiSSF81333. SSF81333. 2 hits.
TIGRFAMsiTIGR01100. V_ATP_synt_C. 1 hit.

Sequencei

Sequence statusi: Complete.

P34546-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSYDLETAER AAYAPFFGYM GAASAQIFTV LGAAYGTAKS AVGICSMGVM
60 70 80 90 100
RPELIMKSVI PVIMAGIIGI YGLVVAMVLK GKVTSASAGY DLNKGFAHLA
110 120 130 140 150
AGLTCGLCGL GAGYAIGIVG DAGVRGTAQQ PRLFVGMILI LIFSEVLGLY
160
GMIVALILGT S
Length:161
Mass (Da):16,410
Last modified:November 1, 1997 - v2
Checksum:i67EDBD2124F12F6E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB000918 mRNA. Translation: BAA22596.1.
AB009566 mRNA. Translation: BAA75066.1.
Z29095 Genomic DNA. Translation: CAA82355.1.
FO080811 Genomic DNA. Translation: CCD66969.1.
PIRiC88565.
S40714.
RefSeqiNP_499166.1. NM_066765.6.
NP_500188.1. NM_067787.6.
UniGeneiCel.19589.
Cel.7940.

Genome annotation databases

EnsemblMetazoaiR10E11.2; R10E11.2; WBGene00006911.
Y38F2AL.4; Y38F2AL.4; WBGene00006912.
GeneIDi177018.
187779.
KEGGicel:CELE_R10E11.2.
cel:CELE_Y38F2AL.4.
UCSCiR10E11.2.1. c. elegans.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB000918 mRNA. Translation: BAA22596.1.
AB009566 mRNA. Translation: BAA75066.1.
Z29095 Genomic DNA. Translation: CAA82355.1.
FO080811 Genomic DNA. Translation: CCD66969.1.
PIRiC88565.
S40714.
RefSeqiNP_499166.1. NM_066765.6.
NP_500188.1. NM_067787.6.
UniGeneiCel.19589.
Cel.7940.

3D structure databases

ProteinModelPortaliP34546.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi52462. 5 interactors.
DIPiDIP-24599N.
MINTiMINT-1055570.
STRINGi6239.Y38F2AL.4.

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.

Proteomic databases

EPDiP34546.
PaxDbiP34546.
PeptideAtlasiP34546.
PRIDEiP34546.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiR10E11.2; R10E11.2; WBGene00006911.
Y38F2AL.4; Y38F2AL.4; WBGene00006912.
GeneIDi177018.
187779.
KEGGicel:CELE_R10E11.2.
cel:CELE_Y38F2AL.4.
UCSCiR10E11.2.1. c. elegans.

Organism-specific databases

CTDi177018.
187779.
WormBaseiR10E11.2; CE06290; WBGene00006911; vha-2.
Y38F2AL.4; CE06290; WBGene00006912; vha-3.

Phylogenomic databases

eggNOGiKOG0232. Eukaryota.
COG0636. LUCA.
GeneTreeiENSGT00550000074873.
HOGENOMiHOG000056520.
InParanoidiP34546.
KOiK02155.
OMAiMSYDLET.
OrthoDBiEOG091G0U1Y.
PhylomeDBiP34546.

Enzyme and pathway databases

ReactomeiR-CEL-1222556. ROS, RNS production in response to bacteria.
R-CEL-6798695. Neutrophil degranulation.
R-CEL-77387. Insulin receptor recycling.
R-CEL-917977. Transferrin endocytosis and recycling.

Miscellaneous databases

PROiP34546.

Gene expression databases

BgeeiWBGene00006911.

Family and domain databases

InterProiIPR002379. ATPase_proteolipid_c-like_dom.
IPR000245. ATPase_proteolipid_csu.
IPR011555. ATPase_proteolipid_su_C_euk.
[Graphical view]
PfamiPF00137. ATP-synt_C. 2 hits.
[Graphical view]
PRINTSiPR00122. VACATPASE.
SUPFAMiSSF81333. SSF81333. 2 hits.
TIGRFAMsiTIGR01100. V_ATP_synt_C. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiVATL2_CAEEL
AccessioniPrimary (citable) accession number: P34546
Secondary accession number(s): P83577
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: November 1, 1997
Last modified: November 30, 2016
This is version 145 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Miscellaneousi

Miscellaneous

Vha-11 and vha-3 are transcribed on a dicistronic transcript where vha-3 is the upstream transcript and vha-11 the downstream.

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.