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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: 4 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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei145 – 1451Essential for proton translocationBy similarity

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, 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:
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)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1515LumenalSequence analysisAdd
BLAST
Transmembranei16 – 3621HelicalSequence analysisAdd
BLAST
Topological domaini37 – 5822CytoplasmicSequence analysisAdd
BLAST
Transmembranei59 – 7921HelicalSequence analysisAdd
BLAST
Topological domaini80 – 9819LumenalSequence analysisAdd
BLAST
Transmembranei99 – 11921HelicalSequence analysisAdd
BLAST
Topological domaini120 – 13718CytoplasmicSequence analysisAdd
BLAST
Transmembranei138 – 15821HelicalSequence analysisAdd
BLAST
Topological domaini159 – 1613LumenalSequence analysis

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 161161V-type proton ATPase 16 kDa proteolipid subunit 2/3PRO_0000071758Add
BLAST

Proteomic databases

EPDiP34546.
PaxDbiP34546.
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

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 interactions.
DIPiDIP-24599N.
MINTiMINT-1055570.
STRINGi6239.Y38F2AL.4.

Structurei

3D structure databases

ProteinModelPortaliP34546.
SMRiP34546. Positions 16-160.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0232. Eukaryota.
COG0636. LUCA.
GeneTreeiENSGT00550000074873.
HOGENOMiHOG000056520.
InParanoidiP34546.
KOiK02155.
OMAiLSMHMTL.
OrthoDBiEOG7FV3RW.
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.
SMRiP34546. Positions 16-160.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi52462. 5 interactions.
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.
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.
OMAiLSMHMTL.
OrthoDBiEOG7FV3RW.
PhylomeDBiP34546.

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

PROiP34546.

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...

Publicationsi

« Hide 'large scale' publications
  1. "Three vha genes encode proteolipids of Caenorhabditis elegans vacuolar-type ATPase. Gene structures and preferential expression in an H-shaped excretory cell and rectal cells."
    Oka T., Yamamoto R., Futai M.
    J. Biol. Chem. 272:24387-24392(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (VHA-2).
  2. "Multiple genes for vacuolar-type ATPase proteolipids in Caenorhabditis elegans: a new gene, vha-3, has a distinct cell-specific distribution."
    Oka T., Yamamoto R., Futai M.
    J. Biol. Chem. 273:22570-22576(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (VHA-3), TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (VHA-2 AND VHA-3).
    Strain: Bristol N2.
  4. "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] (VHA-2 AND VHA-3).
    Strain: Bristol N2.

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: July 6, 2016
This is version 141 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.