Q95X44 · VATE_CAEEL
- ProteinV-type proton ATPase subunit E
- Genevha-8
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids226 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (By similarity).
V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment (By similarity).
Regulates pH homeostasis in the intestine (PubMed:16684534).
Probably by regulating cytoplasmic pH, required for cell survival in the intestine and hypodermis (PubMed:16684534).
Involved in receptor-mediated endocytosis (PubMed:12853134, PubMed:16785323).
Involved in embryogenesis and larval development (PubMed:12853134, PubMed:16785323).
V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment (By similarity).
Regulates pH homeostasis in the intestine (PubMed:16684534).
Probably by regulating cytoplasmic pH, required for cell survival in the intestine and hypodermis (PubMed:16684534).
Involved in receptor-mediated endocytosis (PubMed:12853134, PubMed:16785323).
Involved in embryogenesis and larval development (PubMed:12853134, PubMed:16785323).
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | apical plasma membrane | |
Cellular Component | cytoplasm | |
Cellular Component | plasma membrane | |
Cellular Component | proton-transporting two-sector ATPase complex, catalytic domain | |
Molecular Function | proton-transporting ATPase activity, rotational mechanism |
Keywords
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameV-type proton ATPase subunit E
- Short namesV-ATPase subunit E
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Nematoda > Chromadorea > Rhabditida > Rhabditina > Rhabditomorpha > Rhabditoidea > Rhabditidae > Peloderinae > Caenorhabditis
Accessions
- Primary accessionQ95X44
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Apical cell membrane ; Peripheral membrane protein
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Larvae are arrested at the L1 stage (PubMed:16684534).
Larvae exhibit swollen vacuoles in the hypodermis of the head region, gradually spreading throughout the whole body (PubMed:16684534).
Pharyngeal pumping ceases at L2 larval stage with many vacuoles covering the entire body (PubMed:16684534).
Causes necrotic cell death in intestine and hypodermis (PubMed:16684534).
RNAi-mediated knockdown causes sterility, formation of endomitotic oocytes in the proximal gonads, and impaired ovulation (PubMed:12853134).
Diakinesis stage oocytes are displaced toward distal gonads (PubMed:12853134).
Impaired yolk uptake by the oocytes from the pseudoceolomic cavities (PubMed:12853134, PubMed:16785323).
Impaired acidification and food digestion of the intestine (PubMed:16684534).
Causes an increase in the section of the excretory canal, which often has multiple lumens and abnormal whorls (PubMed:16785323).
Does not affect alae formation in larvae (PubMed:16785323).
Progeny is arrested at the embryonic stage or at the L1 larval stage (PubMed:12853134, PubMed:16785323).
RNAi-mediated knockdown in embryos causes arrest at the one-cell stage (PubMed:12853134).
Larvae exhibit swollen vacuoles in the hypodermis of the head region, gradually spreading throughout the whole body (PubMed:16684534).
Pharyngeal pumping ceases at L2 larval stage with many vacuoles covering the entire body (PubMed:16684534).
Causes necrotic cell death in intestine and hypodermis (PubMed:16684534).
RNAi-mediated knockdown causes sterility, formation of endomitotic oocytes in the proximal gonads, and impaired ovulation (PubMed:12853134).
Diakinesis stage oocytes are displaced toward distal gonads (PubMed:12853134).
Impaired yolk uptake by the oocytes from the pseudoceolomic cavities (PubMed:12853134, PubMed:16785323).
Impaired acidification and food digestion of the intestine (PubMed:16684534).
Causes an increase in the section of the excretory canal, which often has multiple lumens and abnormal whorls (PubMed:16785323).
Does not affect alae formation in larvae (PubMed:16785323).
Progeny is arrested at the embryonic stage or at the L1 larval stage (PubMed:12853134, PubMed:16785323).
RNAi-mediated knockdown in embryos causes arrest at the one-cell stage (PubMed:12853134).
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000454078 | 1-226 | V-type proton ATPase subunit E | |||
Sequence: MGISDNDVQKQLRHMMAFIEQEANEKAEEIDAKAEEEFNIEKGRLVQQQRQKIMEFFEKKEKQVELQRKIQASNSLNAGRLRCLKAREDHIGAVLDEARSNLSRISGDAARYPAILKGLVMQGLLQLLEKEVVLRCREKDLRLVEQLLPECLDGLQKEWGSTTKVVLDKQNFLPSESAGGVELSARAGKIKVSSTLESRLELIANQIVPQVRTALFGPNPNRSFFD |
Proteomic databases
Expression
Tissue specificity
Expressed in the excretory cell and syncytial hypodermal cells (at protein level) (PubMed:12853134, PubMed:16684534, PubMed:16785323).
Expressed in the intestine (at protein level) (PubMed:16684534).
Expressed in the intestine (at protein level) (PubMed:16684534).
Developmental stage
Expressed in embryos, larvae and adults (at protein level) (PubMed:12853134, PubMed:16684534).
Expressed in the excretory cell, intestine and hypodermis throughout all developmental stages and in adults (at protein level) (PubMed:12853134, PubMed:16684534).
Expressed in the excretory cell, intestine and hypodermis throughout all developmental stages and in adults (at protein level) (PubMed:12853134, PubMed:16684534).
Gene expression databases
Interaction
Subunit
V-ATPase is a heteromultimeric enzyme made up of two complexes: the ATP-hydrolytic V1 complex and the proton translocation V0 complex. The V1 complex consists of three catalytic AB heterodimers that form a heterohexamer, three peripheral stalks each consisting of EG heterodimers, one central rotor including subunits D and F, and the regulatory subunits C and H. The proton translocation complex V0 consists of the proton transport subunit a, a ring of proteolipid subunits c9c'', rotary subunit d, subunits e and f, and the accessory subunits vah-19/Ac45 and vah-20/PRR.
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length226
- Mass (Da)25,586
- Last updated2001-12-01 v1
- ChecksumE7F68A74642EE1C8
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
BX284604 EMBL· GenBank· DDBJ | CCD65002.1 EMBL· GenBank· DDBJ | Genomic DNA |