| IED ID | IndEnz0002001096 |
| Enzyme Type ID | protease001096 |
| Protein Name |
V-type proton ATPase 16 kDa proteolipid subunit c 1 V-ATPase 16 kDa proteolipid subunit c 1 Vacuolar proton pump 16 kDa proteolipid subunit c 1 |
| Gene Name | vha-1 R10E11.8 |
| Organism | Caenorhabditis elegans |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Nematoda (roundworms) Chromadorea Rhabditida Rhabditina Rhabditomorpha Rhabditoidea Rhabditidae Peloderinae Caenorhabditis Caenorhabditis elegans |
| Enzyme Sequence | MSTDTKQIIADALLKNEQAMYGPFFGSLGVTSAMAFAAAGSAYGTAKAGTGIASMAVARPDLVMKAIIPVVMAGIVAIYGLVVAVIVSGKVEPAGANYTINNAFSQFAGGLVCGLCGLGAGYAIGIAGDAGVRALSQQPRMFVGMILILIFAEVLGLYGMIVALILGAT |
| Enzyme Length | 169 |
| Uniprot Accession Number | Q21898 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Proton-conducting pore forming of the V0 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). Required along with other vacuolar ATPase components for the removal of protein aggregates which form in immature oocytes in the distal gonad (PubMed:29168500). This removal occurs as the oocytes mature and move to the proximal gonad, is triggered by the introduction of sperm through mating and occurs before fertilization (PubMed:29168500). The introduction of sperm triggers V-ATPase accumulation in proximal oocytes and induces lysosomal acidification which leads to engulfing of protein aggregates by lysosomes and subsequent clearance of the aggregates (PubMed:29168500). Lysosomal acidification also leads to changes in mitochondrial morphology and function (PubMed:29168500). Mitochondria in distal immature oocytes are fragmented, produce high levels of reactive oxygen species (ROS) and have high membrane potential, indicative of metabolic inactivity (PubMed:29168500). In contrast, mitochondria in proximal mature oocytes are tubular with lower ROS levels and membrane potential, indicative of an active metabolic state required for aggregate mobilization before clearance (PubMed:29168500). Plays a role in the processing and secretion of the aspartic protease hrg-7 from the intestine (PubMed:28581477). During embryonic development, the V-ATPase is required to repress fusion of epidermal cells probably by negatively regulating eff-1-mediated cell fusion (PubMed:15866168). Involved in receptor-mediated endocytosis (PubMed:16785323). {ECO:0000250|UniProtKB:P23956, ECO:0000269|PubMed:15866168, ECO:0000269|PubMed:16785323, ECO:0000269|PubMed:28581477, ECO:0000269|PubMed:29168500}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Site (1); Topological domain (5); Transmembrane (4) |
| Keywords | Hydrogen ion transport;Ion transport;Membrane;Reference proteome;Transmembrane;Transmembrane helix;Transport |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10846178; 11099034; 12097347; 12529635; 14551910; 15489339; 15791247; 17704769; 18182484; 21070894; 21085631; 21177967; 21367940; 21529718; 21620137; 22105480; 22180091; 22426883; 22500807; 22560298; 22634595; 23516373; 23800452; 25487147; 25652260; 26109047; 27506200; 29348603; 31110027; |
| Motif | |
| Gene Encoded By | |
| Mass | 16,954 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |