Protein: V-type proton ATPase 116 kDa subunit a 2 (V-ATPase 116 kDa isoform a 2) (Rod-like larval lethality and dye-filling defective protein 1) (G5EEK9)
Organism: Caenorhabditis elegans
Function: Subunit 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). Involved in the assembly of the V-ATPase complex. The V-ATPase is required for the function of the excretory canal. Independently of the V1 complex, the V0 complex of the V-ATPase is required for multivesicular body membrane fusion with the apical membrane of the epidermal cells during exosome release and thus regulates the release of cuticle components such as Hedgehog-related peptide wrt-2 but not collagen. Also, in the epidermis, regulates the trafficking of che-14 and rdy-2. Regulates the secretion of granular material found in the amphid channel and in controlling osmoregulation in the amphid pocket.
Subcellular location: Apical cell membrane {ECO:0000269|PubMed:11441002, ECO:0000269|PubMed:16785323}; Multi-pass membrane protein {ECO:0000255}. Endosome, multivesicular body membrane {ECO:0000269|PubMed:16785323}; Multi-pass membrane protein {ECO:0000255}. Note=In embryos, localizes to dot-like compartments or in cup-shaped structures (PubMed:11441002). Localizes to multivesicular body membranes in the epidermis (PubMed:16785323). Colocalizes with vha-8 to stacked sheets of the apical cell membrane of syncytial hypodermal cells (PubMed:16785323). In the epidermis, localizes to dispersed spots during intermolts which becomes aligned and colocalizes with actin bundles during the molts (PubMed:17179093). {ECO:0000269|PubMed:11441002, ECO:0000269|PubMed:16785323, ECO:0000269|PubMed:17179093}.
Interaction partners:
- V-type proton ATPase catalytic subunit A
- V-type proton ATPase subunit D
- V-type proton ATPase 21 kDa proteolipid subunit c''
- V-type proton ATPase subunit
- V-type proton ATPase subunit C
- V-type proton ATPase 16 kDa proteolipid subunit c 1
- Probable V-type proton ATPase subunit F
- V-type proton ATPase subunit B 1
- V-type proton ATPase subunit E
- Probable V-type proton ATPase subunit G
Sequence:
MGSLSRSEEMRFCQLIVEKDAAFNIVAEIGKQPYVQFKDLNPNVNSFQRTFVKDIRRYDEMERKLRFLESQIVKDEIVIPGRVDTGDYTILPTSELNTLEGTLTELEKDVKSMNDSDSQLKANFMDLKEWDAVLDKTDEFFQGGVDDQAQEELENLDEEGAVPRVEKGPVNYLVGIIRRERLNGFERVLWRACHHTAYIRSSDIEEELEDPGTGEKVHKSVFIIFLKGDRMRSIVEKVCDGFKAKLFKNCPKTFKERQSARNDVRARIQDLQTVLGQTREHRFRVLQAAANNHHQWLKQVRMIKTVFHMLNLFTFDGIGRFFVGECWIPLKHVEDVRKAIEVGAERSGSSVKPVLNILETSVTPPTYNETNKFTAVFQGIVDSYGIATYRELNPAPYTIITFPFLFSCMFGDLGHGCIMLMAGLWFVLREKNLQARNIKDEIFNMFFGGRYIILLMGLFSIHAGIIYNDMFAKSFNIFGSGWKNPYNASEIEGWINRTEHGKEMLVELAPEDAYDHAGGPYSFGVDPIWNIAENKLNFLNSMKMKLSVILGISQMTFGVILSFFNHTYNKSKIDIFTVFIPQMLFMGCIFMYLCLQIILKWLFFWTKEATVFGQIYPGSHCAPSLLIGLINMFMMKDRNAGFVVDGGKVNGEYREVETCYLSQWYPGQSVIEMILVVIAVICVPVMLFGKPIHHVMQQKKKAKELHGNATVRANVVSDSSEIVLNGGSKKEGAAHEEHGHGGHEDESFGDIMVHQAIHTIEYVLGCVSHTASYLRLWALSLAHAQLSEVLWHMVFVTGGLGISGTAGFIAVYVVFFIFFVLTISILVLMEGLSAFLHTLRLHWVEFQSKFYLGLGYPFVPYSFKTALQEAEAA