Search by BoMiProt ID - Bomi10538

Primary Information

BoMiProt ID Bomi10538
Protein Name V-type proton ATPase 16 kDa proteolipid subunit/V-ATPase 16 kDa proteolipid subunit/Vacuolar proton pump 16 kDa proteolipid subunit
Organism Bos taurus
Uniprot IDP23956
Milk FractionWhey
Ref Sequence ID NP_001017954.1
Aminoacid Length 155
Molecular Weight 15720
FASTA Sequence Download
Gene Name ATP6V0C/ATP6C/ ATP6L
Gene ID 550622
Protein Existence Status reviewed

Secondary Information

Protein Function important for proton translocation.acidification of intracellular compartments in eukaryotic cells.Acidification is necessary for protein sorting, zymogen activation, receptor-mediated endocytosis, and synaptic vesicle proton gradient generation.
Biochemical Properties V-ATPase is composed of a cytosolic V1 domain and a transmembrane V0 domain. V1 domain responsible for ATP hydrolysis and an integral V0 domain responsible for proton translocation.The V0 domain is a 250–300-kDa integral complex, which contains three to five subunits, and is responsible for proton translocation.V0 contains six copies of the 17-kDa c subunit and single copies of the remaining subunits.Cys254 has been shown to form a disulfide bond with a second cysteine, Cys532, in the A subunit in folded state.Disulfide bond formation inhibits ATPase activity but does not block nucleotide binding.Peptide sequencing reveals that the A subunit is modified in a region near Cys532, which contains several aromatic residues that may participate in formation of the adenine-binding pocket.
PTMs Ubl conjugation
Site(s) of PTM(s)

N-glycosylation, O-glycosylation,
CATH Matched CATH superfamily
Predicted Disorder Regions NA
DisProt Annotation
TM Helix Prediction 4TMHs; (12-34), (55-77), (92-114) & (127-149)
Significance of PTMs Chemical modification has identified Cys254 of the bovine A subunit as the residue responsible for the sensitivity of V-ATPases to sulfhydryl reagents.Cys254 is located in the glycine-rich loop that, from the crystal structure of F1, is in close contact with the triphosphates of bound ATP.
Additional Comments Vacuolar acidification also plays a role in movement of ligands from endosomes to lysosomes. Iron uptake continuous recycling of transferrin receptors.The entry of certain envelope viruses (such as influenza virus) and toxins (such as diphtheria toxin) into cells, however, is dependent upon an acidic endosomal environment. In the case of influenza virus, the surface hemagglutinin molecule acts as an acid-activated fusogen that promotes fusion between the viral and endosomal membranes .