Primary Information
BoMiProt ID	Bomi92
Protein Name	V-type proton ATPase 116 kDa subunit a isoform 1
Organism	Bos taurus
Uniprot ID	Q29466
Milk Fraction	Exosome
Ref Sequence ID	NP_777179.1
Aminoacid Length	832
Molecular Weight	95631
FASTA Sequence	Download
Gene Name	ATP6V0A1
Gene ID	28676
Protein Existence Status	Reviewed: Experimental evidence at transcript level
Secondary Information
Presence in other biological fluids/tissue/cells	ubiquitous in eukaryotes, distributed mostly on intracellular tubulo-vesicular membranes, but found also at the plasma membrane in specialized cell types
Protein Function	primarily responsible for the establishment and maintenance of the acidic pH of endocytic and secretory organelles, pumping cytosolic H+ into their lumen in an ATP-dependent manner; Plasmalemmal V-ATPase function in renal cells is important for the systemic acid-base balance, through secretion of acid into the urine; Activated neutrophils and macrophages use plasma membrane V-ATPases to maintain a neutral cytoplasmic pH;
Biochemical Properties	The V- are multisubunit proteins of up to 14 different polypeptides, which assemble as two major ring structures: (1) a peripheral V1 complex that interacts with ATP, ADP and inorganic phosphate, and (2) an integral membrane V0 complex that is membrane embedded mediates the transport of H+ or Na+; V-ATPase is largely responsible for the accumulation of H+ in endocytic vesicles; H+ pumping by VATPases accounts for the uniquely acidic lysosomal pH of ,4.5 that is essential for optimal enzyme function;
PTMs	Phosphorylation at Tyr/Thr
Site(s) of PTM(s) N-glycosylation, O-glycosylation, Phosphorylation
Predicted Disorder Regions	NA
DisProt Annotation
TM Helix Prediction	8TMHs; (403-425), (445-463), (505-527), (540-562), (571-593) ,(606-624), (636-658), (772-794)
Linking IDs
Bibliography	1. Brown, D., & Breton, S. (2000). H(+)V-ATPase-dependent luminal acidification in the kidney collecting duct and the epididymis/vas deferens: vesicle recycling and transcytotic pathways. The Journal of Experimental Biology, 203(Pt 1), 137–145. Retrieved from http://www.ncbi.nlm.nih.gov/pubmed/10600682. 2. Hirata, T., Nakamura, N., Omote, H., Wada, Y., & Futai, M. (2000). Regulation and reversibility of vacuolar H(+)-ATPase. The Journal of Biological Chemistry, 275(1), 386–389. https://doi.org/10.1074/jbc.275.1.386. 3. Huynh, K. K., & Grinstein, S. (2007). Regulation of vacuolar pH and its modulation by some microbial species. Microbiology and Molecular Biology Reviews : MMBR, 71(3), 452–462. https://doi.org/10.1128/MMBR.00003-07. 4. Brisseau, G. F., Grinstein, S., Hackam, D. J., Nordström, T., Manolson, M. F., Khine, A. A., & Rotstein, O. D. (1996). Interleukin-1 increases vacuolar-type H+-ATPase activity in murine peritoneal macrophages. The Journal of Biological Chemistry, 271(4), 2005–2011. https://doi.org/10.1074/jbc.271.4.2005.