Search by BoMiProt ID - Bomi2839


Primary Information

BoMiProt ID Bomi2839
Protein Name V-type proton ATPase subunit H
Organism Bos taurus
Uniprot IdO46563
Milk FractionExosome
Ref Sequence Id NP_777129.2
Amino Acid Lenth 483
Molecular Weight 55852
Fasta Sequence https://www.uniprot.org/uniprot/O46563.fasta
Gene Name ATP6V1H
Gene Id 282657
Protein Existence Status Reviewed: Experimental evidence at transcript level

Secondry 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;
Linking IDs Bomi92
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.