ATP6V1H
V-type proton ATPase subunit H is an enzyme that in humans is encoded by the ATP6V1H gene.[1][2][3]
This gene encodes a component of vacuolar ATPase (V-ATPase), a multisubunit enzyme that mediates acidification of eukaryotic intracellular organelles. V-ATPase dependent organelle acidification is necessary for such intracellular processes as protein sorting, zymogen activation, receptor-mediated endocytosis, and synaptic vesicle proton gradient generation. V-ATPase is composed of a cytosolic V1 domain and a transmembrane V0 domain. The V1 domain consists of three A and three B subunits, two G subunits plus the C, D, E, F, and H subunits. The V1 domain contains the ATP catalytic site. The V0 domain consists of five different subunits: a, c, c', c", and d. Additional isoforms of many of the V1 and V0 subunit proteins are encoded by multiple genes or alternatively spliced transcript variants. This gene encodes the regulatory H subunit of the V1 domain which is required for catalysis of ATP but not the assembly of V-ATPase. Three alternatively spliced transcript variants encode two isoforms of the H subunit.[3]
References
- ^ Lu X, Yu H, Liu SH, Brodsky FM, Peterlin BM (Jun 1998). "Interactions between HIV1 Nef and vacuolar ATPase facilitate the internalization of CD4". Immunity 8 (5): 647–56. doi:10.1016/S1074-7613(00)80569-5. PMID 9620685.
- ^ Lai CH, Chou CY, Ch'ang LY, Liu CS, Lin W (Aug 2000). "Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics". Genome Res 10 (5): 703–13. doi:10.1101/gr.10.5.703. PMC 310876. PMID 10810093. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=310876.
- ^ a b "Entrez Gene: ATP6V1H ATPase, H+ transporting, lysosomal 50/57kDa, V1 subunit H". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=51606.
Further reading
- Stevens TH, Forgac M (1998). "Structure, function and regulation of the vacuolar (H+)-ATPase.". Annu. Rev. Cell Dev. Biol. 13: 779–808. doi:10.1146/annurev.cellbio.13.1.779. PMID 9442887.
- Geyer M, Fackler OT, Peterlin BM (2001). "Structure--function relationships in HIV-1 Nef.". EMBO Rep. 2 (7): 580–5. doi:10.1093/embo-reports/kve141. PMC 1083955. PMID 11463741. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1083955.
- Nishi T, Forgac M (2002). "The vacuolar (H+)-ATPases--nature's most versatile proton pumps.". Nat. Rev. Mol. Cell Biol. 3 (2): 94–103. doi:10.1038/nrm729. PMID 11836511.
- Pedersen PL (2003). "Transport ATPases in biological systems and relationship to human disease: a brief overview.". J. Bioenerg. Biomembr. 34 (5): 327–32. doi:10.1023/A:1021249701287. PMID 12539959.
- Kawasaki-Nishi S, Nishi T, Forgac M (2003). "Proton translocation driven by ATP hydrolysis in V-ATPases.". FEBS Lett. 545 (1): 76–85. doi:10.1016/S0014-5793(03)00396-X. PMID 12788495.
- Morel N (2004). "Neurotransmitter release: the dark side of the vacuolar-H+ATPase.". Biol. Cell 95 (7): 453–7. doi:10.1016/S0248-4900(03)00075-3. PMID 14597263.
- Hu RM, Han ZG, Song HD, et al. (2000). "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning.". Proc. Natl. Acad. Sci. U.S.A. 97 (17): 9543–8. doi:10.1073/pnas.160270997. PMC 16901. PMID 10931946. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=16901.
- Mandic R, Fackler OT, Geyer M, et al. (2001). "Negative factor from SIV binds to the catalytic subunit of the V-ATPase to internalize CD4 and to increase viral infectivity.". Mol. Biol. Cell 12 (2): 463–73. PMC 30956. PMID 11179428. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=30956.
- Geyer M, Yu H, Mandic R, et al. (2002). "Subunit H of the V-ATPase binds to the medium chain of adaptor protein complex 2 and connects Nef to the endocytic machinery.". J. Biol. Chem. 277 (32): 28521–9. doi:10.1074/jbc.M200522200. PMID 12032142.
- Geyer M, Fackler OT, Peterlin BM (2002). "Subunit H of the V-ATPase involved in endocytosis shows homology to beta-adaptins.". Mol. Biol. Cell 13 (6): 2045–56. PMC 117623. PMID 12058068. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=117623.
- Lu M, Vergara S, Zhang L, et al. (2002). "The amino-terminal domain of the E subunit of vacuolar H(+)-ATPase (V-ATPase) interacts with the H subunit and is required for V-ATPase function.". J. Biol. Chem. 277 (41): 38409–15. doi:10.1074/jbc.M203521200. PMID 12163484.
- Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241.
- Smith AN, Lovering RC, Futai M, et al. (2003). "Revised nomenclature for mammalian vacuolar-type H+ -ATPase subunit genes.". Mol. Cell 12 (4): 801–3. doi:10.1016/S1097-2765(03)00397-6. PMID 14580332.