ATP6V1H

From Wikipedia, the free encyclopedia

ATPase, H+ transporting, lysosomal 50/57kDa, V1 subunit H

Identifiers

ATP6V1H; SFD; CGI-11; MSTP042; SFDalpha; SFDbeta; VMA13

External IDs

OMIM: 608861 MGI: 1914864 HomoloGene: 7139

Gene ontology
Molecular Function:	• ATPase activator activity • protein binding • ATP binding • hydrolase activity • ATPase activity • enzyme regulator activity • metal ion binding • hydrogen ion transporting ATP synthase activity, rotational mechanism • hydrogen ion transporting ATPase activity, rotational mechanism
Cellular Component:	• vacuolar proton-transporting V-type ATPase, V1 domain • peripheral to membrane of membrane fraction
Biological Process:	• ion transport • endocytosis • vacuolar acidification • ATP synthesis coupled proton transport • ATP hydrolysis coupled proton transport • proton transport

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_015941 (mRNA)
NP_057025 (protein)

NM_133826 (mRNA)
NP_598587 (protein)

Location

Chr 8: 54.79 - 54.92 Mb

Chr 1: 5.07 - 5.15 Mb

Pubmed search

[1]

[2]

ATPase, H+ transporting, lysosomal 50/57kDa, V1 subunit H, also known as ATP6V1H, is a human gene.^[1]

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.^[1]

[edit] References

^ ^a ^b Entrez Gene: ATP6V1H ATPase, H+ transporting, lysosomal 50/57kDa, V1 subunit H.

[edit] 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. PMID 11463741.
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. 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. PMID 12788495.
Morel N (2004). "Neurotransmitter release: the dark side of the vacuolar-H+ATPase.". Biol. Cell 95 (7): 453-7. PMID 14597263.
Lu X, Yu H, Liu SH, et al. (1998). "Interactions between HIV1 Nef and vacuolar ATPase facilitate the internalization of CD4.". Immunity 8 (5): 647-56. PMID 9620685.
Lai CH, Chou CY, Ch'ang LY, et al. (2000). "Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics.". Genome Res. 10 (5): 703-13. PMID 10810093.
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. PMID 10931946.
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. PMID 11179428.
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. doi:02-02-0026. PMID 12058068.
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. PMID 12477932.
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. PMID 14580332.