ATP6V1H

ATP6V1H
Identifiers
Aliases	ATP6V1H , MSTP042, NBP1, SFD, SFDalpha, SFDbeta, VMA13, CGI-11, ATPase H+ transporting V1 subunit H
External IDs	OMIM: 608861 MGI: 1914864 HomoloGene: 7139 GeneCards: ATP6V1H
Gene location (Human)
Chr.	Chromosome 8 (human)
End	53,843,558 bp
Gene location (Mouse)
Chr.	Chromosome 1 (mouse)
End	5,162,529 bp
RNA expression pattern
	Top expressed in
	middle temporal gyrus; ; Brodmann area 9; ; prefrontal cortex; ; amygdala; ; nucleus accumbens; ; caudate nucleus; ; cingulate gyrus; ; hippocampus proper; ; putamen; ; superior frontal gyrus;
	Top expressed in
	anterior horn of spinal cord; ; spermatocyte; ; facial motor nucleus; ; superior cervical ganglion; ; amygdala; ; cingulate gyrus; ; medial vestibular nucleus; ; superior frontal gyrus; ; medial dorsal nucleus; ; ventromedial nucleus;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	enzyme regulator activity ; ATPase activity ; protein binding ; proton-transporting ATPase activity, rotational mechanism ;
Cellular component	cytosol ; plasma membrane ; lysosomal membrane ; extracellular exosome ; vacuolar proton-transporting V-type ATPase, V1 domain ;
Biological process	insulin receptor signaling pathway ; endocytosis ; transferrin transport ; mitigation of host defenses by virus ; ion transport ; ion transmembrane transport ; regulation of macroautophagy ; phagosome acidification ; regulation of catalytic activity ; viral process ; vacuolar acidification ; transport ;
	Sources:Amigo / QuickGO
Orthologs
	51606
	108664
	ENSG00000047249
	ENSMUSG00000033793
	Q9UI12
	Q8BVE3
	NM_015941 ; NM_213619 ; NM_213620
	NM_133826 ; NM_001310442
	NP_057025 ; NP_998784 ; NP_998785 ; NP_998784.1
	NP_001297371 ; NP_598587
	Wikidata
View/Edit Human	View/Edit Mouse

Last updated March 04, 2023

V-type proton ATPase subunit H is an enzyme that in humans is encoded by the ATP6V1H gene.^[5]^[6]^[7]

Function

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.^[7]

Related Research Articles

<span class="mw-page-title-main">V-ATPase</span> Family of transport protein complexes

Vacuolar-type ATPase (V-ATPase) is a highly conserved evolutionarily ancient enzyme with remarkably diverse functions in eukaryotic organisms. V-ATPases acidify a wide array of intracellular organelles and pumps protons across the plasma membranes of numerous cell types. V-ATPases couple the energy of ATP hydrolysis to proton transport across intracellular and plasma membranes of eukaryotic cells. It is generally seen as the polar opposite of ATP synthase because ATP synthase is a proton channel that uses the energy from a proton gradient to produce ATP. V-ATPase however, is a proton pump that uses the energy from ATP hydrolysis to produce a proton gradient.

V-type proton ATPase subunit B, kidney isoform is an enzyme that in humans is encoded by the ATP6V1B1 gene.

V-type proton ATPase subunit E 1 is an enzyme that in humans is encoded by the ATP6V1E1 gene.

The TCIRG1 gene encodes for the V-type proton ATPase (V-ATPase) 116 kDa subunit a isoform 3 enzyme.

V-type proton ATPase 16 kDa proteolipid subunit is an enzyme that in humans is encoded by the ATP6V0C gene.

V-type proton ATPase subunit B, brain isoform is an enzyme that in humans is encoded by the ATP6V1B2 gene.

V-type proton ATPase 116 kDa subunit a isoform 4 is an enzyme that in humans is encoded by the ATP6V0A4 gene.

V-type proton ATPase subunit C 1 is an enzyme that in humans is encoded by the ATP6V1C1 gene.

V-type proton ATPase 116 kDa subunit a isoform 1 is an enzyme that in humans is encoded by the ATP6V0A1 gene.

V-type proton ATPase catalytic subunit A is an enzyme that in humans is encoded by the ATP6V1A gene.

V-type proton ATPase subunit d 1 is an enzyme that in humans is encoded by the ATP6V0D1 gene.

V-type proton ATPase subunit G 2 is an enzyme that in humans is encoded by the ATP6V1G2 gene.

V-type proton ATPase subunit G 1 is an enzyme that in humans is encoded by the ATP6V1G1 gene.

V-type proton ATPase subunit D is an enzyme that in humans is encoded by the ATP6V1D gene.

V-type proton ATPase subunit F is an enzyme that in humans is encoded by the ATP6V1F gene.

V-type proton ATPase subunit G 3 is an enzyme that in humans is encoded by the ATP6V1G3 gene.

V-type proton ATPase 21 kDa proteolipid subunit is an enzyme that in humans is encoded by the ATP6V0B gene.

V-type proton ATPase subunit e 1 is an enzyme that in humans is encoded by the ATP6V0E1 gene.

V-type proton ATPase 116 kDa subunit a isoform 2 also known as V-ATPase 116 kDa isoform a2 is an enzyme that in humans is encoded by the ATP6V0A2 gene.

V-type proton ATPase subunit E 2 is an enzyme that in humans is encoded by the ATP6V1E2 gene.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000047249 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000033793 - Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ Lu X, Yu H, Liu SH, Brodsky FM, Peterlin BM (May 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 (May 2000). "Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics". Genome Research. 10 (5): 703–13. doi:10.1101/gr.10.5.703. PMC 310876 . PMID 10810093.
1 2 "Entrez Gene: ATP6V1H ATPase, H+ transporting, lysosomal 50/57kDa, V1 subunit H".

External links

Human ATP6V1H genome location and ATP6V1H gene details page in the UCSC Genome Browser .

Stevens TH, Forgac M (1998). "Structure, function and regulation of the vacuolar (H+)-ATPase". Annual Review of Cell and Developmental Biology. 13: 779–808. doi:10.1146/annurev.cellbio.13.1.779. PMID 9442887.
Geyer M, Fackler OT, Peterlin BM (Jul 2001). "Structure--function relationships in HIV-1 Nef". EMBO Reports. 2 (7): 580–5. doi:10.1093/embo-reports/kve141. PMC 1083955 . PMID 11463741.
Nishi T, Forgac M (Feb 2002). "The vacuolar (H+)-ATPases--nature's most versatile proton pumps". Nature Reviews Molecular Cell Biology. 3 (2): 94–103. doi:10.1038/nrm729. PMID 11836511. S2CID 21122465.
Pedersen PL (Oct 2002). "Transport ATPases in biological systems and relationship to human disease: a brief overview". Journal of Bioenergetics and Biomembranes. 34 (5): 327–32. doi:10.1023/A:1021249701287. PMID 12539959. S2CID 38318926.
Kawasaki-Nishi S, Nishi T, Forgac M (Jun 2003). "Proton translocation driven by ATP hydrolysis in V-ATPases". FEBS Letters. 545 (1): 76–85. doi:10.1016/S0014-5793(03)00396-X. PMID 12788495. S2CID 10507213.
Morel N (Oct 2003). "Neurotransmitter release: the dark side of the vacuolar-H+ATPase". Biology of the Cell. 95 (7): 453–7. doi: 10.1016/S0248-4900(03)00075-3 . PMID 14597263. S2CID 17519696.
Hu RM, Han ZG, Song HD, Peng YD, Huang QH, Ren SX, Gu YJ, Huang CH, Li YB, Jiang CL, Fu G, Zhang QH, Gu BW, Dai M, Mao YF, Gao GF, Rong R, Ye M, Zhou J, Xu SH, Gu J, Shi JX, Jin WR, Zhang CK, Wu TM, Huang GY, Chen Z, Chen MD, Chen JL (Aug 2000). "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning". Proceedings of the National Academy of Sciences of the United States of America. 97 (17): 9543–8. Bibcode:2000PNAS...97.9543H. doi: 10.1073/pnas.160270997 . PMC 16901 . PMID 10931946.
Mandic R, Fackler OT, Geyer M, Linnemann T, Zheng YH, Peterlin BM (Feb 2001). "Negative factor from SIV binds to the catalytic subunit of the V-ATPase to internalize CD4 and to increase viral infectivity". Molecular Biology of the Cell. 12 (2): 463–73. doi:10.1091/mbc.12.2.463. PMC 30956 . PMID 11179428.
Geyer M, Yu H, Mandic R, Linnemann T, Zheng YH, Fackler OT, Peterlin BM (Aug 2002). "Subunit H of the V-ATPase binds to the medium chain of adaptor protein complex 2 and connects Nef to the endocytic machinery". The Journal of Biological Chemistry. 277 (32): 28521–9. doi: 10.1074/jbc.M200522200 . PMID 12032142.
Geyer M, Fackler OT, Peterlin BM (Jun 2002). "Subunit H of the V-ATPase involved in endocytosis shows homology to beta-adaptins". Molecular Biology of the Cell. 13 (6): 2045–56. doi:10.1091/mbc.02-02-0026. PMC 117623 . PMID 12058068.
Lu M, Vergara S, Zhang L, Holliday LS, Aris J, Gluck SL (Oct 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". The Journal of Biological Chemistry. 277 (41): 38409–15. doi: 10.1074/jbc.M203521200 . PMID 12163484.
Smith AN, Lovering RC, Futai M, Takeda J, Brown D, Karet FE (Oct 2003). "Revised nomenclature for mammalian vacuolar-type H+ -ATPase subunit genes". Molecular Cell. 12 (4): 801–3. doi: 10.1016/S1097-2765(03)00397-6 . PMID 14580332.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000047249 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000033793 - Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid9620685-5] Lu X, Yu H, Liu SH, Brodsky FM, Peterlin BM (May 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.

[pmid10810093-6] Lai CH, Chou CY, Ch'ang LY, Liu CS, Lin W (May 2000). "Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics". Genome Research. 10 (5): 703–13. doi:10.1101/gr.10.5.703. PMC 310876 . PMID 10810093.

[entrez-7] 1 2 "Entrez Gene: ATP6V1H ATPase, H+ transporting, lysosomal 50/57kDa, V1 subunit H".

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ATP6V1H

Contents

Function

Related Research Articles

References

External links

Further reading