ATP6V1A: Difference between revisions

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{{Infobox_gene}}
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'''V-type proton ATPase catalytic subunit A''' is an [[enzyme]] that in humans is encoded by the ''ATP6V1A'' [[gene]].<ref name="pmid8463241">{{cite journal | vauthors = van Hille B, Richener H, Evans DB, Green JR, Bilbe G | title = Identification of two subunit A isoforms of the vacuolar H(+)-ATPase in human osteoclastoma | journal = J Biol Chem | volume = 268 | issue = 10 | pages = 7075–80 |date=May 1993 | pmid = 8463241 | pmc =  | doi =  }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: ATP6V1A ATPase, H+ transporting, lysosomal 70kDa, V1 subunit A| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=523| accessdate = }}</ref>
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{{GNF_Protein_box
| image = 
| image_source = 
| PDB =
| Name = ATPase, H+ transporting, lysosomal 70kDa, V1 subunit A
| HGNCid = 851
| Symbol = ATP6V1A
| AltSymbols =; ATP6A1; ATP6V1A1; HO68; VA68; VPP2; Vma1
| OMIM = 607027
| ECnumber = 
| Homologene = 1277
| MGIid = 1201780
| GeneAtlas_image1 = PBB_GE_ATP6V1A_201972_at_tn.png
| GeneAtlas_image2 = PBB_GE_ATP6V1A_201971_s_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}} {{GNF_GO|id=GO:0046933 |text = hydrogen ion transporting ATP synthase activity, rotational mechanism}} {{GNF_GO|id=GO:0046961 |text = hydrogen ion transporting ATPase activity, rotational mechanism}}
| Component = {{GNF_GO|id=GO:0005739 |text = mitochondrion}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016469 |text = proton-transporting two-sector ATPase complex}}
| Process = {{GNF_GO|id=GO:0006811 |text = ion transport}} {{GNF_GO|id=GO:0015986 |text = ATP synthesis coupled proton transport}} {{GNF_GO|id=GO:0015992 |text = proton transport}}
  | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 523
    | Hs_Ensembl = ENSG00000114573
    | Hs_RefseqProtein = NP_001681
    | Hs_RefseqmRNA = NM_001690
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 3
    | Hs_GenLoc_start = 114948598
    | Hs_GenLoc_end = 115013591
    | Hs_Uniprot = P38606
    | Mm_EntrezGene = 11964
    | Mm_Ensembl = ENSMUSG00000052459
    | Mm_RefseqmRNA = NM_007508
    | Mm_RefseqProtein = NP_031534
    | Mm_GenLoc_db =   
    | Mm_GenLoc_chr = 16
    | Mm_GenLoc_start = 44006114
    | Mm_GenLoc_end = 44058329
    | Mm_Uniprot = Q3TKS0
  }}
}}
'''ATPase, H+ transporting, lysosomal 70kDa, V1 subunit A''', also known as '''ATP6V1A''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ATP6V1A ATPase, H+ transporting, lysosomal 70kDa, V1 subunit A| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=523| accessdate = }}</ref>


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{{PBB_Summary
{{PBB_Summary
| section_title =  
| section_title =  
| summary_text = 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&quot;, and d. Additional isoforms of many of the V1 and V0 subunit proteins are encoded by multiple genes or alternatively spliced transcript variants. This encoded protein is one of two V1 domain A subunit isoforms and is found in all tissues. Transcript variants derived from alternative polyadenylation exist.<ref name="entrez">{{cite web | title = Entrez Gene: ATP6V1A ATPase, H+ transporting, lysosomal 70kDa, V1 subunit A| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=523| accessdate = }}</ref>
| summary_text = 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 encoded protein is one of two V1 domain A subunit isoforms and is found in all tissues. Transcript variants derived from alternative polyadenylation exist.<ref name="entrez" />
}}
}}


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==External links==
* {{UCSC gene info|ATP6V1A}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal  | author=Finbow ME, Harrison MA |title=The vacuolar H+-ATPase: a universal proton pump of eukaryotes. |journal=Biochem. J. |volume=324 ( Pt 3) |issue=  |pages= 697-712 |year= 1997 |pmid= 9210392 |doi=  }}
*{{cite journal  | vauthors=Finbow ME, Harrison MA |title=The vacuolar H+-ATPase: a universal proton pump of eukaryotes |journal=Biochem. J. |volume=324 |issue=  Pt 3|pages= 697–712 |year= 1997 |pmid= 9210392 |doi= 10.1042/bj3240697| pmc=1218484 }}
*{{cite journal  | author=Stevens TH, Forgac M |title=Structure, function and regulation of the vacuolar (H+)-ATPase. |journal=Annu. Rev. Cell Dev. Biol. |volume=13 |issue=  |pages= 779-808 |year= 1998 |pmid= 9442887 |doi= 10.1146/annurev.cellbio.13.1.779 }}
*{{cite journal  | vauthors=Stevens TH, Forgac M |title=Structure, function and regulation of the vacuolar (H+)-ATPase |journal=Annu. Rev. Cell Dev. Biol. |volume=13 |issue=  |pages= 779–808 |year= 1998 |pmid= 9442887 |doi= 10.1146/annurev.cellbio.13.1.779 }}
*{{cite journal  | author=Nelson N, Harvey WR |title=Vacuolar and plasma membrane proton-adenosinetriphosphatases. |journal=Physiol. Rev. |volume=79 |issue= 2 |pages= 361-85 |year= 1999 |pmid= 10221984 |doi=  }}
*{{cite journal  | vauthors=Nelson N, Harvey WR |title=Vacuolar and plasma membrane proton-adenosinetriphosphatases |journal=Physiol. Rev. |volume=79 |issue= 2 |pages= 361–85 |year= 1999 |pmid= 10221984 |doi=  }}
*{{cite journal  | author=Forgac M |title=Structure and properties of the vacuolar (H+)-ATPases. |journal=J. Biol. Chem. |volume=274 |issue= 19 |pages= 12951-4 |year= 1999 |pmid= 10224039 |doi=  }}
*{{cite journal  | author=Forgac M |title=Structure and properties of the vacuolar (H+)-ATPases |journal=J. Biol. Chem. |volume=274 |issue= 19 |pages= 12951–4 |year= 1999 |pmid= 10224039 |doi=10.1074/jbc.274.19.12951 }}
*{{cite journal  | author=Kane PM |title=Introduction: V-ATPases 1992-1998. |journal=J. Bioenerg. Biomembr. |volume=31 |issue= 1 |pages= 3-5 |year= 1999 |pmid= 10340843 |doi=  }}
*{{cite journal  | author=Kane PM |title=Introduction: V-ATPases 1992-1998 |journal=J. Bioenerg. Biomembr. |volume=31 |issue= 1 |pages= 3–5 |year= 1999 |pmid= 10340843 |doi=10.1023/A:1001884227654 }}
*{{cite journal  | author=Wieczorek H, Brown D, Grinstein S, ''et al.'' |title=Animal plasma membrane energization by proton-motive V-ATPases. |journal=Bioessays |volume=21 |issue= 8 |pages= 637-48 |year= 1999 |pmid= 10440860 |doi= 10.1002/(SICI)1521-1878(199908)21:8<637::AID-BIES3>3.0.CO;2-W }}
*{{cite journal  | vauthors=Wieczorek H, Brown D, Grinstein S |title=Animal plasma membrane energization by proton-motive V-ATPases |journal=BioEssays |volume=21 |issue= 8 |pages= 637–48 |year= 1999 |pmid= 10440860 |doi= 10.1002/(SICI)1521-1878(199908)21:8<637::AID-BIES3>3.0.CO;2-W |display-authors=etal}}
*{{cite journal  | author=Nishi T, Forgac M |title=The vacuolar (H+)-ATPases--nature's most versatile proton pumps. |journal=Nat. Rev. Mol. Cell Biol. |volume=3 |issue= 2 |pages= 94-103 |year= 2002 |pmid= 11836511 |doi= 10.1038/nrm729 }}
*{{cite journal  | vauthors=Nishi T, Forgac M |title=The vacuolar (H+)-ATPases--nature's most versatile proton pumps |journal=Nat. Rev. Mol. Cell Biol. |volume=3 |issue= 2 |pages= 94–103 |year= 2002 |pmid= 11836511 |doi= 10.1038/nrm729 }}
*{{cite journal  | author=Kawasaki-Nishi S, Nishi T, Forgac M |title=Proton translocation driven by ATP hydrolysis in V-ATPases. |journal=FEBS Lett. |volume=545 |issue= 1 |pages= 76-85 |year= 2003 |pmid= 12788495 |doi=  }}
*{{cite journal  | vauthors=Kawasaki-Nishi S, Nishi T, Forgac M |title=Proton translocation driven by ATP hydrolysis in V-ATPases |journal=FEBS Lett. |volume=545 |issue= 1 |pages= 76–85 |year= 2003 |pmid= 12788495 |doi=10.1016/S0014-5793(03)00396-X }}
*{{cite journal  | author=Morel N |title=Neurotransmitter release: the dark side of the vacuolar-H+ATPase. |journal=Biol. Cell |volume=95 |issue= 7 |pages= 453-7 |year= 2004 |pmid= 14597263 |doi=  }}
*{{cite journal  | author=Morel N |title=Neurotransmitter release: the dark side of the vacuolar-H+ATPase |journal=Biol. Cell |volume=95 |issue= 7 |pages= 453–7 |year= 2004 |pmid= 14597263 |doi=10.1016/S0248-4900(03)00075-3 }}
*{{cite journal  | author=van Hille B, Richener H, Green JR, Bilbe G |title=The ubiquitous VA68 isoform of subunit A of the vacuolar H(+)-ATPase is highly expressed in human osteoclasts. |journal=Biochem. Biophys. Res. Commun. |volume=214 |issue= 3 |pages= 1108-13 |year= 1995 |pmid= 7575517 |doi= }}
*{{cite journal  | vauthors=van Hille B, Richener H, Green JR, Bilbe G |title=The ubiquitous VA68 isoform of subunit A of the vacuolar H(+)-ATPase is highly expressed in human osteoclasts |journal=Biochem. Biophys. Res. Commun. |volume=214 |issue= 3 |pages= 1108–13 |year= 1995 |pmid= 7575517 |doi=10.1006/bbrc.1995.2400 }}
*{{cite journal  | author=van Hille B, Richener H, Evans DB, ''et al.'' |title=Identification of two subunit A isoforms of the vacuolar H(+)-ATPase in human osteoclastoma. |journal=J. Biol. Chem. |volume=268 |issue= 10 |pages= 7075-80 |year= 1993 |pmid= 8463241 |doi= }}
*{{cite journal  | vauthors=Hu RM, Han ZG, Song HD |title=Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 17 |pages= 9543–8 |year= 2000 |pmid= 10931946 |doi= 10.1073/pnas.160270997 | pmc=16901 |display-authors=etal}}
*{{cite journal  | author=Hu RM, Han ZG, Song HD, ''et al.'' |title=Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 17 |pages= 9543-8 |year= 2000 |pmid= 10931946 |doi= 10.1073/pnas.160270997 }}
*{{cite journal  | vauthors=Chang SY, Park SG, Kim S, Kang CY |title=Interaction of the C-terminal domain of p43 and the alpha subunit of ATP synthase. Its functional implication in endothelial cell proliferation |journal=J. Biol. Chem. |volume=277 |issue= 10 |pages= 8388–94 |year= 2002 |pmid= 11741979 |doi= 10.1074/jbc.M108792200 }}
*{{cite journal  | author=Chang SY, Park SG, Kim S, Kang CY |title=Interaction of the C-terminal domain of p43 and the alpha subunit of ATP synthase. Its functional implication in endothelial cell proliferation. |journal=J. Biol. Chem. |volume=277 |issue= 10 |pages= 8388-94 |year= 2002 |pmid= 11741979 |doi= 10.1074/jbc.M108792200 }}
}}
}}
{{refend}}
{{refend}}


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Latest revision as of 18:27, 29 August 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

V-type proton ATPase catalytic subunit A is an enzyme that in humans is encoded by the ATP6V1A gene.[1][2]

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 encoded protein is one of two V1 domain A subunit isoforms and is found in all tissues. Transcript variants derived from alternative polyadenylation exist.[2]

References

  1. ↑ van Hille B, Richener H, Evans DB, Green JR, Bilbe G (May 1993). "Identification of two subunit A isoforms of the vacuolar H(+)-ATPase in human osteoclastoma". J Biol Chem. 268 (10): 7075–80. PMID 8463241.
  2. ↑ 2.0 2.1 "Entrez Gene: ATP6V1A ATPase, H+ transporting, lysosomal 70kDa, V1 subunit A".

External links

Further reading



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