ATP6V1E1: Difference between revisions

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{{Infobox_gene}}
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'''V-type proton ATPase subunit E 1''' is an [[enzyme]] that in humans is encoded by the ''ATP6V1E1'' [[gene]].<ref name="pmid8004105">{{cite journal | vauthors = Baud V, Mears AJ, Lamour V, Scamps C, Duncan AM, McDermid HE, Lipinski M | title = The E subunit of vacuolar H(+)-ATPase localizes close to the centromere on human chromosome 22 | journal = Hum Mol Genet | volume = 3 | issue = 2 | pages = 335–9 |date=Jul 1994 | pmid = 8004105 | pmc =  | doi =10.1093/hmg/3.2.335 }}</ref><ref name="pmid8250920">{{cite journal | vauthors = van Hille B, Vanek M, Richener H, Green JR, Bilbe G | title = Cloning and tissue distribution of subunits C, D, and E of the human vacuolar H(+)-ATPase | journal = Biochem Biophys Res Commun | volume = 197 | issue = 1 | pages = 15–21 |date=Jan 1994 | pmid = 8250920 | pmc =  | doi =10.1006/bbrc.1993.2434 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: ATP6V1E1 ATPase, H+ transporting, lysosomal 31kDa, V1 subunit E1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=529| accessdate = }}</ref>
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{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = ATPase, H+ transporting, lysosomal 31kDa, V1 subunit E1
| HGNCid = 857
| Symbol = ATP6V1E1
| AltSymbols =; ATP6E; ATP6E2; ATP6V1E; P31; Vma4
| OMIM = 108746
| ECnumber =
| Homologene = 1282
| MGIid = 894326
  | GeneAtlas_image1 = PBB_GE_ATP6V1E1_208678_at_tn.png
  | Function = {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008553 |text = hydrogen-exporting ATPase activity, phosphorylative mechanism}} {{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:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005739 |text = mitochondrion}} {{GNF_GO|id=GO:0005886 |text = 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:0015991 |text = ATP hydrolysis coupled proton transport}} {{GNF_GO|id=GO:0015992 |text = proton transport}}
  | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 529
    | Hs_Ensembl = ENSG00000131100
    | Hs_RefseqProtein = NP_001034455
    | Hs_RefseqmRNA = NM_001039366
    | Hs_GenLoc_db =   
    | Hs_GenLoc_chr = 22
    | Hs_GenLoc_start = 16454960
    | Hs_GenLoc_end = 16491584
    | Hs_Uniprot = P36543
    | Mm_EntrezGene = 11973
    | Mm_Ensembl = ENSMUSG00000019210
    | Mm_RefseqmRNA = NM_007510
    | Mm_RefseqProtein = NP_031536
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 6
    | Mm_GenLoc_start = 120760865
    | Mm_GenLoc_end = 120788320
    | Mm_Uniprot = Q3UK59
  }}
}}
'''ATPase, H+ transporting, lysosomal 31kDa, V1 subunit E1''', also known as '''ATP6V1E1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ATP6V1E1 ATPase, H+ transporting, lysosomal 31kDa, V1 subunit E1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=529| 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, three B, and two G subunits, as well as a C, D, E, F, and H subunit. The V1 domain contains the ATP catalytic site. This gene encodes alternate transcriptional splice variants, encoding different V1 domain E subunit isoforms. Pseudogenes for this gene have been found in the genome.<ref name="entrez">{{cite web | title = Entrez Gene: ATP6V1E1 ATPase, H+ transporting, lysosomal 31kDa, V1 subunit E1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=529| 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, three B, and two G subunits, as well as a C, D, E, F, and H subunit. The V1 domain contains the ATP catalytic site. This gene encodes [[alternate transcriptional splice]] variants, encoding different V1 domain E subunit isoforms. [[Pseudogene]]s for this gene have been found in the genome.<ref name="entrez" />
}}
}}


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==External links==
* {{UCSC gene info|ATP6V1E1}}
 
==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. | series=324 |journal=Biochem. J. |volume=( Pt 3) |issue=  |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=  1|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=Hemken P, Guo XL, Wang ZQ, ''et al.'' |title=Immunologic evidence that vacuolar H+ ATPases with heterogeneous forms of Mr = 31,000 subunit have different membrane distributions in mammalian kidney. |journal=J. Biol. Chem. |volume=267 |issue= 14 |pages= 9948-57 |year= 1992 |pmid= 1533641 |doi=  }}
*{{cite journal  | vauthors=Hemken P, Guo XL, Wang ZQ |title=Immunologic evidence that vacuolar H+ ATPases with heterogeneous forms of Mr = 31,000 subunit have different membrane distributions in mammalian kidney. |journal=J. Biol. Chem. |volume=267 |issue= 14 |pages= 9948–57 |year= 1992 |pmid= 1533641 |doi=  |display-authors=etal}}
*{{cite journal  | author=Baud V, Mears AJ, Lamour V, ''et al.'' |title=The E subunit of vacuolar H(+)-ATPase localizes close to the centromere on human chromosome 22. |journal=Hum. Mol. Genet. |volume=3 |issue= 2 |pages= 335-9 |year= 1994 |pmid= 8004105 |doi=  }}
*{{cite journal  | vauthors=Puech A, Saint-Jore B, Funke B |title=Comparative mapping of the human 22q11 chromosomal region and the orthologous region in mice reveals complex changes in gene organization. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=94 |issue= 26 |pages= 14608–13 |year= 1998 |pmid= 9405660 |doi=10.1073/pnas.94.26.14608  | pmc=25069 |display-authors=etal}}
*{{cite journal  | author=van Hille B, Vanek M, Richener H, ''et al.'' |title=Cloning and tissue distribution of subunits C, D, and E of the human vacuolar H(+)-ATPase. |journal=Biochem. Biophys. Res. Commun. |volume=197 |issue= 1 |pages= 15-21 |year= 1994 |pmid= 8250920 |doi=  }}
*{{cite journal  | vauthors=Breton S, Wiederhold T, Marshansky V |title=The B1 subunit of the H+ATPase is a PDZ domain-binding protein. Colocalization with NHE-RF in renal B-intercalated cells. |journal=J. Biol. Chem. |volume=275 |issue= 24 |pages= 18219–24 |year= 2000 |pmid= 10748165 |doi= 10.1074/jbc.M909857199 |display-authors=etal}}
*{{cite journal  | author=Puech A, Saint-Jore B, Funke B, ''et al.'' |title=Comparative mapping of the human 22q11 chromosomal region and the orthologous region in mice reveals complex changes in gene organization. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=94 |issue= 26 |pages= 14608-13 |year= 1998 |pmid= 9405660 |doi=  }}
*{{cite journal  | author=Breton S, Wiederhold T, Marshansky V, ''et al.'' |title=The B1 subunit of the H+ATPase is a PDZ domain-binding protein. Colocalization with NHE-RF in renal B-intercalated cells. |journal=J. Biol. Chem. |volume=275 |issue= 24 |pages= 18219-24 |year= 2000 |pmid= 10748165 |doi= 10.1074/jbc.M909857199 }}
}}
}}
{{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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Location (UCSC)n/an/a
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Wikidata
View/Edit Human

V-type proton ATPase subunit E 1 is an enzyme that in humans is encoded by the ATP6V1E1 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, three B, and two G subunits, as well as a C, D, E, F, and H subunit. The V1 domain contains the ATP catalytic site. This gene encodes alternate transcriptional splice variants, encoding different V1 domain E subunit isoforms. Pseudogenes for this gene have been found in the genome.[3]

References

  1. ↑ Baud V, Mears AJ, Lamour V, Scamps C, Duncan AM, McDermid HE, Lipinski M (Jul 1994). "The E subunit of vacuolar H(+)-ATPase localizes close to the centromere on human chromosome 22". Hum Mol Genet. 3 (2): 335–9. doi:10.1093/hmg/3.2.335. PMID 8004105.
  2. ↑ van Hille B, Vanek M, Richener H, Green JR, Bilbe G (Jan 1994). "Cloning and tissue distribution of subunits C, D, and E of the human vacuolar H(+)-ATPase". Biochem Biophys Res Commun. 197 (1): 15–21. doi:10.1006/bbrc.1993.2434. PMID 8250920.
  3. ↑ 3.0 3.1 "Entrez Gene: ATP6V1E1 ATPase, H+ transporting, lysosomal 31kDa, V1 subunit E1".

External links

Further reading



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