ATP6V0C: Difference between revisions

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{{Infobox_gene}}
{{PBB_Controls
'''V-type proton ATPase 16 kDa proteolipid subunit''' is an [[enzyme]] that in humans is encoded by the ''ATP6V0C'' [[gene]].<ref name="pmid1709739">{{cite journal | vauthors = Gillespie GA, Somlo S, Germino GG, Weinstat-Saslow D, Reeders ST | title = CpG island in the region of an autosomal dominant polycystic kidney disease locus defines the 5' end of a gene encoding a putative proton channel | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 88 | issue = 10 | pages = 4289–93 | date = May 1991 | pmid = 1709739 | pmc = 51644 | doi = 10.1073/pnas.88.10.4289 }}</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 = Biochemical and Biophysical Research Communications | volume = 197 | issue = 1 | pages = 15–21 | date = Nov 1993 | pmid = 8250920 | pmc = | doi = 10.1006/bbrc.1993.2434 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: ATP6V0C ATPase, H+ transporting, lysosomal 16kDa, V0 subunit c| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=527| accessdate = }}</ref>
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = ATPase, H+ transporting, lysosomal 16kDa, V0 subunit c
| HGNCid = 855
| Symbol = ATP6V0C
| AltSymbols =; ATP6C; ATP6L; ATPL; VATL; Vma3
| OMIM = 108745
| ECnumber = 
| Homologene = 68199
| MGIid = 88116
| GeneAtlas_image1 = PBB_GE_ATP6V0C_36994_at_tn.png
| GeneAtlas_image2 = PBB_GE_ATP6V0C_200954_at_tn.png
| Function = {{GNF_GO|id=GO:0005515 |text = protein 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:0005773 |text = vacuole}} {{GNF_GO|id=GO:0016020 |text = 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 = 527
    | Hs_Ensembl = ENSG00000185883
    | Hs_RefseqProtein = XP_001130742
    | Hs_RefseqmRNA = XM_001130742
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 16
    | Hs_GenLoc_start = 2503872
    | Hs_GenLoc_end = 2510213
    | Hs_Uniprot = P27449
    | Mm_EntrezGene = 11984
    | Mm_Ensembl = ENSMUSG00000024121
    | Mm_RefseqmRNA = NM_009729
    | Mm_RefseqProtein = NP_033859
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 17
    | Mm_GenLoc_start = 23891488
    | Mm_GenLoc_end = 23897038
    | Mm_Uniprot = Q3UK60
  }}
}}
'''ATPase, H+ transporting, lysosomal 16kDa, V0 subunit c''', also known as '''ATP6V0C''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ATP6V0C ATPase, H+ transporting, lysosomal 16kDa, V0 subunit c| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=527| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
This gene encodes a component of [[vacuolar]] [[ATPase]] (V-ATPase), a multisubunit enzyme that mediates acidification of [[eukaryotic]] intracellular [[organelle]]s. 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 part of the V0 domain. This gene had the previous symbols of ATP6C and ATP6L.<ref name="entrez" />
{{PBB_Summary
| 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 part of the V0 domain. This gene had the previous symbols of ATP6C and ATP6L.<ref name="entrez">{{cite web | title = Entrez Gene: ATP6V0C ATPase, H+ transporting, lysosomal 16kDa, V0 subunit c| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=527| accessdate = }}</ref>
}}


==References==
== References ==
{{reflist|2}}
{{reflist}}
==Further reading==
 
==External links==
* {{UCSC gene info|ATP6V0C}}
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Finbow ME, Harrison MA | title = The vacuolar H+-ATPase: a universal proton pump of eukaryotes | journal = The Biochemical Journal | volume = 324 | issue = Pt 3 | pages = 697–712 | date = Jun 1997 | pmid = 9210392 | pmc = 1218484 | doi =  10.1042/bj3240697}}
| citations =
* {{cite journal | vauthors = Stevens TH, Forgac M | title = Structure, function and regulation of the vacuolar (H+)-ATPase | journal = Annual Review of Cell and Developmental Biology | volume = 13 | issue =  | pages = 779–808 | year = 1998 | pmid = 9442887 | doi = 10.1146/annurev.cellbio.13.1.779 }}
*{{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 = Nelson N, Harvey WR | title = Vacuolar and plasma membrane proton-adenosinetriphosphatases | journal = Physiological Reviews | volume = 79 | issue = 2 | pages = 361–85 | date = Apr 1999 | pmid = 10221984 | doi =  }}
*{{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 = Forgac M | title = Structure and properties of the vacuolar (H+)-ATPases | journal = The Journal of Biological Chemistry | volume = 274 | issue = 19 | pages = 12951–4 | date = May 1999 | pmid = 10224039 | doi = 10.1074/jbc.274.19.12951 }}
*{{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 = Kane PM | title = Introduction: V-ATPases 1992-1998 | journal = Journal of Bioenergetics and Biomembranes | volume = 31 | issue = 1 | pages = 3–5 | date = Feb 1999 | pmid = 10340843 | doi = 10.1023/A:1001884227654 }}
*{{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 | vauthors = Wieczorek H, Brown D, Grinstein S, Ehrenfeld J, Harvey WR | title = Animal plasma membrane energization by proton-motive V-ATPases | journal = BioEssays | volume = 21 | issue = 8 | pages = 637–48 | date = Aug 1999 | pmid = 10440860 | doi = 10.1002/(SICI)1521-1878(199908)21:8<637::AID-BIES3>3.0.CO;2-W }}
*{{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 | vauthors = Nishi T, Forgac M | title = The vacuolar (H+)-ATPases--nature's most versatile proton pumps | journal = Nature Reviews Molecular Cell Biology | volume = 3 | issue = 2 | pages = 94–103 | date = Feb 2002 | pmid = 11836511 | doi = 10.1038/nrm729 }}
*{{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 = Kawasaki-Nishi S, Nishi T, Forgac M | title = Proton translocation driven by ATP hydrolysis in V-ATPases | journal = FEBS Letters | volume = 545 | issue = 1 | pages = 76–85 | date = Jun 2003 | pmid = 12788495 | doi = 10.1016/S0014-5793(03)00396-X }}
*{{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 = Morel N | title = Neurotransmitter release: the dark side of the vacuolar-H+ATPase | journal = Biology of the Cell / Under the Auspices of the European Cell Biology Organization | volume = 95 | issue = 7 | pages = 453–7 | date = Oct 2003 | pmid = 14597263 | doi = 10.1016/S0248-4900(03)00075-3 }}
*{{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 = Hasebe M, Hanada H, Moriyama Y, Maeda M, Futai M | title = Vacuolar type H(+)-ATPase genes: presence of four genes including pseudogenes for the 16-kDa proteolipid subunit in the human genome | journal = Biochemical and Biophysical Research Communications | volume = 183 | issue = 2 | pages = 856–63 | date = Mar 1992 | pmid = 1532310 | doi = 10.1016/0006-291X(92)90562-Y }}
*{{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 | vauthors = Koralnik IJ, Mulloy JC, Andresson T, Fullen J, Franchini G | title = Mapping of the intermolecular association of human T cell leukaemia/lymphotropic virus type I p12I and the vacuolar H+-ATPase 16 kDa subunit protein | journal = The Journal of General Virology | volume = 76 | issue = 8 | pages = 1909–16 | date = Aug 1995 | pmid = 7636472 | doi = 10.1099/0022-1317-76-8-1909 }}
*{{cite journal | author=Hasebe M, Hanada H, Moriyama Y, ''et al.'' |title=Vacuolar type H(+)-ATPase genes: presence of four genes including pseudogenes for the 16-kDa proteolipid subunit in the human genome. |journal=Biochem. Biophys. Res. Commun. |volume=183 |issue= 2 |pages= 856-63 |year= 1992 |pmid= 1532310 |doi= }}
* {{cite journal | vauthors = Laitala-Leinonen T, Howell ML, Dean GE, Väänänen HK | title = Resorption-cycle-dependent polarization of mRNAs for different subunits of V-ATPase in bone-resorbing osteoclasts | journal = Molecular Biology of the Cell | volume = 7 | issue = 1 | pages = 129–42 | date = Jan 1996 | pmid = 8741845 | pmc = 278618 | doi = 10.1091/mbc.7.1.129 }}
*{{cite journal  | author=Gillespie GA, Somlo S, Germino GG, ''et al.'' |title=CpG island in the region of an autosomal dominant polycystic kidney disease locus defines the 5' end of a gene encoding a putative proton channel. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=88 |issue= 10 |pages= 4289-93 |year= 1991 |pmid= 1709739 |doi=  }}
*{{cite journal | author=Koralnik IJ, Mulloy JC, Andresson T, ''et al.'' |title=Mapping of the intermolecular association of human T cell leukaemia/lymphotropic virus type I p12I and the vacuolar H+-ATPase 16 kDa subunit protein. |journal=J. Gen. Virol. |volume=76 ( Pt 8) |issue= |pages= 1909-16 |year= 1995 |pmid= 7636472 |doi= }}
*{{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 | author=Laitala-Leinonen T, Howell ML, Dean GE, Väänänen HK |title=Resorption-cycle-dependent polarization of mRNAs for different subunits of V-ATPase in bone-resorbing osteoclasts. |journal=Mol. Biol. Cell |volume=7 |issue= 1 |pages= 129-42 |year= 1996 |pmid= 8741845 |doi= }}
}}
{{refend}}
{{refend}}


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Latest revision as of 18:26, 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 16 kDa proteolipid subunit is an enzyme that in humans is encoded by the ATP6V0C gene.[1][2][3]

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 encoded protein is part of the V0 domain. This gene had the previous symbols of ATP6C and ATP6L.[3]

References

  1. ↑ Gillespie GA, Somlo S, Germino GG, Weinstat-Saslow D, Reeders ST (May 1991). "CpG island in the region of an autosomal dominant polycystic kidney disease locus defines the 5' end of a gene encoding a putative proton channel". Proceedings of the National Academy of Sciences of the United States of America. 88 (10): 4289–93. doi:10.1073/pnas.88.10.4289. PMC 51644. PMID 1709739.
  2. ↑ van Hille B, Vanek M, Richener H, Green JR, Bilbe G (Nov 1993). "Cloning and tissue distribution of subunits C, D, and E of the human vacuolar H(+)-ATPase". Biochemical and Biophysical Research Communications. 197 (1): 15–21. doi:10.1006/bbrc.1993.2434. PMID 8250920.
  3. ↑ 3.0 3.1 "Entrez Gene: ATP6V0C ATPase, H+ transporting, lysosomal 16kDa, V0 subunit c".

External links

Further reading


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