ATP6V1G3: Difference between revisions

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{{Infobox_gene}}
{{PBB_Controls
'''V-type proton ATPase subunit G 3''' is an [[enzyme]] that in humans is encoded by the ''ATP6V1G3'' [[gene]].<ref name="pmid9442887">{{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 | date = Feb 1998 | pmid = 9442887 | pmc = | doi = 10.1146/annurev.cellbio.13.1.779 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: ATP6V1G3 ATPase, H+ transporting, lysosomal 13kDa, V1 subunit G3| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=127124| accessdate = }}</ref>
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| update_protein_box = yes
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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 13kDa, V1 subunit G3
| HGNCid = 18265
| Symbol = ATP6V1G3
| AltSymbols =; Vma10; ATP6G3; MGC119810; MGC119813
| OMIM = 
| ECnumber = 
| Homologene = 13630
| MGIid = 2450548
| Function = {{GNF_GO|id=GO:0015078 |text = hydrogen ion transmembrane transporter activity}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component =
| Process = {{GNF_GO|id=GO:0006754 |text = ATP biosynthetic process}} {{GNF_GO|id=GO:0006811 |text = ion transport}} {{GNF_GO|id=GO:0015992 |text = proton transport}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 127124
    | Hs_Ensembl = ENSG00000151418
    | Hs_RefseqProtein = NP_573569
    | Hs_RefseqmRNA = NM_133262
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 1
    | Hs_GenLoc_start = 196758975
    | Hs_GenLoc_end = 196776698
    | Hs_Uniprot = Q96LB4
    | Mm_EntrezGene = 338375
    | Mm_Ensembl = ENSMUSG00000026394
    | Mm_RefseqmRNA = NM_177397
    | Mm_RefseqProtein = NP_796371
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 1
    | Mm_GenLoc_start = 140090149
    | Mm_GenLoc_end = 140105873
    | Mm_Uniprot = 
  }}
}}
'''ATPase, H+ transporting, lysosomal 13kDa, V1 subunit G3''', also known as '''ATP6V1G3''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ATP6V1G3 ATPase, H+ transporting, lysosomal 13kDa, V1 subunit G3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=127124| 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<nowiki>''</nowiki> 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 one of three G subunit proteins. Transcript variants encoding different isoforms have been found for this gene.<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'' 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 one of three G subunit proteins. Transcript variants encoding different isoforms have been found for this gene.<ref name="entrez">{{cite web | title = Entrez Gene: ATP6V1G3 ATPase, H+ transporting, lysosomal 13kDa, V1 subunit G3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=127124| accessdate = }}</ref>
}}


==References==
== References ==
{{reflist|2}}
{{reflist}}
==Further reading==
 
==External links==
* {{UCSC gene info|ATP6V1G3}}
 
== 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 = 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=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 = 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=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 = 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=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 = 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=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 = 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=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 = 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=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 = 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=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 = Brown D, Lui B, Gluck S, Sabolić I | title = A plasma membrane proton ATPase in specialized cells of rat epididymis | journal = The American Journal of Physiology | volume = 263 | issue = 4 Pt 1 | pages = C913–6 | date = Oct 1992 | pmid = 1415677 | doi =  }}
*{{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 = Smith AN, Borthwick KJ, Karet FE | title = Molecular cloning and characterization of novel tissue-specific isoforms of the human vacuolar H(+)-ATPase C, G and d subunits, and their evaluation in autosomal recessive distal renal tubular acidosis | journal = Gene | volume = 297 | issue = 1-2 | pages = 169–77 | date = Sep 2002 | pmid = 12384298 | doi = 10.1016/S0378-1119(02)00884-3 }}
*{{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=Brown D, Lui B, Gluck S, Sabolić I |title=A plasma membrane proton ATPase in specialized cells of rat epididymis. |journal=Am. J. Physiol. |volume=263 |issue= 4 Pt 1 |pages= C913-6 |year= 1992 |pmid= 1415677 |doi=  }}
*{{cite journal | author=Smith AN, Borthwick KJ, Karet FE |title=Molecular cloning and characterization of novel tissue-specific isoforms of the human vacuolar H(+)-ATPase C, G and d subunits, and their evaluation in autosomal recessive distal renal tubular acidosis. |journal=Gene |volume=297 |issue= 1-2 |pages= 169-77 |year= 2003 |pmid= 12384298 |doi= }}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
}}
{{refend}}
{{refend}}


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Latest revision as of 18:28, 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

n/a

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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 subunit G 3 is an enzyme that in humans is encoded by the ATP6V1G3 gene.[1][2]

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 one of three G subunit proteins. Transcript variants encoding different isoforms have been found for this gene.[2]

References

  1. ↑ Stevens TH, Forgac M (Feb 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.
  2. ↑ 2.0 2.1 "Entrez Gene: ATP6V1G3 ATPase, H+ transporting, lysosomal 13kDa, V1 subunit G3".

External links

Further reading


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