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{{Infobox_gene}}
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'''V-type proton ATPase subunit G 2''' is an [[enzyme]] that in humans is encoded by the ''ATP6V1G2'' [[gene]].<ref name="pmid10202016">{{cite journal | vauthors = Neville MJ, Campbell RD | title = A new member of the Ig superfamily and a V-ATPase G subunit are among the predicted products of novel genes close to the TNF locus in the human MHC | journal = J Immunol | volume = 162 | issue = 8 | pages = 4745–54 |date=May 1999 | pmid = 10202016 | pmc =  | doi =  }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: ATP6V1G2 ATPase, H+ transporting, lysosomal 13kDa, V1 subunit G2| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=534| accessdate = }}</ref>
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{{GNF_Protein_box
| image =
| image_source = 
| PDB =
| Name = ATPase, H+ transporting, lysosomal 13kDa, V1 subunit G2
| HGNCid = 862
| Symbol = ATP6V1G2
| AltSymbols =; ATP6G; ATP6G2; NG38; VMA10
| OMIM = 606853
| ECnumber = 
| Homologene = 41518
| MGIid = 1913487
| Function = {{GNF_GO|id=GO:0005515 |text = protein binding}} {{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 = 534
    | Hs_Ensembl = 
    | Hs_RefseqProtein = NP_569730
    | Hs_RefseqmRNA = NM_130463
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 
    | Hs_GenLoc_start =
    | Hs_GenLoc_end =
    | Hs_Uniprot =   
    | Mm_EntrezGene = 66237
    | Mm_Ensembl = ENSMUSG00000024403
    | Mm_RefseqmRNA = NM_023179
    | Mm_RefseqProtein = NP_075668
    | Mm_GenLoc_db =   
    | Mm_GenLoc_chr = 17
    | Mm_GenLoc_start = 34844652
    | Mm_GenLoc_end = 34846817
    | Mm_Uniprot = Q54A87
  }}
}}
'''ATPase, H+ transporting, lysosomal 13kDa, V1 subunit G2''', also known as '''ATP6V1G2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ATP6V1G2 ATPase, H+ transporting, lysosomal 13kDa, V1 subunit G2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=534| 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 intracellular compartments of eukaryotic cells. V-ATPase dependent 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 three V1 domain G subunit proteins. This gene had previous gene symbols of ATP6G and ATP6G2. Alternatively spliced transcript variants encoding different isoforms have been described.<ref name="entrez">{{cite web | title = Entrez Gene: ATP6V1G2 ATPase, H+ transporting, lysosomal 13kDa, V1 subunit G2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=534| accessdate = }}</ref>
| summary_text = This gene encodes a component of vacuolar ATPase (V-ATPase), a multisubunit enzyme that mediates acidification of intracellular compartments of eukaryotic cells. V-ATPase dependent 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 three V1 domain G subunit proteins. This gene had previous gene symbols of ATP6G and ATP6G2. Alternatively spliced transcript variants encoding different isoforms have been described.<ref name="entrez"/>
}}
}}


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==External links==
* {{UCSC gene info|ATP6V1G2}}
 
==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=  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=Neville MJ, Campbell RD |title=A new member of the Ig superfamily and a V-ATPase G subunit are among the predicted products of novel genes close to the TNF locus in the human MHC. |journal=J. Immunol. |volume=162 |issue= 8 |pages= 4745-54 |year= 1999 |pmid= 10202016 |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 |year= 2003 |pmid= 12384298 |doi=10.1016/S0378-1119(02)00884-3 }}
*{{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  | vauthors=Strausberg RL, Feingold EA, Grouse LH |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 | pmc=139241 |display-authors=etal}}
*{{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 }}
*{{cite journal  | vauthors=Gevaert K, Goethals M, Martens L |title=Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. |journal=Nat. Biotechnol. |volume=21 |issue= 5 |pages= 566–9 |year= 2004 |pmid= 12665801 |doi= 10.1038/nbt810 |display-authors=etal}}
*{{cite journal  | author=Gevaert K, Goethals M, Martens L, ''et al.'' |title=Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. |journal=Nat. Biotechnol. |volume=21 |issue= 5 |pages= 566-9 |year= 2004 |pmid= 12665801 |doi= 10.1038/nbt810 }}
}}
}}
{{refend}}
{{refend}}
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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

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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 2 is an enzyme that in humans is encoded by the ATP6V1G2 gene.[1][2]

This gene encodes a component of vacuolar ATPase (V-ATPase), a multisubunit enzyme that mediates acidification of intracellular compartments of eukaryotic cells. V-ATPase dependent 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 three V1 domain G subunit proteins. This gene had previous gene symbols of ATP6G and ATP6G2. Alternatively spliced transcript variants encoding different isoforms have been described.[2]

References

  1. ↑ Neville MJ, Campbell RD (May 1999). "A new member of the Ig superfamily and a V-ATPase G subunit are among the predicted products of novel genes close to the TNF locus in the human MHC". J Immunol. 162 (8): 4745–54. PMID 10202016.
  2. ↑ 2.0 2.1 "Entrez Gene: ATP6V1G2 ATPase, H+ transporting, lysosomal 13kDa, V1 subunit G2".

External links

Further reading



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