ATP6V1G3

Protein-coding gene in the species Homo sapiens
ATP6V1G3
Identifiers
AliasesATP6V1G3, ATP6G3, Vma10, ATPase H+ transporting V1 subunit G3
External IDsOMIM: 618071; MGI: 2450548; HomoloGene: 13630; GeneCards: ATP6V1G3; OMA:ATP6V1G3 - orthologs
Gene location (Human)
Chromosome 1 (human)
Chr.Chromosome 1 (human)[1]
Chromosome 1 (human)
Genomic location for ATP6V1G3
Genomic location for ATP6V1G3
Band1q31.3Start198,523,222 bp[1]
End198,540,945 bp[1]
Gene location (Mouse)
Chromosome 1 (mouse)
Chr.Chromosome 1 (mouse)[2]
Chromosome 1 (mouse)
Genomic location for ATP6V1G3
Genomic location for ATP6V1G3
Band1|1 E4Start138,201,476 bp[2]
End138,217,200 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • kidney

  • minor salivary glands

  • lymph node

  • ganglionic eminence

  • thymus

  • bone marrow

  • prostate

  • placenta

  • spleen

  • liver
Top expressed in
  • kidney

  • renal cortex

  • skin

  • zone of skin

  • limb
More reference expression data
BioGPS
n/a
Gene ontology
Molecular function
  • ATPase binding
  • P-type proton-exporting transporter activity
  • ATPase-coupled transmembrane transporter activity
Cellular component
  • cytosol
  • plasma membrane
  • vacuolar proton-transporting V-type ATPase complex
Biological process
  • proton transmembrane transport
  • insulin receptor signaling pathway
  • ion transmembrane transport
  • ion transport
  • transferrin transport
  • phagosome acidification
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

127124

338375

Ensembl

ENSG00000151418
ENSG00000263014

ENSMUSG00000026394

UniProt

Q96LB4

Q8BMC1

RefSeq (mRNA)
NM_133262
NM_133326
NM_001320218
NM_001376861
NM_001376862

NM_001376863

NM_177397

RefSeq (protein)
NP_001307147
NP_573569
NP_579872
NP_001363790
NP_001363791

NP_001363792

NP_796371

Location (UCSC)Chr 1: 198.52 – 198.54 MbChr 1: 138.2 – 138.22 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

V-type proton ATPase subunit G 3 is an enzyme that in humans is encoded by the ATP6V1G3 gene.[5][6]

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.[6]

References

  1. ^ a b c ENSG00000263014 GRCh38: Ensembl release 89: ENSG00000151418, ENSG00000263014 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000026394 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ 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.
  6. ^ a b "Entrez Gene: ATP6V1G3 ATPase, H+ transporting, lysosomal 13kDa, V1 subunit G3".


Further reading

  • Finbow ME, Harrison MA (Jun 1997). "The vacuolar H+-ATPase: a universal proton pump of eukaryotes". The Biochemical Journal. 324 (Pt 3): 697–712. doi:10.1042/bj3240697. PMC 1218484. PMID 9210392.
  • Nelson N, Harvey WR (Apr 1999). "Vacuolar and plasma membrane proton-adenosinetriphosphatases". Physiological Reviews. 79 (2): 361–85. doi:10.1152/physrev.1999.79.2.361. PMID 10221984. S2CID 1477911.
  • Forgac M (May 1999). "Structure and properties of the vacuolar (H+)-ATPases". The Journal of Biological Chemistry. 274 (19): 12951–4. doi:10.1074/jbc.274.19.12951. PMID 10224039.
  • Kane PM (Feb 1999). "Introduction: V-ATPases 1992-1998". Journal of Bioenergetics and Biomembranes. 31 (1): 3–5. doi:10.1023/A:1001884227654. PMID 10340843.
  • Wieczorek H, Brown D, Grinstein S, Ehrenfeld J, Harvey WR (Aug 1999). "Animal plasma membrane energization by proton-motive V-ATPases". BioEssays. 21 (8): 637–48. doi:10.1002/(SICI)1521-1878(199908)21:8<637::AID-BIES3>3.0.CO;2-W. PMID 10440860. S2CID 23505139.
  • Nishi T, Forgac M (Feb 2002). "The vacuolar (H+)-ATPases--nature's most versatile proton pumps". Nature Reviews Molecular Cell Biology. 3 (2): 94–103. doi:10.1038/nrm729. PMID 11836511. S2CID 21122465.
  • Kawasaki-Nishi S, Nishi T, Forgac M (Jun 2003). "Proton translocation driven by ATP hydrolysis in V-ATPases". FEBS Letters. 545 (1): 76–85. doi:10.1016/S0014-5793(03)00396-X. PMID 12788495. S2CID 10507213.
  • Morel N (Oct 2003). "Neurotransmitter release: the dark side of the vacuolar-H+ATPase". Biology of the Cell. 95 (7): 453–7. doi:10.1016/S0248-4900(03)00075-3. PMID 14597263.
  • Brown D, Lui B, Gluck S, Sabolić I (Oct 1992). "A plasma membrane proton ATPase in specialized cells of rat epididymis". The American Journal of Physiology. 263 (4 Pt 1): C913–6. doi:10.1152/ajpcell.1992.263.4.C913. PMID 1415677.
  • Smith AN, Borthwick KJ, Karet FE (Sep 2002). "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". Gene. 297 (1–2): 169–77. doi:10.1016/S0378-1119(02)00884-3. PMID 12384298.

External links


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