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ATPase, H+ transporting, lysosomal 21kDa, V0 subunit b
Symbols ATP6V0B ; ATP6F; HATPL; VMA16
External IDs OMIM603717 MGI1890510 HomoloGene2986 GeneCards: ATP6V0B Gene
EC number
RNA expression pattern
PBB GE ATP6V0B 200078 s at tn.png
More reference expression data
Species Human Mouse
Entrez 533 114143
Ensembl ENSG00000117410 ENSMUSG00000033379
UniProt Q99437 Q91V37
RefSeq (mRNA) NM_001039457 NM_033617
RefSeq (protein) NP_001034546 NP_291095
Location (UCSC) Chr 1:
43.97 – 43.98 Mb
Chr 4:
117.88 – 117.89 Mb
PubMed search [1] [2]

V-type proton ATPase 21 kDa proteolipid subunit is an enzyme that in humans is encoded by the ATP6V0B gene.[1][2]

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 transmembrane V0 domain and is the human counterpart of yeast VMA16. Two alternatively spliced transcript variants that encode different proteins have been found for this gene.[2]


  1. ^ Nishigori H, Yamada S, Tomura H, Fernald AA, Le Beau MM, Takeuchi T, Takeda J (Oct 1998). "Identification and characterization of the gene encoding a second proteolipid subunit of human vacuolar H(+)-ATPase (ATP6F)". Genomics 50 (2): 222–8. doi:10.1006/geno.1998.5310. PMID 9653649. 
  2. ^ a b "Entrez Gene: ATP6V0B ATPase, H+ transporting, lysosomal 21kDa, V0 subunit b". 

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