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Literature summary for 7.2.2.19 extracted from

  • Pestov, N.B.; Korneenko, T.V.; Shakhparonov, M.I.; Shull, G.E.; Modyanov, N.N.
    Loss of acidification of anterior prostate fluids in Atp12a-null mutant mice indicates that nongastric H-K-ATPase functions as proton pump in vivo (2006), Am. J. Physiol., 291, C366-C374.
    View publication on PubMed

Application

Application Comment Organism
medicine nongastric H-K-ATPase is required for acidification of luminal prostate fluids, operates as a proton pump, beta1 is an authentic subunit of nongastric H-K-ATPase in vivo, apical localization of beta1 in the prostate is completely dependent on its association with the enzyme alpha-subunit Mus musculus

Protein Variants

Protein Variants Comment Organism
additional information targeted deletion of the nongastric H-K-ATPase alpha-subunit, mutant transcript present in amounts comparable to those of wild-type Mus musculus

Localization

Localization Comment Organism GeneOntology No. Textmining
apical plasma membrane in complex with beta1-subunit Mus musculus 16324
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Organism

Organism UniProt Comment Textmining
Mus musculus
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-
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Source Tissue

Source Tissue Comment Organism Textmining
prostate gland anterior Mus musculus
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Synonyms

Synonyms Comment Organism
Atp12a
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Mus musculus
H-K-ATPase
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Mus musculus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.3 8 remarkable reduction in acidification of anterior prostate fluids from 6.38 for wild-type to 6.96 for homozygous mutants Mus musculus