Difference between revisions of "YGR105W"

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'''Description of YGR105W:''' Integral membrane protein that is required for vacuolar H+-ATPase (V-ATPase) function, although not an actual component of the V-ATPase complex; functions in the assembly of the V-ATPase; localized to the yeast endoplasmic reticulum (ER)<ref name='S000058276'>Stevens TH and Forgac M (1997) Structure, function and regulation of the vacuolar (H+)-ATPase. Annu Rev Cell Dev Biol 13():779-808 {{SGDpaper|S000058276}} PMID 9442887</ref><ref name='S000056370'>Graham LA and Stevens TH (1999) Assembly of the yeast vacuolar proton-translocating ATPase. J Bioenerg Biomembr 31(1):39-47 {{SGDpaper|S000056370}} PMID 10340847</ref><ref name='S000051726'>Hirata R, et al. (1993) VMA12 is essential for assembly of the vacuolar H(+)-ATPase subunits onto the vacuolar membrane in Saccharomyces cerevisiae. J Biol Chem 268(2):961-7 {{SGDpaper|S000051726}} PMID 8419376</ref><ref name='S000045629'>Hill KJ and Stevens TH (1994) Vma21p is a yeast membrane protein retained in the endoplasmic reticulum by a di-lysine motif and is required for the assembly of the vacuolar H(+)-ATPase complex. Mol Biol Cell 5(9):1039-50
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'''Description of YGR105W:''' Integral membrane protein that is required for vacuolar H+-ATPase (V-ATPase) function, although not an actual component of the V-ATPase complex; functions in the assembly of the V-ATPase; localized to the yeast endoplasmic reticulum (ER)<ref name='S000058276'>Stevens TH and Forgac M (1997) Structure, function and regulation of the vacuolar (H+)-ATPase. Annu Rev Cell Dev Biol 13:779-808 {{SGDpaper|S000058276}} PMID 9442887</ref><ref name='S000056370'>Graham LA and Stevens TH (1999) Assembly of the yeast vacuolar proton-translocating ATPase. J Bioenerg Biomembr 31(1):39-47 {{SGDpaper|S000056370}} PMID 10340847</ref><ref name='S000051726'>Hirata R, et al. (1993) VMA12 is essential for assembly of the vacuolar H(+)-ATPase subunits onto the vacuolar membrane in Saccharomyces cerevisiae. J Biol Chem 268(2):961-7 {{SGDpaper|S000051726}} PMID 8419376</ref><ref name='S000045629'>Hill KJ and Stevens TH (1994) Vma21p is a yeast membrane protein retained in the endoplasmic reticulum by a di-lysine motif and is required for the assembly of the vacuolar H(+)-ATPase complex. Mol Biol Cell 5(9):1039-50
 
  {{SGDpaper|S000045629}} PMID 7841520</ref>
 
  {{SGDpaper|S000045629}} PMID 7841520</ref>
 
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Revision as of 14:05, 18 July 2007

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Systematic name YGR105W
Gene name VMA21
Aliases
Feature type ORF, Verified
Coordinates Chr VII:698603..698836
Primary SGDID S000003337


Description of YGR105W: Integral membrane protein that is required for vacuolar H+-ATPase (V-ATPase) function, although not an actual component of the V-ATPase complex; functions in the assembly of the V-ATPase; localized to the yeast endoplasmic reticulum (ER)[1][2][3][4]




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References

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  1. Stevens TH and Forgac M (1997) Structure, function and regulation of the vacuolar (H+)-ATPase. Annu Rev Cell Dev Biol 13:779-808 SGD PMID 9442887
  2. Graham LA and Stevens TH (1999) Assembly of the yeast vacuolar proton-translocating ATPase. J Bioenerg Biomembr 31(1):39-47 SGD PMID 10340847
  3. Hirata R, et al. (1993) VMA12 is essential for assembly of the vacuolar H(+)-ATPase subunits onto the vacuolar membrane in Saccharomyces cerevisiae. J Biol Chem 268(2):961-7 SGD PMID 8419376
  4. Hill KJ and Stevens TH (1994) Vma21p is a yeast membrane protein retained in the endoplasmic reticulum by a di-lysine motif and is required for the assembly of the vacuolar H(+)-ATPase complex. Mol Biol Cell 5(9):1039-50 SGD PMID 7841520

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