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Search results 1 to 14 out of 14 for Vma12

0.012s

Type

Details

Score

Protein

Q5SYH2

Organism:	Mus musculus/domesticus
Length:	208
Fragment?:	false

•

Protein

Q3TZ80

Organism:	Mus musculus/domesticus
Length:	208
Fragment?:	false

•

Protein

B2RV69

Organism:	Mus musculus/domesticus
Length:	208
Fragment?:	false

•

Protein

Q3U0H6

Organism:	Mus musculus/domesticus
Length:	206
Fragment?:	true

•

Publication

10340847 | -

First Author:	Graham LA
Year:	1999
Journal:	J Bioenerg Biomembr
Title:	Assembly of the yeast vacuolar proton-translocating ATPase.
Volume:	31
Issue:	1
Pages:	39-47

•

Protein Domain

IPR021013 | ATPase_Vma12

Type:

Family

Description:

Transmembrane ATPases are membrane-bound enzyme complexes/ion transporters that use ATP hydrolysis to drive the transport of protons across a membrane. Some transmembrane ATPases also work in reverse, harnessing the energy from a proton gradient, using the flux of ions across the membrane via the ATPase proton channel to drive the synthesis of ATP. There are several different types of transmembrane ATPases, which can differ in function (ATP hydrolysis and/or synthesis), structure (e.g., F-, V- and A-ATPases, which contain rotary motors) and in the type of ions they transport [, ]. The different types include:F-ATPases (ATP synthases, F1F0-ATPases), which are found in mitochondria, chloroplasts and bacterial plasma membranes where they are the prime producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts).V-ATPases (V1V0-ATPases), which are primarily found in eukaryotes and they function as proton pumps that acidify intracellular compartments and, in some cases, transport protons across the plasma membrane []. They are also found in bacteria [].A-ATPases (A1A0-ATPases), which are found in Archaea and function like F-ATPases, though with respect to their structure and some inhibitor responses, A-ATPases are more closely related to the V-ATPases [, ].P-ATPases (E1E2-ATPases), which are found in bacteria and in eukaryotic plasma membranes and organelles, and function to transport a variety of different ions across membranes.E-ATPases, which are cell-surface enzymes that hydrolyse a range of NTPs, including extracellular ATP.V-ATPases (also known as V1V0-ATPase or vacuolar ATPase) are found in the eukaryotic endomembrane system, and in the plasma membrane of prokaryotes and certain specialised eukaryotic cells. V-ATPases hydrolyse ATP to drive a proton pump, and are involved in a variety of vital intra- and inter-cellular processes such as receptor mediated endocytosis, protein trafficking, active transport of metabolites, homeostasis and neurotransmitter release []. V-ATPases are composed of two linked complexes: the V1 complex (subunits A-H) contains the catalytic core that hydrolyses ATP, while the V0 complex (subunits a, c, c', c'', d) forms the membrane-spanning pore. V-ATPases may have an additional role in membrane fusion through binding to t-SNARE proteins [].The yeast vacuolar proton-translocating ATPase (V-ATPase) is the best characterised member of the V-ATPase family. A total of thirteen genes are required for encoding the subunits of the enzyme complex itself and an additional three for providing factors necessary for the assembly of the whole. Vma12 is one of these latter, all three of which are localised to the endoplasmic reticulum [].

•

Publication

15907459 | -

First Author:	Bajjalieh S
Year:	2005
Journal:	Cell
Title:	A new view of an old pore.
Volume:	121
Issue:	4
Pages:	496-7

•

Publication

15629643 | -

First Author:	Wilkens S
Year:	2005
Journal:	Micron
Title:	A structural model of the vacuolar ATPase from transmission electron microscopy.
Volume:	36
Issue:	2
Pages:	109-26

•

Publication

15473999 | -

First Author:	Cross RL
Year:	2004
Journal:	FEBS Lett
Title:	The evolution of A-, F-, and V-type ATP synthases and ATPases: reversals in function and changes in the H+/ATP coupling ratio.
Volume:	576
Issue:	1-2
Pages:	1-4

•

Publication

15078220 | -

First Author:	Rappas M
Year:	2004
Journal:	Curr Protein Pept Sci
Title:	Mechanisms of ATPases--a multi-disciplinary approach.
Volume:	5
Issue:	2
Pages:	89-105

•

Publication

20450191 | -

First Author:	Toei M
Year:	2010
Journal:	Biochemistry
Title:	Regulation and isoform function of the V-ATPases.
Volume:	49
Issue:	23
Pages:	4715-23

•

Publication

18937357 | -

First Author:	Grüber G
Year:	2008
Journal:	Bioessays
Title:	New insights into structure-function relationships between archeal ATP synthase (A1A0) and vacuolar type ATPase (V1V0).
Volume:	30
Issue:	11-12
Pages:	1096-109

•

Publication

1385979 | -

First Author:	Schäfer G
Year:	1992
Journal:	Biochim Biophys Acta
Title:	F-type or V-type? The chimeric nature of the archaebacterial ATP synthase.
Volume:	1101
Issue:	2
Pages:	232-5

•

Publication

9741106 | -

First Author:	Radax C
Year:	1998
Journal:	Syst Appl Microbiol
Title:	F-and V-ATPases in the genus Thermus and related species.
Volume:	21
Issue:	1
Pages:	12-22

•

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