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Complex: Vacuolar proton translocating ATPase complex, Golgi variant

Macromolecular complex annotations are imported from the Complex Portal. These annotations have been derived from physical molecular interaction evidence extracted from the literature and cross-referenced in the entry, or by curator inference from information on homologs in closely related species or by inference from scientific background.

Curated by
IntAct
ComplexAc
CPX-1192
Systematic Name
STV1:3xVMA1:3xVMA2:8xVMA3:3xVMA4:VMA5:VMA6:VMA7:VMA8:VMA9:3xVMA10:VMA11:VMA13:VMA16:VOA1:YPR170W-B
SGD ID
SGD:S000217614
Aliases
V-ATPase complex ; Vacuolar (H+)-ATPase complex
Description
Translocates protons across a lipid bilayer via an ATP-driven rotary mechanism, thus acidifing the lumen of its resident organelle. As newly synthesized proteins traverse the Golgi apparatus they undergo post-translational modifications, including glycosylation, sulfation, and phosphorylation, and are targeted to their appropriate destination in a pH-dependent manner. Membrane-bound ion transporters/proton exchangers use the pH gradient to sequester metal ions to the vacuole and other cellular organelles. The combined action of the V-ATPase and membrane transporters plays a key role in maintaining cellular homoeostasis. The variant of the complex containing the STV1 subunit results in the retention of the V-ATPase complex on Golgi and endosomal membranes. The N-terminal domain of STV1 contains the W83KY sequence, which is necessary and sufficient for targeting the complex to the Golgi apparatus. When yeast cells are deprived of glucose, the V1 and VO regions separate and are no longer able to hydrolyze ATP and transport protons.

Complex Diagram

This diagram displays the protein subunits (blue) of the complex and how they interact with each other. Interactions with other relevant participants such as small molecules (purple), sub-complexes (yellow), and other subunits (red) are also shown. If a participant appears in the diagram with no lines connected to it, then its specific interactions with other participants are currently unknown.

PDB Structure

When available from the Protein Data Bank (PDB), the physical structure of the macromolecular complex is displayed. Click on the image or link for further information about the physical structure.

5BW9 5BW9 5D80 5D80 6C6L 6C6L 6O7U 6O7U 6O7V 6O7V 6O7W 6O7W 6O7X 6O7X EMD-0647 EMD-0647

Subunits

This table lists all participants of the complex (proteins, small molecules, nucleic acids, etc.) and their respective stoichiometry. A brief description is also provided for each participant in the table.

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Subunit Description Stoichiometry

Gene Ontology

Gene Ontology (GO) terms that describe the function of a complex, the biological process in which it participates, or its cellular location. Click on a term for its definition and other objects annotated to that term.

Shared Annotations

This diagram displays Gene Ontology terms (green) and subunits (blue) that are shared between the given macromolecular complex (black) and other yeast complexes (yellow). The shared GO terms or subunits can be visualized separately using the radio button at the bottom of the graph. Note: No diagram is shown ("No shared annotations") if there are less than 2 shared annotations (either GO terms or subunits of other complexes) between this complex and any other complexes.

References

List of references used specifically to curate the information on this page.

External Identifiers

EMDB: EMD-0645 | EMDB: EMD-0646 | EMDB: EMD-0648 | EMDB: EMD-7348 | IntEnz: 7.1.2.2

Resources

IntAct | ModelArchive | PDB:5BW9 | PDB:5D80 | PDB:6C6L | PDB:6O7U | PDB:6O7V | PDB:6O7W | PDB:6O7X | PDB:EMD-0647 ... Show all