UniProt functional annotation for P17255



	UniProt functional annotation for P17255

UniProt code: P17255.

Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).

Taxonomy: Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.

Function: Catalytic subunit of the peripheral V1 complex of vacuolar ATPase. V-ATPase (vacuolar ATPase) is responsible for acidifying a variety of intracellular compartments in eukaryotic cells. It is an electrogenic proton pump that generates a proton motive force of 180 mV, inside positive and acidic, in the vacuolar membrane vesicles. It may participate in maintenance of cytoplasmic Ca(2+) homeostasis. This is a catalytic subunit. {ECO:0000269|PubMed:1534148}.

Function: PI-SceI is an endonuclease that can cleave at a site present in a VMA1 allele that lacks the derived endonuclease segment of the open reading frame; cleavage at this site only occurs during meiosis and initiates 'homing', a genetic event that converts a VMA1 allele lacking VDE into one that contains it. {ECO:0000269|PubMed:1534148}.

Catalytic activity: Reaction=ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate; Xref=Rhea:RHEA:57720, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.1.2.2; Evidence={ECO:0000255|PROSITE-ProRule:PRU10106};

Subunit: V-ATPase is a heteromultimeric enzyme composed of a peripheral catalytic V1 complex (components A to H) attached to an integral membrane V0 proton pore complex (components: a, c, c', c'', d and e). Interacts with RAV1 and RAV2 components of the RAVE complex, which are essential for the stability and assembly of V-ATPase. {ECO:0000269|PubMed:11283612, ECO:0000269|PubMed:2139027}.

Subcellular location: Endomembrane system {ECO:0000269|PubMed:14562095}. Vacuole membrane {ECO:0000305|PubMed:14562095}. Note=Membranes of various intracellular acidic compartments.

Ptm: This protein undergoes a protein self splicing that involves a post-translational excision of the VDE intervening region (intein) followed by peptide ligation.

Miscellaneous: Present with 199895 molecules/cell in log phase SD medium. {ECO:0000269|PubMed:14562106}.

Similarity: Belongs to the ATPase alpha/beta chains family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Taxonomy:		Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.



Function:		Catalytic subunit of the peripheral V1 complex of vacuolar ATPase. V-ATPase (vacuolar ATPase) is responsible for acidifying a variety of intracellular compartments in eukaryotic cells. It is an electrogenic proton pump that generates a proton motive force of 180 mV, inside positive and acidic, in the vacuolar membrane vesicles. It may participate in maintenance of cytoplasmic Ca(2+) homeostasis. This is a catalytic subunit. {ECO:0000269\|PubMed:1534148}.



Function:		PI-SceI is an endonuclease that can cleave at a site present in a VMA1 allele that lacks the derived endonuclease segment of the open reading frame; cleavage at this site only occurs during meiosis and initiates 'homing', a genetic event that converts a VMA1 allele lacking VDE into one that contains it. {ECO:0000269\|PubMed:1534148}.


Catalytic activity:		Reaction=ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate; Xref=Rhea:RHEA:57720, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.1.2.2; Evidence={ECO:0000255\|PROSITE-ProRule:PRU10106};
Subunit:		V-ATPase is a heteromultimeric enzyme composed of a peripheral catalytic V1 complex (components A to H) attached to an integral membrane V0 proton pore complex (components: a, c, c', c'', d and e). Interacts with RAV1 and RAV2 components of the RAVE complex, which are essential for the stability and assembly of V-ATPase. {ECO:0000269\|PubMed:11283612, ECO:0000269\|PubMed:2139027}.
Subcellular location:		Endomembrane system {ECO:0000269\|PubMed:14562095}. Vacuole membrane {ECO:0000305\|PubMed:14562095}. Note=Membranes of various intracellular acidic compartments.
Ptm:		This protein undergoes a protein self splicing that involves a post-translational excision of the VDE intervening region (intein) followed by peptide ligation.
Miscellaneous:		Present with 199895 molecules/cell in log phase SD medium. {ECO:0000269\|PubMed:14562106}.
Similarity:		Belongs to the ATPase alpha/beta chains family. {ECO:0000305}.