Cardiolipin synthase; produces cardiolipin, which is a phospholipid of the mitochondrial inner membrane that is required for normal mitochondrial membrane potential and function and for correct integration of membrane-multispanning proteins into the mitochondrial outer membrane; required to maintain tubular mitochondrial morphology and functions in mitochondrial fusion; also required for normal vacuolar ion homeostasis; Belongs to the CDP-alcohol phosphatidyltransferase class-I family.

Phosphatidylserine decarboxylase of the mitochondrial inner membrane; converts phosphatidylserine to phosphatidylethanolamine; regulates mitochondrial fusion and morphology by affecting lipid mixing in the mitochondrial membrane and by influencing the ratio of long to short forms of Mgm1p; partly exposed to the mitochondrial intermembrane space; autocatalytically processed; Belongs to the phosphatidylserine decarboxylase family. PSD-B subfamily. Eukaryotic type I sub-subfamily.

Cardiolipin synthase; produces cardiolipin, which is a phospholipid of the mitochondrial inner membrane that is required for normal mitochondrial membrane potential and function and for correct integration of membrane-multispanning proteins into the mitochondrial outer membrane; required to maintain tubular mitochondrial morphology and functions in mitochondrial fusion; also required for normal vacuolar ion homeostasis; Belongs to the CDP-alcohol phosphatidyltransferase class-I family.

Phosphatidylserine decarboxylase 2 alpha chain; Phosphatidylserine decarboxylase of the Golgi and vacuolar membranes; converts phosphatidylserine to phosphatidylethanolamine; controls vacuolar membrane phospholipid content by regulating phospholipids in compartments that will eventually give rise to the vacuole; loss of Psd2p causes a specific reduction in vacuolar membrane PE levels while total PE levels are not significantly affected.

Cardiolipin synthase; produces cardiolipin, which is a phospholipid of the mitochondrial inner membrane that is required for normal mitochondrial membrane potential and function and for correct integration of membrane-multispanning proteins into the mitochondrial outer membrane; required to maintain tubular mitochondrial morphology and functions in mitochondrial fusion; also required for normal vacuolar ion homeostasis; Belongs to the CDP-alcohol phosphatidyltransferase class-I family.

V-type proton ATPase subunit B; Subunit B of V1 peripheral membrane domain of vacuolar H+-ATPase; electrogenic proton pump found throughout the endomembrane system; contains nucleotide binding sites; also detected in the cytoplasm; protein abundance increases in response to DNA replication stress; human homolog ATP6V1B1, implicated in autosomal-recessive distal renal tubular acidosis (RTA) with sensorineural deafness, complements yeast null mutant; Belongs to the ATPase alpha/beta chains family.

Phosphatidylserine decarboxylase of the mitochondrial inner membrane; converts phosphatidylserine to phosphatidylethanolamine; regulates mitochondrial fusion and morphology by affecting lipid mixing in the mitochondrial membrane and by influencing the ratio of long to short forms of Mgm1p; partly exposed to the mitochondrial intermembrane space; autocatalytically processed; Belongs to the phosphatidylserine decarboxylase family. PSD-B subfamily. Eukaryotic type I sub-subfamily.

Cardiolipin synthase; produces cardiolipin, which is a phospholipid of the mitochondrial inner membrane that is required for normal mitochondrial membrane potential and function and for correct integration of membrane-multispanning proteins into the mitochondrial outer membrane; required to maintain tubular mitochondrial morphology and functions in mitochondrial fusion; also required for normal vacuolar ion homeostasis; Belongs to the CDP-alcohol phosphatidyltransferase class-I family.

Phosphatidylserine decarboxylase of the mitochondrial inner membrane; converts phosphatidylserine to phosphatidylethanolamine; regulates mitochondrial fusion and morphology by affecting lipid mixing in the mitochondrial membrane and by influencing the ratio of long to short forms of Mgm1p; partly exposed to the mitochondrial intermembrane space; autocatalytically processed; Belongs to the phosphatidylserine decarboxylase family. PSD-B subfamily. Eukaryotic type I sub-subfamily.

Phosphatidylserine decarboxylase 2 alpha chain; Phosphatidylserine decarboxylase of the Golgi and vacuolar membranes; converts phosphatidylserine to phosphatidylethanolamine; controls vacuolar membrane phospholipid content by regulating phospholipids in compartments that will eventually give rise to the vacuole; loss of Psd2p causes a specific reduction in vacuolar membrane PE levels while total PE levels are not significantly affected.

Phosphatidylserine decarboxylase 2 alpha chain; Phosphatidylserine decarboxylase of the Golgi and vacuolar membranes; converts phosphatidylserine to phosphatidylethanolamine; controls vacuolar membrane phospholipid content by regulating phospholipids in compartments that will eventually give rise to the vacuole; loss of Psd2p causes a specific reduction in vacuolar membrane PE levels while total PE levels are not significantly affected.

Cardiolipin synthase; produces cardiolipin, which is a phospholipid of the mitochondrial inner membrane that is required for normal mitochondrial membrane potential and function and for correct integration of membrane-multispanning proteins into the mitochondrial outer membrane; required to maintain tubular mitochondrial morphology and functions in mitochondrial fusion; also required for normal vacuolar ion homeostasis; Belongs to the CDP-alcohol phosphatidyltransferase class-I family.

Phosphatidylserine decarboxylase 2 alpha chain; Phosphatidylserine decarboxylase of the Golgi and vacuolar membranes; converts phosphatidylserine to phosphatidylethanolamine; controls vacuolar membrane phospholipid content by regulating phospholipids in compartments that will eventually give rise to the vacuole; loss of Psd2p causes a specific reduction in vacuolar membrane PE levels while total PE levels are not significantly affected.

Phosphatidylserine decarboxylase of the mitochondrial inner membrane; converts phosphatidylserine to phosphatidylethanolamine; regulates mitochondrial fusion and morphology by affecting lipid mixing in the mitochondrial membrane and by influencing the ratio of long to short forms of Mgm1p; partly exposed to the mitochondrial intermembrane space; autocatalytically processed; Belongs to the phosphatidylserine decarboxylase family. PSD-B subfamily. Eukaryotic type I sub-subfamily.

Subunit A of the V1 peripheral membrane domain of V-ATPase; protein precursor undergoes self-catalyzed splicing to yield the extein Tfp1p and the intein Vde (PI-SceI), which is a site-specific endonuclease; the V1 peripheral membrane domain of the vacuolar H+-ATPase (V-ATPase) has eight subunits; involved in methionine restriction extension of chronological lifespan in an autophagy-dependent manner; Belongs to the ATPase alpha/beta chains family.

Vacuolar ATPase V0 domain subunit c'; involved in proton transport activity; hydrophobic integral membrane protein (proteolipid) containing four transmembrane segments; N and C termini are in the vacuolar lumen.

Subunit A of the V1 peripheral membrane domain of V-ATPase; protein precursor undergoes self-catalyzed splicing to yield the extein Tfp1p and the intein Vde (PI-SceI), which is a site-specific endonuclease; the V1 peripheral membrane domain of the vacuolar H+-ATPase (V-ATPase) has eight subunits; involved in methionine restriction extension of chronological lifespan in an autophagy-dependent manner; Belongs to the ATPase alpha/beta chains family.

Subunit H of the V1 peripheral membrane domain of V-ATPase; part of the electrogenic proton pump found throughout the endomembrane system; serves as an activator or a structural stabilizer of the V-ATPase; the V1 peripheral membrane domain of the vacuolar H+-ATPase (V-ATPase) has eight subunits.

Subunit A of the V1 peripheral membrane domain of V-ATPase; protein precursor undergoes self-catalyzed splicing to yield the extein Tfp1p and the intein Vde (PI-SceI), which is a site-specific endonuclease; the V1 peripheral membrane domain of the vacuolar H+-ATPase (V-ATPase) has eight subunits; involved in methionine restriction extension of chronological lifespan in an autophagy-dependent manner; Belongs to the ATPase alpha/beta chains family.

V-type proton ATPase subunit B; Subunit B of V1 peripheral membrane domain of vacuolar H+-ATPase; electrogenic proton pump found throughout the endomembrane system; contains nucleotide binding sites; also detected in the cytoplasm; protein abundance increases in response to DNA replication stress; human homolog ATP6V1B1, implicated in autosomal-recessive distal renal tubular acidosis (RTA) with sensorineural deafness, complements yeast null mutant; Belongs to the ATPase alpha/beta chains family.

Subunit A of the V1 peripheral membrane domain of V-ATPase; protein precursor undergoes self-catalyzed splicing to yield the extein Tfp1p and the intein Vde (PI-SceI), which is a site-specific endonuclease; the V1 peripheral membrane domain of the vacuolar H+-ATPase (V-ATPase) has eight subunits; involved in methionine restriction extension of chronological lifespan in an autophagy-dependent manner; Belongs to the ATPase alpha/beta chains family.

V-type proton ATPase subunit c; Proteolipid subunit c of the V0 domain of vacuolar H(+)-ATPase; dicyclohexylcarbodiimide binding subunit; required for vacuolar acidification and important for copper and iron metal ion homeostasis; Belongs to the V-ATPase proteolipid subunit family.

Subunit A of the V1 peripheral membrane domain of V-ATPase; protein precursor undergoes self-catalyzed splicing to yield the extein Tfp1p and the intein Vde (PI-SceI), which is a site-specific endonuclease; the V1 peripheral membrane domain of the vacuolar H+-ATPase (V-ATPase) has eight subunits; involved in methionine restriction extension of chronological lifespan in an autophagy-dependent manner; Belongs to the ATPase alpha/beta chains family.

Integral membrane protein required for V-ATPase function; not an actual component of the vacuolar H+-ATPase (V-ATPase) complex; functions in the assembly of the V-ATPase; localized to the endoplasmic reticulum (ER); involved in methionine restriction extension of chronological lifespan in an autophagy-dependent manner.

Vacuolar ATPase V0 domain subunit c'; involved in proton transport activity; hydrophobic integral membrane protein (proteolipid) containing four transmembrane segments; N and C termini are in the vacuolar lumen.

Subunit A of the V1 peripheral membrane domain of V-ATPase; protein precursor undergoes self-catalyzed splicing to yield the extein Tfp1p and the intein Vde (PI-SceI), which is a site-specific endonuclease; the V1 peripheral membrane domain of the vacuolar H+-ATPase (V-ATPase) has eight subunits; involved in methionine restriction extension of chronological lifespan in an autophagy-dependent manner; Belongs to the ATPase alpha/beta chains family.

Vacuolar ATPase V0 domain subunit c'; involved in proton transport activity; hydrophobic integral membrane protein (proteolipid) containing four transmembrane segments; N and C termini are in the vacuolar lumen.

Subunit H of the V1 peripheral membrane domain of V-ATPase; part of the electrogenic proton pump found throughout the endomembrane system; serves as an activator or a structural stabilizer of the V-ATPase; the V1 peripheral membrane domain of the vacuolar H+-ATPase (V-ATPase) has eight subunits.

Vacuolar ATPase V0 domain subunit c'; involved in proton transport activity; hydrophobic integral membrane protein (proteolipid) containing four transmembrane segments; N and C termini are in the vacuolar lumen.

V-type proton ATPase subunit B; Subunit B of V1 peripheral membrane domain of vacuolar H+-ATPase; electrogenic proton pump found throughout the endomembrane system; contains nucleotide binding sites; also detected in the cytoplasm; protein abundance increases in response to DNA replication stress; human homolog ATP6V1B1, implicated in autosomal-recessive distal renal tubular acidosis (RTA) with sensorineural deafness, complements yeast null mutant; Belongs to the ATPase alpha/beta chains family.

Vacuolar ATPase V0 domain subunit c'; involved in proton transport activity; hydrophobic integral membrane protein (proteolipid) containing four transmembrane segments; N and C termini are in the vacuolar lumen.

V-type proton ATPase subunit c; Proteolipid subunit c of the V0 domain of vacuolar H(+)-ATPase; dicyclohexylcarbodiimide binding subunit; required for vacuolar acidification and important for copper and iron metal ion homeostasis; Belongs to the V-ATPase proteolipid subunit family.

Vacuolar ATPase V0 domain subunit c'; involved in proton transport activity; hydrophobic integral membrane protein (proteolipid) containing four transmembrane segments; N and C termini are in the vacuolar lumen.

Integral membrane protein required for V-ATPase function; not an actual component of the vacuolar H+-ATPase (V-ATPase) complex; functions in the assembly of the V-ATPase; localized to the endoplasmic reticulum (ER); involved in methionine restriction extension of chronological lifespan in an autophagy-dependent manner.

Subunit H of the V1 peripheral membrane domain of V-ATPase; part of the electrogenic proton pump found throughout the endomembrane system; serves as an activator or a structural stabilizer of the V-ATPase; the V1 peripheral membrane domain of the vacuolar H+-ATPase (V-ATPase) has eight subunits.

Subunit A of the V1 peripheral membrane domain of V-ATPase; protein precursor undergoes self-catalyzed splicing to yield the extein Tfp1p and the intein Vde (PI-SceI), which is a site-specific endonuclease; the V1 peripheral membrane domain of the vacuolar H+-ATPase (V-ATPase) has eight subunits; involved in methionine restriction extension of chronological lifespan in an autophagy-dependent manner; Belongs to the ATPase alpha/beta chains family.

Subunit H of the V1 peripheral membrane domain of V-ATPase; part of the electrogenic proton pump found throughout the endomembrane system; serves as an activator or a structural stabilizer of the V-ATPase; the V1 peripheral membrane domain of the vacuolar H+-ATPase (V-ATPase) has eight subunits.

Vacuolar ATPase V0 domain subunit c'; involved in proton transport activity; hydrophobic integral membrane protein (proteolipid) containing four transmembrane segments; N and C termini are in the vacuolar lumen.

Subunit H of the V1 peripheral membrane domain of V-ATPase; part of the electrogenic proton pump found throughout the endomembrane system; serves as an activator or a structural stabilizer of the V-ATPase; the V1 peripheral membrane domain of the vacuolar H+-ATPase (V-ATPase) has eight subunits.

V-type proton ATPase subunit B; Subunit B of V1 peripheral membrane domain of vacuolar H+-ATPase; electrogenic proton pump found throughout the endomembrane system; contains nucleotide binding sites; also detected in the cytoplasm; protein abundance increases in response to DNA replication stress; human homolog ATP6V1B1, implicated in autosomal-recessive distal renal tubular acidosis (RTA) with sensorineural deafness, complements yeast null mutant; Belongs to the ATPase alpha/beta chains family.