UniProt functional annotation for P00829



	UniProt functional annotation for P00829

UniProt code: P00829.

Organism: Bos taurus (Bovine).

Taxonomy: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; Bovinae; Bos.

Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. {ECO:0000269|PubMed:23407638, ECO:0000269|PubMed:9687365}.

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;

Subunit: F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a, b and c. Component of an ATP synthase complex composed of ATP5PB, ATP5MC1, ATP5F1E, ATP5PD, ATP5ME, ATP5PF, ATP5MF, MT-ATP6, MT- ATP8, ATP5F1A, ATP5F1B, ATP5F1D, ATP5F1C, ATP5PO, ATP5MG, ATP5MK and ATP5MJ (PubMed:17570365, PubMed:12923572, PubMed:17895376, PubMed:25851905). Interacts with PPIF (PubMed:19801635). Interacts with BCL2L1 isoform BCL-X(L); the interaction mediates the association of BCL2L1 isoform BCL-X(L) with the mitochondrial membrane F(1)F(0) ATP synthase and enhances neurons metabolic efficiency. Interacts with CLN5 and PPT1 (By similarity). Interacts with S100A1; this interaction increases F1-ATPase activity (By similarity). Interacts with MTLN (By similarity). {ECO:0000250|UniProtKB:P06576, ECO:0000250|UniProtKB:P10719, ECO:0000250|UniProtKB:P56480, ECO:0000269|PubMed:12923572, ECO:0000269|PubMed:17570365, ECO:0000269|PubMed:17895376, ECO:0000269|PubMed:19801635, ECO:0000269|PubMed:23407638, ECO:0000269|PubMed:25851905, ECO:0000269|PubMed:8065448, ECO:0000269|PubMed:8790345, ECO:0000269|PubMed:9687365}.

Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:14633978, ECO:0000269|PubMed:23407638, ECO:0000269|PubMed:2864455, ECO:0000269|PubMed:8065448, ECO:0000269|PubMed:95168}; Peripheral membrane protein {ECO:0000269|PubMed:14633978, ECO:0000269|PubMed:23407638, ECO:0000269|PubMed:2864455, ECO:0000269|PubMed:8065448, ECO:0000269|PubMed:95168}; Matrix side {ECO:0000269|PubMed:14633978, ECO:0000269|PubMed:95168}.

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

Annotations taken from UniProtKB at the EBI.


Organism:		Bos taurus (Bovine).
Taxonomy:		Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; Bovinae; Bos.



Function:		Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. {ECO:0000269\|PubMed:23407638, ECO:0000269\|PubMed:9687365}.


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;
Subunit:		F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a, b and c. Component of an ATP synthase complex composed of ATP5PB, ATP5MC1, ATP5F1E, ATP5PD, ATP5ME, ATP5PF, ATP5MF, MT-ATP6, MT- ATP8, ATP5F1A, ATP5F1B, ATP5F1D, ATP5F1C, ATP5PO, ATP5MG, ATP5MK and ATP5MJ (PubMed:17570365, PubMed:12923572, PubMed:17895376, PubMed:25851905). Interacts with PPIF (PubMed:19801635). Interacts with BCL2L1 isoform BCL-X(L); the interaction mediates the association of BCL2L1 isoform BCL-X(L) with the mitochondrial membrane F(1)F(0) ATP synthase and enhances neurons metabolic efficiency. Interacts with CLN5 and PPT1 (By similarity). Interacts with S100A1; this interaction increases F1-ATPase activity (By similarity). Interacts with MTLN (By similarity). {ECO:0000250\|UniProtKB:P06576, ECO:0000250\|UniProtKB:P10719, ECO:0000250\|UniProtKB:P56480, ECO:0000269\|PubMed:12923572, ECO:0000269\|PubMed:17570365, ECO:0000269\|PubMed:17895376, ECO:0000269\|PubMed:19801635, ECO:0000269\|PubMed:23407638, ECO:0000269\|PubMed:25851905, ECO:0000269\|PubMed:8065448, ECO:0000269\|PubMed:8790345, ECO:0000269\|PubMed:9687365}.
Subcellular location:		Mitochondrion inner membrane {ECO:0000269\|PubMed:14633978, ECO:0000269\|PubMed:23407638, ECO:0000269\|PubMed:2864455, ECO:0000269\|PubMed:8065448, ECO:0000269\|PubMed:95168}; Peripheral membrane protein {ECO:0000269\|PubMed:14633978, ECO:0000269\|PubMed:23407638, ECO:0000269\|PubMed:2864455, ECO:0000269\|PubMed:8065448, ECO:0000269\|PubMed:95168}; Matrix side {ECO:0000269\|PubMed:14633978, ECO:0000269\|PubMed:95168}.
Similarity:		Belongs to the ATPase alpha/beta chains family. {ECO:0000305}.