UniProt functional annotation for P19483



	UniProt functional annotation for P19483

UniProt code: P19483.

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. Subunit alpha does not bear the catalytic high-affinity ATP-binding sites. Binds the bacterial siderophore enterobactin and can promote mitochondrial accumulation of enterobactin-derived iron ions (By similarity). {ECO:0000250|UniProtKB:P25705, ECO:0000269|PubMed:17570365, ECO:0000269|PubMed:23407638}.

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) (PubMed:2864455, PubMed:17570365, PubMed:23407638). CF(0) has three main subunits: a, b and c (PubMed:2864455, PubMed:17570365, PubMed:23407638). Interacts with ATPAF2 (By similarity). Interacts with HRG; the interaction occurs on the surface of T-cells and alters the cell morphology when associated with concanavalin (in vitro) (By similarity). 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:2864455, PubMed:17570365, PubMed:23407638, PubMed:25851905). Interacts with BLOC1S1. 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 ABCB7; this interaction allows the regulation of cellular iron homeostasis and cellular reactive oxygen species (ROS) levels in cardiomyocytes (By similarity). {ECO:0000250|UniProtKB:P15999, ECO:0000250|UniProtKB:P25705, ECO:0000250|UniProtKB:Q03265, ECO:0000269|PubMed:12923572, ECO:0000269|PubMed:17570365, ECO:0000269|PubMed:17895376, ECO:0000269|PubMed:23407638, ECO:0000269|PubMed:25851905, ECO:0000269|PubMed:2864455}.

Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:14633978, ECO:0000269|PubMed:23407638, ECO:0000269|PubMed:2864455, ECO:0000269|PubMed:95168}; Peripheral membrane protein {ECO:0000269|PubMed:14633978, ECO:0000269|PubMed:23407638, ECO:0000269|PubMed:2864455, ECO:0000269|PubMed:95168}; Matrix side {ECO:0000269|PubMed:14633978, ECO:0000269|PubMed:95168}. Cell membrane {ECO:0000250|UniProtKB:P25705}; Peripheral membrane protein {ECO:0000250|UniProtKB:P25705}; Extracellular side {ECO:0000250|UniProtKB:P25705}. Note=Colocalizes with HRG on the cell surface of T-cells. {ECO:0000250|UniProtKB:P25705}.

Tissue specificity: Heart muscle (at protein level) (PubMed:2864455). Heart and liver. {ECO:0000269|PubMed:2864455}.

Ptm: Acetylated on lysine residues. BLOC1S1 is required for acetylation. {ECO:0000250|UniProtKB:P25705}.

Miscellaneous: The siderophore enterobactin (Ent) produced by enteric bacteria binds Fe(3+) and helps bacteria scavenge iron ions from the environment. As a consequence, the mammalian siderocalin LCN2 plays an important role in defense against bacterial infections by sequestering iron bound to microbial siderophores. LCN2 can also bind iron bound to endogenous or nutrient-derived iron chelators and plays an important role in cellular iron homeostasis. Enterobactin produced by non- pathogenic E.coli strains can facilitate mitochondrial iron assimilation, suggesting that iron bound to siderophores from non- pathogenic bacteria may contribute to iron absorption by the host. {ECO:0000250|UniProtKB:P25705}.

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. Subunit alpha does not bear the catalytic high-affinity ATP-binding sites. Binds the bacterial siderophore enterobactin and can promote mitochondrial accumulation of enterobactin-derived iron ions (By similarity). {ECO:0000250\|UniProtKB:P25705, ECO:0000269\|PubMed:17570365, ECO:0000269\|PubMed:23407638}.


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) (PubMed:2864455, PubMed:17570365, PubMed:23407638). CF(0) has three main subunits: a, b and c (PubMed:2864455, PubMed:17570365, PubMed:23407638). Interacts with ATPAF2 (By similarity). Interacts with HRG; the interaction occurs on the surface of T-cells and alters the cell morphology when associated with concanavalin (in vitro) (By similarity). 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:2864455, PubMed:17570365, PubMed:23407638, PubMed:25851905). Interacts with BLOC1S1. 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 ABCB7; this interaction allows the regulation of cellular iron homeostasis and cellular reactive oxygen species (ROS) levels in cardiomyocytes (By similarity). {ECO:0000250\|UniProtKB:P15999, ECO:0000250\|UniProtKB:P25705, ECO:0000250\|UniProtKB:Q03265, ECO:0000269\|PubMed:12923572, ECO:0000269\|PubMed:17570365, ECO:0000269\|PubMed:17895376, ECO:0000269\|PubMed:23407638, ECO:0000269\|PubMed:25851905, ECO:0000269\|PubMed:2864455}.
Subcellular location:		Mitochondrion inner membrane {ECO:0000269\|PubMed:14633978, ECO:0000269\|PubMed:23407638, ECO:0000269\|PubMed:2864455, ECO:0000269\|PubMed:95168}; Peripheral membrane protein {ECO:0000269\|PubMed:14633978, ECO:0000269\|PubMed:23407638, ECO:0000269\|PubMed:2864455, ECO:0000269\|PubMed:95168}; Matrix side {ECO:0000269\|PubMed:14633978, ECO:0000269\|PubMed:95168}. Cell membrane {ECO:0000250\|UniProtKB:P25705}; Peripheral membrane protein {ECO:0000250\|UniProtKB:P25705}; Extracellular side {ECO:0000250\|UniProtKB:P25705}. Note=Colocalizes with HRG on the cell surface of T-cells. {ECO:0000250\|UniProtKB:P25705}.
Tissue specificity:		Heart muscle (at protein level) (PubMed:2864455). Heart and liver. {ECO:0000269\|PubMed:2864455}.
Ptm:		Acetylated on lysine residues. BLOC1S1 is required for acetylation. {ECO:0000250\|UniProtKB:P25705}.
Miscellaneous:		The siderophore enterobactin (Ent) produced by enteric bacteria binds Fe(3+) and helps bacteria scavenge iron ions from the environment. As a consequence, the mammalian siderocalin LCN2 plays an important role in defense against bacterial infections by sequestering iron bound to microbial siderophores. LCN2 can also bind iron bound to endogenous or nutrient-derived iron chelators and plays an important role in cellular iron homeostasis. Enterobactin produced by non- pathogenic E.coli strains can facilitate mitochondrial iron assimilation, suggesting that iron bound to siderophores from non- pathogenic bacteria may contribute to iron absorption by the host. {ECO:0000250\|UniProtKB:P25705}.
Similarity:		Belongs to the ATPase alpha/beta chains family. {ECO:0000305}.