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MGP000253

UniProt Annotations

Entry Information
Gene NameATP synthase, H+ transporting, mitochondrial F1 complex, alpha subunit 1, cardiac muscle
Protein EntryATPA_HUMAN
UniProt IDP25705
SpeciesHuman
Comments
Comment typeDescription
Alternative ProductsEvent=Alternative splicing; Named isoforms=3; Name=1; IsoId=P25705-1; Sequence=Displayed; Name=2; IsoId=P25705-2; Sequence=VSP_045129; Name=3; IsoId=P25705-3; Sequence=VSP_054688; Note=No experimental confirmation available.;
DiseaseCombined oxidative phosphorylation deficiency 22 (COXPD22) [MIM:616045]: A mitochondrial disorder characterized by intrauterine growth retardation, microcephaly, hypotonia, pulmonary hypertension, failure to thrive, encephalopathy, and heart failure. {ECO:0000269|PubMed:23596069}. Note=The disease is caused by mutations affecting the gene represented in this entry.
DiseaseMitochondrial complex V deficiency, nuclear 4 (MC5DN4) [MIM:615228]: A mitochondrial disorder with heterogeneous clinical manifestations including dysmorphic features, psychomotor retardation, hypotonia, growth retardation, cardiomyopathy, enlarged liver, hypoplastic kidneys and elevated lactate levels in urine, plasma and cerebrospinal fluid. {ECO:0000269|PubMed:23599390}. Note=The disease is caused by mutations affecting the gene represented in this entry.
FunctionMitochondrial 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 (By similarity). {ECO:0000250}.
InteractionP78537:BLOC1S1; NbExp=2; IntAct=EBI-351437, EBI-348630; Q9NTG7:SIRT3; NbExp=2; IntAct=EBI-351437, EBI-724621; P63104:YWHAZ; NbExp=3; IntAct=EBI-351437, EBI-347088;
PtmAcetylated on lysine residues. BLOC1S1 is required for acetylation. {ECO:0000269|PubMed:19608861, ECO:0000269|PubMed:22309213}.
PtmThe N-terminus is blocked.
SimilarityBelongs to the ATPase alpha/beta chains family. {ECO:0000305}.
Subcellular LocationMitochondrion inner membrane. Cell membrane; Peripheral membrane protein; Extracellular side. Note=Colocalizes with HRG on the cell surface of T-cells.
SubunitF-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. Interacts with ATPAF2. Interacts with HRG; the interaction occurs on the surface of T- cells and alters the cell morphology when associated with concanavalin (in vitro). Interacts with PLG (angiostatin peptide); the interaction inhibits most of the angiogenic properties of angiostatin. Component of an ATP synthase complex composed of ATP5F1, ATP5G1, ATP5E, ATP5H, ATP5I, ATP5J, ATP5J2, MT-ATP6, MT- ATP8, ATP5A1, ATP5B, ATP5D, ATP5C1, ATP5O, ATP5L, USMG5 and MP68. 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 efficency. {ECO:0000269|PubMed:10077593, ECO:0000269|PubMed:11410595, ECO:0000269|PubMed:19285951, ECO:0000269|PubMed:22309213}.
Tissue SpecificityFetal lung, heart, liver, gut and kidney. Expressed at higher levels in the fetal brain, retina and spinal cord. {ECO:0000269|PubMed:8428659}.
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