Description: Homo sapiens ATP synthase, H+ transporting, mitochondrial F1 complex, alpha subunit 1, cardiac muscle (ATP5F1A), nuclear gene encoding mitochondrial protein, transcript variant 2, mRNA. RefSeq Summary (NM_004046): This gene encodes a subunit of mitochondrial ATP synthase. Mitochondrial ATP synthase catalyzes ATP synthesis, using an electrochemical gradient of protons across the inner membrane during oxidative phosphorylation. ATP synthase is composed of two linked multi-subunit complexes: the soluble catalytic core, F1, and the membrane-spanning component, Fo, comprising the proton channel. The catalytic portion of mitochondrial ATP synthase consists of 5 different subunits (alpha, beta, gamma, delta, and epsilon) assembled with a stoichiometry of 3 alpha, 3 beta, and a single representative of the other 3. The proton channel consists of three main subunits (a, b, c). This gene encodes the alpha subunit of the catalytic core. Alternatively spliced transcript variants encoding the different isoforms have been identified. Pseudogenes of this gene are located on chromosomes 9, 2, and 16. [provided by RefSeq, Mar 2012]. Transcript (Including UTRs) Position: hg19 chr18:43,664,110-43,678,319 Size: 14,210 Total Exon Count: 12 Strand: - Coding Region Position: hg19 chr18:43,664,248-43,678,197 Size: 13,950 Coding Exon Count: 12
ID:ATPA_HUMAN DESCRIPTION: RecName: Full=ATP synthase subunit alpha, mitochondrial; Flags: Precursor; 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 (By similarity). 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. 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 (By similarity). Interacts with BLOC1S1. INTERACTION: P78537:BLOC1S1; NbExp=2; IntAct=EBI-351437, EBI-348630; Q9NTG7:SIRT3; NbExp=2; IntAct=EBI-351437, EBI-724621; SUBCELLULAR LOCATION: Mitochondrion inner membrane. Cell membrane; Peripheral membrane protein; Extracellular side. Note=Colocalizes with HRG on the cell surface of T-cells. TISSUE SPECIFICITY: Fetal lung, heart, liver, gut and kidney. Expressed at higher levels in the fetal brain, retina and spinal cord. PTM: The N-terminus is blocked. PTM: Acetylated on lysine residues. BLOC1S1 is required for acetylation. SIMILARITY: Belongs to the ATPase alpha/beta chains family.
The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.
Pfam Domains: PF00006 - ATP synthase alpha/beta family, nucleotide-binding domain PF00306 - ATP synthase alpha/beta chain, C terminal domain PF02874 - ATP synthase alpha/beta family, beta-barrel domain
SCOP Domains: 47917 - C-terminal domain of alpha and beta subunits of F1 ATP synthase 50615 - N-terminal domain of alpha and beta subunits of F1 ATP synthase 52540 - P-loop containing nucleoside triphosphate hydrolases
ModBase Predicted Comparative 3D Structure on P25705
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Orthologous Genes in Other Species
Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.
Biological Process: GO:0001937 negative regulation of endothelial cell proliferation GO:0006629 lipid metabolic process GO:0006754 ATP biosynthetic process GO:0006811 ion transport GO:0015986 ATP synthesis coupled proton transport GO:0042407 cristae formation GO:0042776 mitochondrial ATP synthesis coupled proton transport GO:0043536 positive regulation of blood vessel endothelial cell migration GO:0046034 ATP metabolic process GO:0099132 ATP hydrolysis coupled cation transmembrane transport GO:1902600 hydrogen ion transmembrane transport
Protein P25705 (Reactome details) participates in the following event(s):
R-HSA-1268022 TOMM40 complex translocates proteins from the cytosol to the mitochondrial intermembrane space R-HSA-164840 ADP and Pi bind to ATPase R-HSA-8949580 F1Fo ATP synthase dimerizes R-HSA-164834 Enzyme-bound ATP is released R-HSA-164832 ATPase synthesizes ATP R-HSA-1268020 Mitochondrial protein import R-HSA-163210 Formation of ATP by chemiosmotic coupling R-HSA-8949613 Cristae formation R-HSA-392499 Metabolism of proteins R-HSA-163200 Respiratory electron transport, ATP synthesis by chemiosmotic coupling, and heat production by uncoupling proteins. R-HSA-1592230 Mitochondrial biogenesis R-HSA-1428517 The citric acid (TCA) cycle and respiratory electron transport R-HSA-1852241 Organelle biogenesis and maintenance R-HSA-1430728 Metabolism