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General description of the gene and the encoded protein(s) using information from HGNC and Ensembl, as well as predictions made by the Human Protein Atlas project.
Gene namei
Official gene symbol, which is typically a short form of the gene name, according to HGNC.
Assigned HPA protein class(es) for the encoded protein(s).
Metabolic proteins Transporters
Predicted locationi
All transcripts of all genes have been analyzed regarding the location(s) of corresponding protein based on prediction methods for signal peptides and transmembrane regions.
Genes with at least one transcript predicted to encode a secreted protein, according to prediction methods or to UniProt location data, have been further annotated and classified with the aim to determine if the corresponding protein(s) are secreted or actually retained in intracellular locations or membrane-attached.
Remaining genes, with no transcript predicted to encode a secreted protein, will be assigned the prediction-based location(s).
The annotated location overrules the predicted location, so that a gene encoding a predicted secreted protein that has been annotated as intracellular will have intracellular as the final location.
Gene information from Ensembl and Entrez, as well as links to available gene identifiers are displayed here. Information was retrieved from Ensembl if not indicated otherwise.
Chromosome
7
Cytoband
q22.1
Chromosome location (bp)
99448475 - 99466186
Number of transcriptsi
Number of protein-coding transcripts from the gene as defined by Ensembl.
Useful information about the protein provided by UniProt.
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. Part of the complex F(0) domain. Minor subunit located with subunit a in the membrane....show less
Biological process (UniProt)i
Keywords assigned by UniProt to proteins because they are involved in a particular biological process.
ATP synthesis, Hydrogen ion transport, Ion transport, Transport
Gene summary (Entrez)i
Useful information about the gene from Entrez
Mitochondrial ATP synthase catalyzes ATP synthesis, utilizing an electrochemical gradient of protons across the inner membrane during oxidative phosphorylation. It is composed of two linked multi-subunit complexes: the soluble catalytic core, F1, and the membrane-spanning component, Fo, which comprises the proton channel. The catalytic portion of mitochondrial ATP synthase consists of five different subunits (alpha, beta, gamma, delta, and epsilon) assembled with a stoichiometry of 3 alpha, 3 beta, and single representatives of the gamma, delta, and epsilon subunits. The proton channel likely has nine subunits (a, b, c, d, e, f, g, F6 and 8). This gene encodes the f subunit of the Fo complex. Alternatively spliced transcript variants encoding different isoforms have been identified for this gene. This gene has multiple pseudogenes. Naturally occurring read-through transcription also exists between this gene and the downstream pentatricopeptide repeat domain 1 (PTCD1) gene. [provided by RefSeq, Nov 2010]...show less
PROTEIN INFORMATIONi
The protein information section displays alternative protein-coding transcripts (splice variants) encoded by this gene according to the Ensembl database.
The Splice variant identifier links to the Ensembl website protein summary for the selected splice variant. The data in the Swissprot and TrEMBL columns links to corresponding pages in the UniProt database.
The protein classes assigned to this protein are shown if expanding the data in the protein class column. Parent protein classes are in bold font and subclasses are listed under the parent class.
The length of the protein (amino acid residues according to Ensembl), molecular mass (kDalton), predicted signal peptide and number of predicted transmembrane region(s) according to in-house majority decision methods based on sets of predictors are also reported.
P56134 [Direct mapping] ATP synthase subunit f, mitochondrial
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Metabolic proteins Transporters Primary Active Transporters Predicted intracellular proteins Intracellular proteins predicted by MDM and MDSEC Mapped to neXtProt neXtProt - Evidence at protein level Protein evidence (Kim et al 2014) Protein evidence (Ezkurdia et al 2014)
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GO:0005739[mitochondrion] GO:0005743[mitochondrial inner membrane] GO:0005753[mitochondrial proton-transporting ATP synthase complex] GO:0006754[ATP biosynthetic process] GO:0006811[ion transport] GO:0015986[proton motive force-driven ATP synthesis] GO:0016020[membrane] GO:0031965[nuclear membrane] GO:0042776[proton motive force-driven mitochondrial ATP synthesis] GO:0045263[proton-transporting ATP synthase complex, coupling factor F(o)] GO:0046933[proton-transporting ATP synthase activity, rotational mechanism] GO:1902600[proton transmembrane transport]
P56134 [Direct mapping] ATP synthase subunit f, mitochondrial
Show all
Metabolic proteins Transporters Primary Active Transporters Predicted intracellular proteins Intracellular proteins predicted by MDM and MDSEC Mapped to neXtProt neXtProt - Evidence at protein level Protein evidence (Ezkurdia et al 2014)
Show all
GO:0005739[mitochondrion] GO:0005743[mitochondrial inner membrane] GO:0005753[mitochondrial proton-transporting ATP synthase complex] GO:0006754[ATP biosynthetic process] GO:0006811[ion transport] GO:0015986[proton motive force-driven ATP synthesis] GO:0016020[membrane] GO:0031965[nuclear membrane] GO:0042776[proton motive force-driven mitochondrial ATP synthesis] GO:0045263[proton-transporting ATP synthase complex, coupling factor F(o)] GO:0046933[proton-transporting ATP synthase activity, rotational mechanism] GO:1902600[proton transmembrane transport]
The Human Protein Atlas project is funded
