ATP5PF

Last updated
ATP5PF
Identifiers
Aliases ATP5PF , ATP5, ATP5A, ATPM, CF6, F6, ATP synthase, H+ transporting, mitochondrial Fo complex subunit F6, ATP synthase peripheral stalk subunit F6, ATP5J
External IDs OMIM: 603152 MGI: 107777 HomoloGene: 1272 GeneCards: ATP5PF
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)
RefSeq (protein)
Location (UCSC) Chr 21: 25.72 – 25.74 Mb Chr 16: 84.62 – 84.63 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse
Mitochondrial ATP synthase coupling factor 6 (F6)
PDB 1vzs EBI.jpg
solution structure of subunit f6 from the peripheral stalk region of atp synthase from bovine heart mitochondria
Identifiers
SymbolATP-synt_F6
Pfam PF05511
InterPro IPR008387
Available protein structures:
Pfam   structures / ECOD  
PDB RCSB PDB; PDBe; PDBj
PDBsum structure summary

ATP synthase-coupling factor 6, mitochondrial is an enzyme subunit that in humans is encoded by the ATP5PF gene. [5] [6] [7]

Contents

Function

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 F1 complex consists of 5 different subunits (alpha, beta, gamma, delta, and epsilon) assembled in a ratio of 3 alpha, 3 beta, and a single representative of the other 3. The FO seems to have nine subunits (a, b, c, d, e, f, g, F6 and 8). This gene encodes the F6 subunit of the FO complex, required for F1 and FO interactions. Alternatively spliced transcript variants encoding different isoforms have been identified for this gene. [7]

The F6 subunit is part of the peripheral stalk that links the F1 and FO complexes together, and which acts as a stator to prevent certain subunits from rotating with the central rotary element. The peripheral stalk differs in subunit composition between mitochondrial, chloroplast and bacterial F-ATPases. In mitochondria, the peripheral stalk is composed of one copy each of subunits OSCP (oligomycin sensitivity conferral protein), F6, b and d. [8] There is no homologue of subunit F6 in bacterial or chloroplast F-ATPase, whose peripheral stalks are composed of one copy of the delta subunit (homologous to OSCP), and two copies of subunit b in bacteria, or one copy each of subunits b and b' in chloroplasts and photosynthetic bacteria.

Related Research Articles

<span class="mw-page-title-main">ATPase</span> Dephosphorylation enzyme

ATPases (EC 3.6.1.3, Adenosine 5'-TriPhosphatase, adenylpyrophosphatase, ATP monophosphatase, triphosphatase, SV40 T-antigen, ATP hydrolase, complex V (mitochondrial electron transport), (Ca2+ + Mg2+)-ATPase, HCO3-ATPase, adenosine triphosphatase) are a class of enzymes that catalyze the decomposition of ATP into ADP and a free phosphate ion or the inverse reaction. This dephosphorylation reaction releases energy, which the enzyme (in most cases) harnesses to drive other chemical reactions that would not otherwise occur. This process is widely used in all known forms of life.

<span class="mw-page-title-main">ATP synthase</span> Enzyme

ATP synthase is a protein that catalyzes the formation of the energy storage molecule adenosine triphosphate (ATP) using adenosine diphosphate (ADP) and inorganic phosphate (Pi). ATP synthase is a molecular machine. The overall reaction catalyzed by ATP synthase is:

<span class="mw-page-title-main">MT-ATP8</span> Mitochondrial protein-coding gene whose product is involved in ATP synthesis

MT-ATP8 is a mitochondrial gene with the full name 'mitochondrially encoded ATP synthase membrane subunit 8' that encodes a subunit of mitochondrial ATP synthase, ATP synthase Fo subunit 8. This subunit belongs to the Fo complex of the large, transmembrane F-type ATP synthase. This enzyme, which is also known as complex V, is responsible for the final step of oxidative phosphorylation in the electron transport chain. Specifically, one segment of ATP synthase allows positively charged ions, called protons, to flow across a specialized membrane inside mitochondria. Another segment of the enzyme uses the energy created by this proton flow to convert a molecule called adenosine diphosphate (ADP) to ATP. Subunit 8 differs in sequence between Metazoa, plants and Fungi.

<span class="mw-page-title-main">MT-ATP6</span> Mitochondrial protein-coding gene whose product is involved in ATP synthesis

MT-ATP6 is a mitochondrial gene with the full name 'mitochondrially encoded ATP synthase membrane subunit 6' that encodes the ATP synthase Fo subunit 6. This subunit belongs to the Fo complex of the large, transmembrane F-type ATP synthase. This enzyme, which is also known as complex V, is responsible for the final step of oxidative phosphorylation in the electron transport chain. Specifically, one segment of ATP synthase allows positively charged ions, called protons, to flow across a specialized membrane inside mitochondria. Another segment of the enzyme uses the energy created by this proton flow to convert a molecule called adenosine diphosphate (ADP) to ATP. Mutations in the MT-ATP6 gene have been found in approximately 10 to 20 percent of people with Leigh syndrome.

<span class="mw-page-title-main">ATP5B</span> Protein-coding gene in the species Homo sapiens

ATP synthase F1 subunit beta, mitochondrial is an enzyme that in humans is encoded by the ATP5F1B gene.

<span class="mw-page-title-main">ATP5F1A</span>

ATP synthase F1 subunit alpha, mitochondrial is an enzyme that in humans is encoded by the ATP5F1A gene.

<span class="mw-page-title-main">ATP5G1</span> Protein-coding gene in the species Homo sapiens

The ATP5MC1 gene is one of three human paralogs that encode membrane subunit c of the mitochondrial ATP synthase.

<span class="mw-page-title-main">ATP5J2</span> Protein-coding gene in the species Homo sapiens

The ATP5MF gene encodes the ATP synthase subunit f, mitochondrial enzyme in humans.

<span class="mw-page-title-main">ATP synthase delta/OSCP subunit</span> Subunit of bacterial and chloroplast F-ATPase/synthase

ATP synthase delta subunit is a subunit of bacterial and chloroplast F-ATPase/synthase. It is known as OSCP in mitochondrial ATPase.

<span class="mw-page-title-main">ATP5L</span> Protein-coding gene in the species Homo sapiens

ATP synthase subunit g, mitochondrial is an enzyme that in humans is encoded by the ATP5MG gene.

<span class="mw-page-title-main">ATP5C1</span> Protein-coding gene in the species Homo sapiens

The human ATP5F1C gene encodes the gamma subunit of an enzyme called mitochondrial ATP synthase.

<span class="mw-page-title-main">ATP5F1</span> Protein-coding gene in the species Homo sapiens

ATP synthase subunit b, mitochondrial is an enzyme that in humans is encoded by the ATP5PB gene.

<span class="mw-page-title-main">ATP5S</span> Protein-coding gene in the species Homo sapiens

ATP synthase subunit s, mitochondrial is an enzyme that in humans is encoded by the ATP5S gene.

<span class="mw-page-title-main">ATP5G2</span> Protein-coding gene in the species Homo sapiens

The ATP5MC2 gene is one of three human paralogs that encode membrane subunit c of the mitochondrial ATP synthase.

<span class="mw-page-title-main">ATP5I</span> Protein-coding gene in the species Homo sapiens

ATP synthase subunit e, mitochondrial is an enzyme that in humans is encoded by the ATP5ME gene.

<span class="mw-page-title-main">ATP5H</span> Protein-coding gene in the species Homo sapiens

The human gene ATP5PD encodes subunit d of the peripheral stalk part of the enzyme mitochondrial ATP synthase.

<span class="mw-page-title-main">ATP5D</span> Protein-coding gene in the species Homo sapiens

ATP synthase subunit delta, mitochondrial, also known as ATP synthase F1 subunit delta or F-ATPase delta subunit is an enzyme that in humans is encoded by the ATP5F1D gene. This gene encodes a subunit of mitochondrial ATP synthase. Mitochondrial ATP synthase catalyzes ATP synthesis, utilizing an electrochemical gradient of protons across the inner membrane during oxidative phosphorylation.

<span class="mw-page-title-main">ATP5E</span> Protein-coding gene in the species Homo sapiens

ATP synthase F1 subunit epsilon, mitochondrial is an enzyme that in humans is encoded by the ATP5F1E gene. The protein encoded by ATP5F1E is a subunit of ATP synthase, also known as Complex V. Variations of this gene have been associated with mitochondrial complex V deficiency, nuclear 3 (MC5DN3) and Papillary Thyroid Cancer.

<span class="mw-page-title-main">ATP5G3</span>

The ATP5MC3 gene is one of three human paralogs that encode membrane subunit c of the mitochondrial ATP synthase.

<span class="mw-page-title-main">ATP5PO</span> Protein-coding gene in the species Homo sapiens

ATP synthase subunit O, mitochondrial is an enzyme that in humans is encoded by the ATP5PO gene.

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000154723 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000022890 - Ensembl, May 2017
  3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. Higuti T, Tsurumi C, Kawamura Y, Tsujita H, Osaka F, Yoshihara Y, Tani I, Tanaka K, Ichihara A (Jul 1991). "Molecular cloning of cDNA for the import precursor of human coupling factor 6 of H(+)-ATP synthase in mitochondria". Biochemical and Biophysical Research Communications. 178 (2): 793–9. doi:10.1016/0006-291X(91)90178-A. PMID   1830479.
  6. Javed AA, Ogata K, Sanadi DR (Jan 1991). "Human mitochondrial ATP synthase: cloning cDNA for the nuclear-encoded precursor of coupling factor 6". Gene. 97 (2): 307–10. doi:10.1016/0378-1119(91)90068-M. PMID   1825642.
  7. 1 2 "Entrez Gene: ATP5PF ATP synthase peripheral stalk subunit F6".
  8. Carbajo RJ, Kellas FA, Runswick MJ, Montgomery MG, Walker JE, Neuhaus D (Aug 2005). "Structure of the F1-binding domain of the stator of bovine F1Fo-ATPase and how it binds an alpha-subunit". Journal of Molecular Biology. 351 (4): 824–38. doi:10.1016/j.jmb.2005.06.012. PMID   16045926.

Further reading

This article incorporates text from the public domain Pfam and InterPro: IPR008387