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5  structures 102  species 0  interactions 159  sequences 1  architecture

Family: ATP-synt_F6 (PF05511)

Summary: Mitochondrial ATP synthase coupling factor 6

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ATP5J Edit Wikipedia article

ATP synthase, H+ transporting, mitochondrial Fo complex, subunit F6
Identifiers
Symbols ATP5J; ATP5; ATP5A; ATPM; CF6; F6
External IDs OMIM603152 MGI107777 HomoloGene1272 GeneCards: ATP5J Gene
EC number 3.6.1.14
RNA expression pattern
PBB GE ATP5J 202325 s at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 522 11957
Ensembl ENSG00000154723 ENSMUSG00000022890
UniProt P18859 P97450
RefSeq (mRNA) NM_001003696 NM_016755
RefSeq (protein) NP_001003696 NP_058035
Location (UCSC) Chr 21:
27.09 – 27.11 Mb
Chr 16:
84.83 – 84.84 Mb
PubMed search [1] [2]
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
Symbol ATP-synt_F6
Pfam PF05511
InterPro IPR008387

ATP synthase-coupling factor 6, mitochondrial is an enzyme that in humans is encoded by the ATP5J gene.[1][2][3]

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, F0, 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 F0 seems to have nine subunits (a, b, c, d, e, f, g, F6 and 8). This gene encodes the F6 subunit of the F0 complex, required for F1 and F0 interactions. Alternatively spliced transcript variants encoding different isoforms have been identified for this gene.[3]

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.[4] 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.

References[edit]

  1. ^ Higuti T, Tsurumi C, Kawamura Y, Tsujita H, Osaka F, Yoshihara Y, Tani I, Tanaka K, Ichihara A (Aug 1991). "Molecular cloning of cDNA for the import precursor of human coupling factor 6 of H(+)-ATP synthase in mitochondria". Biochem Biophys Res Commun 178 (2): 793–9. doi:10.1016/0006-291X(91)90178-A. PMID 1830479. 
  2. ^ Javed AA, Ogata K, Sanadi DR (Apr 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. 
  3. ^ a b "Entrez Gene: ATP5J ATP synthase, H+ transporting, mitochondrial F0 complex, subunit F6". 
  4. ^ Carbajo RJ, Kellas FA, Runswick MJ, Montgomery MG, Walker JE, Neuhaus D (August 2005). "Structure of the F1-binding domain of the stator of bovine F1Fo-ATPase and how it binds an alpha-subunit". J. Mol. Biol. 351 (4): 824–38. doi:10.1016/j.jmb.2005.06.012. PMID 16045926. 

Further reading[edit]


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


This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

Mitochondrial ATP synthase coupling factor 6 Provide feedback

Coupling factor 6 (F6) is a component of mitochondrial ATP synthase which is required for the interactions of the catalytic and proton-translocating segments [1].

Literature references

  1. Javed AA, Ogata K, Sanadi DR; , Gene 1991;97:307-310.: Human mitochondrial ATP synthase: cloning cDNA for the nuclear-encoded precursor of coupling factor 6. PUBMED:1825642 EPMC:1825642


External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR008387

Transmembrane ATPases are membrane-bound enzyme complexes/ion transporters that use ATP hydrolysis to drive the transport of protons across a membrane. Some transmembrane ATPases also work in reverse, harnessing the energy from a proton gradient, using the flux of ions across the membrane via the ATPase proton channel to drive the synthesis of ATP.

There are several different types of transmembrane ATPases, which can differ in function (ATP hydrolysis and/or synthesis), structure (e.g., F-, V- and A-ATPases, which contain rotary motors) and in the type of ions they transport [PUBMED:15473999, PUBMED:15078220]. The different types include:

  • F-ATPases (F1F0-ATPases), which are found in mitochondria, chloroplasts and bacterial plasma membranes where they are the prime producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts).
  • V-ATPases (V1V0-ATPases), which are primarily found in eukaryotic vacuoles and catalyse ATP hydrolysis to transport solutes and lower pH in organelles.
  • A-ATPases (A1A0-ATPases), which are found in Archaea and function like F-ATPases (though with respect to their structure and some inhibitor responses, A-ATPases are more closely related to the V-ATPases).
  • P-ATPases (E1E2-ATPases), which are found in bacteria and in eukaryotic plasma membranes and organelles, and function to transport a variety of different ions across membranes.
  • E-ATPases, which are cell-surface enzymes that hydrolyse a range of NTPs, including extracellular ATP.

F-ATPases (also known as F1F0-ATPase, or H(+)-transporting two-sector ATPase) (EC) are composed of two linked complexes: the F1 ATPase complex is the catalytic core and is composed of 5 subunits (alpha, beta, gamma, delta, epsilon), while the F0 ATPase complex is the membrane-embedded proton channel that is composed of at least 3 subunits (A-C), nine in mitochondria (A-G, F6, F8). Both the F1 and F0 complexes are rotary motors that are coupled back-to-back. In the F1 complex, the central gamma subunit forms the rotor inside the cylinder made of the alpha(3)beta(3) subunits, while in the F0 complex, the ring-shaped C subunits forms the rotor. The two rotors rotate in opposite directions, but the F0 rotor is usually stronger, using the force from the proton gradient to push the F1 rotor in reverse in order to drive ATP synthesis [PUBMED:11309608]. These ATPases can also work in reverse to hydrolyse ATP to create a proton gradient.

This entry represents subunit F6 (or coupling factor 6) found in the F0 complex of F-ATPases in mitochondria. The F6 subunit is part of the peripheral stalk that links the F1 and F0 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 [PUBMED:16045926]. 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.

More information about this protein can be found at Protein of the Month: ATP Synthases [PUBMED:].

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Representative proteomes NCBI
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RP55
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Full
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Representative proteomes NCBI
(157)
Meta
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RP15
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RP35
(33)
RP55
(56)
RP75
(80)
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Seed source: Pfam-B_9347 (release 8.0)
Previous IDs: none
Type: Family
Author: Moxon SJ
Number in seed: 17
Number in full: 159
Average length of the domain: 92.10 aa
Average identity of full alignment: 42 %
Average coverage of the sequence by the domain: 71.49 %

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HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 27.9 27.9
Trusted cut-off 28.5 31.6
Noise cut-off 27.7 27.8
Model length: 99
Family (HMM) version: 6
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Structures

For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the ATP-synt_F6 domain has been found. There are 5 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.

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