Summary: ATP synthase E chain
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ATP5I Edit Wikipedia article
|ATP synthase, H+ transporting, mitochondrial Fo complex, subunit E|
|RNA expression pattern|
|ATP synthase E chain|
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 e subunit of the F0 complex.
In yeast, the FO complex E subunit appears to play an important role in supporting F-ATPase dimerisation. This subunit is anchored to the inner mitochondrial membrane via its N-terminal region, which is involved in stabilising subunits G and K of the FO complex. The C-terminal region of subunit E is hydrophilic, protruding into the intermembrane space where it can also help stabilise the F-ATPase dimer complex.
- Swartz DA, Park EI, Visek WJ, Kaput J (Oct 1996). "The e subunit gene of murine F1F0-ATP synthase. Genomic sequence, chromosomal mapping, and diet regulation". J Biol Chem 271 (34): 20942–8. doi:10.1074/jbc.271.34.20942. PMID 8702853.
- "Entrez Gene: ATP5I ATP synthase, H+ transporting, mitochondrial F0 complex, subunit E".
- Everard-Gigot V, Dunn CD, Dolan BM, Brunner S, Jensen RE, Stuart RA (February 2005). "Functional analysis of subunit e of the F1Fo-ATP synthase of the yeast Saccharomyces cerevisiae: importance of the N-terminal membrane anchor region". Eukaryotic Cell 4 (2): 346–55. doi:10.1128/EC.4.2.346-355.2005. PMC 549337. PMID 15701797.
- Kinosita K, Yasuda R, Noji H (2003). "F1-ATPase: a highly efficient rotary ATP machine". Essays Biochem. 35: 3–18. PMID 12471886.
- Oster G, Wang H (2003). "Rotary protein motors". Trends Cell Biol. 13 (3): 114–21. doi:10.1016/S0962-8924(03)00004-7. PMID 12628343.
- Leyva JA, Bianchet MA, Amzel LM (2003). "Understanding ATP synthesis: structure and mechanism of the F1-ATPase (Review)". Mol. Membr. Biol. 20 (1): 27–33. doi:10.1080/0968768031000066532. PMID 12745923.
- Elston T, Wang H, Oster G (1998). "Energy transduction in ATP synthase". Nature 391 (6666): 510–3. doi:10.1038/35185. PMID 9461222.
- Wang H, Oster G (1998). "Energy transduction in the F1 motor of ATP synthase". Nature 396 (6708): 279–82. doi:10.1038/24409. PMID 9834036.
- Gubin AN, Njoroge JM, Bouffard GG, Miller JL (1999). "Gene expression in proliferating human erythroid cells". Genomics 59 (2): 168–77. doi:10.1006/geno.1999.5855. PMID 10409428.
- Ying H, Yu Y, Xu Y (2002). "Antisense of ATP synthase subunit e inhibits the growth of human hepatocellular carcinoma cells". Oncol. Res. 12 (11–12): 485–90. PMID 11939412.
- Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
- Cross RL (2004). "Molecular motors: turning the ATP motor". Nature 427 (6973): 407–8. doi:10.1038/427407b. PMID 14749816.
- Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
- Papathanassiu AE, MacDonald NJ, Bencsura A, Vu HA (2006). "F1F0-ATP synthase functions as a co-chaperone of Hsp90-substrate protein complexes". Biochem. Biophys. Res. Commun. 345 (1): 419–29. doi:10.1016/j.bbrc.2006.04.104. PMID 16682002.
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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.
ATP synthase E chain Provide feedback
This family consists of several ATP synthase E chain sequences which are components of the CF(0) subunit .
Collinson IR, Runswick MJ, Buchanan SK, Fearnley IM, Skehel JM, van Raaij MJ, Griffiths DE, Walker JE; , Biochemistry 1994;33:7971-7978.: Fo membrane domain of ATP synthase from bovine heart mitochondria: purification, subunit composition, and reconstitution with F1-ATPase. PUBMED:8011660 EPMC:8011660
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR008386
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 E found in the F0 complex of F-ATPases. Mitochondrial F-ATPases can associate together to form dimeric or oligomeric complexes, such interactions involving the physical association of membrane-embedded F0 complexes. In yeast, the F0 complex E subunit appears to play an important role in supporting F-ATPase dimerisation. This subunit is anchored to the inner mitochondrial membrane via its N-terminal region, which is involved in stabilising subunits G and K of the F0 complex. The C-terminal region of subunit E is hydrophilic, protruding into the intermembrane space where it can also help stabilise the F-ATPase dimer complex [PUBMED:15701797].
More information about this protein can be found at Protein of the Month: ATP Synthases [PUBMED:].
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Cellular component||mitochondrial proton-transporting ATP synthase complex, coupling factor F(o) (GO:0000276)|
|Molecular function||hydrogen ion transmembrane transporter activity (GO:0015078)|
|Biological process||ATP synthesis coupled proton transport (GO:0015986)|
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|Seed source:||Pfam-B_6116 (release 8.0)|
|Number in seed:||17|
|Number in full:||264|
|Average length of the domain:||78.20 aa|
|Average identity of full alignment:||28 %|
|Average coverage of the sequence by the domain:||86.96 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||7|
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