ATP5L

From Wikipedia, the free encyclopedia

ATP synthase, H+ transporting, mitochondrial F0 complex, subunit G

Identifiers

ATP5L; ATP5JG

External IDs

Gene ontology
Molecular Function:	• metal ion binding • hydrogen ion transporting ATP synthase activity, rotational mechanism • hydrogen ion transporting ATPase activity, rotational mechanism
Cellular Component:	• mitochondrion • proton-transporting two-sector ATPase complex • proton-transporting ATP synthase complex, coupling factor F(o)
Biological Process:	• ion transport • ATP synthesis coupled proton transport • proton transport

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

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Refseq

NM_006476 (mRNA)
NP_006467 (protein)

n/a (mRNA)
n/a (protein)

Location

Chr 11: 117.78 - 117.79 Mb

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Pubmed search

[1]

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ATP synthase, H+ transporting, mitochondrial F0 complex, subunit G, also known as ATP5L, is a human gene.^[1]

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 g subunit of the F0 complex.^[1]

[edit] References

^ ^a ^b Entrez Gene: ATP5L ATP synthase, H+ transporting, mitochondrial F0 complex, subunit G.

[edit] Further reading

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. 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. 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.
Zhang QH, Ye M, Wu XY, et al. (2001). "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells.". Genome Res. 10 (10): 1546–60. PMID 11042152.
Hartley JL, Temple GF, Brasch MA (2001). "DNA cloning using in vitro site-specific recombination.". Genome Res. 10 (11): 1788–95. PMID 11076863.
Wiemann S, Weil B, Wellenreuther R, et al. (2001). "Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs.". Genome Res. 11 (3): 422–35. doi:10.1101/gr.154701. PMID 11230166.
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. 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. PMID 15489334.
Wiemann S, Arlt D, Huber W, et al. (2004). "From ORFeome to biology: a functional genomics pipeline.". Genome Res. 14 (10B): 2136–44. doi:10.1101/gr.2576704. PMID 15489336.
Mehrle A, Rosenfelder H, Schupp I, et al. (2006). "The LIFEdb database in 2006.". Nucleic Acids Res. 34 (Database issue): D415–8. doi:10.1093/nar/gkj139. PMID 16381901.
Ewing RM, Chu P, Elisma F, et al. (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry.". Mol. Syst. Biol. 3: 89. doi:10.1038/msb4100134. PMID 17353931.