ATP5I

From Wikipedia, the free encyclopedia

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

Identifiers

ATP5I; ATP5K; MGC12532

External IDs

OMIM: 601519 MGI: 106636 HomoloGene: 5148

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

n/a

n/a

Refseq

NM_007100 (mRNA)
NP_009031 (protein)

NM_007507 (mRNA)
NP_031533 (protein)

Location

Chr 4: 0.66 - 0.66 Mb

n/a

Pubmed search

[1]

[2]

ATP synthase, H+ transporting, mitochondrial F0 complex, subunit E, also known as ATP5I, 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 e subunit of the F0 complex.^[1]

[edit] References

^ ^a ^b Entrez Gene: ATP5I ATP synthase, H+ transporting, mitochondrial F0 complex, subunit E.

[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.
Swartz DA, Park EI, Visek WJ, Kaput J (1996). "The e subunit gene of murine F1F0-ATP synthase. Genomic sequence, chromosomal mapping, and diet regulation.". J. Biol. Chem. 271 (34): 20942–8. PMID 8702853.
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. 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.
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.