ATP5I

VALUE_ERROR (nil)
Identifiers
Aliases
External IDs	GeneCards: [1]
Orthologs
Species	Human	Mouse
Entrez	n/a	n/a
Ensembl	n/a	n/a
UniProt	n/a	n/a
RefSeq (mRNA)	n/a	n/a
RefSeq (protein)	n/a	n/a
Location (UCSC)	n/a	n/a
PubMed search	n/a	n/a
Wikidata
View/Edit Human

ATP synthase E chain
Identifiers
Symbol	ATP-synt_E
Pfam	PF05680
InterPro	IPR008386
SCOP	1e79
SUPERFAMILY	1e79
Available protein structures: Pfam structures PDB RCSB PDB; PDBe; PDBj PDBsum structure summary

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

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 e subunit of the Fo complex.

In yeast, the F_O 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 F_O 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.

External links

• Human ATP5ME genome location and ATP5ME gene details page in the UCSC Genome Browser.

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. 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.

This article incorporates text from the public domain Pfam and InterPro: IPR008386