ATP5I

ATP synthase subunit e, mitochondrial is an enzyme that in humans is encoded by the ATP5ME gene.[3][4]

ATP5ME
Identifiers
Aliases	ATP5ME, ATP5K, ATP synthase, H+ transporting, mitochondrial Fo complex subunit E, ATP synthase membrane subunit e, ATP5I
External IDs	OMIM: 601519 HomoloGene: 136813 GeneCards: ATP5ME
Gene location (Human) Chr. Chromosome 4 (human)[1] Band 4p16.3 Start 672,436 bp[1] End 674,330 bp[1]
RNA expression pattern More reference expression data
Gene ontology Molecular function • ATPase activity • GO:0022891 transmembrane transporter activity • hydrogen ion transmembrane transporter activity • GO:0032403 macromolecular complex binding Cellular component • mitochondrial inner membrane • mitochondrial proton-transporting ATP synthase complex, coupling factor F(o) • mitochondrial proton-transporting ATP synthase complex • mitochondrion • membrane • proton-transporting ATP synthase complex, coupling factor F(o) Biological process • ATP metabolic process • mitochondrial ATP synthesis coupled proton transport • ATP synthesis coupled proton transport • ion transport • ATP biosynthetic process • cristae formation Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	521	n/a
Ensembl	ENSG00000169020	n/a
UniProt	P56385	n/a
RefSeq (mRNA)	NM_007100	n/a
RefSeq (protein)	NP_009031	n/a
Location (UCSC)	Chr 4: 0.67 – 0.67 Mb	n/a
PubMed search	[2]	n/a
Wikidata
View/Edit Human

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

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.[4]

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.[5]

References

1. GRCh38: Ensembl release 89: ENSG00000169020 - Ensembl, May 2017
2. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
3. 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.
4. "Entrez Gene: ATP5ME ATP synthase membrane subunit e".
5. 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.

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. doi:10.1042/bse0350003. 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" (PDF). 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. doi:10.3727/096504001108747495. 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