ATP5I

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; OMA:ATP5ME - orthologs
Gene location (Human) Chr. Chromosome 4 (human)[1] Band 4p16.3 Start 672,436 bp[1] End 674,330 bp[1]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in apex of heart left ventricle right auricle of heart mucosa of transverse colon tendon of biceps brachii C1 segment Brodmann area 9 internal globus pallidus right ventricle muscle of thigh n/a More reference expression data BioGPS More reference expression data
Gene ontology Molecular function ATPase activity transmembrane transporter activity proton transmembrane transporter activity protein-containing 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 subunit e, mitochondrial is an enzyme that in humans is encoded by the ATP5ME gene.^[3][4]

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]

• 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. S2CID 218895820.
• Elston T, Wang H, Oster G (1998). "Energy transduction in ATP synthase". Nature. 391 (6666): 510–3. Bibcode:1998Natur.391..510E. doi:10.1038/35185. PMID 9461222. S2CID 4406161.
• Wang H, Oster G (1998). "Energy transduction in the F1 motor of ATP synthase". Nature. 396 (6708): 279–82. Bibcode:1998Natur.396..279W. doi:10.1038/24409. PMID 9834036. S2CID 4424498.
• 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. 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. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Cross RL (2004). "Molecular motors: turning the ATP motor". Nature. 427 (6973): 407–8. Bibcode:2004Natur.427..407C. doi:10.1038/427407b. PMID 14749816. S2CID 52819856.
• 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

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