ATP5I

Available protein structures:
Pfam	structures / ECOD
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

ATP synthase E chain
ATP synthase E chain
Identifiers
Symbol	ATP-synt_E
Pfam	PF05680
InterPro	IPR008386
SCOP2	1e79 / SCOPe / SUPFAM
Pfam
Available protein structures:
Pfam	structures / ECOD
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

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)
End	674,330 bp
RNA expression pattern
	Top expressed in
	apex of heart; ; left ventricle; ; right auricle; ; 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
	; ;
	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
	521
	n/a
	ENSG00000169020
	n/a
	P56385
	n/a
	NM_007100
	n/a
	NP_009031
	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]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000169020 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ 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.
^ ^a ^b "Entrez Gene: ATP5ME ATP synthase membrane subunit e".
^ 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.

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

This article on a gene on human chromosome 4 is a stub. You can help Wikipedia by expanding it.

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[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000169020 – Ensembl, May 2017

[2] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid8702853-3] 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.

[entrez-4] "Entrez Gene: ATP5ME ATP synthase membrane subunit e".

[pmid15701797-5] 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.

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References

External links

Further reading