ATP5L

ATP synthase, H+ transporting, mitochondrial Fo complex, subunit G
Identifiers
Symbols	ATP5L ; ATP5JG
External IDs	HomoloGene: 86074 GeneCards: ATP5L Gene
EC number	3.6.1.14
Gene ontology Molecular function • hydrogen ion transmembrane transporter activity • ATPase activity • transmembrane transporter activity Cellular component • mitochondrial proton-transporting ATP synthase complex, coupling factor F(o) • mitochondrion • mitochondrial inner membrane • mitochondrial proton-transporting ATP synthase complex • extracellular exosome Biological process • respiratory electron transport chain • mitochondrial ATP synthesis coupled proton transport • cellular metabolic process • small molecule metabolic process Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	10632	27425
Ensembl	ENSG00000167283	ENSMUSG00000038717
UniProt	O75964	Q9CPQ8
RefSeq (mRNA)	NM_006476	NM_013795
RefSeq (protein)	NP_006467	NP_038823
Location (UCSC)	Chr 11: 118.4 – 118.43 Mb	Chr 9: 44.91 – 44.92 Mb
PubMed search

ATP-synt_G
Identifiers
Symbol	ATP-synt_G
Pfam	PF04718
InterPro	IPR006808
Available protein structures: Pfam structures PDB RCSB PDB; PDBe; PDBj PDBsum structure summary

ATP synthase subunit g, mitochondrial is an enzyme that in humans is encoded by the ATP5L gene.^[1][2][3]

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 g subunit of the F0 complex.^[3]

The function of subunit G is currently unknown. There is no counterpart in chloroplast or bacterial F-ATPases identified so far.^[4]

References

1. Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Bocher M, Blocker H, Bauersachs S, Blum H, Lauber J, Dusterhoft A, Beyer A, Kohrer K, Strack N, Mewes HW, Ottenwalder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A (Mar 2001). "Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs". Genome Res 11 (3): 422–35. doi:10.1101/gr.GR1547R. PMC 311072. PMID 11230166.
2. Zhang QH, Ye M, Wu XY, Ren SX, Zhao M, Zhao CJ, Fu G, Shen Y, Fan HY, Lu G, Zhong M, Xu XR, Han ZG, Zhang JW, Tao J, Huang QH, Zhou J, Hu GX, Gu J, Chen SJ, Chen Z (Nov 2000). "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells". Genome Res 10 (10): 1546–60. doi:10.1101/gr.140200. PMC 310934. PMID 11042152.
3. "Entrez Gene: ATP5L ATP synthase, H+ transporting, mitochondrial F0 complex, subunit G".
4. Collinson IR, Runswick MJ, Buchanan SK, Fearnley IM, Skehel JM, van Raaij MJ, Griffiths DE, Walker JE (June 1994). "Fo membrane domain of ATP synthase from bovine heart mitochondria: purification, subunit composition, and reconstitution with F1-ATPase". Biochemistry 33 (25): 7971–8. doi:10.1021/bi00191a026. PMID 8011660.

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.
• Hartley JL, Temple GF, Brasch MA (2001). "DNA cloning using in vitro site-specific recombination.". Genome Res. 10 (11): 1788–95. doi:10.1101/gr.143000. PMC 310948. PMID 11076863.
• 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.
• Wiemann S, Arlt D, Huber W; et al. (2004). "From ORFeome to biology: a functional genomics pipeline.". Genome Res. 14 (10B): 2136–44. doi:10.1101/gr.2576704. PMC 528930. PMID 15489336.
• Mehrle A, Rosenfelder H, Schupp I; et al. (2006). "The LIFEdb database in 2006.". Nucleic Acids Res. 34 (Database issue): D415–8. doi:10.1093/nar/gkj139. PMC 1347501. PMID 16381901.
• Ewing RM, Chu P, Elisma F; et al. (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry.". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.

This article incorporates text from the public domain Pfam and InterPro IPR006808