ATP5S

ATP synthase, H+ transporting, mitochondrial Fo complex, subunit s (factor B)
Identifiers
Symbols	ATP5S ; ATPW; FB; HSU79253
External IDs	MGI: 1915305 HomoloGene: 12232 GeneCards: ATP5S Gene
EC number	3.6.1.14
Gene ontology Molecular function • hydrogen ion transmembrane transporter activity • metal ion binding Cellular component • mitochondrial inner membrane • proton-transporting ATP synthase complex, coupling factor F(o) Biological process • proton transport • respiratory electron transport chain • mitochondrial ATP synthesis coupled proton transport • cellular metabolic process • small molecule metabolic process Sources: Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	27109	68055
Ensembl	ENSG00000125375	ENSMUSG00000054894
UniProt	Q99766	Q9CRA7
RefSeq (mRNA)	NM_001003803	NM_026536
RefSeq (protein)	NP_001003803	NP_080812
Location (UCSC)	Chr 14: 50.31 – 50.34 Mb	Chr 12: 69.72 – 69.74 Mb
PubMed search

ATP synthase subunit s, mitochondrial is an enzyme that in humans is encoded by the ATP5S gene.^[1][2][3]

This gene encodes a subunit of mitochondrial ATP synthase. Mitochondrial ATP synthase catalyzes ATP synthesis, utilizing an electrochemical gradient of protons across the inner membrane during oxidative phosphorylation. ATP synthase is composed of two linked multi-subunit complexes: the soluble catalytic core, F1, and the membrane-spanning component, Fo, comprising the proton channel. This gene encodes the subunit s, also known as factor B, of the proton channel. This subunit is necessary for the energy transduction activity of the ATP synthase complexes. Alternatively spliced transcript variants encoding different isoforms have been identified.^[3]

References

1. Belogrudov GI, Hatefi Y (Feb 2002). "Factor B and the mitochondrial ATP synthase complex". J Biol Chem 277 (8): 6097–103. doi:10.1074/jbc.M111256200. PMID 11744738.
2. Andersson B, Wentland MA, Ricafrente JY, Liu W, Gibbs RA (Jun 1996). "A "double adaptor" method for improved shotgun library construction". Anal Biochem 236 (1): 107–13. doi:10.1006/abio.1996.0138. PMID 8619474.
3. "Entrez Gene: ATP5S ATP synthase, H+ transporting, mitochondrial F0 complex, subunit s (factor B)".

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.
• Sanadi DR, Pringle M, Kantham L; et al. (1984). "Evidence for the involvement of coupling factor B in the H+ channel of the mitochondrial H+-ATPase". Proc. Natl. Acad. Sci. U.S.A. 81 (5): 1371–4. doi:10.1073/pnas.81.5.1371. PMC 344835. PMID 6143319.
• Yu W, Andersson B, Worley KC; et al. (1997). "Large-Scale Concatenation cDNA Sequencing". Genome Res. 7 (4): 353–8. doi:10.1101/gr.7.4.353. PMC 139146. PMID 9110174.
• 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.
• 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.
• Ma J, Dempsey AA, Stamatiou D; et al. (2007). "Identifying leukocyte gene expression patterns associated with plasma lipid levels in human subjects". Atherosclerosis 191 (1): 63–72. doi:10.1016/j.atherosclerosis.2006.05.032. PMID 16806233.