ATP5O

ATP5O
Identifiers
Aliases	ATP5O, ATPO, OSCP, HMC08D05, ATP synthase, H+ transporting, mitochondrial F1 complex, O subunit
External IDs	HomoloGene: 1283 GeneCards: ATP5O
Gene ontology Molecular function • proton-transporting ATP synthase activity, rotational mechanism • transmembrane transporter activity • transporter activity • ATPase activity • protein binding • drug binding Cellular component • mitochondrial proton-transporting ATP synthase complex • membrane • plasma membrane • mitochondrion • mitochondrial inner membrane • extracellular exosome • nucleus • extracellular matrix Biological process • mitochondrial ATP synthesis coupled proton transport • ion transport • proton transport • transport • ATP synthesis coupled proton transport • ATP biosynthetic process Sources:Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	539	n/a
Ensembl	ENSG00000241837	n/a
UniProt	P48047	n/a
RefSeq (mRNA)	NM_001697	n/a
RefSeq (protein)	NP_001688.1	n/a
Location (UCSC)	Chr 21: 33.9 – 33.92 Mb	n/a
PubMed search	[1]	n/a
Wikidata

View/Edit Human

ATP synthase subunit O, mitochondrial is an enzyme that in humans is encoded by the ATP5O gene.^[2]

The protein encoded by this gene is a component of the F-type ATPase found in the mitochondrial matrix. F-type ATPases are composed of a catalytic core and a membrane proton channel. The encoded protein appears to be part of the connector linking these two components and may be involved in transmission of conformational changes or proton conductance.^[2]

References

1. "Human PubMed Reference:".
2. "Entrez Gene: ATP5O ATP synthase, H+ transporting, mitochondrial F1 complex, O subunit (oligomycin sensitivity conferring protein)".

Further reading

• Chen H, Morris MA, Rossier C, et al. (1996). "Cloning of the cDNA for the human ATP synthase OSCP subunit (ATP5O) by exon trapping and mapping to chromosome 21q22.1-q22.2.". Genomics. 28 (3): 470–6. doi:10.1006/geno.1995.1176. PMID 7490082.
• Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
• Hattori M, Fujiyama A, Taylor TD, et al. (2000). "The DNA sequence of human chromosome 21". Nature. 405 (6784): 311–9. doi:10.1038/35012518. PMID 10830953.
• Aggeler R, Coons J, Taylor SW, et al. (2002). "A functionally active human F1F0 ATPase can be purified by immunocapture from heart tissue and fibroblast cell lines. Subunit structure and activity studies". J. Biol. Chem. 277 (37): 33906–12. doi:10.1074/jbc.M204538200. PMID 12110673.
• 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.
• Gevaert K, Goethals M, Martens L, et al. (2004). "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides". Nat. Biotechnol. 21 (5): 566–9. doi:10.1038/nbt810. PMID 12665801.
• Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
• 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.
• Johnson KM, Chen X, Boitano A, et al. (2005). "Identification and validation of the mitochondrial F1F0-ATPase as the molecular target of the immunomodulatory benzodiazepine Bz-423". Chem. Biol. 12 (4): 485–96. doi:10.1016/j.chembiol.2005.02.012. PMID 15850986.