ATP5O

ATP synthase, H+ transporting, mitochondrial F1 complex, O subunit

Identifiers

ATP5O ; ATPO; OSCP

External IDs

OMIM: 600828 MGI: 106341 HomoloGene: 1283 GeneCards: ATP5O Gene

Gene ontology
Molecular function	• transporter activity • drug binding • ATPase activity • transmembrane transporter activity • proton-transporting ATP synthase activity, rotational mechanism
Cellular component	• nucleus • mitochondrion • mitochondrial inner membrane • mitochondrial proton-transporting ATP synthase complex • plasma membrane • extracellular vesicular exosome
Biological process	• ATP catabolic process • ATP biosynthetic process • proton transport • 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

ENSG00000241837

ENSMUSG00000022956

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 21:
35.28 – 35.29 Mb

Chr 16:
91.68 – 91.93 Mb

PubMed search

ATP synthase subunit O, mitochondrial is an enzyme that in humans is encoded by the ATP5O gene.^[1]

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.^[1]

References

↑ 1.0 1.1 "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.