ATP5D

ATP5D

ATP synthase, H+ transporting, mitochondrial F1 complex, delta subunit, also known as ATP5D, is a human gene.cite web | title = Entrez Gene: ATP5D ATP synthase, H+ transporting, mitochondrial F1 complex, delta subunit| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=513| accessdate = ]

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summary_text = 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. The catalytic portion of mitochondrial ATP synthase consists of 5 different subunits (alpha, beta, gamma, delta, and epsilon) assembled with a stoichiometry of 3 alpha, 3 beta, and a single representative of the other 3. The proton channel consists of three main subunits (a, b, c). This gene encodes the delta subunit of the catalytic core. Alternatively spliced transcript variants encoding the same isoform have been identified.cite web | title = Entrez Gene: ATP5D ATP synthase, H+ transporting, mitochondrial F1 complex, delta subunit| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=513| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Yoshida M, Muneyuki E, Hisabori T |title=ATP synthase--a marvellous rotary engine of the cell. |journal=Nat. Rev. Mol. Cell Biol. |volume=2 |issue= 9 |pages= 669–77 |year= 2001 |pmid= 11533724 |doi= 10.1038/35089509
*cite journal | author=Hochstrasser DF, Frutiger S, Paquet N, "et al." |title=Human liver protein
journal=Electrophoresis |volume=13 |issue= 12 |pages= 992–1001 |year= 1993 |pmid= 1286669 |doi=

*cite journal | author=Jordan EM, Breen GA |title=Molecular cloning of an import precursor of the delta-subunit of the human mitochondrial ATP synthase complex. |journal=Biochim. Biophys. Acta |volume=1130 |issue= 1 |pages= 123–6 |year= 1992 |pmid= 1531933 |doi=
*cite journal | author=Yasuda R, Noji H, Kinosita K, Yoshida M |title=F1-ATPase is a highly efficient molecular motor that rotates with discrete 120 degree steps. |journal=Cell |volume=93 |issue= 7 |pages= 1117–24 |year= 1998 |pmid= 9657145 |doi=
*cite journal | author=Wang H, Oster G |title=Energy transduction in the F1 motor of ATP synthase. |journal=Nature |volume=396 |issue= 6708 |pages= 279–82 |year= 1998 |pmid= 9834036 |doi= 10.1038/24409
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899
*cite journal | author=Ota T, Suzuki Y, Nishikawa T, "et al." |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285
*cite journal | author=Cross RL |title=Molecular motors: turning the ATP motor. |journal=Nature |volume=427 |issue= 6973 |pages= 407–8 |year= 2004 |pmid= 14749816 |doi= 10.1038/427407b
*cite journal | author=Itoh H, Takahashi A, Adachi K, "et al." |title=Mechanically driven ATP synthesis by F1-ATPase. |journal=Nature |volume=427 |issue= 6973 |pages= 465–8 |year= 2004 |pmid= 14749837 |doi= 10.1038/nature02212
*cite journal | author=Grimwood J, Gordon LA, Olsen A, "et al." |title=The DNA sequence and biology of human chromosome 19. |journal=Nature |volume=428 |issue= 6982 |pages= 529–35 |year= 2004 |pmid= 15057824 |doi= 10.1038/nature02399
*cite journal | author=Gerhard DS, Wagner L, Feingold EA, "et al." |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504

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