ATP synthase subunit delta, mitochondrial

Details

Name
ATP synthase subunit delta, mitochondrial
Synonyms
  • F-ATPase delta subunit
Gene Name
ATP5D
Organism
Humans
Amino acid sequence
>lcl|BSEQ0018957|ATP synthase subunit delta, mitochondrial
MLPAALLRRPGLGRLVRHARAYAEAAAAPAAASGPNQMSFTFASPTQVFFNGANVRQVDV
PTLTGAFGILAAHVPTLQVLRPGLVVVHAEDGTTSKYFVSSGSIAVNADSSVQLLAEEAV
TLDMLDLGAAKANLEKAQAELVGTADEATRAEIQIRIEANEALVKALE
Number of residues
168
Molecular Weight
17489.755
Theoretical pI
5.19
GO Classification
Functions
proton-transporting ATP synthase activity, rotational mechanism / proton-transporting ATPase activity, rotational mechanism / transmembrane transporter activity / transporter activity
Processes
ATP biosynthetic process / ATP synthesis coupled proton transport / cellular metabolic process / mitochondrial ATP synthesis coupled proton transport / oxidative phosphorylation / respiratory electron transport chain / response to copper ion / small molecule metabolic process
Components
mitochondrial inner membrane / mitochondrial matrix / mitochondrial proton-transporting ATP synthase complex / mitochondrial proton-transporting ATP synthase complex, catalytic core F(1) / mitochondrion
General Function
Transporter activity
Specific Function
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP turnover in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(1) domain and of the central stalk which is part of the complex rotary element. Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Mitochondrion
Gene sequence
>lcl|BSEQ0018958|ATP synthase subunit delta, mitochondrial (ATP5D)
ATGCTGCCCGCCGCGCTGCTCCGCCGCCCGGGACTTGGCCGCCTCGTCCGCCACGCCCGT
GCCTATGCCGAGGCCGCCGCCGCCCCGGCTGCCGCCTCTGGCCCCAACCAGATGTCCTTC
ACCTTCGCCTCTCCCACGCAGGTGTTCTTCAACGGTGCCAACGTCCGGCAGGTGGACGTG
CCCACGCTGACCGGAGCCTTCGGCATCCTGGCGGCCCACGTGCCCACGCTGCAGGTCCTG
CGGCCGGGGCTGGTCGTGGTGCATGCAGAGGACGGCACCACCTCCAAATACTTTGTGAGC
AGCGGTTCCATCGCAGTGAACGCCGACTCTTCGGTGCAGTTGTTGGCCGAAGAGGCCGTG
ACGCTGGACATGTTGGACCTGGGGGCAGCCAAGGCAAACTTGGAGAAGGCCCAGGCGGAG
CTGGTGGGGACAGCTGACGAGGCCACGCGGGCAGAGATCCAGATCCGAATCGAGGCCAAC
GAGGCCCTGGTGAAGGCCCTGGAGTAG
Chromosome Location
19
Locus
19p13.3
External Identifiers
ResourceLink
UniProtKB IDP30049
UniProtKB Entry NameATPD_HUMAN
GenBank Protein ID12586
GenBank Gene IDX63422
GenAtlas IDATP5D
HGNC IDHGNC:837
General References
  1. Jordan EM, Breen GA: Molecular cloning of an import precursor of the delta-subunit of the human mitochondrial ATP synthase complex. Biochim Biophys Acta. 1992 Feb 28;1130(1):123-6. [Article]
  2. Grimwood J, Gordon LA, Olsen A, Terry A, Schmutz J, Lamerdin J, Hellsten U, Goodstein D, Couronne O, Tran-Gyamfi M, Aerts A, Altherr M, Ashworth L, Bajorek E, Black S, Branscomb E, Caenepeel S, Carrano A, Caoile C, Chan YM, Christensen M, Cleland CA, Copeland A, Dalin E, Dehal P, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Garcia C, Georgescu AM, Glavina T, Gomez M, Gonzales E, Groza M, Hammon N, Hawkins T, Haydu L, Ho I, Huang W, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Larionov V, Leem SH, Lopez F, Lou Y, Lowry S, Malfatti S, Martinez D, McCready P, Medina C, Morgan J, Nelson K, Nolan M, Ovcharenko I, Pitluck S, Pollard M, Popkie AP, Predki P, Quan G, Ramirez L, Rash S, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, She X, Smith D, Slezak T, Solovyev V, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wagner M, Wheeler J, Wu K, Xie G, Yang J, Dubchak I, Furey TS, DeJong P, Dickson M, Gordon D, Eichler EE, Pennacchio LA, Richardson P, Stubbs L, Rokhsar DS, Myers RM, Rubin EM, Lucas SM: The DNA sequence and biology of human chromosome 19. Nature. 2004 Apr 1;428(6982):529-35. [Article]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [Article]
  4. Hochstrasser DF, Frutiger S, Paquet N, Bairoch A, Ravier F, Pasquali C, Sanchez JC, Tissot JD, Bjellqvist B, Vargas R, et al.: Human liver protein map: a reference database established by microsequencing and gel comparison. Electrophoresis. 1992 Dec;13(12):992-1001. [Article]
  5. Burkard TR, Planyavsky M, Kaupe I, Breitwieser FP, Burckstummer T, Bennett KL, Superti-Furga G, Colinge J: Initial characterization of the human central proteome. BMC Syst Biol. 2011 Jan 26;5:17. doi: 10.1186/1752-0509-5-17. [Article]
  6. Bian Y, Song C, Cheng K, Dong M, Wang F, Huang J, Sun D, Wang L, Ye M, Zou H: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. J Proteomics. 2014 Jan 16;96:253-62. doi: 10.1016/j.jprot.2013.11.014. Epub 2013 Nov 22. [Article]
  7. Vaca Jacome AS, Rabilloud T, Schaeffer-Reiss C, Rompais M, Ayoub D, Lane L, Bairoch A, Van Dorsselaer A, Carapito C: N-terminome analysis of the human mitochondrial proteome. Proteomics. 2015 Jul;15(14):2519-24. doi: 10.1002/pmic.201400617. Epub 2015 Jun 8. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB00753Isofluraneapproved, vet_approvedunknownunknownDetails
DB01189Desfluraneapprovedunknownother/unknownDetails
DB13749Magnesium gluconateapproved, investigationalyessubstrateDetails