ATP synthase subunit delta, mitochondrial

Details

Name
ATP synthase subunit delta, mitochondrial
Synonyms
  • ATP synthase F1 subunit delta
  • ATP5D
  • F-ATPase delta subunit
Gene Name
ATP5F1D
UniProtKB Entry
P30049Swiss-Prot
Organism
Humans
NCBI Taxonomy ID
9606
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
Processes
response to copper ion
Components
mitochondrial inner membrane / mitochondrial matrix / mitochondrial proton-transporting ATP synthase complex / mitochondrion
General 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 (PubMed:29478781). 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 (PubMed:1531933)
Specific Function
proton-transporting ATP synthase activity, rotational mechanism
Pfam Domain Function
Signal Regions
Not Available
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
GeneCard IDATP5F1D
GenAtlas IDATP5D
HGNC IDHGNC:837
PDB ID(s)8H9F, 8H9J, 8H9M, 8H9Q, 8H9S, 8H9T, 8H9U, 8H9V, 8KHF, 8KI3
KEGG IDhsa:513
NCBI Gene ID513
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]

Associated Data

Bio-Entities
Bio-EntityType
ATP synthase subunit delta, mitochondrial (Humans)protein
primary
Mitochondrial ATP synthase F1 domain (Humans)protein
Drug Relations
DrugDrug groupPharmacological action?TypeActionsDetails
Isofluraneapproved, vet_approvedunknowntargetunknownDetails
Desfluraneapprovedunknowntargetother/unknownDetails
Magnesium gluconateapproved, investigationalnoenzymesubstrateDetails
DiazoxideapprovedunknowntargetinhibitorDetails