ATP5H

The human gene ATP5PD encodes subunit d of the peripheral stalk part of the enzyme mitochondrial ATP synthase.

ATP5PD
Identifiers
Aliases	ATP5PD, ATPQ, ATP synthase, H+ transporting, mitochondrial Fo complex subunit D, ATP5H, ATP synthase peripheral stalk subunit d, APT5H
External IDs	OMIM: 618121; MGI: 1918929; HomoloGene: 130552; GeneCards: ATP5PD; OMA:ATP5PD - orthologs
Gene location (Human) Chr. Chromosome 17 (human) Band 17q25.1 Start 75,038,863 bp End 75,046,985 bp
Gene location (Mouse) Chr. Chromosome 11 (mouse) Band 11|11 E2 Start 115,306,515 bp End 115,310,788 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in right ventricle myocardium myocardium of left ventricle atrium right auricle Skeletal muscle tissue of biceps brachii cardiac muscle tissue of right atrium apex of heart body of tongue Skeletal muscle tissue of rectus abdominis Top expressed in heart cerebellar cortex muscle tissue skeletal muscle tissue right kidney muscle of thigh human kidney quadriceps femoris muscle olfactory bulb neural tube More reference expression data BioGPS More reference expression data
Gene ontology Molecular function ATPase activity transmembrane transporter activity proton transmembrane transporter activity proton-transporting ATP synthase activity, rotational mechanism protein binding protein-containing complex binding Cellular component mitochondrial inner membrane mitochondrial proton-transporting ATP synthase complex, coupling factor F(o) mitochondrial proton-transporting ATP synthase complex mitochondrion extracellular exosome membrane nucleoplasm proton-transporting ATP synthase complex, coupling factor F(o) mitochondrial proton-transporting ATP synthase, stator stalk cytosol Biological process mitochondrial ATP synthesis coupled proton transport ion transport ATP synthesis coupled proton transport ATP biosynthetic process cristae formation transport ATP metabolic process cellular response to peptide Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 10476 71679 Ensembl ENSG00000167863 ENSMUSG00000034566 UniProt O75947 Q9DCX2 RefSeq (mRNA) NM_006356 NM_001003785 NM_027862 RefSeq (protein) NP_001003785 NP_006347 NP_082138 Location (UCSC) Chr 17: 75.04 – 75.05 Mb Chr 11: 115.31 – 115.31 Mb PubMed search
Wikidata
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ATP synthase D chain, mitochondrial
Identifiers
Symbol	ATP5H
Pfam	PF05873
Available protein structures: Pfam   structures / ECOD   PDB RCSB PDB; PDBe; PDBj PDBsum structure summary

Mitochondrial ATP synthase catalyzes ATP synthesis, utilizing an electrochemical gradient of protons across the inner membrane during oxidative phosphorylation. It is composed of two linked multi-subunit complexes: the soluble catalytic core, F₁, and the membrane-spanning component, F₀, which comprises the proton channel. The F₁ complex consists of 5 different subunits (alpha, beta, gamma, delta, and epsilon) assembled in a ratio of 3 alpha, 3 beta, and a single representative of the other 3. The F_o seems to have nine subunits (a, b, c, d, e, f, g, F6 and 8). This gene encodes the d subunit of the F_o complex. Alternatively spliced transcript variants encoding different isoforms have been identified for this gene. In addition, three pseudogenes are located on chromosomes 9, 12 and 15.

External links

• Human ATP5PD genome location and ATP5PD gene details page in the UCSC Genome Browser.

Further reading

• Kinosita K, Yasuda R, Noji H (2003). "F1-ATPase: a highly efficient rotary ATP machine". Essays Biochem. 35: 3–18. doi:10.1042/bse0350003. PMID 12471886.
• Oster G, Wang H (2003). "Rotary protein motors". Trends Cell Biol. 13 (3): 114–21. doi:10.1016/S0962-8924(03)00004-7. PMID 12628343.
• Leyva JA, Bianchet MA, Amzel LM (2003). "Understanding ATP synthesis: structure and mechanism of the F1-ATPase (Review)". Mol. Membr. Biol. 20 (1): 27–33. doi:10.1080/0968768031000066532. PMID 12745923. S2CID 218895820.
• Higuti T, Kuroiwa K, Miyazaki S, et al. (1994). "The complete amino acid sequence of subunit d of rat liver mitochondrial H(+)-ATP synthase". J. Biochem. 114 (5): 714–7. doi:10.1093/oxfordjournals.jbchem.a124242. PMID 7509337.
• Elston T, Wang H, Oster G (1998). "Energy transduction in ATP synthase". Nature. 391 (6666): 510–3. Bibcode:1998Natur.391..510E. doi:10.1038/35185. PMID 9461222. S2CID 4406161.
• Wang H, Oster G (1998). "Energy transduction in the F1 motor of ATP synthase". Nature. 396 (6708): 279–82. Bibcode:1998Natur.396..279W. doi:10.1038/24409. PMID 9834036. S2CID 4424498.
• 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. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• 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.
• Cross RL (2004). "Molecular motors: turning the ATP motor". Nature. 427 (6973): 407–8. Bibcode:2004Natur.427..407C. doi:10.1038/427407b. PMID 14749816. S2CID 52819856.
• 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.