ATP5J

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ATP synthase, H+ transporting, mitochondrial Fo complex, subunit F6
Identifiers
Symbols ATP5J ; ATP5; ATP5A; ATPM; CF6; F6
External IDs OMIM603152 MGI107777 HomoloGene1272 GeneCards: ATP5J Gene
EC number 3.6.1.14
RNA expression pattern
PBB GE ATP5J 202325 s at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 522 11957
Ensembl ENSG00000154723 ENSMUSG00000022890
UniProt P18859 P97450
RefSeq (mRNA) NM_001003696 NM_001302213
RefSeq (protein) NP_001003696 NP_001289142
Location (UCSC) Chr 21:
25.72 – 25.74 Mb
Chr 16:
84.83 – 84.84 Mb
PubMed search [1] [2]
Mitochondrial ATP synthase coupling factor 6 (F6)
PDB 1vzs EBI.jpg
solution structure of subunit f6 from the peripheral stalk region of atp synthase from bovine heart mitochondria
Identifiers
Symbol ATP-synt_F6
Pfam PF05511
InterPro IPR008387

ATP synthase-coupling factor 6, mitochondrial is an enzyme that in humans is encoded by the ATP5J gene.[1][2][3]

Function[edit]

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 F0 seems to have nine subunits (a, b, c, d, e, f, g, F6 and 8). This gene encodes the F6 subunit of the F0 complex, required for F1 and F0 interactions. Alternatively spliced transcript variants encoding different isoforms have been identified for this gene.[3]

The F6 subunit is part of the peripheral stalk that links the F1 and FO complexes together, and which acts as a stator to prevent certain subunits from rotating with the central rotary element. The peripheral stalk differs in subunit composition between mitochondrial, chloroplast and bacterial F-ATPases. In mitochondria, the peripheral stalk is composed of one copy each of subunits OSCP (oligomycin sensitivity conferral protein), F6, B and D.[4] There is no homologue of subunit F6 in bacterial or chloroplast F-ATPase, whose peripheral stalks are composed of one copy of the delta subunit (homologous to OSCP), and two copies of subunit B in bacteria, or one copy each of subunits B and B' in chloroplasts and photosynthetic bacteria.

References[edit]

  1. ^ Higuti T, Tsurumi C, Kawamura Y, Tsujita H, Osaka F, Yoshihara Y, Tani I, Tanaka K, Ichihara A (Jul 1991). "Molecular cloning of cDNA for the import precursor of human coupling factor 6 of H(+)-ATP synthase in mitochondria". Biochemical and Biophysical Research Communications 178 (2): 793–9. doi:10.1016/0006-291X(91)90178-A. PMID 1830479. 
  2. ^ Javed AA, Ogata K, Sanadi DR (Jan 1991). "Human mitochondrial ATP synthase: cloning cDNA for the nuclear-encoded precursor of coupling factor 6". Gene 97 (2): 307–10. doi:10.1016/0378-1119(91)90068-M. PMID 1825642. 
  3. ^ a b "Entrez Gene: ATP5J ATP synthase, H+ transporting, mitochondrial F0 complex, subunit F6". 
  4. ^ Carbajo RJ, Kellas FA, Runswick MJ, Montgomery MG, Walker JE, Neuhaus D (Aug 2005). "Structure of the F1-binding domain of the stator of bovine F1Fo-ATPase and how it binds an alpha-subunit". Journal of Molecular Biology 351 (4): 824–38. doi:10.1016/j.jmb.2005.06.012. PMID 16045926. 

Further reading[edit]

  • Kinosita K, Yasuda R, Noji H (2003). "F1-ATPase: a highly efficient rotary ATP machine". Essays in Biochemistry 35: 3–18. PMID 12471886. 
  • Oster G, Wang H (Mar 2003). "Rotary protein motors". Trends in Cell Biology 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)". Molecular Membrane Biology 20 (1): 27–33. doi:10.1080/0968768031000066532. PMID 12745923. 
  • Hochstrasser DF, Frutiger S, Paquet N, Bairoch A, Ravier F, Pasquali C, Sanchez JC, Tissot JD, Bjellqvist B, Vargas R (Dec 1992). "Human liver protein map: a reference database established by microsequencing and gel comparison". Electrophoresis 13 (12): 992–1001. doi:10.1002/elps.11501301201. PMID 1286669. 
  • Yan WL, Lerner TJ, Haines JL, Gusella JF (Nov 1994). "Sequence analysis and mapping of a novel human mitochondrial ATP synthase subunit 9 cDNA (ATP5G3)". Genomics 24 (2): 375–7. doi:10.1006/geno.1994.1631. PMID 7698763. 
  • Elston T, Wang H, Oster G (Jan 1998). "Energy transduction in ATP synthase". Nature 391 (6666): 510–3. doi:10.1038/35185. PMID 9461222. 
  • Webster KA, Oliver NA, Wallace DC (Mar 1982). "Assignment of an oligomycin-resistance locus to human chromosome 10". Somatic Cell Genetics 8 (2): 223–44. doi:10.1007/BF01538679. PMID 9732751. 
  • Wang H, Oster G (Nov 1998). "Energy transduction in the F1 motor of ATP synthase". Nature 396 (6708): 279–82. doi:10.1038/24409. PMID 9834036. 
  • Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Böcher M, Blöcker H, Bauersachs S, Blum H, Lauber J, Düsterhöft A, Beyer A, Köhrer K, Strack N, Mewes HW, Ottenwälder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A (Mar 2001). "Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs". Genome Research 11 (3): 422–35. doi:10.1101/gr.GR1547R. PMC 311072. PMID 11230166. 
  • Osanai T, Nakamura M, Sasaki S, Tomita H, Saitoh M, Osawa H, Yamabe H, Murakami S, Magota K, Okumura K (Dec 2003). "Plasma concentration of coupling factor 6 and cardiovascular events in patients with end-stage renal disease". Kidney International 64 (6): 2291–7. doi:10.1046/j.1523-1755.2003.00334.x. PMID 14633154. 
  • Cross RL (Jan 2004). "Molecular motors: turning the ATP motor". Nature 427 (6973): 407–8. doi:10.1038/427407b. PMID 14749816. 
  • Jacobs LJ, de Coo IF, Nijland JG, Galjaard RJ, Los FJ, Schoonderwoerd K, Niermeijer MF, Geraedts JP, Scholte HR, Smeets HJ (Mar 2005). "Transmission and prenatal diagnosis of the T9176C mitochondrial DNA mutation". Molecular Human Reproduction 11 (3): 223–8. doi:10.1093/molehr/gah152. PMID 15709156. 

This article incorporates text from the public domain Pfam and InterPro IPR008387