MT-ATP8

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ATP synthase protein 8 (metazoa)
Identifiers
SymbolATP-synt_8
PfamPF00895
Pfam clanCL0255
InterProIPR001421
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
Plant ATP synthase F0 subunit 8
Identifiers
SymbolYMF19
PfamPF02326
Pfam clanCL0255
InterProIPR003319
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
Fungal ATP synthase protein 8 (A6L)
Identifiers
SymbolFun_ATP-synt_8
PfamPF05933
Pfam clanCL0255
InterProIPR009230
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

The protein

ATP synthase protein 8 is a subunit of mitochondrial ATP synthase.

This protein subunit appears to be an integral component of the stator stalk in yeast mitochondrial F-ATPases.[1] The stator stalk is anchored in the membrane, and acts to prevent futile rotation of the ATPase subunits relative to the rotor during coupled ATP synthesis/hydrolysis. This subunit may have an analogous function in Metazoa.

Subunit 8 differs in sequence between Metazoa, plants and Fungi.

The gene

The ATP synthase protein 8 of human and other mammals is encoded in the mitochondrial genome by the MT-ATP8 gene. When the complete human mitochondrial genome was first published, the MT-ATP8 gene was described as the unidentified reading frame URF A6L.[2]

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References

  1. ^ Stephens AN, Khan MA, Roucou X, Nagley P, Devenish RJ (May 2003). "The molecular neighborhood of subunit 8 of yeast mitochondrial F1F0-ATP synthase probed by cysteine scanning mutagenesis and chemical modification". J. Biol. Chem. 278 (20): 17867–75. doi:10.1074/jbc.M300967200. PMID 12626501.{{cite journal}}: CS1 maint: multiple names: authors list (link) CS1 maint: unflagged free DOI (link)
  2. ^ Anderson S, Bankier AT, Barrell BG, de Bruijn MH, Coulson AR, Drouin J, Eperon IC, Nierlich DP, Roe BA, Sanger F, Schreier PH, Smith AJ, Staden R, Young IG (April 1981). "Sequence and organization of the human mitochondrial genome". Nature. 290 (5806): 457–65. doi:10.1038/290457a0. PMID 7219534.{{cite journal}}: CS1 maint: multiple names: authors list (link)

Further reading

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This article incorporates text from the public domain Pfam and InterPro: IPR001421