ATPAF2
{{Short description|Protein-coding gene in the species Homo sapiens}}
{{Infobox_gene}}
ATP synthase mitochondrial F1 complex assembly factor 2 is an enzyme that in humans is encoded by the ATPAF2 gene.{{cite journal | vauthors = Wang ZG, White PS, Ackerman SH | title = Atp11p and Atp12p are assembly factors for the F(1)-ATPase in human mitochondria | journal = The Journal of Biological Chemistry | volume = 276 | issue = 33 | pages = 30773–30778 | date = August 2001 | pmid = 11410595 | doi = 10.1074/jbc.M104133200 | doi-access = free }}{{cite journal | vauthors = Bi W, Yan J, Stankiewicz P, Park SS, Walz K, Boerkoel CF, Potocki L, Shaffer LG, Devriendt K, Nowaczyk MJ, Inoue K, Lupski JR | title = Genes in a refined Smith-Magenis syndrome critical deletion interval on chromosome 17p11.2 and the syntenic region of the mouse | journal = Genome Research | volume = 12 | issue = 5 | pages = 713–728 | date = May 2002 | pmid = 11997338 | pmc = 186594 | doi = 10.1101/gr.73702 }}{{cite web | title = Entrez Gene: ATPAF2 ATP synthase mitochondrial F1 complex assembly factor 2| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=91647}}{{PD-notice}}
This gene encodes an assembly factor for the F(1) component of the mitochondrial ATP synthase. This protein binds specifically to the F1 alpha subunit and is thought to prevent the subunit from forming nonproductive homooligomers during enzyme assembly. This gene is located within the Smith–Magenis syndrome region on chromosome 17. An alternatively spliced transcript variant has been described, but its biological validity has not been determined. A mutation in this gene has caused nuclear type 1 Complex V deficiency, characterized by lactic acidosis, encephalopathy, and developmental delays.{{cite journal | vauthors = De Meirleir L, Seneca S, Lissens W, De Clercq I, Eyskens F, Gerlo E, Smet J, Van Coster R | title = Respiratory chain complex V deficiency due to a mutation in the assembly gene ATP12 | journal = Journal of Medical Genetics | volume = 41 | issue = 2 | pages = 120–124 | date = February 2004 | pmid = 14757859 | pmc = 1735674 | doi = 10.1136/jmg.2003.012047 | url = }}Online Mendelian Inheritance in Man, OMIM. Johns Hopkins University, Baltimore, MD. MIM Number: {608918}: {2017-08-17}: . World Wide Web URL: https://omim.org/
Structure
The ATPAF2 gene is located on the p arm of chromosome 17 in position 11.2 and spans 24,110 base pairs. The gene produces a 32.8 kDa protein composed of 289 amino acids.{{cite journal | vauthors = Zong NC, Li H, Li H, Lam MP, Jimenez RC, Kim CS, Deng N, Kim AK, Choi JH, Zelaya I, Liem D, Meyer D, Odeberg J, Fang C, Lu HJ, Xu T, Weiss J, Duan H, Uhlen M, Yates JR, Apweiler R, Ge J, Hermjakob H, Ping P | display-authors = 6 | title = Integration of cardiac proteome biology and medicine by a specialized knowledgebase | journal = Circulation Research | volume = 113 | issue = 9 | pages = 1043–1053 | date = October 2013 | pmid = 23965338 | pmc = 4076475 | doi = 10.1161/CIRCRESAHA.113.301151 }}{{cite web | url = https://amino.heartproteome.org/web/protein/Q8N5M1 | work = Cardiac Organellar Protein Atlas Knowledgebase (COPaKB) | title = ATPAF2 - ATP synthase mitochondrial F1 complex assembly factor 2 }}{{Dead link|date=September 2019 |bot=InternetArchiveBot |fix-attempted=yes }} This gene has at least 8 exons and is located within the Smith-Magenis syndrome region on chromosome 17.
Function
The ATPAF2 gene encodes an essential housekeeping protein, an assembly factor for the F1 component of mitochondrial ATP synthase. This protein binds specifically to the F1 alpha subunit and is thought to prevent this subunit from forming nonproductive homooligomers during enzyme assembly.
Clinical significance
In the only report of a mutation in the ATPAF2 gene, the resulting phenotype was nuclear type 1 Complex V deficiency inherited in an autosomal recessive manner. A homozygous 280T-A transversion caused a W94R amino acid substitution adjacent to a highly conserved glutamine. Symptoms included elevated blood, CSF, and urine lactate levels, developmental delays with failure to thrive and seizures, and a degenerative encephalopathy with cortical and subcortical atrophy.
Interactions
The encoded protein interacts with ATP5F1A and FMC1, along with many other proteins.{{cite journal | vauthors = Li Y, Jourdain AA, Calvo SE, Liu JS, Mootha VK | title = CLIC, a tool for expanding biological pathways based on co-expression across thousands of datasets | journal = PLOS Computational Biology | volume = 13 | issue = 7 | pages = e1005653 | date = July 2017 | pmid = 28719601 | pmc = 5546725 | doi = 10.1371/journal.pcbi.1005653 | bibcode = 2017PLSCB..13E5653L | doi-access = free }}{{cite journal | title = UniProt: the universal protein knowledgebase | journal = Nucleic Acids Research | volume = 45 | issue = D1 | pages = D158–D169 | date = January 2017 | pmid = 27899622 | pmc = 5210571 | doi = 10.1093/nar/gkw1099 }}
References
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Further reading
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- {{cite journal | vauthors = Andersson B, Wentland MA, Ricafrente JY, Liu W, Gibbs RA | title = A "double adaptor" method for improved shotgun library construction | journal = Analytical Biochemistry | volume = 236 | issue = 1 | pages = 107–113 | date = April 1996 | pmid = 8619474 | doi = 10.1006/abio.1996.0138 }}
- {{cite journal | vauthors = Yu W, Andersson B, Worley KC, Muzny DM, Ding Y, Liu W, Ricafrente JY, Wentland MA, Lennon G, Gibbs RA | title = Large-scale concatenation cDNA sequencing | journal = Genome Research | volume = 7 | issue = 4 | pages = 353–358 | date = April 1997 | pmid = 9110174 | pmc = 139146 | doi = 10.1101/gr.7.4.353 }}
- {{cite journal | vauthors = Hartley JL, Temple GF, Brasch MA | title = DNA cloning using in vitro site-specific recombination | journal = Genome Research | volume = 10 | issue = 11 | pages = 1788–1795 | date = November 2000 | pmid = 11076863 | pmc = 310948 | doi = 10.1101/gr.143000 }}
- {{cite journal | vauthors = De Meirleir L, Seneca S, Lissens W, De Clercq I, Eyskens F, Gerlo E, Smet J, Van Coster R | title = Respiratory chain complex V deficiency due to a mutation in the assembly gene ATP12 | journal = Journal of Medical Genetics | volume = 41 | issue = 2 | pages = 120–124 | date = February 2004 | pmid = 14757859 | pmc = 1735674 | doi = 10.1136/jmg.2003.012047 }}
- {{cite journal | vauthors = Wiemann S, Arlt D, Huber W, Wellenreuther R, Schleeger S, Mehrle A, Bechtel S, Sauermann M, Korf U, Pepperkok R, Sültmann H, Poustka A | title = From ORFeome to biology: a functional genomics pipeline | journal = Genome Research | volume = 14 | issue = 10B | pages = 2136–2144 | date = October 2004 | pmid = 15489336 | pmc = 528930 | doi = 10.1101/gr.2576704 }}
- {{cite journal | vauthors = Mehrle A, Rosenfelder H, Schupp I, del Val C, Arlt D, Hahne F, Bechtel S, Simpson J, Hofmann O, Hide W, Glatting KH, Huber W, Pepperkok R, Poustka A, Wiemann S | title = The LIFEdb database in 2006 | journal = Nucleic Acids Research | volume = 34 | issue = Database issue | pages = D415–8 | date = January 2006 | pmid = 16381901 | pmc = 1347501 | doi = 10.1093/nar/gkj139 }}
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