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NDUFA10
NADH dehydrogenase () 1 alpha subcomplex subunit 10 is an enzyme that in humans is encoded by the NDUFA10 gene.〔(【引用サイトリンク】 url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4705 )〕 The NDUFA10 protein is a subunit of NADH dehydrogenase (ubiquinone), which is located in the mitochondrial inner membrane and is the largest of the five complexes of the electron transport chain. Mutations in subunits of NADH dehydrogenase (ubiquinone), also known as Complex I, frequently lead to complex neurodegenerative diseases such as Leigh's syndrome.〔 Furthermore, reduced NDUFA10 expression levels due to FOXM1-directed hypermethylation are associated with human squamous cell carcinoma and may be related to other forms of cancer.
== Structure ==
The NDUFA10 gene is located on the q arm of chromosome 2 in position 37.3 and spans 68,031 base pairs.〔 The gene produces a 41 kDa protein composed of 355 amino acids.〔(【引用サイトリンク】 work = Cardiac Organellar Protein Atlas Knowledgebase (COPaKB) )〕 NDUFA10 is a subunit of the enzyme NADH dehydrogenase (ubiquinone), the largest of the respiratory complexes. The structure is L-shaped with a long, hydrophobic transmembrane domain and a hydrophilic domain for the peripheral arm that includes all the known redox centers and the NADH binding site.〔 It has been noted that the N-terminal hydrophobic domain has the potential to be folded into an alpha helix spanning the inner mitochondrial membrane with a C-terminal hydrophilic domain interacting with globular subunits of Complex I. The highly conserved two-domain structure suggests that this feature is critical for the protein function and that the hydrophobic domain acts as an anchor for the NADH dehydrogenase (ubiquinone) complex at the inner mitochondrial membrane. NDUFA10 is one of about 31 hydrophobic subunits that form the transmembrane region of Complex I, but it is an accessory subunit that is believed not to be involved in catalysis.〔(【引用サイトリンク】) 1 alpha subcomplex subunit 10 ">url=http://www.uniprot.org/uniprot/O95299 )〕 The predicted secondary structure is primarily alpha helix, but the carboxy-terminal half of the protein has high potential to adopt a coiled-coil form. The amino-terminal part contains a putative beta sheet rich in hydrophobic amino acids that may serve as mitochondrial import signal.〔〔
抄文引用元・出典: フリー百科事典『 ウィキペディア（Wikipedia）』
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