8phe: Difference between revisions

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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8phe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8phe OCA], [https://pdbe.org/8phe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8phe RCSB], [https://www.ebi.ac.uk/pdbsum/8phe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8phe ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8phe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8phe OCA], [https://pdbe.org/8phe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8phe RCSB], [https://www.ebi.ac.uk/pdbsum/8phe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8phe ProSAT]</span></td></tr>
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</table>
== Disease ==
[https://www.uniprot.org/uniprot/ACAD9_HUMAN ACAD9_HUMAN] Acyl-CoA dehydrogenase 9 deficiency. The disease is caused by variants affecting the gene represented in this entry.
== Function ==
[https://www.uniprot.org/uniprot/ACAD9_HUMAN ACAD9_HUMAN] As part of the MCIA complex, primarily participates in the assembly of the mitochondrial complex I and therefore plays a role in oxidative phosphorylation (PubMed:20816094, PubMed:24158852, PubMed:32320651). This moonlighting protein has also a dehydrogenase activity toward a broad range of substrates with greater specificity for long-chain unsaturated acyl-CoAs (PubMed:12359260, PubMed:16020546, PubMed:21237683, PubMed:24158852). However, in vivo, it does not seem to play a primary role in fatty acid oxidation (PubMed:20816094, PubMed:24158852). In addition, the function in complex I assembly is independent of the dehydrogenase activity of the protein (PubMed:24158852).<ref>PMID:12359260</ref> <ref>PMID:16020546</ref> <ref>PMID:20816094</ref> <ref>PMID:21237683</ref> <ref>PMID:24158852</ref> <ref>PMID:32320651</ref>
== References ==
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