ACAD9
entrez
28976
canonical
uniprot
Q9H845
canonical
ensembl
ENSG00000177646
resolver
ensp
ENSP00000312618
resolver
ensp
ENSP00000506228
resolver
ensp
ENSP00000506340
resolver
enst
ENST00000308982
resolver
enst
ENST00000679715
resolver
enst
ENST00000681583
resolver
genesymbol
ACAD9
resolver
hgnc
HGNC:21497
resolver
uniprot
A0A7P0TAJ6
resolver
uniprot
D3DNB8
resolver
uniprot
Q8WXX3
resolver
uniprot
Q9H9W4
resolver
uniprot_entry
A0A7P0TAJ6_HUMAN
resolver
uniprot_entry
ACAD9_HUMAN
resolver
uniprot_entry
Q9H9W4_HUMAN
resolver
uniprot_sec
D3DNB8
resolver
uniprot_sec
Q8WXX3
resolver
amino_acid_sequence
MSGCGLFLRTTAAARACRGLVVSTANRRLLRTSPPVRAFAKELFLGKIKKKEVFPFPEVSQDELNEINQFLGPVEKFFTEEVDSRKIDQEGKIPDETLEKLKSLGLFGLQVPEEYGGLGFSNTMYSRLGEIISMDGSITVTLAAHQAIGLKGIILAGTEEQKAKYLPKLASGEHIAAFCLTEPASGSDAASIRSRATLSEDKKHYILNGSKVWITNGGLANIFTVFAKTEVVDSDGSVKDKITAFIVERDFGGVTNGKPEDKLGIRGSNTCEVHFENTKIPVENILGEVGDGFKVAMNILNSGRFSMGSVVAGLLKRLIEMTAEYACTRKQFNKRLSEFGLIQEKFALMAQKAYVMESMTYLTAGMLDQPGFPDCSIEAAMVKVFSSEAAWQCVSEALQILGGLGYTRDYPYERILRDTRILLIFEGTNEILRMYIALTGLQHAGRILTTRIHELKQAKVSTVMDTVGRRLRDSLGRTVDLGLTGNHGVVHPSLADSANKFEENTYCFGRTVETLLLRFGKTIMEEQLVLKRVANILINLYGMTAVLSRASRSIRIGLRNHDHEVLLANTFCVEAYLQNLFSLSQLDKYAPENLDEQIKKVSQQILEKRAYICAHPLDRTC
uniprot
proteins
disease_involvement
DISEASE: Mitochondrial complex I deficiency, nuclear type 20 (MC1DN20) [MIM:611126]: An autosomal recessive metabolic disorder associated with mitochondrial complex I deficiency, resulting in multisystemic and variable manifestations. Clinical features include infantile onset of acute metabolic acidosis, Reye-like episodes (brain edema and vomiting that may rapidly progress to seizures, coma and death), exercise intolerance, hypertrophic cardiomyopathy, liver failure, muscle weakness, and neurologic dysfunction. {ECO:0000269|PubMed:17564966, ECO:0000269|PubMed:20816094, ECO:0000269|PubMed:20929961, ECO:0000269|PubMed:21057504, ECO:0000269|PubMed:22499348, ECO:0000269|PubMed:23836383, ECO:0000269|PubMed:23996478, ECO:0000269|PubMed:26741492}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
1.3.8.7
uniprot
proteins
ec_number
1.3.8.8
uniprot
proteins
function
FUNCTION: Together with NDUFAF1 and ECSIT, forms part of the mitochondrial complex I (MCIA),which is required for the biogenesis of respiratory Complex I (CI) and is therefore crucial for the activation of the oxidative phosphorylation system (PubMed:20816094, PubMed:24158852, PubMed:32320651, PubMed:38086790). ECSIT binding triggers a large conformational change, switching ACAD9 from a fatty acid oxidation (FAO) enzyme to a CI assembly factor (PubMed:38086790). The function in CI assembly is independent of the fatty acid oxidation (FAO) activity of the protein (PubMed:24158852). As FAO enzyme, it catalyzes the first step in mitochondrial FAO, which consists in the proR-proR stereospecific alpha, beta-dehydrogenation of fatty acyl-CoA thioesters using the electron transfer flavoprotein (ETF) as their physiologic electron acceptor, resulting in the formation of trans-2-enoyl-CoA ((2E)-enoyl-CoA) (PubMed:12359260, PubMed:16020546, PubMed:17564966, PubMed:21237683, PubMed:24158852). Its preferred substrates are both saturated and unsaturated long-chain acyl-CoA substrates, with optimum activity toward the latter (PubMed:12359260, PubMed:16020546, PubMed:17564966, PubMed:21237683, PubMed:24158852). In addition, based on its established catalytic mechanism, and combined genetic interaction or mutant phenotype evidence, it is predicted to act also on substrates that have not been tested experimentally but are metabolized by mitochondrial FAO, including long-chain unsaturated fatty acids such as linoleate (9Z,12Z-octadecadienoate), linolenate (9Z,12Z,15Z-octadecatrienoate), and others (PubMed:26474213). Among the different mitochondrial acyl-CoA dehydrogenases, its FAO activity overlaps with that of ACADV and ACADL, but plays a primary role in tissues where it is the main long-chain ACAD expressed, such as the central nervous system (PubMed:16020546, PubMed:17564966, PubMed:24158852, PubMed:25721401, PubMed:26474213). It differs significantly from ACADVL in the use of polyunsaturated substrates in vitro, especially docosahexaenoic acid (which is not primarily used for energy but mainly beta-oxidized in the peroxisomes) (PubMed:16020546, PubMed:17564966). {ECO:0000269|PubMed:12359260, ECO:0000269|PubMed:16020546, ECO:0000269|PubMed:17564966, ECO:0000269|PubMed:20816094, ECO:0000269|PubMed:21237683, ECO:0000269|PubMed:24158852, ECO:0000269|PubMed:25721401, ECO:0000269|PubMed:32320651, ECO:0000269|PubMed:38086790, ECO:0000303|PubMed:26474213}.
uniprot
proteins
mass_dalton
68760
uniprot
proteins
mutagenesis
MUTAGEN 426; /note="E->Q: Loss of long-chain-acyl-CoA dehydrogenase activity. Does not affect mitochondrial complex I assembly."; /evidence="ECO:0000269|PubMed:24158852
uniprot
proteins
protein_family
Acyl-CoA dehydrogenase family
uniprot
proteins
pubmed
12359260
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16020546
uniprot
proteins
pubmed
17564966
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
20816094
uniprot
proteins
pubmed
20929961
uniprot
proteins
pubmed
21057504
uniprot
proteins
pubmed
21237683
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
22499348
uniprot
proteins
pubmed
23836383
uniprot
proteins
pubmed
23996478
uniprot
proteins
pubmed
24158852
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25721401
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
26474213
uniprot
proteins
pubmed
26741492
uniprot
proteins
pubmed
32320651
uniprot
proteins
pubmed
33753518
uniprot
proteins
pubmed
38086790
uniprot
proteins
pubmed
40255280
uniprot
proteins
sequence_length
621
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:16020546, ECO:0000269|PubMed:20816094}; Peripheral membrane protein {ECO:0000269|PubMed:16020546}; Matrix side {ECO:0000269|PubMed:16020546}. Note=Essentially associated with membranes. {ECO:0000269|PubMed:16020546}.
uniprot
proteins