ACADL
entrez
33
canonical
uniprot
P28330
canonical
ensembl
ENSG00000115361
resolver
ensp
ENSP00000233710
resolver
enst
ENST00000233710
resolver
genesymbol
ACADL
resolver
hgnc
HGNC:88
resolver
uniprot
B2R8T3
resolver
uniprot
Q8IUN8
resolver
uniprot_entry
ACADL_HUMAN
resolver
uniprot_sec
B2R8T3
resolver
uniprot_sec
Q8IUN8
resolver
amino_acid_sequence
MAARLLRGSLRVLGGHRAPRQLPAARCSHSGGEERLETPSAKKLTDIGIRRIFSPEHDIFRKSVRKFFQEEVIPHHSEWEKAGEVSREVWEKAGKQGLLGVNIAEHLGGIGGDLYSAAIVWEEQAYSNCSGPGFSIHSGIVMSYITNHGSEEQIKHFIPQMTAGKCIGAIAMTEPGAGSDLQGIKTNAKKDGSDWILNGSKVFISNGSLSDVVIVVAVTNHEAPSPAHGISLFLVENGMKGFIKGRKLHKMGLKAQDTAELFFEDIRLPASALLGEENKGFYYIMKELPQERLLIADVAISASEFMFEETRNYVKQRKAFGKTVAHLQTVQHKLAELKTHICVTRAFVDNCLQLHEAKRLDSATACMAKYWASELQNSVAYDCVQLHGGWGYMWEYPIAKAYVDARVQPIYGGTNEIMKELIAREIVFDK
uniprot
proteins
ec_number
1.3.8.7
uniprot
proteins
ec_number
1.3.8.8
uniprot
proteins
function
FUNCTION: Catalyzes the first of the four reactions of the mitochondrial fatty acid beta-oxidation (FAO) pathway, 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:17564966, PubMed:21237683, PubMed:24591516, PubMed:32389575). The mitochondrial FAO pathway is the major energy-producing process in tissues and is performed through cycles of four consecutive reactions (PubMed:17564966, PubMed:26474213). Each FAO cycle shortens the fatty acyl-CoA by two carbons, yielding one acetyl-CoA (for the citric acid cycle), one FADH(2), and one NADH (which donate electrons to the respiratory chain for ATP production) (PubMed:17564966, PubMed:26474213). Among the different mitochondrial acyl-CoA dehydrogenases, long-chain specific acyl-CoA dehydrogenase activity overlaps with that of ACADV and ACAD9, acting on saturated and unsaturated acyl-CoAs with 6 to 24 carbons with a preference for 8 to 18 carbons long primary chains (PubMed:17564966, PubMed:21237683, PubMed:32389575, PubMed:8823175). Can use (4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate as substrate in vitro (which is not primarily used for energy but mainly beta-oxidized in the peroxisomes) (PubMed:17564966, PubMed:26474213). 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). Plays a primary role in FAO in tissues where it is the main long-chain ACAD expressed, such as the lung, specifically in type 2 alveolar cells (responsible for surfactant production) (PubMed:17564966, PubMed:24591516). Probably responsible for beta-oxidation of bulky substrates including branched chain fatty acyl-CoAs and sterol derivatives thanks to its enlarged substrate-binding cavity (PubMed:38839792). {ECO:0000269|PubMed:17564966, ECO:0000269|PubMed:21237683, ECO:0000269|PubMed:24591516, ECO:0000269|PubMed:32389575, ECO:0000269|PubMed:8823175, ECO:0000303|PubMed:26474213, ECO:0000303|PubMed:38839792}.
uniprot
proteins
mass_dalton
47656
uniprot
proteins
mutagenesis
MUTAGEN 291; /note="E->Q: Loss of long-chain-acyl-CoA dehydrogenase activity. No effect on protein abundance. No effect on solubility. No effect on substrate binding."; /evidence="ECO:0000269|PubMed:8155643
uniprot
proteins
pathway_participation
PATHWAY: Lipid metabolism; mitochondrial fatty acid beta-oxidation. {ECO:0000250|UniProtKB:P15650}.
uniprot
proteins
post_translational_modification
PTM: Acetylation at Lys-318 and Lys-322 in proximity of the cofactor-binding sites strongly reduces catalytic activity. These sites are deacetylated by SIRT3. {ECO:0000250|UniProtKB:P51174}.
uniprot
proteins
protein_family
Acyl-CoA dehydrogenase family
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
1559716
uniprot
proteins
pubmed
15815621
uniprot
proteins
pubmed
17564966
uniprot
proteins
pubmed
1774065
uniprot
proteins
pubmed
21237683
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24591516
uniprot
proteins
pubmed
26474213
uniprot
proteins
pubmed
32389575
uniprot
proteins
pubmed
38839792
uniprot
proteins
pubmed
8155643
uniprot
proteins
pubmed
8823175
uniprot
proteins
sequence_length
430
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250|UniProtKB:P15650}.
uniprot
proteins