ACADVL
entrez
37
canonical
uniprot
P49748
canonical
ensembl
ENSG00000072778
resolver
ensp
ENSP00000344152
resolver
ensp
ENSP00000349297
resolver
ensp
ENSP00000438689
resolver
ensp
ENSP00000553825
resolver
ensp
ENSP00000615365
resolver
ensp
ENSP00000615370
resolver
ensp
ENSP00000690338
resolver
genesymbol
ACADVL
resolver
genesymbol_syn
VLCAD
resolver
hgnc
HGNC:92
resolver
uniprot
B3KPA6
resolver
uniprot
B4DEB6
resolver
uniprot
F5H2A9
resolver
uniprot
O76056
resolver
uniprot
Q8WUL0
resolver
uniprot_entry
ACADV_HUMAN
resolver
uniprot_entry
B3KPA6_HUMAN
resolver
uniprot_sec
B4DEB6
resolver
uniprot_sec
F5H2A9
resolver
uniprot_sec
O76056
resolver
uniprot_sec
Q8WUL0
resolver
amino_acid_sequence
MQAARMAASLGRQLLRLGGGSSRLTALLGQPRPGPARRPYAGGAAQLALDKSDSHPSDALTRKKPAKAESKSFAVGMFKGQLTTDQVFPYPSVLNEEQTQFLKELVEPVSRFFEEVNDPAKNDALEMVEETTWQGLKELGAFGLQVPSELGGVGLCNTQYARLVEIVGMHDLGVGITLGAHQSIGFKGILLFGTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRTSAVPSPCGKYYTLNGSKLWISNGGLADIFTVFAKTPVTDPATGAVKEKITAFVVERGFGGITHGPPEKKMGIKASNTAEVFFDGVRVPSENVLGEVGSGFKVAMHILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQFGEKIHNFGLIQEKLARMVMLQYVTESMAYMVSANMDQGATDFQIEAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRLFVALQGCMDKGKELSGLGSALKNPFGNAGLLLGEAGKQLRRRAGLGSGLSLSGLVHPELSRSGELAVRALEQFATVVEAKLIKHKKGIVNEQFLLQRLADGAIDLYAMVVVLSRASRSLSEGHPTAQHEKMLCDTWCIEAAARIREGMAALQSDPWQQELYRNFKSISKALVERGGVVTSNPLGF
uniprot
proteins
disease_involvement
DISEASE: Acyl-CoA dehydrogenase very long-chain deficiency (ACADVLD) [MIM:201475]: An inborn error of mitochondrial fatty acid beta-oxidation which leads to impaired long-chain fatty acid beta-oxidation. It is clinically heterogeneous, with three major phenotypes: a severe childhood form characterized by early onset, high mortality and high incidence of cardiomyopathy; a milder childhood form with later onset, characterized by hypoketotic hypoglycemia, low mortality and rare cardiomyopathy; an adult form, with isolated skeletal muscle involvement, rhabdomyolysis and myoglobinuria, usually triggered by exercise or fasting. {ECO:0000269|PubMed:10077518, ECO:0000269|PubMed:17374501, ECO:0000269|PubMed:7668252, ECO:0000269|PubMed:8554073, ECO:0000269|PubMed:8845838, ECO:0000269|PubMed:9461620, ECO:0000269|PubMed:9546340, ECO:0000269|PubMed:9599005, ECO:0000269|PubMed:9839948, ECO:0000269|PubMed:9973285}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
1.3.8.8
uniprot
proteins
ec_number
1.3.8.9
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:18227065, PubMed:26474213, PubMed:7668252, PubMed:9461620, PubMed:9599005, PubMed:9839948). The mitochondrial FAO pathway is the major energy-producing process in tissues and is performed through cycles of four consecutive reactions (PubMed:26474213, PubMed:7668252). 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:26474213, PubMed:7668252). Among the different mitochondrial acyl-CoA dehydrogenases, very long-chain specific acyl-CoA dehydrogenase acts specifically on fatty acyl-CoAs with saturated 12 to 24 carbons long primary chains (PubMed:17564966, PubMed:21237683, PubMed:9839948), but can also catalyze monounsaturated fatty acids such as oleate ((9Z)-octadecenoate), (9Z)-hexadecenoate, and others (PubMed:17564966). 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). Among the different mitochondrial acyl-CoA dehydrogenases, its FAO activity overlaps with that of ACAD9 and ACADL, but plays a primary role in tissues where it is the main long-chain ACAD expressed, such as the heart and skeletal muscle (PubMed:17564966). {ECO:0000269|PubMed:17564966, ECO:0000269|PubMed:18227065, ECO:0000269|PubMed:21237683, ECO:0000269|PubMed:7668252, ECO:0000269|PubMed:9461620, ECO:0000269|PubMed:9599005, ECO:0000269|PubMed:9839948, ECO:0000303|PubMed:26474213}.
uniprot
proteins
mass_dalton
70390
uniprot
proteins
mutagenesis
MUTAGEN 458; /note="F->T: Decreased acyl-CoA dehydrogenase activity. Decreased affinity for acyl-CoA. No effect on FAD cofactor-binding."; /evidence="ECO:0000269|PubMed:9461620"; MUTAGEN 458; /note="F->V: Loss of acyl-CoA dehydrogenase activity. Loss of FAD cofactor-binding."; /evidence="ECO:0000269|PubMed:9461620"; MUTAGEN 458; /note="F->Y: Decreased acyl-CoA dehydrogenase activity. No effect on affinity for acyl-CoA. Decreased FAD cofactor-binding."; /evidence="ECO:0000269|PubMed:9461620"; MUTAGEN 462; /note="E->D: Decreased acyl-CoA dehydrogenase activity. No effect on affinity for acyl-CoA. No effect on FAD cofactor-binding."; /evidence="ECO:0000269|PubMed:9461620"; MUTAGEN 462; /note="E->Q: Loss of acyl-CoA dehydrogenase activity. No effect on FAD cofactor-binding."; /evidence="ECO:0000269|PubMed:9461620"; MUTAGEN 490; /note="A->G,V,S,D,H: Changed substrate specificity with decreased affinity for tetradecanoyl-CoA and hexadecanoyl-CoA."; /evidence="ECO:0000269|PubMed:9839948
uniprot
proteins
pathway_participation
PATHWAY: Lipid metabolism; mitochondrial fatty acid beta-oxidation. {ECO:0000269|PubMed:7668252, ECO:0000269|PubMed:9599005, ECO:0000269|PubMed:9839948}.
uniprot
proteins
post_translational_modification
PTM: S-nitrosylation at Cys-237 in liver improves catalytic efficiency. {ECO:0000250|UniProtKB:P50544}.
uniprot
proteins
protein_family
Acyl-CoA dehydrogenase family
uniprot
proteins
pubmed
10077518
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16625196
uniprot
proteins
pubmed
17374501
uniprot
proteins
pubmed
17564966
uniprot
proteins
pubmed
18227065
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
21237683
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
26474213
uniprot
proteins
pubmed
7668252
uniprot
proteins
pubmed
7769092
uniprot
proteins
pubmed
8554073
uniprot
proteins
pubmed
8554625
uniprot
proteins
pubmed
8845838
uniprot
proteins
pubmed
9461620
uniprot
proteins
pubmed
9546340
uniprot
proteins
pubmed
9599005
uniprot
proteins
pubmed
9839948
uniprot
proteins
pubmed
9973285
uniprot
proteins
sequence_length
655
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:9461620, ECO:0000269|PubMed:9599005}; Peripheral membrane protein {ECO:0000269|PubMed:9599005}.; SUBCELLULAR LOCATION: [Isoform 2]: Mitochondrion inner membrane {ECO:0000269|PubMed:17374501}; Peripheral membrane protein {ECO:0000269|PubMed:17374501}.
uniprot
proteins