Acad9
entrez
229211
canonical
uniprot
Q8JZN5
canonical
ensembl
ENSMUSG00000027710
resolver
ensp
ENSMUSP00000011492
resolver
enst
ENSMUST00000011492
resolver
genesymbol
Acad9
resolver
uniprot
Q3ULL9
resolver
uniprot
Q8BK76
resolver
uniprot
Q8C0B5
resolver
uniprot_entry
ACAD9_MOUSE
resolver
uniprot_sec
Q3ULL9
resolver
uniprot_sec
Q8BK76
resolver
uniprot_sec
Q8C0B5
resolver
amino_acid_sequence
MSGCVLLSRGATAAAAAARASRVLREFTARRRPLHTSLQSCSFAKELFLGNIEQKGVFPFPEVSQHELSEINQFVGPLEKFFTEEVDSRKIDQEGKIPVDTLEKLKSLGLFGIQVPEEYGGLGLSNTMYARLGEIISLDASITVTLAAHQAIGLKGIILVGNEEQKAKYLPKLSSGEHIAAFCLTEPASGSDAASIQTRATLSEDKKYFILNGSKVWITNGGLANIFTVFAKTEVVDSDGSKTDKMTAFIVERDFGGITNGKPEDKLGIRGSNTCEVHFENTRVPVENVLGEVGGGFKVAMNILNSGRFSMGSAVAGMLKKLIELTAEYACTRKQFNRNLSEFGLIQEKFALMAQKAYVMESMAYLTSGMLDQPGFPDCSIEAAMVKVFSSEAAWQCVSEALQILGGSGYMKDYPYERMLRDARILLIFEGTNEILRLFIALTGLQHAGRILTSRIKELKSGNVTTVMETIGRKLRDSLGRTVDLGLTGDLGVVHPSLGDSANKLEENVHYFGRTVETLLLRFGKNIVEEQLVLKRVANILINLYGMTAVLSRASRSIRIGLRNHDHEVLLANMFCVEAYFQNLFSLSQLDKNAPENLDEQIKKVSRQILEKRAYICAHPLDRAS
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. ECSIT binding triggers a large conformational change, switching ACAD9 from a fatty acid oxidation (FAO) enzyme to a CI assembly factor. The function in CI assembly is independent of the fatty acid oxidation (FAO) activity of the protein. 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). Its preferred substrates are both saturated and unsaturated long-chain acyl-CoA substrates, with optimum activity toward the latter. 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. 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. 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). {ECO:0000250|UniProtKB:Q9H845}.
uniprot
proteins
mass_dalton
68722
uniprot
proteins
protein_family
Acyl-CoA dehydrogenase family
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
23576753
uniprot
proteins
pubmed
23806337
uniprot
proteins
sequence_length
625
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q9H845}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9H845}; Matrix side {ECO:0000250|UniProtKB:Q9H845}. Note=Essentially associated with membranes. {ECO:0000250|UniProtKB:Q9H845}.
uniprot
proteins