Acsl4
entrez
113976
canonical
uniprot
O35547
canonical
ensembl
ENSRNOG00000019180
resolver
ensembl
ENSRNOG00055024794
resolver
ensembl
ENSRNOG00060018877
resolver
ensembl
ENSRNOG00065026083
resolver
ensp
ENSRNOP00000026057
resolver
genesymbol
Acsl4
resolver
genesymbol_syn
Acs4
resolver
genesymbol_syn
Facl4
resolver
uniprot_entry
ACSL4_RAT
resolver
activity_regulation
ACTIVITY REGULATION: Both triacsin C and rosiglitazone inhibit arachidonoyl-CoA ligase activity. {ECO:0000250|UniProtKB:O60488}.
uniprot
proteins
amino_acid_sequence
MKLKLNVLTIVLLPVHLLITIYSALIFIPWYFLTNAKKKNAMAKRIKAKPTSDKPGSPYRSVTHFDSLAVIDIPGADTLDKLFDHAVAKFGKKDSLGTREILSEENEMQPNGKVFKKLILGNYKWINYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLITSVELLESKLKAALLDINCVKHIIYVDNKTINRAEYPEGLEIHSMQSVEELGSKPENSSIPPSRPTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPGLGPKDTYIGYLPLAHVLELTAEISCFTYGCRIGYSSPLTLSDQSSKIKKGSKGDCTVLKPTLMAAVPEIMDRIYKNVMSKVQEMNYIQKTLFKIGYDYKLEQIKKGYDAPLCNLILFKKVKALLGGNVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCGAGTVTEVTDYTTGRVGAPLICCEIKLKDWQEGGYTVHDKPNPRGEIVIGGQNISMGYFKNEEKTAEDYSVDENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQAGEYVSLGKVEAALKNCPLIDNICAFAKSDQSYVISFVVPNQKKLTLLAQQKGVEGSWVDICNNPAMEAEILKEIREAANAMKLERFEIPIKVRLSPEPWTPETGLVTDAFKLKRKELKNHYLKDIERMYGGK
uniprot
proteins
ec_number
6.2.1.15
uniprot
proteins
ec_number
6.2.1.3
uniprot
proteins
function
FUNCTION: Catalyzes the conversion of long-chain fatty acids to their active form acyl-CoA for both synthesis of cellular lipids, and degradation via beta-oxidation (PubMed:23766516, PubMed:28209804, PubMed:9096315). Preferentially activates arachidonate and eicosapentaenoate as substrates (PubMed:9096315). Preferentially activates 8,9-EET > 14,15-EET > 5,6-EET > 11,12-EET (PubMed:23766516). Modulates glucose-stimulated insulin secretion by regulating the levels of unesterified EETs (PubMed:23766516). Modulates prostaglandin E2 secretion (By similarity). Acts as an activator of ferroptosis by activating polyunsaturated fatty acids, especially arachidonate and adrenate, to their active form, generating the primary lipid-peroxidation substrates that contribute to ferroptosis (By similarity). {ECO:0000250|UniProtKB:O60488, ECO:0000269|PubMed:23766516, ECO:0000269|PubMed:28209804, ECO:0000269|PubMed:9096315}.
uniprot
proteins
mass_dalton
79065
uniprot
proteins
post_translational_modification
PTM: Phosphorylation at Thr-328 by isoform Beta-II of PRKCB promotes activation and lipid peroxidation, thereby inducing ferroptosis. Phosphorylation at Thr-679 by PCK2 promotes ferroptosis. {ECO:0000250|UniProtKB:O60488}.
uniprot
proteins
protein_family
ATP-dependent AMP-binding enzyme family
uniprot
proteins
pubmed
15683247
uniprot
proteins
pubmed
23766516
uniprot
proteins
pubmed
28209804
uniprot
proteins
pubmed
29196521
uniprot
proteins
pubmed
9096315
uniprot
proteins
sequence_length
711
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250|UniProtKB:O60488}; Single-pass type III membrane protein {ECO:0000250|UniProtKB:O60488}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O60488}; Single-pass type III membrane protein {ECO:0000250|UniProtKB:O60488}. Cell membrane {ECO:0000250|UniProtKB:O60488}; Single-pass type III membrane protein {ECO:0000250|UniProtKB:O60488}.
uniprot
proteins
transmembrane_region
TRANSMEM 8..28; /note="Helical; Signal-anchor for type III membrane protein"; /evidence="ECO:0000255
uniprot
proteins