ACSL4
entrez
2182
canonical
uniprot
O60488
canonical
ensembl
ENSG00000068366
resolver
ensp
ENSP00000262835
resolver
ensp
ENSP00000339787
resolver
ensp
ENSP00000419171
resolver
ensp
ENSP00000425408
resolver
ensp
ENSP00000499969
resolver
ensp
ENSP00000500273
resolver
ensp
ENSP00000500678
resolver
ensp
ENSP00000500897
resolver
ensp
ENSP00000521314
resolver
ensp
ENSP00000521315
resolver
ensp
ENSP00000585959
resolver
genesymbol
ACSL4
resolver
genesymbol
FACL4
resolver
genesymbol_syn
ACS4
resolver
genesymbol_syn
FACL4
resolver
genesymbol_syn
LACS4
resolver
hgnc
HGNC:3571
resolver
uniprot
D3DUY2
resolver
uniprot
O60848
resolver
uniprot
O60849
resolver
uniprot
Q5JWV8
resolver
uniprot
Q8TAF6
resolver
uniprot_entry
ACSL4_HUMAN
resolver
uniprot_entry
Q8TAF6_HUMAN
resolver
uniprot_sec
D3DUY2
resolver
uniprot_sec
O60848
resolver
uniprot_sec
O60849
resolver
uniprot_sec
Q5JWV8
resolver
activity_regulation
ACTIVITY REGULATION: Both triacsin C and rosiglitazone inhibit arachidonoyl-CoA ligase activity (PubMed:21242590). Specifically inhibited by thiazolidinediones, preventing ferroptosis (PubMed:27842070). {ECO:0000269|PubMed:21242590, ECO:0000269|PubMed:27842070}.
uniprot
proteins
amino_acid_sequence
MKLKLNVLTIILLPVHLLITIYSALIFIPWYFLTNAKKKNAMAKRIKAKPTSDKPGSPYRSVTHFDSLAVIDIPGADTLDKLFDHAVSKFGKKDSLGTREILSEENEMQPNGKVFKKLILGNYKWMNYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLITSVELLESKLKTALLDISCVKHIIYVDNKAINKAEYPEGFEIHSMQSVEELGSNPENLGIPPSRPTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPGLGPKDTYIGYLPLAHVLELTAEISCFTYGCRIGYSSPLTLSDQSSKIKKGSKGDCTVLKPTLMAAVPEIMDRIYKNVMSKVQEMNYIQKTLFKIGYDYKLEQIKKGYDAPLCNLLLFKKVKALLGGNVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCGAGTVTEVTDYTTGRVGAPLICCEIKLKDWQEGGYTINDKPNPRGEIVIGGQNISMGYFKNEEKTAEDYSVDENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQAGEYVSLGKVEAALKNCPLIDNICAFAKSDQSYVISFVVPNQKRLTLLAQQKGVEGTWVDICNNPAMEAEILKEIREAANAMKLERFEIPIKVRLSPEPWTPETGLVTDAFKLKRKELRNHYLKDIERMYGGK
uniprot
proteins
disease_involvement
DISEASE: Intellectual developmental disorder, X-linked 63 (XLID63) [MIM:300387]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. Intellectual deficiency is the only primary symptom of non-syndromic X-linked intellectual disability, while syndromic forms presents with associated physical, neurological and/or psychiatric manifestations. {ECO:0000269|PubMed:11889465}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: AMME complex (ATS-MR) [MIM:300194]: An X-linked contiguous gene deletion syndrome characterized by glomerulonephritis, sensorineural hearing loss, intellectual disability, midface hypoplasia and elliptocytosis. {ECO:0000269|PubMed:9480748}. Note=The gene represented in this entry may be involved in disease pathogenesis.
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:21242590, PubMed:22633490, PubMed:24269233, PubMed:31061331, PubMed:38720107). Preferentially activates arachidonate and eicosapentaenoate as substrates (PubMed:21242590). Preferentially activates 8,9-EET > 14,15-EET > 5,6-EET > 11,12-EET (PubMed:21242590). Modulates glucose-stimulated insulin secretion by regulating the levels of unesterified EETs (By similarity). Modulates prostaglandin E2 secretion (PubMed:21242590). 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 (PubMed:27842070, PubMed:35027735, PubMed:38720107). {ECO:0000250|UniProtKB:O35547, ECO:0000269|PubMed:21242590, ECO:0000269|PubMed:22633490, ECO:0000269|PubMed:24269233, ECO:0000269|PubMed:27842070, ECO:0000269|PubMed:31061331, ECO:0000269|PubMed:35027735, ECO:0000269|PubMed:38720107}.
uniprot
proteins
mass_dalton
79188
uniprot
proteins
mutagenesis
MUTAGEN 328; /note="T->A: Abolished phosphorylation by isoform Beta-II of PRKCB, preventing ferroptosis."; /evidence="ECO:0000269|PubMed:35027735"; MUTAGEN 679; /note="T->A: Abolished phosphorylation by PCK2, preventing ferroptosis."; /evidence="ECO:0000269|PubMed:38720107
uniprot
proteins
post_translational_modification
PTM: Phosphorylation at Thr-328 by isoform Beta-II of PRKCB promotes activation and lipid peroxidation, thereby inducing ferroptosis (PubMed:35027735). Phosphorylation at Thr-679 by PCK2 promotes ferroptosis (PubMed:38720107). {ECO:0000269|PubMed:35027735, ECO:0000269|PubMed:38720107}.
uniprot
proteins
protein_family
ATP-dependent AMP-binding enzyme family
uniprot
proteins
pubmed
11889465
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16959974
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
21242590
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
22633490
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24269233
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
27842070
uniprot
proteins
pubmed
29961568
uniprot
proteins
pubmed
31061331
uniprot
proteins
pubmed
35027735
uniprot
proteins
pubmed
38720107
uniprot
proteins
pubmed
9480748
uniprot
proteins
pubmed
9598324
uniprot
proteins
sequence_length
711
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000269|PubMed:38720107}; Single-pass type III membrane protein {ECO:0000305}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:24269233}; Single-pass type III membrane protein {ECO:0000305}. Cell membrane {ECO:0000269|PubMed:24269233}; Single-pass type III membrane protein {ECO:0000305}.
uniprot
proteins
transmembrane_region
TRANSMEM 8..28; /note="Helical; Signal-anchor for type III membrane protein"; /evidence="ECO:0000255
uniprot
proteins