ACSL3_HUMAN
ID ACSL3_HUMAN Reviewed; 720 AA.
AC O95573; Q60I92; Q8IUM9;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 3.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Fatty acid CoA ligase Acsl3 {ECO:0000305};
DE AltName: Full=Arachidonate--CoA ligase {ECO:0000250|UniProtKB:Q63151};
DE EC=6.2.1.15 {ECO:0000250|UniProtKB:Q63151};
DE AltName: Full=Long-chain acyl-CoA synthetase 3;
DE Short=LACS 3;
DE AltName: Full=Long-chain-fatty-acid--CoA ligase 3 {ECO:0000305};
DE EC=6.2.1.3 {ECO:0000269|PubMed:22633490};
DE AltName: Full=Medium-chain acyl-CoA ligase Acsl3 {ECO:0000250|UniProtKB:Q63151};
DE EC=6.2.1.2 {ECO:0000250|UniProtKB:Q63151};
GN Name=ACSL3 {ECO:0000312|HGNC:HGNC:3570}; Synonyms=ACS3, FACL3, LACS3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT SER-551.
RC TISSUE=Placenta;
RX PubMed=9177793; DOI=10.1006/geno.1997.4710;
RA Minekura H., Fujino T., Kang M.-J., Fujita T., Endo Y., Yamamoto T.T.;
RT "Human acyl-coenzyme A synthetase 3 cDNA and localization of its gene
RT (ACS3) to chromosome band 2q34-q35.";
RL Genomics 42:180-181(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND VARIANT SER-551.
RX PubMed=11707336; DOI=10.1016/s0378-1119(01)00714-4;
RA Minekura H., Kang M.-J., Inagaki Y., Suzuki H., Sato H., Fujino T.,
RA Yamamoto T.T.;
RT "Genomic organization and transcription units of the human acyl-CoA
RT synthetase 3 gene.";
RL Gene 278:185-192(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pancreas;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP FUNCTION.
RX PubMed=18003621; DOI=10.1074/jbc.m706160200;
RA Yao H., Ye J.;
RT "Long chain acyl-CoA synthetase 3-mediated phosphatidylcholine synthesis is
RT required for assembly of very low density lipoproteins in human hepatoma
RT Huh7 cells.";
RL J. Biol. Chem. 283:849-854(2008).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-683, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [7]
RP CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=22633490; DOI=10.1016/j.molcel.2012.04.033;
RA Nakahara K., Ohkuni A., Kitamura T., Abe K., Naganuma T., Ohno Y.,
RA Zoeller R.A., Kihara A.;
RT "The Sjogren-Larsson syndrome gene encodes a hexadecenal dehydrogenase of
RT the sphingosine 1-phosphate degradation pathway.";
RL Mol. Cell 46:461-471(2012).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-683, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: Acyl-CoA synthetases (ACSL) activates long-chain fatty acids
CC for both synthesis of cellular lipids, and degradation via beta-
CC oxidation (PubMed:22633490). Required for the incorporation of fatty
CC acids into phosphatidylcholine, the major phospholipid located on the
CC surface of VLDL (very low density lipoproteins) (PubMed:18003621). Has
CC mainly an anabolic role in energy metabolism. Mediates hepatic
CC lipogenesis. Preferentially uses myristate, laurate, arachidonate and
CC eicosapentaenoate as substrates. Both isoforms exhibit the same level
CC of activity (By similarity). {ECO:0000250|UniProtKB:Q63151,
CC ECO:0000269|PubMed:18003621, ECO:0000269|PubMed:22633490}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a long-chain fatty acid + ATP + CoA = a long-chain fatty acyl-
CC CoA + AMP + diphosphate; Xref=Rhea:RHEA:15421, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57560,
CC ChEBI:CHEBI:83139, ChEBI:CHEBI:456215; EC=6.2.1.3;
CC Evidence={ECO:0000269|PubMed:22633490};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15422;
CC Evidence={ECO:0000305|PubMed:22633490};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + ATP + CoA =
CC (5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + AMP + diphosphate;
CC Xref=Rhea:RHEA:19713, ChEBI:CHEBI:30616, ChEBI:CHEBI:32395,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57368,
CC ChEBI:CHEBI:456215; EC=6.2.1.15;
CC Evidence={ECO:0000250|UniProtKB:Q63151};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19714;
CC Evidence={ECO:0000250|UniProtKB:Q63151};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-hexadec-2-enoate + ATP + CoA = (2E)-hexadecenoyl-CoA + AMP
CC + diphosphate; Xref=Rhea:RHEA:36139, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:61526,
CC ChEBI:CHEBI:72745, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000269|PubMed:22633490};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36140;
CC Evidence={ECO:0000305|PubMed:22633490};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=15-hydroxy-(5Z,8Z,11Z,13E)-eicosatetraenoate + ATP + CoA = 15-
CC hydroxy-(5Z,8Z,11Z,13E)-eicosatetraenoyl-CoA + AMP + diphosphate;
CC Xref=Rhea:RHEA:52116, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:78832, ChEBI:CHEBI:136409,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:Q63151};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52117;
CC Evidence={ECO:0000250|UniProtKB:Q63151};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=12-hydroxy-(5Z,8Z,10E,14Z)-eicosatetraenoate + ATP + CoA = 12-
CC hydroxy-(5Z,8Z,10E,14Z)-eicosatetraenoyl-CoA + AMP + diphosphate;
CC Xref=Rhea:RHEA:52112, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:90718, ChEBI:CHEBI:136408,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:Q63151};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52113;
CC Evidence={ECO:0000250|UniProtKB:Q63151};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-hydroxy-(6E,8Z,11Z,14Z)-eicosatetraenoate + ATP + CoA = 5-
CC hydroxy-(6E,8Z,11Z,14Z)-eicosatetraenoyl-CoA + AMP + diphosphate;
CC Xref=Rhea:RHEA:52108, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:65341, ChEBI:CHEBI:136407,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:Q63151};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52109;
CC Evidence={ECO:0000250|UniProtKB:Q63151};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=14,15-epoxy-(5Z,8Z,11Z)-eicosatrienoate + ATP + CoA = 14,15-
CC epoxy-(5Z,8Z,11Z)-eicosatrienoyl-CoA + AMP + diphosphate;
CC Xref=Rhea:RHEA:52016, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:84024, ChEBI:CHEBI:136117,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:Q63151};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52017;
CC Evidence={ECO:0000250|UniProtKB:Q63151};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=11,12-epoxy-(5Z,8Z,14Z)-eicosatrienoate + ATP + CoA = 11,12-
CC epoxy-(5Z,8Z,14Z)-eicosatrienoyl-CoA + AMP + diphosphate;
CC Xref=Rhea:RHEA:52012, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:76625, ChEBI:CHEBI:136115,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:Q63151};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52013;
CC Evidence={ECO:0000250|UniProtKB:Q63151};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a medium chain fatty acid + ATP + CoA = a medium-chain fatty
CC acyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:48340,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:59558, ChEBI:CHEBI:90546, ChEBI:CHEBI:456215; EC=6.2.1.2;
CC Evidence={ECO:0000250|UniProtKB:Q63151};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48341;
CC Evidence={ECO:0000250|UniProtKB:Q63151};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + hexadecanoate = AMP + diphosphate + hexadecanoyl-
CC CoA; Xref=Rhea:RHEA:30751, ChEBI:CHEBI:7896, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:Q63151};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30752;
CC Evidence={ECO:0000250|UniProtKB:Q63151};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + tetradecanoate = AMP + diphosphate +
CC tetradecanoyl-CoA; Xref=Rhea:RHEA:33619, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:30807, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57385, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000250|UniProtKB:Q63151};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33620;
CC Evidence={ECO:0000250|UniProtKB:Q63151};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + dodecanoate = AMP + diphosphate + dodecanoyl-CoA;
CC Xref=Rhea:RHEA:33623, ChEBI:CHEBI:18262, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57375,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:Q63151};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33624;
CC Evidence={ECO:0000250|UniProtKB:Q63151};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + octadecanoate = AMP + diphosphate + octadecanoyl-
CC CoA; Xref=Rhea:RHEA:33615, ChEBI:CHEBI:25629, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57394,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:Q63151};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33616;
CC Evidence={ECO:0000250|UniProtKB:Q63151};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + eicosanoate = AMP + diphosphate + eicosanoyl-CoA;
CC Xref=Rhea:RHEA:46208, ChEBI:CHEBI:30616, ChEBI:CHEBI:32360,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57380,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:Q63151};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46209;
CC Evidence={ECO:0000250|UniProtKB:Q63151};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoate + ATP + CoA = (9Z)-octadecenoyl-CoA + AMP +
CC diphosphate; Xref=Rhea:RHEA:33607, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57387, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000250|UniProtKB:Q63151};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33608;
CC Evidence={ECO:0000250|UniProtKB:Q63151};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-hexadecenoate + ATP + CoA = (9Z)-hexadecenoyl-CoA + AMP +
CC diphosphate; Xref=Rhea:RHEA:33647, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:32372, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:61540, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000250|UniProtKB:Q63151};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33648;
CC Evidence={ECO:0000250|UniProtKB:Q63151};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoate + ATP + CoA = (9Z,12Z)-
CC octadecadienoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:33651,
CC ChEBI:CHEBI:30245, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57383, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000250|UniProtKB:Q63151};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z,15Z)-octadecatrienoate + ATP + CoA = (9Z,12Z,15Z)-
CC octadecatrienoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:44936,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:32387, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:74034, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000250|UniProtKB:Q63151};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44937;
CC Evidence={ECO:0000250|UniProtKB:Q63151};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + ATP + CoA =
CC (4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoyl-CoA + AMP + diphosphate;
CC Xref=Rhea:RHEA:44932, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:74298, ChEBI:CHEBI:77016,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:Q63151};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44933;
CC Evidence={ECO:0000250|UniProtKB:Q63151};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + ATP + CoA =
CC (5Z,8Z,11Z,14Z,17Z)-eicosapentaenoyl-CoA + AMP + diphosphate;
CC Xref=Rhea:RHEA:67848, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:58562, ChEBI:CHEBI:73862,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:Q63151};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67849;
CC Evidence={ECO:0000250|UniProtKB:Q63151};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a fatty acid + ATP + CoA = a fatty acyl-CoA + AMP +
CC diphosphate; Xref=Rhea:RHEA:38883, ChEBI:CHEBI:28868,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:77636, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000250|UniProtKB:Q63151};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38884;
CC Evidence={ECO:0000250|UniProtKB:Q63151};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- INTERACTION:
CC O95573; P56962: STX17; NbExp=5; IntAct=EBI-1190822, EBI-2797775;
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250};
CC Single-pass type III membrane protein {ECO:0000250}. Peroxisome
CC membrane {ECO:0000250}; Single-pass type III membrane protein
CC {ECO:0000250}. Microsome membrane {ECO:0000250}; Single-pass type III
CC membrane protein {ECO:0000250}. Endoplasmic reticulum membrane
CC {ECO:0000250}; Single-pass type III membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; D89053; BAA37142.1; -; mRNA.
DR EMBL; AB061712; BAB72074.1; -; mRNA.
DR EMBL; AB061436; BAB72139.1; -; Genomic_DNA.
DR EMBL; BC041692; AAH41692.1; -; mRNA.
DR CCDS; CCDS2455.1; -.
DR RefSeq; NP_004448.2; NM_004457.3.
DR RefSeq; NP_976251.1; NM_203372.1.
DR RefSeq; XP_016859073.1; XM_017003584.1.
DR AlphaFoldDB; O95573; -.
DR SMR; O95573; -.
DR BioGRID; 108477; 225.
DR IntAct; O95573; 71.
DR MINT; O95573; -.
DR STRING; 9606.ENSP00000350012; -.
DR BindingDB; O95573; -.
DR ChEMBL; CHEMBL4680023; -.
DR SwissLipids; SLP:000000200; -.
DR GlyGen; O95573; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O95573; -.
DR MetOSite; O95573; -.
DR PhosphoSitePlus; O95573; -.
DR SwissPalm; O95573; -.
DR BioMuta; ACSL3; -.
DR EPD; O95573; -.
DR jPOST; O95573; -.
DR MassIVE; O95573; -.
DR MaxQB; O95573; -.
DR PaxDb; O95573; -.
DR PeptideAtlas; O95573; -.
DR PRIDE; O95573; -.
DR ProteomicsDB; 50946; -.
DR Antibodypedia; 1945; 204 antibodies from 29 providers.
DR DNASU; 2181; -.
DR Ensembl; ENST00000357430.8; ENSP00000350012.3; ENSG00000123983.15.
DR Ensembl; ENST00000392066.7; ENSP00000375918.3; ENSG00000123983.15.
DR Ensembl; ENST00000679514.1; ENSP00000506361.1; ENSG00000123983.15.
DR Ensembl; ENST00000679558.1; ENSP00000504907.1; ENSG00000123983.15.
DR Ensembl; ENST00000680147.1; ENSP00000504861.1; ENSG00000123983.15.
DR Ensembl; ENST00000680251.1; ENSP00000505400.1; ENSG00000123983.15.
DR Ensembl; ENST00000680395.1; ENSP00000505793.1; ENSG00000123983.15.
DR Ensembl; ENST00000680684.1; ENSP00000506468.1; ENSG00000123983.15.
DR Ensembl; ENST00000680921.1; ENSP00000505940.1; ENSG00000123983.15.
DR Ensembl; ENST00000681383.1; ENSP00000505654.1; ENSG00000123983.15.
DR Ensembl; ENST00000681697.1; ENSP00000505856.1; ENSG00000123983.15.
DR GeneID; 2181; -.
DR KEGG; hsa:2181; -.
DR MANE-Select; ENST00000357430.8; ENSP00000350012.3; NM_004457.5; NP_004448.2.
DR UCSC; uc002vni.4; human.
DR CTD; 2181; -.
DR DisGeNET; 2181; -.
DR GeneCards; ACSL3; -.
DR HGNC; HGNC:3570; ACSL3.
DR HPA; ENSG00000123983; Tissue enhanced (parathyroid).
DR MIM; 602371; gene.
DR neXtProt; NX_O95573; -.
DR OpenTargets; ENSG00000123983; -.
DR PharmGKB; PA27967; -.
DR VEuPathDB; HostDB:ENSG00000123983; -.
DR eggNOG; KOG1180; Eukaryota.
DR GeneTree; ENSGT00940000155954; -.
DR HOGENOM; CLU_000022_45_2_1; -.
DR InParanoid; O95573; -.
DR OMA; GEGEKMP; -.
DR PhylomeDB; O95573; -.
DR TreeFam; TF314012; -.
DR BioCyc; MetaCyc:HS04703-MON; -.
DR BRENDA; 6.2.1.3; 2681.
DR PathwayCommons; O95573; -.
DR Reactome; R-HSA-434313; Intracellular metabolism of fatty acids regulates insulin secretion.
DR Reactome; R-HSA-75876; Synthesis of very long-chain fatty acyl-CoAs.
DR SignaLink; O95573; -.
DR BioGRID-ORCS; 2181; 208 hits in 1095 CRISPR screens.
DR ChiTaRS; ACSL3; human.
DR GeneWiki; ACSL3; -.
DR GenomeRNAi; 2181; -.
DR Pharos; O95573; Tbio.
DR PRO; PR:O95573; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; O95573; protein.
DR Bgee; ENSG00000123983; Expressed in endothelial cell and 205 other tissues.
DR ExpressionAtlas; O95573; baseline and differential.
DR Genevisible; O95573; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005811; C:lipid droplet; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005741; C:mitochondrial outer membrane; TAS:Reactome.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0005778; C:peroxisomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0047676; F:arachidonate-CoA ligase activity; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004467; F:long-chain fatty acid-CoA ligase activity; IMP:UniProtKB.
DR GO; GO:0031956; F:medium-chain fatty acid-CoA ligase activity; IEA:RHEA.
DR GO; GO:0090433; F:palmitoyl-CoA ligase activity; TAS:Reactome.
DR GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0006631; P:fatty acid metabolic process; TAS:Reactome.
DR GO; GO:0044539; P:long-chain fatty acid import into cell; IDA:UniProtKB.
DR GO; GO:0001676; P:long-chain fatty acid metabolic process; IMP:UniProtKB.
DR GO; GO:0035338; P:long-chain fatty-acyl-CoA biosynthetic process; TAS:Reactome.
DR GO; GO:0035336; P:long-chain fatty-acyl-CoA metabolic process; IBA:GO_Central.
DR GO; GO:0030182; P:neuron differentiation; IBA:GO_Central.
DR GO; GO:0042998; P:positive regulation of Golgi to plasma membrane protein transport; IMP:UniProtKB.
DR GO; GO:2001247; P:positive regulation of phosphatidylcholine biosynthetic process; IMP:UniProtKB.
DR GO; GO:0051047; P:positive regulation of secretion; IMP:UniProtKB.
DR GO; GO:0034379; P:very-low-density lipoprotein particle assembly; IMP:UniProtKB.
DR Gene3D; 3.40.50.12780; -; 1.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR InterPro; IPR042099; ANL_N_sf.
DR Pfam; PF00501; AMP-binding; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Endoplasmic reticulum; Fatty acid metabolism; Ligase;
KW Lipid metabolism; Magnesium; Membrane; Microsome; Mitochondrion;
KW Mitochondrion outer membrane; Nucleotide-binding; Peroxisome;
KW Phosphoprotein; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..720
FT /note="Fatty acid CoA ligase Acsl3"
FT /id="PRO_0000193107"
FT TRANSMEM 21..41
FT /note="Helical; Signal-anchor for type III membrane
FT protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 42..720
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 683
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:23186163"
FT VARIANT 551
FT /note="F -> S (in dbSNP:rs1046032)"
FT /evidence="ECO:0000269|PubMed:11707336,
FT ECO:0000269|PubMed:9177793"
FT /id="VAR_026716"
FT CONFLICT 246
FT /note="E -> D (in Ref. 1; BAA37142 and 2; BAB72074/
FT BAB72139)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 720 AA; 80420 MW; AAC4B0B4543EC8DD CRC64;
MNNHVSSKPS TMKLKHTINP ILLYFIHFLI SLYTILTYIP FYFFSESRQE KSNRIKAKPV
NSKPDSAYRS VNSLDGLASV LYPGCDTLDK VFTYAKNKFK NKRLLGTREV LNEEDEVQPN
GKIFKKVILG QYNWLSYEDV FVRAFNFGNG LQMLGQKPKT NIAIFCETRA EWMIAAQACF
MYNFQLVTLY ATLGGPAIVH ALNETEVTNI ITSKELLQTK LKDIVSLVPR LRHIITVDGK
PPTWSEFPKG IIVHTMAAVE ALGAKASMEN QPHSKPLPSD IAVIMYTSGS TGLPKGVMIS
HSNIIAGITG MAERIPELGE EDVYIGYLPL AHVLELSAEL VCLSHGCRIG YSSPQTLADQ
SSKIKKGSKG DTSMLKPTLM AAVPEIMDRI YKNVMNKVSE MSSFQRNLFI LAYNYKMEQI
SKGRNTPLCD SFVFRKVRSL LGGNIRLLLC GGAPLSATTQ RFMNICFCCP VGQGYGLTES
AGAGTISEVW DYNTGRVGAP LVCCEIKLKN WEEGGYFNTD KPHPRGEILI GGQSVTMGYY
KNEAKTKADF FEDENGQRWL CTGDIGEFEP DGCLKIIDRK KDLVKLQAGE YVSLGKVEAA
LKNLPLVDNI CAYANSYHSY VIGFVVPNQK ELTELARKKG LKGTWEELCN SCEMENEVLK
VLSEAAISAS LEKFEIPVKI RLSPEPWTPE TGLVTDAFKL KRKELKTHYQ ADIERMYGRK
