ACSL3_MOUSE
ID ACSL3_MOUSE Reviewed; 720 AA.
AC Q9CZW4; Q8K1J7;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 162.
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:0000250|UniProtKB:O95573};
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|MGI:MGI:1921455}; Synonyms=Acs3, Facl3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary tumor;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [5]
RP INDUCTION.
RX PubMed=19737935; DOI=10.1074/jbc.m109.036665;
RA Bu S.Y., Mashek M.T., Mashek D.G.;
RT "Suppression of long chain acyl-CoA synthetase 3 (ACSL3) decreases hepatic
RT de novo fatty acid synthesis through decreased transcriptional activity.";
RL J. Biol. Chem. 284:30474-30483(2009).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Acyl-CoA synthetases (ACSL) activates long-chain fatty acids
CC for both synthesis of cellular lipids, and degradation via beta-
CC oxidation (By similarity). ACSL3 is required for the incorporation of
CC fatty acids into phosphatidylcholine, the major phospholipid located on
CC the surface of VLDL (very low density lipoproteins) (By similarity).
CC Has 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,
CC ECO:0000250|UniProtKB:O95573, ECO:0000250|UniProtKB:Q63151}.
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:0000250|UniProtKB:Q63151};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15422;
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:0000250|UniProtKB:O95573};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36140;
CC Evidence={ECO:0000250|UniProtKB:O95573};
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=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 -!- 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 -!- INDUCTION: High expression in ob/ob mice (obese) and mice fed at high
CC sucrose diet. {ECO:0000269|PubMed:19737935}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; AK012088; BAB28022.1; -; mRNA.
DR EMBL; AK161708; BAE36543.1; -; mRNA.
DR EMBL; CH466548; EDL00440.1; -; Genomic_DNA.
DR EMBL; CH466548; EDL00441.1; -; Genomic_DNA.
DR EMBL; BC031529; AAH31529.1; -; mRNA.
DR CCDS; CCDS15087.1; -.
DR RefSeq; NP_001028778.2; NM_001033606.2.
DR RefSeq; NP_001129694.1; NM_001136222.1.
DR RefSeq; NP_083093.2; NM_028817.3.
DR AlphaFoldDB; Q9CZW4; -.
DR SMR; Q9CZW4; -.
DR BioGRID; 216576; 4.
DR STRING; 10090.ENSMUSP00000045291; -.
DR iPTMnet; Q9CZW4; -.
DR PhosphoSitePlus; Q9CZW4; -.
DR SwissPalm; Q9CZW4; -.
DR CPTAC; non-CPTAC-3442; -.
DR EPD; Q9CZW4; -.
DR MaxQB; Q9CZW4; -.
DR PaxDb; Q9CZW4; -.
DR PeptideAtlas; Q9CZW4; -.
DR PRIDE; Q9CZW4; -.
DR ProteomicsDB; 285657; -.
DR Antibodypedia; 1945; 204 antibodies from 29 providers.
DR DNASU; 74205; -.
DR Ensembl; ENSMUST00000035779; ENSMUSP00000045291; ENSMUSG00000032883.
DR Ensembl; ENSMUST00000142704; ENSMUSP00000121695; ENSMUSG00000032883.
DR GeneID; 74205; -.
DR KEGG; mmu:74205; -.
DR UCSC; uc007bqo.2; mouse.
DR CTD; 2181; -.
DR MGI; MGI:1921455; Acsl3.
DR VEuPathDB; HostDB:ENSMUSG00000032883; -.
DR eggNOG; KOG1180; Eukaryota.
DR GeneTree; ENSGT00940000155954; -.
DR InParanoid; Q9CZW4; -.
DR OMA; GEGEKMP; -.
DR OrthoDB; 293865at2759; -.
DR PhylomeDB; Q9CZW4; -.
DR TreeFam; TF314012; -.
DR BRENDA; 6.2.1.3; 3474.
DR Reactome; R-MMU-434313; Intracellular metabolism of fatty acids regulates insulin secretion.
DR Reactome; R-MMU-75876; Synthesis of very long-chain fatty acyl-CoAs.
DR BioGRID-ORCS; 74205; 7 hits in 79 CRISPR screens.
DR ChiTaRS; Acsl3; mouse.
DR PRO; PR:Q9CZW4; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q9CZW4; protein.
DR Bgee; ENSMUSG00000032883; Expressed in otolith organ and 238 other tissues.
DR ExpressionAtlas; Q9CZW4; baseline and differential.
DR Genevisible; Q9CZW4; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005811; C:lipid droplet; ISO:MGI.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
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; ISS:UniProtKB.
DR GO; GO:0031956; F:medium-chain fatty acid-CoA ligase activity; IEA:RHEA.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0006633; P:fatty acid biosynthetic process; ISO:MGI.
DR GO; GO:0044539; P:long-chain fatty acid import into cell; ISO:MGI.
DR GO; GO:0001676; P:long-chain fatty acid metabolic process; ISS:UniProtKB.
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; ISO:MGI.
DR GO; GO:2001247; P:positive regulation of phosphatidylcholine biosynthetic process; ISO:MGI.
DR GO; GO:0051047; P:positive regulation of secretion; ISO:MGI.
DR GO; GO:0034379; P:very-low-density lipoprotein particle assembly; ISO:MGI.
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_0000193108"
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:0000250|UniProtKB:O95573"
FT CONFLICT 223
FT /note="D -> E (in Ref. 1; BAB28022)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 720 AA; 80492 MW; 27F9CCA6961B5BA0 CRC64;
MNNHVSSTPS TMKLKQTINP ILLYFIHFII SLYTILTYIP FYFLCESKQE KPNQIKAKPV
SSKPDSAYRS INSVDGLASV LYPGCDTLDK VFMYAKNKFK NKRLLGTREI LNEEDEIQPN
GKIFKKVILG HYNWLSYEDV FIRALDFGNG LQMLGQKPKA NIAIFCETRA EWMIAAQACF
MYNFQLVTLY ATLGGPAIVH GLNETEVTNI ITSKELLQTK LKDIVSLVPR LRHIITVDGK
PPTWSEFPKG VIVHTMAAVQ ALGVKANVEK KAHSKPLPSD IAVIMYTSGS TGIPKGVMIS
HSNIIASITG MARRIPRLGE EDVYIGYLPL AHVLELSAEL VCLSHGCRIG YSSPQTLADQ
SSKIKKGSKG DTSVLKPTLM AAVPEIMDRI YKNVMNKVNE MSAFQRNLFI LAYNYKMEQI
SKGCSTPLCD RFVFRNVRRL LGGNIRLLLC GGAPLSATTQ RFMNICFCCP VGQGYGLTES
TGAGTITEVW DYNTGRVGAP LVCCEIKLKN WEEGGYFNTD KPHPRGEILI GGQNVTMGYY
KNEAKTKTDF FEDENGQRWL CTGDIGEFDP DGCLKIIDRK KDLVKLQAGE YVSLGKVEAA
LKNLPLIDNI CAYANSYHSY VIGFVVPNQK ELTELARTKG FKGTWEELCN SSEMENEVLK
VLSEAAISAS LEKFEIPLKI RLSPDPWTPE TGLVTDAFKL KRKELKTHYQ ADIERMYGRK
