ACSL3_RAT
ID ACSL3_RAT Reviewed; 720 AA.
AC Q63151;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Fatty acid CoA ligase Acsl3 {ECO:0000305};
DE AltName: Full=Arachidonate--CoA ligase Acsl3 {ECO:0000305};
DE EC=6.2.1.15 {ECO:0000269|PubMed:28209804};
DE AltName: Full=Brain acyl-CoA synthetase II;
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:28209804};
DE AltName: Full=Medium-chain acyl-CoA ligase Acsl3 {ECO:0000305};
DE EC=6.2.1.2 {ECO:0000269|PubMed:8663269};
GN Name=Acsl3 {ECO:0000312|RGD:70552}; Synonyms=Acs3, Facl3;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=Wistar; TISSUE=Brain;
RX PubMed=8663269; DOI=10.1074/jbc.271.28.16748;
RA Fujino T., Kang M.-J., Suzuki H., Iijima H., Yamamoto T.T.;
RT "Molecular characterization and expression of rat acyl-CoA synthetase 3.";
RL J. Biol. Chem. 271:16748-16752(1996).
RN [2]
RP ALTERNATIVE INITIATION, FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=9276691; DOI=10.1093/oxfordjournals.jbchem.a021731;
RA Fujino T., Kang M.-J., Minekura H., Suzuki H., Yamamoto T.T.;
RT "Alternative translation initiation generates acyl-CoA synthetase 3
RT isoforms with heterogeneous amino termini.";
RL J. Biochem. 122:212-216(1997).
RN [3]
RP BIOPHYSICOCHEMICAL PROPERTIES, FUNCTION, AND CATALYTIC ACTIVITY.
RC TISSUE=Brain;
RX PubMed=15683247; DOI=10.1021/bi047721l;
RA Van Horn C.G., Caviglia J.M., Li L.O., Wang S., Granger D.A., Coleman R.A.;
RT "Characterization of recombinant long-chain rat acyl-CoA synthetase
RT isoforms 3 and 6: identification of a novel variant of isoform 6.";
RL Biochemistry 44:1635-1642(2005).
RN [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
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 [5]
RP CATALYTIC ACTIVITY, FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=28209804; DOI=10.1194/jlr.m072512;
RA Klett E.L., Chen S., Yechoor A., Lih F.B., Coleman R.A.;
RT "Long-chain acyl-CoA synthetase isoforms differ in preferences for
RT eicosanoid species and long-chain fatty acids.";
RL J. Lipid Res. 58:884-894(2017).
RN [6]
RP ERRATUM OF PUBMED:28209804.
RX PubMed=29196521; DOI=10.1194/jlr.m072512err;
RA Klett E.L., Chen S., Yechoor A., Lih F.B., Coleman R.A.;
RL J. Lipid Res. 58:2365-2365(2017).
CC -!- FUNCTION: Catalyzes the conversion of long-chain fatty acids to their
CC active form acyl-CoA for both synthesis of cellular lipids, and
CC degradation via beta-oxidation (PubMed:28209804, PubMed:19737935,
CC PubMed:15683247). ACSL3 is required for the incorporation of fatty
CC acids into phosphatidylcholine, the major phospholipid located on the
CC surface of VLDL (very low density lipoproteins) (By similarity). Has
CC mainly an anabolic role in energy metabolism. Mediates hepatic
CC lipogenesis (PubMed:19737935). Preferentially uses myristate, laurate,
CC arachidonate and eicosapentaenoate as substrates (PubMed:9276691,
CC PubMed:8663269). Both isoforms exhibit the same level of activity
CC (PubMed:9276691). {ECO:0000250, ECO:0000250|UniProtKB:O95573,
CC ECO:0000269|PubMed:15683247, ECO:0000269|PubMed:19737935,
CC ECO:0000269|PubMed:28209804, ECO:0000269|PubMed:8663269,
CC ECO:0000269|PubMed:9276691}.
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:15683247, ECO:0000269|PubMed:19737935,
CC ECO:0000269|PubMed:28209804, ECO:0000269|PubMed:8663269,
CC ECO:0000269|PubMed:9276691};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15422;
CC Evidence={ECO:0000269|PubMed:28209804};
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:0000269|PubMed:28209804, ECO:0000269|PubMed:8663269};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19714;
CC Evidence={ECO:0000269|PubMed:28209804};
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:0000269|PubMed:8663269};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48341;
CC Evidence={ECO:0000305|PubMed:8663269};
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:0000269|PubMed:28209804};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52117;
CC Evidence={ECO:0000269|PubMed:28209804};
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:0000269|PubMed:28209804};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52113;
CC Evidence={ECO:0000269|PubMed:28209804};
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:0000269|PubMed:28209804};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52109;
CC Evidence={ECO:0000269|PubMed:28209804};
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:0000269|PubMed:28209804};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52017;
CC Evidence={ECO:0000269|PubMed:28209804};
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:0000269|PubMed:28209804};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52013;
CC Evidence={ECO:0000269|PubMed:28209804};
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=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:0000269|PubMed:8663269,
CC ECO:0000269|PubMed:9276691};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30752;
CC Evidence={ECO:0000305|PubMed:9276691};
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:0000269|PubMed:8663269, ECO:0000269|PubMed:9276691};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33620;
CC Evidence={ECO:0000305|PubMed:9276691};
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:0000269|PubMed:8663269};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33624;
CC Evidence={ECO:0000305|PubMed:8663269};
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:0000269|PubMed:8663269};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33616;
CC Evidence={ECO:0000305|PubMed:8663269};
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:0000269|PubMed:8663269};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46209;
CC Evidence={ECO:0000305|PubMed:8663269};
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:0000269|PubMed:8663269};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33608;
CC Evidence={ECO:0000305|PubMed:8663269};
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:0000269|PubMed:8663269};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33648;
CC Evidence={ECO:0000305|PubMed:8663269};
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:0000269|PubMed:8663269};
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:0000269|PubMed:8663269};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44937;
CC Evidence={ECO:0000305|PubMed:8663269};
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:0000269|PubMed:8663269};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44933;
CC Evidence={ECO:0000305|PubMed:8663269};
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:0000269|PubMed:8663269};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67849;
CC Evidence={ECO:0000305|PubMed:8663269};
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:0000269|PubMed:8663269, ECO:0000269|PubMed:9276691};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38884;
CC Evidence={ECO:0000305|PubMed:8663269};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=402 uM for ATP {ECO:0000269|PubMed:15683247};
CC KM=3.0 uM for CoA {ECO:0000269|PubMed:15683247};
CC KM=4.3 uM for palmitate {ECO:0000269|PubMed:15683247};
CC KM=5.1 uM for oleate {ECO:0000269|PubMed:15683247};
CC KM=8.9 uM for arachidonate {ECO:0000269|PubMed:15683247};
CC KM=4 uM for palmitate (when expressed in bacteria)
CC {ECO:0000269|PubMed:28209804};
CC KM=3.1 uM for stearate (when expressed in bacteria)
CC {ECO:0000269|PubMed:28209804};
CC KM=5.3 uM for oleate (when expressed in bacteria)
CC {ECO:0000269|PubMed:28209804};
CC KM=7.3 uM for linoleate (when expressed in bacteria)
CC {ECO:0000269|PubMed:28209804};
CC KM=4.3 uM for arachidonate (when expressed in bacteria)
CC {ECO:0000269|PubMed:28209804};
CC Vmax=2306 nmol/min/mg enzyme with palmitate as substrate
CC {ECO:0000269|PubMed:15683247};
CC Vmax=2399 nmol/min/mg enzyme with oleate as substrate
CC {ECO:0000269|PubMed:15683247};
CC Vmax=4022 nmol/min/mg enzyme with arachidonate as substrate
CC {ECO:0000269|PubMed:15683247};
CC Vmax=2763 nmol/min/mg enzyme with palmitate as substrate (when
CC expressed in bacteria) {ECO:0000269|PubMed:28209804};
CC Vmax=2099 nmol/min/mg enzyme with stearate as substrate (when
CC expressed in bacteria) {ECO:0000269|PubMed:28209804};
CC Vmax=2109 nmol/min/mg enzyme with oleate as substrate (when expressed
CC in bacteria) {ECO:0000269|PubMed:28209804};
CC Vmax=1394 nmol/min/mg enzyme with linoleate as substrate (when
CC expressed in bacteria) {ECO:0000269|PubMed:28209804};
CC Vmax=2627 nmol/min/mg enzyme with arachidonate as substrate (when
CC expressed in bacteria) {ECO:0000269|PubMed:28209804};
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=Long;
CC IsoId=Q63151-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=Q63151-2; Sequence=VSP_018649;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in the brain, and to a much
CC lesser extent, in lung, adrenal gland, kidney, small intestine, and
CC adipose tissue but not detected in heart or liver.
CC -!- DEVELOPMENTAL STAGE: Detected 5 days after birth, increased to a
CC maximal level at 15 days, and then decreased gradually to 10% of its
CC maximum level in adult.
CC -!- MISCELLANEOUS: 5 rat isozymes encoded by different genes have been
CC described. ACSL6 corresponds to isozyme 2 (ACS2).
CC {ECO:0000303|PubMed:15683247}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; D30666; BAA06340.1; -; mRNA.
DR RefSeq; NP_476448.1; NM_057107.1. [Q63151-1]
DR AlphaFoldDB; Q63151; -.
DR SMR; Q63151; -.
DR IntAct; Q63151; 1.
DR STRING; 10116.ENSRNOP00000020161; -.
DR SwissLipids; SLP:000001684; -.
DR iPTMnet; Q63151; -.
DR PhosphoSitePlus; Q63151; -.
DR jPOST; Q63151; -.
DR PaxDb; Q63151; -.
DR PRIDE; Q63151; -.
DR GeneID; 114024; -.
DR KEGG; rno:114024; -.
DR UCSC; RGD:70552; rat. [Q63151-1]
DR CTD; 2181; -.
DR RGD; 70552; Acsl3.
DR VEuPathDB; HostDB:ENSRNOG00000014718; -.
DR eggNOG; KOG1180; Eukaryota.
DR HOGENOM; CLU_000022_45_2_1; -.
DR InParanoid; Q63151; -.
DR OMA; GEGEKMP; -.
DR OrthoDB; 293865at2759; -.
DR PhylomeDB; Q63151; -.
DR TreeFam; TF314012; -.
DR BRENDA; 6.2.1.3; 5301.
DR Reactome; R-RNO-434313; Intracellular metabolism of fatty acids regulates insulin secretion.
DR Reactome; R-RNO-75876; Synthesis of very long-chain fatty acyl-CoAs.
DR PRO; PR:Q63151; -.
DR Proteomes; UP000002494; Chromosome 9.
DR Bgee; ENSRNOG00000014718; Expressed in cerebellum and 20 other tissues.
DR Genevisible; Q63151; RN.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; ISO:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005811; C:lipid droplet; ISO:RGD.
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:RGD.
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; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004467; F:long-chain fatty acid-CoA ligase activity; IDA: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:RGD.
DR GO; GO:0019901; F:protein kinase binding; ISO:RGD.
DR GO; GO:0007420; P:brain development; IEP:RGD.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IDA:RGD.
DR GO; GO:0044539; P:long-chain fatty acid import into cell; ISO:RGD.
DR GO; GO:0001676; P:long-chain fatty acid metabolic process; IDA: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:RGD.
DR GO; GO:2001247; P:positive regulation of phosphatidylcholine biosynthetic process; ISO:RGD.
DR GO; GO:0051047; P:positive regulation of secretion; ISO:RGD.
DR GO; GO:0007584; P:response to nutrient; IEP:RGD.
DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR GO; GO:0034379; P:very-low-density lipoprotein particle assembly; ISO:RGD.
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 Alternative initiation; ATP-binding; Endoplasmic reticulum;
KW Fatty acid metabolism; Ligase; Lipid metabolism; Magnesium; Membrane;
KW Microsome; Mitochondrion; Mitochondrion outer membrane; Nucleotide-binding;
KW Peroxisome; Phosphoprotein; Reference proteome; Signal-anchor;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..720
FT /note="Fatty acid CoA ligase Acsl3"
FT /id="PRO_0000001313"
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 VAR_SEQ 1..11
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000305"
FT /id="VSP_018649"
SQ SEQUENCE 720 AA; 80458 MW; 4D79FAEF25ADA527 CRC64;
MNNHVSSTPS TMKLKQTIHP ILLYFIHFII SLYTILTYIP FYFLCESKQE KPNHIKAKPV
SSKPDSAYRS VNSMDGLASV LYPGCDTLDK VFMYAKNKFK DKRLLGTREI LNEEDEIQPN
GKVFKKVILG HYNWLSYEDV FIRALDFGNG LQMLGQKPKA NIAIFCETRA EWMIAAQACF
MYNFQLVTLY ATLGGPAIVH GLNETEVTNI ITSKELLQTK LKDIVSLVPR LRHIITVDGK
PPTWSEFPKG VIVHTMAAVQ ALGVKADVDK KAHSKPLPSD IAVIMYTSGS TGIPKGVMIS
HSNIIASITG MARRIPRLGE EDVYIGYLPL AHVLELSAEL VCLSHGCRIG YSSPQTLADQ
SSKIKKGSKG DTSVLKPTLM AAVPEIMDRI YKNVMNKVNE MSAFQRNLFI LAYNYKMEQI
SKGCSTPLCD RFVFRNVRRL LGGNIRVLLC GGAPLSATTQ RFMNICFCCP VGQGYGLTES
TGAGTITEVW DYNTGRVGAP LVCCEIKLKN WEEGGYFNTD KPHPRGEILI GGQNVTMGYY
KNEAKTKADF FEDENGQRWL CTGDIGEFDP DGCLKIIDRK KDLVKLQAGE YVSLGKVEAA
LKNLPLIDNI CAYANSYHSY VIGFVVPNQK ELTELARTKG FNGTWEELCN SSEMENEVLK
VLSEAAISAS LEKFEIPLKI RLSPDPWTPE TGLVTDAFKL KRKELKTHYQ ADIERMYGRK
