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Long-chain-fatty-acid--CoA ligase 1 (EC 6.2.1.3) (Arachidonate--CoA ligase) (EC 6.2.1.15) (Long-chain acyl-CoA synthetase 1) (LACS 1) (Long-chain-fatty-acid--CoA ligase, liver isozyme) (Phytanate--CoA ligase) (EC 6.2.1.24)

 ACSL1_RAT               Reviewed;         699 AA.
P18163;
01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
01-NOV-1990, sequence version 1.
18-SEP-2019, entry version 158.
RecName: Full=Long-chain-fatty-acid--CoA ligase 1 {ECO:0000305};
EC=6.2.1.3 {ECO:0000269|PubMed:28209804};
AltName: Full=Arachidonate--CoA ligase;
EC=6.2.1.15 {ECO:0000269|PubMed:28209804};
AltName: Full=Long-chain acyl-CoA synthetase 1;
Short=LACS 1;
AltName: Full=Long-chain-fatty-acid--CoA ligase, liver isozyme;
AltName: Full=Phytanate--CoA ligase;
EC=6.2.1.24 {ECO:0000269|PubMed:10198260, ECO:0000269|PubMed:8978480};
Name=Acsl1 {ECO:0000312|RGD:2015}; Synonyms=Acs1, Acsl2, Facl2;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
STRAIN=Wistar; TISSUE=Liver;
PubMed=2341402;
Suzuki H., Kawarabayasi Y., Kondo J., Abe T., Nishikawa K., Kimura S.,
Hashimoto T., Yamamoto T.;
"Structure and regulation of rat long-chain acyl-CoA synthetase.";
J. Biol. Chem. 265:8681-8685(1990).
[2]
PROTEIN SEQUENCE OF 1-19; 82-91 AND 628-641, ACETYLATION AT MET-1 AND
LYS-633, NITRATION AT TYR-9 AND TYR-86, PHOSPHORYLATION AT TYR-85, AND
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Liver;
PubMed=17478130; DOI=10.1016/j.bbapap.2007.03.012;
Distler A.M., Kerner J., Hoppel C.L.;
"Post-translational modifications of rat liver mitochondrial outer
membrane proteins identified by mass spectrometry.";
Biochim. Biophys. Acta 1774:628-636(2007).
[3]
CHARACTERIZATION.
PubMed=8973631; DOI=10.1111/j.1432-1033.1996.0186r.x;
Iijima H., Fujino T., Minekura H., Suzuki H., Kang M.-J.,
Yamamoto T.T.;
"Biochemical studies of two rat acyl-CoA synthetases, ACS1 and ACS2.";
Eur. J. Biochem. 242:186-190(1996).
[4]
CATALYTIC ACTIVITY, FUNCTION, AND ACTIVITY REGULATION.
PubMed=8978480;
Watkins P.A., Howard A.E., Gould S.J., Avigan J., Mihalik S.J.;
"Phytanic acid activation in rat liver peroxisomes is catalyzed by
long-chain acyl-CoA synthetase.";
J. Lipid Res. 37:2288-2295(1996).
[5]
CATALYTIC ACTIVITY, AND FUNCTION.
PubMed=10198260; DOI=10.1006/bbrc.1999.0510;
Steinberg S.J., Wang S.J., Kim D.G., Mihalik S.J., Watkins P.A.;
"Human very-long-chain acyl-CoA synthetase: cloning, topography, and
relevance to branched-chain fatty acid metabolism.";
Biochem. Biophys. Res. Commun. 257:615-621(1999).
[6]
CATALYTIC ACTIVITY, AND FUNCTION.
PubMed=10749848; DOI=10.1074/jbc.c000015200;
Steinberg S.J., Mihalik S.J., Kim D.G., Cuebas D.A., Watkins P.A.;
"The human liver-specific homolog of very long-chain acyl-CoA
synthetase is cholate:CoA ligase.";
J. Biol. Chem. 275:15605-15608(2000).
[7]
BIOPHYSICOCHEMICAL PROPERTIES.
TISSUE=Brain;
PubMed=15683247; DOI=10.1021/bi047721l;
Van Horn C.G., Caviglia J.M., Li L.O., Wang S., Granger D.A.,
Coleman R.A.;
"Characterization of recombinant long-chain rat acyl-CoA synthetase
isoforms 3 and 6: identification of a novel variant of isoform 6.";
Biochemistry 44:1635-1642(2005).
[8]
GLYCOSYLATION AT SER-136.
PubMed=24098488; DOI=10.1371/journal.pone.0076399;
Cao W., Cao J., Huang J., Yao J., Yan G., Xu H., Yang P.;
"Discovery and confirmation of O-GlcNAcylated proteins in rat liver
mitochondria by combination of mass spectrometry and immunological
methods.";
PLoS ONE 8:E76399-E76399(2013).
[9]
CATALYTIC ACTIVITY, FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=28209804; DOI=10.1194/jlr.m072512;
Klett E.L., Chen S., Yechoor A., Lih F.B., Coleman R.A.;
"Long-chain acyl-CoA synthetase isoforms differ in preferences for
eicosanoid species and long-chain fatty acids.";
J. Lipid Res. 58:884-894(2017).
[10]
ERRATUM.
PubMed=29196521; DOI=10.1194/jlr.m072512err;
Klett E.L., Chen S., Yechoor A., Lih F.B., Coleman R.A.;
J. Lipid Res. 58:2365-2365(2017).
-!- FUNCTION: Catalyzes the conversion of long-chain fatty acids to
their active form acyl-CoAs for both synthesis of cellular lipids,
and degradation via beta-oxidation (PubMed:8978480,
PubMed:10198260, PubMed:10749848, PubMed:28209804). Preferentially
uses palmitoleate, oleate and linoleate (By similarity).
Preferentially activates arachidonate than epoxyeicosatrienoic
acids (EETs) or hydroxyeicosatrienoic acids (HETEs)
(PubMed:28209804). {ECO:0000250|UniProtKB:P33121,
ECO:0000269|PubMed:10198260, ECO:0000269|PubMed:10749848,
ECO:0000269|PubMed:28209804, ECO:0000269|PubMed:8978480}.
-!- CATALYTIC ACTIVITY:
Reaction=a long-chain fatty acid + ATP + CoA = a long-chain fatty
acyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:15421,
ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
ChEBI:CHEBI:57560, ChEBI:CHEBI:83139, ChEBI:CHEBI:456215;
EC=6.2.1.3; Evidence={ECO:0000269|PubMed:28209804};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15422;
Evidence={ECO:0000269|PubMed:28209804};
-!- CATALYTIC ACTIVITY:
Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + ATP + CoA =
(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + AMP + diphosphate;
Xref=Rhea:RHEA:19713, ChEBI:CHEBI:30616, ChEBI:CHEBI:32395,
ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57368,
ChEBI:CHEBI:456215; EC=6.2.1.15;
Evidence={ECO:0000269|PubMed:28209804};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19714;
Evidence={ECO:0000269|PubMed:28209804};
-!- CATALYTIC ACTIVITY:
Reaction=3,7,11,15-tetramethylhexadecanoate + ATP + CoA = AMP +
diphosphate + phytanoyl-CoA; Xref=Rhea:RHEA:21380,
ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:37257,
ChEBI:CHEBI:57287, ChEBI:CHEBI:57391, ChEBI:CHEBI:456215;
EC=6.2.1.24; Evidence={ECO:0000269|PubMed:10198260,
ECO:0000269|PubMed:8978480};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21381;
Evidence={ECO:0000305|PubMed:10198260,
ECO:0000305|PubMed:8978480};
-!- CATALYTIC ACTIVITY:
Reaction=ATP + CoA + hexadecanoate = AMP + diphosphate +
hexadecanoyl-CoA; Xref=Rhea:RHEA:30751, ChEBI:CHEBI:7896,
ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
ChEBI:CHEBI:57379, ChEBI:CHEBI:456215;
Evidence={ECO:0000269|PubMed:10749848,
ECO:0000269|PubMed:8978480};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30752;
Evidence={ECO:0000305|PubMed:10749848,
ECO:0000305|PubMed:8978480};
-!- CATALYTIC ACTIVITY:
Reaction=(E)-hexadec-2-enoate + ATP + CoA = (2E)-hexadecenoyl-CoA
+ AMP + diphosphate; Xref=Rhea:RHEA:36139, ChEBI:CHEBI:30616,
ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:61526,
ChEBI:CHEBI:72745, ChEBI:CHEBI:456215;
Evidence={ECO:0000250|UniProtKB:P33121};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36140;
Evidence={ECO:0000250|UniProtKB:P33121};
-!- CATALYTIC ACTIVITY:
Reaction=2,6,10,14-tetramethylpentadecanoate + ATP + CoA = AMP +
diphosphate + pristanoyl-CoA; Xref=Rhea:RHEA:47264,
ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
ChEBI:CHEBI:77250, ChEBI:CHEBI:77268, ChEBI:CHEBI:456215;
Evidence={ECO:0000269|PubMed:10198260};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47265;
Evidence={ECO:0000305|PubMed:10198260};
-!- CATALYTIC ACTIVITY:
Reaction=14,15-epoxy-(5Z,8Z,11Z)-eicosatrienoate + ATP + CoA =
14,15-epoxy-(5Z,8Z,11Z)-eicosatrienoyl-CoA + AMP + diphosphate;
Xref=Rhea:RHEA:52016, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
ChEBI:CHEBI:57287, ChEBI:CHEBI:84024, ChEBI:CHEBI:136117,
ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:28209804};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52017;
Evidence={ECO:0000269|PubMed:28209804};
-!- CATALYTIC ACTIVITY:
Reaction=5-hydroxy-(6E,8Z,11Z,14Z)-eicosatetraenoate + ATP + CoA =
5-hydroxy-(6E,8Z,11Z,14Z)-eicosatetraenoyl-CoA + AMP +
diphosphate; Xref=Rhea:RHEA:52108, ChEBI:CHEBI:30616,
ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:65341,
ChEBI:CHEBI:136407, ChEBI:CHEBI:456215;
Evidence={ECO:0000269|PubMed:28209804};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52109;
Evidence={ECO:0000269|PubMed:28209804};
-!- CATALYTIC ACTIVITY:
Reaction=12-hydroxy-(5Z,8Z,10E,14Z)-eicosatetraenoate + ATP + CoA
= 12-hydroxy-(5Z,8Z,10E,14Z)-eicosatetraenoyl-CoA + AMP +
diphosphate; Xref=Rhea:RHEA:52112, ChEBI:CHEBI:30616,
ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:90718,
ChEBI:CHEBI:136408, ChEBI:CHEBI:456215;
Evidence={ECO:0000269|PubMed:28209804};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52113;
Evidence={ECO:0000269|PubMed:28209804};
-!- CATALYTIC ACTIVITY:
Reaction=15-hydroxy-(5Z,8Z,11Z,13E)-eicosatetraenoate + ATP + CoA
= 15-hydroxy-(5Z,8Z,11Z,13E)-eicosatetraenoyl-CoA + AMP +
diphosphate; Xref=Rhea:RHEA:52116, ChEBI:CHEBI:30616,
ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:78832,
ChEBI:CHEBI:136409, ChEBI:CHEBI:456215;
Evidence={ECO:0000269|PubMed:28209804};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52117;
Evidence={ECO:0000269|PubMed:28209804};
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
-!- ACTIVITY REGULATION: Inhibited at high temperature and by
arachidonate. {ECO:0000269|PubMed:8978480}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=649 uM for ATP {ECO:0000269|PubMed:15683247};
KM=6.4 uM for CoA {ECO:0000269|PubMed:15683247};
KM=5.0 uM for palmitate {ECO:0000269|PubMed:15683247};
KM=2.7 uM for palmitate (when expressed in bacteria)
{ECO:0000269|PubMed:28209804};
KM=6.6 uM for stearate (when expressed in bacteria)
{ECO:0000269|PubMed:28209804};
KM=6.7 uM for oleate (when expressed in bacteria)
{ECO:0000269|PubMed:28209804};
KM=5 uM for linoleate (when expressed in bacteria)
{ECO:0000269|PubMed:28209804};
KM=6.3 uM for arachidonate (when expressed in bacteria)
{ECO:0000269|PubMed:28209804};
KM=2.1 uM for palmitate (when expressed in mammalian cell)
{ECO:0000269|PubMed:28209804};
KM=11.5 uM for stearate (when expressed in mammalian cell)
{ECO:0000269|PubMed:28209804};
KM=14.7 uM for oleate (when expressed in mammalian cell)
{ECO:0000269|PubMed:28209804};
KM=7 uM for linoleate (when expressed in mammalian cell)
{ECO:0000269|PubMed:28209804};
KM=7.3 uM for arachidonate (when expressed in mammalian cell)
{ECO:0000269|PubMed:28209804};
Vmax=1695 nmol/min/mg enzyme with palmitate as substrate
{ECO:0000269|PubMed:15683247};
Vmax=3068 nmol/min/mg enzyme with palmitate as substrate (when
expressed in mammalian cell) {ECO:0000269|PubMed:28209804};
Vmax=2342 nmol/min/mg enzyme with stearate as substrate (when
expressed in mammalian cell) {ECO:0000269|PubMed:28209804};
Vmax=2607 nmol/min/mg enzyme with oleate as substrate (when
expressed in mammalian cell) {ECO:0000269|PubMed:28209804};
Vmax=2525 nmol/min/mg enzyme with linoleate as substrate (when
expressed in mammalian cell) {ECO:0000269|PubMed:28209804};
Vmax=1745 nmol/min/mg enzyme with arachidonate as substrate
(when expressed in mammalian cell)
{ECO:0000269|PubMed:28209804};
Vmax=3754 nmol/min/mg enzyme with palmitate as substrate (when
expressed in bacteria) {ECO:0000269|PubMed:28209804};
Vmax=2874 nmol/min/mg enzyme with stearate as substrate (when
expressed in bacteria) {ECO:0000269|PubMed:28209804};
Vmax=2089 nmol/min/mg enzyme with oleate as substrate (when
expressed in bacteria) {ECO:0000269|PubMed:28209804};
Vmax=1635 nmol/min/mg enzyme with linoleate as substrate (when
expressed in bacteria) {ECO:0000269|PubMed:28209804};
Vmax=3363 nmol/min/mg enzyme with arachidonate as substrate
(when expressed in bacteria) {ECO:0000269|PubMed:28209804};
-!- SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250};
Single-pass type III membrane protein {ECO:0000250}. Peroxisome
membrane {ECO:0000250}; Single-pass type III membrane protein
{ECO:0000250}. Microsome membrane {ECO:0000250}; Single-pass type
III membrane protein {ECO:0000250}. Endoplasmic reticulum membrane
{ECO:0000250|UniProtKB:P33121}; Single-pass type III membrane
protein {ECO:0000250}.
-!- TISSUE SPECIFICITY: Liver, heart, epididymal adipose and to a
lesser extent brain, small intestine and lung.
-!- DEVELOPMENTAL STAGE: Levels remain constant during development.
-!- INDUCTION: By high fat and high carbohydrate diets.
-!- MISCELLANEOUS: 5 rat isozymes encoded by different genes have been
described. ACSL6 corresponds to isozyme 2 (ACS2).
{ECO:0000303|PubMed:15683247}.
-!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme
family. {ECO:0000305}.
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EMBL; D90109; BAA14136.1; -; mRNA.
PIR; A36275; A36275.
RefSeq; NP_036952.1; NM_012820.1.
RefSeq; XP_006253184.1; XM_006253122.1.
RefSeq; XP_006253185.1; XM_006253123.1.
RefSeq; XP_006253186.1; XM_006253124.2.
RefSeq; XP_006253187.1; XM_006253125.3.
RefSeq; XP_006253188.1; XM_006253126.2.
RefSeq; XP_006253189.1; XM_006253127.1.
RefSeq; XP_008769476.1; XM_008771254.1.
SMR; P18163; -.
BioGrid; 247327; 1.
CORUM; P18163; -.
IntAct; P18163; 29.
STRING; 10116.ENSRNOP00000014235; -.
SwissLipids; SLP:000001018; -.
CarbonylDB; P18163; -.
iPTMnet; P18163; -.
PhosphoSitePlus; P18163; -.
jPOST; P18163; -.
PaxDb; P18163; -.
PRIDE; P18163; -.
Ensembl; ENSRNOT00000014235; ENSRNOP00000014235; ENSRNOG00000010633.
Ensembl; ENSRNOT00000089501; ENSRNOP00000072677; ENSRNOG00000010633.
GeneID; 25288; -.
KEGG; rno:25288; -.
CTD; 2180; -.
RGD; 2015; Acsl1.
eggNOG; KOG1256; Eukaryota.
eggNOG; COG1022; LUCA.
GeneTree; ENSGT00940000154508; -.
HOGENOM; HOG000159459; -.
InParanoid; P18163; -.
KO; K01897; -.
OMA; TCYEWGV; -.
OrthoDB; 630541at2759; -.
PhylomeDB; P18163; -.
TreeFam; TF313877; -.
BioCyc; MetaCyc:MONOMER-14442; -.
BRENDA; 6.2.1.3; 5301.
Reactome; R-RNO-2046106; alpha-linolenic acid (ALA) metabolism.
Reactome; R-RNO-75876; Synthesis of very long-chain fatty acyl-CoAs.
SABIO-RK; P18163; -.
PRO; PR:P18163; -.
Proteomes; UP000002494; Chromosome 16.
Bgee; ENSRNOG00000010633; Expressed in 10 organ(s), highest expression level in liver.
Genevisible; P18163; RN.
GO; GO:0005783; C:endoplasmic reticulum; IDA:RGD.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005741; C:mitochondrial outer membrane; IDA:RGD.
GO; GO:0005778; C:peroxisomal membrane; IDA:HGNC.
GO; GO:0005886; C:plasma membrane; IDA:RGD.
GO; GO:0003987; F:acetate-CoA ligase activity; TAS:RGD.
GO; GO:0003996; F:acyl-CoA ligase activity; IEA:UniProtKB-EC.
GO; GO:0047676; F:arachidonate-CoA ligase activity; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0102391; F:decanoate-CoA ligase activity; IEA:UniProtKB-EC.
GO; GO:0004467; F:long-chain fatty acid-CoA ligase activity; IDA:UniProtKB.
GO; GO:0050197; F:phytanate-CoA ligase activity; IDA:UniProtKB.
GO; GO:0033211; P:adiponectin-activated signaling pathway; IEA:Ensembl.
GO; GO:0006631; P:fatty acid metabolic process; IMP:RGD.
GO; GO:0015908; P:fatty acid transport; IGI:RGD.
GO; GO:0006629; P:lipid metabolic process; TAS:RGD.
GO; GO:0044539; P:long-chain fatty acid import into cell; IEA:Ensembl.
GO; GO:0001676; P:long-chain fatty acid metabolic process; IDA:UniProtKB.
GO; GO:0035338; P:long-chain fatty-acyl-CoA biosynthetic process; IGI:RGD.
GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; ISS:YuBioLab.
GO; GO:0071902; P:positive regulation of protein