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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.
26-FEB-2020, entry version 162.
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; CLU_000022_45_4_1; -.
InParanoid; P18163; -.
KO; K01897; -.
OMA; EHEDHAM; -.
OrthoDB; 630541at2759; -.
PhylomeDB; P18163; -.
TreeFam; TF313877; -.
BioCyc; MetaCyc:MONOMER-14442; -.
BRENDA; 6.2.1.3; 5301.
Reactome; R-RNO-2046105; Linoleic acid (LA) metabolism.
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 liver and 9 other tissues.
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:0005739; C:mitochondrion; ISO:RGD.
GO; GO:0005778; C:peroxisomal membrane; IDA:HGNC-UCL.
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; ISO:RGD.
GO; GO:0006631; P:fatty acid metabolic process; IMP:RGD.
GO; GO:0015908; P:fatty acid transport; IGI:RGD.
GO; GO:0008610; P:lipid biosynthetic process; ISO:RGD.
GO; GO:0006629; P:lipid metabolic process; TAS:RGD.
GO; GO:0044539; P:long-chain fatty acid import into cell; ISO:RGD.
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 serine/threonine kinase activity; ISO:RGD.
GO; GO:0042493; P:response to drug; IEP:RGD.
GO; GO:0007584; P:response to nutrient; IEP:RGD.
GO; GO:0034201; P:response to oleic acid; IEP:RGD.
GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
GO; GO:0010033; P:response to organic substance; IDA:RGD.
GO; GO:0019432; P:triglyceride biosynthetic process; IGI:RGD.
GO; GO:0000038; P:very long-chain fatty acid metabolic process; IDA:UniProtKB.
GO; GO:0042178; P:xenobiotic catabolic process; IDA:RGD.
Gene3D; 3.40.50.12780; -; 2.
InterPro; IPR020845; AMP-binding_CS.
InterPro; IPR000873; AMP-dep_Synth/Lig.
InterPro; IPR042099; AMP-dep_Synthh-like_sf.
Pfam; PF00501; AMP-binding; 1.
PROSITE; PS00455; AMP_BINDING; 1.
1: Evidence at protein level;
Acetylation; ATP-binding; Direct protein sequencing; Endoplasmic reticulum;
Fatty acid metabolism; Glycoprotein; Ligase; Lipid metabolism; Magnesium;
Membrane; Microsome; Mitochondrion; Mitochondrion outer membrane;
Nitration; Nucleotide-binding; Peroxisome; Phosphoprotein;
Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
CHAIN 1..699
/note="Long-chain-fatty-acid--CoA ligase 1"
/id="PRO_0000193106"
TRANSMEM 25..45
/note="Helical; Signal-anchor for type III membrane
protein"
/evidence="ECO:0000255"
TOPO_DOM 46..699
/note="Cytoplasmic"
/evidence="ECO:0000255"
MOD_RES 1
/note="N-acetylmethionine"
/evidence="ECO:0000269|PubMed:17478130"
MOD_RES 9
/note="Nitrated tyrosine"
/evidence="ECO:0000269|PubMed:17478130"
MOD_RES 85
/note="Phosphotyrosine"
/evidence="ECO:0000269|PubMed:17478130"
MOD_RES 86
/note="Nitrated tyrosine"
/evidence="ECO:0000269|PubMed:17478130"
MOD_RES 208
/note="N6-acetyllysine"
/evidence="ECO:0000250|UniProtKB:P41216"
MOD_RES 357
/note="N6-acetyllysine"
/evidence="ECO:0000250|UniProtKB:P41216"
MOD_RES 387
/note="N6-acetyllysine"
/evidence="ECO:0000250|UniProtKB:P41216"
MOD_RES 621
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P33121"
MOD_RES 633
/note="N6-acetyllysine"
/evidence="ECO:0000269|PubMed:17478130"
CARBOHYD 136
/note="O-linked (GlcNAc) serine"
/evidence="ECO:0000269|PubMed:24098488"
SEQUENCE 699 AA; 78179 MW; 6E1EACE0EAE8A85C CRC64;
MEVHELFRYF RMPELIDIRQ YVRTLPTNTL MGFGAFAALT TFWYATRPKA LKPPCDLSMQ
SVEVTGTTEG VRRSAVLEDD KLLLYYYDDV RTMYDGFQRG IQVSNDGPCL GSRKPNQPYE
WISYKQVAEM AECIGSALIQ KGFKPCSEQF IGIFSQNRPE WVTIEQGCFT YSMVVVPLYD
TLGTDAITYI VNKAELSVIF ADKPEKAKLL LEGVENKLTP CLKIIVIMDS YDNDLVERGQ
KCGVEIIGLK ALEDLGRVNR TKPKPPEPED LAIICFTSGT TGNPKGAMVT HQNIMNDCSG
FIKATESAFI ASPEDVLISF LPLAHMFETV VECVMLCHGA KIGFFQGDIR LLMDDLKVLQ
PTIFPVVPRL LNRMFDRIFG QANTSVKRWL LDFASKRKEA ELRSGIVRNN SLWDKLIFHK
IQSSLGGKVR LMITGAAPVS ATVLTFLRAA LGCQFYEGYG QTECTAGCCL SLPGDWTAGH
VGAPMPCNYI KLVDVEDMNY QAAKGEGEVC VKGANVFKGY LKDPARTAEA LDKDGWLHTG
DIGKWLPNGT LKIIDRKKHI FKLAQGEYIA PEKIENIYLR SEAVAQVFVH GESLQAFLIA
IVVPDVEILP SWAQKRGFQG SFEELCRNKD INKAILEDMV KLGKNAGLKP FEQVKGIAVH
PELFSIDNGL LTPTLKAKRP ELRNYFRSQI DELYSTIKI


Related products :

Catalog number Product name Quantity
18-003-42285 Long-chain-fatty-acid--CoA ligase 1 - EC 6.2.1.3; Long-chain acyl-CoA synthetase 1; LACS 1; Palmitoyl-CoA ligase 1; Long-chain fatty acid CoA ligase 2; Long-chain acyl-CoA synthetase 2; LACS 2; Acyl-C 0.05 mg Aff Pur
EIAAB36858 ACSB,ACSVL6,BA-CoA ligase,BACS,BAL,Bile acid-CoA ligase,Bile acyl-CoA synthetase,Cholate--CoA ligase,FACVL3,FATP5,FATP-5,Fatty acid transport protein 5,Fatty-acid-coenzyme A ligase, very long-chain 3,
EIAAB36851 Acsvl1,Facvl1,Fatp2,FATP-2,Fatty acid transport protein 2,Fatty-acid-coenzyme A ligase, very long-chain 1,Long-chain-fatty-acid--CoA ligase,Mouse,Mus musculus,Slc27a2,Solute carrier family 27 member 2
EIAAB36850 Acsvl1,Facvl1,Fatp2,FATP-2,Fatty acid transport protein 2,Fatty-acid-coenzyme A ligase, very long-chain 1,Long-chain-fatty-acid--CoA ligase,Rat,Rattus norvegicus,Slc27a2,Solute carrier family 27 membe
EIAAB36852 ACSVL1,FACVL1,FATP2,FATP-2,Fatty acid transport protein 2,Fatty-acid-coenzyme A ligase, very long-chain 1,Homo sapiens,Human,Long-chain-fatty-acid--CoA ligase,SLC27A2,Solute carrier family 27 member 2
EIAAB36860 ACSVL2,FACVL2,FATP1,FATP-6,Fatty acid transport protein 6,Fatty-acid-coenzyme A ligase, very long-chain 2,Homo sapiens,Human,hVLCS-H1,Long-chain fatty acid transport protein 6,SLC27A6,Solute carrier f
E1090m Rat ELISA Kit FOR Long-chain-fatty-acid--CoA ligase 3 96T
CSB-EL001194RA Rat Long-chain-fatty-acid--CoA ligase 5(ACSL5) ELISA kit 96T
E1477r Mouse ELISA Kit FOR Long-chain-fatty-acid--CoA ligase 4 96T
E14531h Human ELISA Kit FOR Long-chain-fatty-acid--CoA ligase 3 96T
CSB-EL001195RA Rat Long-chain-fatty-acid--CoA ligase 6(ACSL6) ELISA kit 96T
E1061Rb Human ELISA Kit FOR Long-chain-fatty-acid--CoA ligase 6 96T
E1437r Human ELISA Kit FOR Long-chain-fatty-acid--CoA ligase 5 96T
CSB-EL001192RA Rat Long-chain-fatty-acid--CoA ligase 3(ACSL3) ELISA kit 96T
E10511h Human ELISA Kit FOR Long-chain-fatty-acid--CoA ligase 1 96T
CSB-EL001193RA Rat Long-chain-fatty-acid--CoA ligase 4(ACSL4) ELISA kit 96T
E10451r Rat ELISA Kit FOR Long-chain-fatty-acid--CoA ligase ACSBG2 96T
CSB-EP300208EKN Recombinant Ba(E.coli-k12) Long-chain-fatty-acid--CoA ligase 500ug
27-706 ACSL1 encodes an isozyme of the long-chain fatty-acid-coenzyme A ligase family. Although differing in substrate specificity, subcellular localization, and tissue distribution, all isozymes of this fam 0.05 mg
27-705 ACSL1 encodes an isozyme of the long-chain fatty-acid-coenzyme A ligase family. Although differing in substrate specificity, subcellular localization, and tissue distribution, all isozymes of this fam 0.05 mg
CSB-EL001191GU Guinea pig Long-chain-fatty-acid--CoA ligase 1(ACSL1) ELISA kit 96T
E10608h Bovine ELISA Kit FOR Long-chain-fatty-acid--CoA ligase ACSBG1 96T
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CSB-EL001194MO Mouse Long-chain-fatty-acid--CoA ligase 5(ACSL5) ELISA kit 96T
Pathways :
WP1996: Linoleate Biosynthesis
WP2434: very-long-chain-fatty-acid-biosynthesis
WP2347: vitamin B5 (pantothenate) and CoA biosynthesis Pathway
WP1647: Fatty acid biosynthesis
WP1654: gamma-Hexachlorocyclohexane degradation
WP16: Fatty Acid Elongation, Unsaturated
WP2102: Fatty acid metabolism
WP38: Fatty Acid Biosynthesis
WP1201: Non-homologous end joining
WP1676: Non-homologous end-joining
WP401: Mitochondrial LC-Fatty Acid Beta-Oxidation
WP852: Fatty Acid Omega Oxidation
WP568: Fatty Acid Biosynthesis
WP1020: Fatty Acid Biosynthesis
WP1324: Non-homologous end joining
WP1352: Fatty Acid Biosynthesis
WP419: Mitochondrial LC-Fatty Acid Beta-Oxidation
WP1228: Fatty Acid Biosynthesis
WP903: Fatty Acid Biosynthesis
WP25: Fatty Acid Beta Oxidation 3
WP143: Fatty Acid Beta Oxidation
WP499: Fatty Acid Beta Oxidation 3
WP970: Fatty Acid Omega Oxidation
WP1269: Fatty Acid Beta Oxidation
WP1648: Fatty acid metabolism

Related Genes :
[Acsl1 Acs1 Acsl2 Facl2] 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 FACL1 FACL2 LACS LACS1 LACS2] Long-chain-fatty-acid--CoA ligase 1 (EC 6.2.1.3) (Acyl-CoA synthetase 1) (ACS1) (Arachidonate--CoA ligase) (EC 6.2.1.15) (Long-chain acyl-CoA synthetase 1) (LACS 1) (Long-chain acyl-CoA synthetase 2) (LACS 2) (Long-chain fatty acid-CoA ligase 2) (Palmitoyl-CoA ligase 1) (Palmitoyl-CoA ligase 2) (Phytanate--CoA ligase) (EC 6.2.1.24)
[Acsl1 Acsl2 Facl2] 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) (Phytanate--CoA ligase) (EC 6.2.1.24)
[ACSL1 FACL1 LACS1] 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) (Palmitoyl-CoA ligase) (Phytanate--CoA ligase) (EC 6.2.1.24)
[Acsl3 Acs3 Facl3] Long-chain-fatty-acid--CoA ligase 3 (EC 6.2.1.3) (Arachidonate--CoA ligase) (EC 6.2.1.15) (Brain acyl-CoA synthetase II) (Long-chain acyl-CoA synthetase 3) (LACS 3)
[ACSL5 ACS5 FACL5 UNQ633/PRO1250] Long-chain-fatty-acid--CoA ligase 5 (EC 6.2.1.3) (Arachidonate--CoA ligase) (EC 6.2.1.15) (Long-chain acyl-CoA synthetase 5) (LACS 5)
[ACSL4 ACS4 FACL4 LACS4] Long-chain-fatty-acid--CoA ligase 4 (EC 6.2.1.3) (Arachidonate--CoA ligase) (EC 6.2.1.15) (Long-chain acyl-CoA synthetase 4) (LACS 4)
[ACSBG2 BGR UNQ2443/PRO5005] Long-chain-fatty-acid--CoA ligase ACSBG2 (EC 6.2.1.3) (Acyl-CoA synthetase bubblegum family member 2) (Arachidonate--CoA ligase ACSBG2) (EC 6.2.1.15) (Bubblegum-related protein) (PRTD-NY3)
[SLC27A5 ACSB ACSVL6 FACVL3 FATP5] Bile acyl-CoA synthetase (BACS) (EC 6.2.1.7) (Bile acid-CoA ligase) (BA-CoA ligase) (BAL) (Cholate--CoA ligase) (Fatty acid transport protein 5) (FATP-5) (Fatty-acid-coenzyme A ligase, very long-chain 3) (Solute carrier family 27 member 5) (Very long-chain acyl-CoA synthetase homolog 2) (VLCS-H2) (VLCSH2) (Very long-chain acyl-CoA synthetase-related protein) (VLACS-related) (VLACSR)
[fadD13 Rv3089] Long-chain-fatty-acid--CoA ligase FadD13 (EC 6.2.1.3) (Fatty acyl-CoA ligase) (FACL) (FACL13) (Fatty acyl-CoA synthetase) (ACS) (FACS) (Very-long-chain fatty-acyl-CoA synthetase) (ACSVL)
[FAA2 FAM1 YER015W] Long-chain-fatty-acid--CoA ligase 2 (EC 6.2.1.3) (Fatty acid activator 2) (Long-chain acyl-CoA synthetase 2)
[Slc27a5 Acsb Acsvl6 Fatp5 Vlacsr] Bile acyl-CoA synthetase (BACS) (EC 6.2.1.7) (Bile acid-CoA ligase) (BA-CoA ligase) (BAL) (Cholate--CoA ligase) (Fatty acid transport protein 5) (FATP-5) (Solute carrier family 27 member 5) (Very long-chain acyl-CoA synthetase-related protein) (VLACS-related) (VLACSR)
[Slc27a5 Acsb Fatp5 Vlacsr] Bile acyl-CoA synthetase (BACS) (EC 6.2.1.7) (Bile acid-CoA ligase) (BA-CoA ligase) (BAL) (Cholate--CoA ligase) (Fatty acid transport protein 5) (FATP-5) (Solute carrier family 27 member 5) (Very long-chain acyl-CoA synthetase-related protein) (VLACS-related) (VLACSR)
[fadD oldD b1805 JW1794] Long-chain-fatty-acid--CoA ligase (EC 6.2.1.3) (Long-chain acyl-CoA synthetase) (Acyl-CoA synthetase)
[Slc27a3 Acsvl3 Fatp3] Solute carrier family 27 member 3 (EC 6.2.1.-) (Long-chain fatty acid transport protein 3) (FATP-3) (Fatty acid transport protein 3) (Very long-chain acyl-CoA synthetase homolog 3) (VLCS-3)
[FAA1 YOR317W O6136] Long-chain-fatty-acid--CoA ligase 1 (EC 6.2.1.3) (Fatty acid activator 1) (Long-chain acyl-CoA synthetase 1)
[ACSM1 BUCS1 LAE MACS1] Acyl-coenzyme A synthetase ACSM1, mitochondrial (EC 6.2.1.2) (Acyl-CoA synthetase medium-chain family member 1) (Benzoate--CoA ligase) (EC 6.2.1.25) (Butyrate--CoA ligase 1) (Butyryl-coenzyme A synthetase 1) (Lipoate-activating enzyme) (Middle-chain acyl-CoA synthetase 1) (Xenobiotic/medium-chain fatty acid-CoA ligase HXM-B)
[ACSM2B ACSM2 HYST1046] Acyl-coenzyme A synthetase ACSM2B, mitochondrial (EC 6.2.1.2) (Acyl-CoA synthetase medium-chain family member 2B) (Benzoate--CoA ligase) (EC 6.2.1.25) (Butyrate--CoA ligase 2B) (Butyryl-coenzyme A synthetase 2B) (Middle-chain acyl-CoA synthetase 2B) (Xenobiotic/medium-chain fatty acid-CoA ligase HXM-A)
[Elovl4] Elongation of very long chain fatty acids protein 4 (EC 2.3.1.199) (3-keto acyl-CoA synthase Elovl4) (ELOVL fatty acid elongase 4) (ELOVL FA elongase 4) (Very long chain 3-ketoacyl-CoA synthase 4) (Very long chain 3-oxoacyl-CoA synthase 4)
[Baat] Bile acid-CoA:amino acid N-acyltransferase (BACAT) (BAT) (EC 2.3.1.65) (Bile acid-CoA thioesterase) (Choloyl-CoA hydrolase) (EC 3.1.2.27) (Glycine N-choloyltransferase) (Long-chain fatty-acyl-CoA hydrolase) (EC 3.1.2.2)
[Acsm3 Sa Sah] Acyl-coenzyme A synthetase ACSM3, mitochondrial (EC 6.2.1.2) (Acyl-CoA synthetase medium-chain family member 3) (Butyrate--CoA ligase 3) (Butyryl-coenzyme A synthetase 3) (Middle-chain acyl-CoA synthetase 3) (Propionate--CoA ligase) (EC 6.2.1.17) (Protein SA homolog)
[ELOVL5 ELOVL2 PRO0530] Elongation of very long chain fatty acids protein 5 (EC 2.3.1.199) (3-keto acyl-CoA synthase ELOVL5) (ELOVL fatty acid elongase 5) (ELOVL FA elongase 5) (Fatty acid elongase 1) (hELO1) (Very long chain 3-ketoacyl-CoA synthase 5) (Very long chain 3-oxoacyl-CoA synthase 5)
[ELOVL4] Elongation of very long chain fatty acids protein 4 (EC 2.3.1.199) (3-keto acyl-CoA synthase ELOVL4) (ELOVL fatty acid elongase 4) (ELOVL FA elongase 4) (Very long chain 3-ketoacyl-CoA synthase 4) (Very long chain 3-oxoacyl-CoA synthase 4)
[ELOVL7] Elongation of very long chain fatty acids protein 7 (EC 2.3.1.199) (3-keto acyl-CoA synthase ELOVL7) (ELOVL fatty acid elongase 7) (ELOVL FA elongase 7) (Very long chain 3-ketoacyl-CoA synthase 7) (Very long chain 3-oxoacyl-CoA synthase 7)
[Elovl7] Elongation of very long chain fatty acids protein 7 (EC 2.3.1.199) (3-keto acyl-CoA synthase Elovl7) (ELOVL fatty acid elongase 7) (ELOVL FA elongase 7) (Very long chain 3-ketoacyl-CoA synthase 7) (Very long chain 3-oxoacyl-CoA synthase 7)
[Baat] Bile acid-CoA:amino acid N-acyltransferase (BACAT) (BAT) (EC 2.3.1.65) (Bile acid-CoA thioesterase) (Choloyl-CoA hydrolase) (EC 3.1.2.27) (Glycine N-choloyltransferase) (Kan-1) (Long-chain fatty-acyl-CoA hydrolase) (EC 3.1.2.2)
[Slc27a1 Fatp Fatp1] Long-chain fatty acid transport protein 1 (FATP-1) (Fatty acid transport protein 1) (EC 6.2.1.-) (Fatty acid transport protein) (Solute carrier family 27 member 1)
[Acot1 Cte1] Acyl-coenzyme A thioesterase 1 (Acyl-CoA thioesterase 1) (EC 3.1.2.-) (CTE-I) (Inducible cytosolic acyl-coenzyme A thioester hydrolase) (Long chain acyl-CoA thioester hydrolase) (Long chain acyl-CoA hydrolase) (Palmitoyl-coenzyme A thioesterase) (EC 3.1.2.2)
[Awat2 Dgat2l4 Ws] Acyl-CoA wax alcohol acyltransferase 2 (EC 2.3.1.75) (11-cis-specific retinyl-ester synthase) (11-cis-RE-synthase) (Acyl-CoA retinol O-fatty-acyltransferase) (ARAT) (Retinol O-fatty-acyltransferase) (EC 2.3.1.76) (Diacylglycerol O-acyltransferase 2-like protein 4) (Long-chain-alcohol O-fatty-acyltransferase 2) (Wax synthase) (mWS)
[ELOVL5 QflA-11914] Elongation of very long chain fatty acids protein 5 (EC 2.3.1.199) (3-keto acyl-CoA synthase ELOVL5) (ELOVL fatty acid elongase 5) (ELOVL FA elongase 5) (Very long chain 3-ketoacyl-CoA synthase 5) (Very long chain 3-oxoacyl-CoA synthase 5)

Bibliography :