ACSL1_RAT
ID ACSL1_RAT Reviewed; 699 AA.
AC P18163;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Long-chain-fatty-acid--CoA ligase 1 {ECO:0000305};
DE EC=6.2.1.3 {ECO:0000269|PubMed:28209804};
DE AltName: Full=Arachidonate--CoA ligase;
DE EC=6.2.1.15 {ECO:0000269|PubMed:28209804};
DE AltName: Full=Long-chain acyl-CoA synthetase 1;
DE Short=LACS 1;
DE AltName: Full=Long-chain-fatty-acid--CoA ligase, liver isozyme;
DE AltName: Full=Phytanate--CoA ligase;
DE EC=6.2.1.24 {ECO:0000269|PubMed:10198260, ECO:0000269|PubMed:8978480};
GN Name=Acsl1 {ECO:0000312|RGD:2015}; Synonyms=Acs1, Acsl2, Facl2;
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], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=Wistar; TISSUE=Liver;
RX PubMed=2341402; DOI=10.1016/s0021-9258(19)38942-2;
RA Suzuki H., Kawarabayasi Y., Kondo J., Abe T., Nishikawa K., Kimura S.,
RA Hashimoto T., Yamamoto T.;
RT "Structure and regulation of rat long-chain acyl-CoA synthetase.";
RL J. Biol. Chem. 265:8681-8685(1990).
RN [2]
RP PROTEIN SEQUENCE OF 1-19; 82-91 AND 628-641, ACETYLATION AT MET-1 AND
RP LYS-633, NITRATION AT TYR-9 AND TYR-86, PHOSPHORYLATION AT TYR-85, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Liver;
RX PubMed=17478130; DOI=10.1016/j.bbapap.2007.03.012;
RA Distler A.M., Kerner J., Hoppel C.L.;
RT "Post-translational modifications of rat liver mitochondrial outer membrane
RT proteins identified by mass spectrometry.";
RL Biochim. Biophys. Acta 1774:628-636(2007).
RN [3]
RP CHARACTERIZATION.
RX PubMed=8973631; DOI=10.1111/j.1432-1033.1996.0186r.x;
RA Iijima H., Fujino T., Minekura H., Suzuki H., Kang M.-J., Yamamoto T.T.;
RT "Biochemical studies of two rat acyl-CoA synthetases, ACS1 and ACS2.";
RL Eur. J. Biochem. 242:186-190(1996).
RN [4]
RP CATALYTIC ACTIVITY, FUNCTION, AND ACTIVITY REGULATION.
RX PubMed=8978480;
RA Watkins P.A., Howard A.E., Gould S.J., Avigan J., Mihalik S.J.;
RT "Phytanic acid activation in rat liver peroxisomes is catalyzed by long-
RT chain acyl-CoA synthetase.";
RL J. Lipid Res. 37:2288-2295(1996).
RN [5]
RP CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=10198260; DOI=10.1006/bbrc.1999.0510;
RA Steinberg S.J., Wang S.J., Kim D.G., Mihalik S.J., Watkins P.A.;
RT "Human very-long-chain acyl-CoA synthetase: cloning, topography, and
RT relevance to branched-chain fatty acid metabolism.";
RL Biochem. Biophys. Res. Commun. 257:615-621(1999).
RN [6]
RP CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=10749848; DOI=10.1074/jbc.c000015200;
RA Steinberg S.J., Mihalik S.J., Kim D.G., Cuebas D.A., Watkins P.A.;
RT "The human liver-specific homolog of very long-chain acyl-CoA synthetase is
RT cholate:CoA ligase.";
RL J. Biol. Chem. 275:15605-15608(2000).
RN [7]
RP BIOPHYSICOCHEMICAL PROPERTIES.
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 [8]
RP GLYCOSYLATION AT SER-136.
RX PubMed=24098488; DOI=10.1371/journal.pone.0076399;
RA Cao W., Cao J., Huang J., Yao J., Yan G., Xu H., Yang P.;
RT "Discovery and confirmation of O-GlcNAcylated proteins in rat liver
RT mitochondria by combination of mass spectrometry and immunological
RT methods.";
RL PLoS ONE 8:E76399-E76399(2013).
RN [9]
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 [10]
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-CoAs for both synthesis of cellular lipids, and
CC degradation via beta-oxidation (PubMed:8978480, PubMed:10198260,
CC PubMed:10749848, PubMed:28209804). Preferentially uses palmitoleate,
CC oleate and linoleate (By similarity). Preferentially activates
CC arachidonate than epoxyeicosatrienoic acids (EETs) or
CC hydroxyeicosatrienoic acids (HETEs) (PubMed:28209804).
CC {ECO:0000250|UniProtKB:P33121, ECO:0000269|PubMed:10198260,
CC ECO:0000269|PubMed:10749848, ECO:0000269|PubMed:28209804,
CC ECO:0000269|PubMed:8978480}.
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:28209804};
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};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19714;
CC Evidence={ECO:0000269|PubMed:28209804};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3,7,11,15-tetramethylhexadecanoate + ATP + CoA = AMP +
CC diphosphate + phytanoyl-CoA; Xref=Rhea:RHEA:21380, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:37257, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57391, ChEBI:CHEBI:456215; EC=6.2.1.24;
CC Evidence={ECO:0000269|PubMed:10198260, ECO:0000269|PubMed:8978480};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21381;
CC Evidence={ECO:0000305|PubMed:10198260, ECO:0000305|PubMed:8978480};
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:10749848,
CC ECO:0000269|PubMed:8978480};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30752;
CC Evidence={ECO:0000305|PubMed:10749848, ECO:0000305|PubMed:8978480};
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:P33121};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36140;
CC Evidence={ECO:0000250|UniProtKB:P33121};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2,6,10,14-tetramethylpentadecanoate + ATP + CoA = AMP +
CC diphosphate + pristanoyl-CoA; Xref=Rhea:RHEA:47264,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:77250, ChEBI:CHEBI:77268, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000269|PubMed:10198260};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47265;
CC Evidence={ECO:0000305|PubMed:10198260};
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=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=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=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=(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:P33121};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33608;
CC Evidence={ECO:0000250|UniProtKB:P33121};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC -!- ACTIVITY REGULATION: Inhibited at high temperature and by arachidonate.
CC {ECO:0000269|PubMed:8978480}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=649 uM for ATP {ECO:0000269|PubMed:15683247};
CC KM=6.4 uM for CoA {ECO:0000269|PubMed:15683247};
CC KM=5.0 uM for palmitate {ECO:0000269|PubMed:15683247};
CC KM=2.7 uM for palmitate (when expressed in bacteria)
CC {ECO:0000269|PubMed:28209804};
CC KM=6.6 uM for stearate (when expressed in bacteria)
CC {ECO:0000269|PubMed:28209804};
CC KM=6.7 uM for oleate (when expressed in bacteria)
CC {ECO:0000269|PubMed:28209804};
CC KM=5 uM for linoleate (when expressed in bacteria)
CC {ECO:0000269|PubMed:28209804};
CC KM=6.3 uM for arachidonate (when expressed in bacteria)
CC {ECO:0000269|PubMed:28209804};
CC KM=2.1 uM for palmitate (when expressed in mammalian cell)
CC {ECO:0000269|PubMed:28209804};
CC KM=11.5 uM for stearate (when expressed in mammalian cell)
CC {ECO:0000269|PubMed:28209804};
CC KM=14.7 uM for oleate (when expressed in mammalian cell)
CC {ECO:0000269|PubMed:28209804};
CC KM=7 uM for linoleate (when expressed in mammalian cell)
CC {ECO:0000269|PubMed:28209804};
CC KM=7.3 uM for arachidonate (when expressed in mammalian cell)
CC {ECO:0000269|PubMed:28209804};
CC Vmax=1695 nmol/min/mg enzyme with palmitate as substrate
CC {ECO:0000269|PubMed:15683247};
CC Vmax=3068 nmol/min/mg enzyme with palmitate as substrate (when
CC expressed in mammalian cell) {ECO:0000269|PubMed:28209804};
CC Vmax=2342 nmol/min/mg enzyme with stearate as substrate (when
CC expressed in mammalian cell) {ECO:0000269|PubMed:28209804};
CC Vmax=2607 nmol/min/mg enzyme with oleate as substrate (when expressed
CC in mammalian cell) {ECO:0000269|PubMed:28209804};
CC Vmax=2525 nmol/min/mg enzyme with linoleate as substrate (when
CC expressed in mammalian cell) {ECO:0000269|PubMed:28209804};
CC Vmax=1745 nmol/min/mg enzyme with arachidonate as substrate (when
CC expressed in mammalian cell) {ECO:0000269|PubMed:28209804};
CC Vmax=3754 nmol/min/mg enzyme with palmitate as substrate (when
CC expressed in bacteria) {ECO:0000269|PubMed:28209804};
CC Vmax=2874 nmol/min/mg enzyme with stearate as substrate (when
CC expressed in bacteria) {ECO:0000269|PubMed:28209804};
CC Vmax=2089 nmol/min/mg enzyme with oleate as substrate (when expressed
CC in bacteria) {ECO:0000269|PubMed:28209804};
CC Vmax=1635 nmol/min/mg enzyme with linoleate as substrate (when
CC expressed in bacteria) {ECO:0000269|PubMed:28209804};
CC Vmax=3363 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|UniProtKB:P33121}; Single-pass type III membrane protein
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Liver, heart, epididymal adipose and to a lesser
CC extent brain, small intestine and lung.
CC -!- DEVELOPMENTAL STAGE: Levels remain constant during development.
CC -!- INDUCTION: By high fat and high carbohydrate diets.
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; D90109; BAA14136.1; -; mRNA.
DR PIR; A36275; A36275.
DR RefSeq; NP_036952.1; NM_012820.1.
DR RefSeq; XP_006253184.1; XM_006253122.1.
DR RefSeq; XP_006253185.1; XM_006253123.1.
DR RefSeq; XP_006253186.1; XM_006253124.2.
DR RefSeq; XP_006253187.1; XM_006253125.3.
DR RefSeq; XP_006253188.1; XM_006253126.2.
DR RefSeq; XP_006253189.1; XM_006253127.1.
DR RefSeq; XP_008769476.1; XM_008771254.1.
DR AlphaFoldDB; P18163; -.
DR SMR; P18163; -.
DR BioGRID; 247327; 1.
DR CORUM; P18163; -.
DR IntAct; P18163; 29.
DR STRING; 10116.ENSRNOP00000014235; -.
DR SwissLipids; SLP:000001018; -.
DR CarbonylDB; P18163; -.
DR GlyGen; P18163; 1 site.
DR iPTMnet; P18163; -.
DR PhosphoSitePlus; P18163; -.
DR jPOST; P18163; -.
DR PaxDb; P18163; -.
DR PRIDE; P18163; -.
DR Ensembl; ENSRNOT00000014235; ENSRNOP00000014235; ENSRNOG00000010633.
DR GeneID; 25288; -.
DR KEGG; rno:25288; -.
DR CTD; 2180; -.
DR RGD; 2015; Acsl1.
DR eggNOG; KOG1256; Eukaryota.
DR GeneTree; ENSGT00940000154508; -.
DR HOGENOM; CLU_000022_45_4_1; -.
DR InParanoid; P18163; -.
DR OMA; RTTYEWT; -.
DR OrthoDB; 630541at2759; -.
DR PhylomeDB; P18163; -.
DR TreeFam; TF313877; -.
DR BioCyc; MetaCyc:MON-14442; -.
DR BRENDA; 6.2.1.3; 5301.
DR Reactome; R-RNO-2046105; Linoleic acid (LA) metabolism.
DR Reactome; R-RNO-2046106; alpha-linolenic acid (ALA) metabolism.
DR Reactome; R-RNO-75876; Synthesis of very long-chain fatty acyl-CoAs.
DR SABIO-RK; P18163; -.
DR PRO; PR:P18163; -.
DR Proteomes; UP000002494; Chromosome 16.
DR Bgee; ENSRNOG00000010633; Expressed in liver and 19 other tissues.
DR Genevisible; P18163; RN.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:RGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005741; C:mitochondrial outer membrane; IDA:RGD.
DR GO; GO:0005739; C:mitochondrion; IDA:ARUK-UCL.
DR GO; GO:0005778; C:peroxisomal membrane; IDA:HGNC-UCL.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0003987; F:acetate-CoA ligase activity; TAS:RGD.
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:0090434; F:oleoyl-CoA ligase activity; IMP:ARUK-UCL.
DR GO; GO:0050197; F:phytanate-CoA ligase activity; IDA:UniProtKB.
DR GO; GO:0070251; F:pristanate-CoA ligase activity; IEA:RHEA.
DR GO; GO:0033211; P:adiponectin-activated signaling pathway; ISO:RGD.
DR GO; GO:0006631; P:fatty acid metabolic process; IMP:RGD.
DR GO; GO:0015908; P:fatty acid transport; IGI:RGD.
DR GO; GO:0008610; P:lipid biosynthetic process; ISO:RGD.
DR GO; GO:0006629; P:lipid metabolic process; TAS:RGD.
DR GO; GO:0044539; P:long-chain fatty acid import into cell; IMP:ARUK-UCL.
DR GO; GO:0001676; P:long-chain fatty acid metabolic process; IDA:UniProtKB.
DR GO; GO:0035338; P:long-chain fatty-acyl-CoA biosynthetic process; IGI:RGD.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR GO; GO:0010747; P:positive regulation of long-chain fatty acid import across plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; ISO:RGD.
DR GO; GO:0007584; P:response to nutrient; IEP:RGD.
DR GO; GO:0034201; P:response to oleic acid; IEP:RGD.
DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR GO; GO:0010033; P:response to organic substance; IDA:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0019432; P:triglyceride biosynthetic process; IGI:RGD.
DR GO; GO:0000038; P:very long-chain fatty acid metabolic process; IDA:UniProtKB.
DR GO; GO:0042178; P:xenobiotic catabolic process; IDA:RGD.
DR CDD; cd05927; LC-FACS_euk; 1.
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 InterPro; IPR045311; LC-FACS_euk.
DR Pfam; PF00501; AMP-binding; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Direct protein sequencing; Endoplasmic reticulum;
KW Fatty acid metabolism; Glycoprotein; Ligase; Lipid metabolism; Magnesium;
KW Membrane; Microsome; Mitochondrion; Mitochondrion outer membrane;
KW Nitration; Nucleotide-binding; Peroxisome; Phosphoprotein;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..699
FT /note="Long-chain-fatty-acid--CoA ligase 1"
FT /id="PRO_0000193106"
FT TRANSMEM 25..45
FT /note="Helical; Signal-anchor for type III membrane
FT protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 46..699
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|PubMed:17478130"
FT MOD_RES 9
FT /note="3'-nitrotyrosine"
FT /evidence="ECO:0000269|PubMed:17478130"
FT MOD_RES 85
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:17478130"
FT MOD_RES 86
FT /note="3'-nitrotyrosine"
FT /evidence="ECO:0000269|PubMed:17478130"
FT MOD_RES 208
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P41216"
FT MOD_RES 357
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P41216"
FT MOD_RES 387
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P41216"
FT MOD_RES 621
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P33121"
FT MOD_RES 633
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:17478130"
FT CARBOHYD 136
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000269|PubMed:24098488"
SQ 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
