ACSL1_MOUSE
ID ACSL1_MOUSE Reviewed; 699 AA.
AC P41216; Q6GTG6; Q9DBK5;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 2.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Long-chain-fatty-acid--CoA ligase 1 {ECO:0000305};
DE EC=6.2.1.3 {ECO:0000250|UniProtKB:P33121};
DE AltName: Full=Arachidonate--CoA ligase;
DE EC=6.2.1.15 {ECO:0000250|UniProtKB:P18163};
DE AltName: Full=Long-chain acyl-CoA synthetase 1;
DE Short=LACS 1;
DE AltName: Full=Phytanate--CoA ligase;
DE EC=6.2.1.24 {ECO:0000250|UniProtKB:P18163};
GN Name=Acsl1 {ECO:0000312|MGI:MGI:102797}; Synonyms=Acsl2, Facl2;
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 [MRNA].
RC STRAIN=SWR/J;
RA Schaffer J.E.;
RL Submitted (OCT-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=BALB/cJ, and C57BL/6J; TISSUE=Liver;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Liver;
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 PROTEIN SEQUENCE OF 1-8; 358-369; 389-396; 563-573; 617-627 AND 634-641,
RP ACETYLATION AT MET-1, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Liver;
RA Bienvenut W.V.;
RL Submitted (JUL-2005) to UniProtKB.
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-621, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-621, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and 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).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-208; LYS-357 AND LYS-387, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
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 (By similarity). Preferentially uses
CC palmitoleate, oleate and linoleate (By similarity). Preferentially
CC activates arachidonate than epoxyeicosatrienoic acids (EETs) or
CC hydroxyeicosatrienoic acids (HETEs). {ECO:0000250|UniProtKB:P18163,
CC ECO:0000250|UniProtKB:P33121}.
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:P18163};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15422;
CC Evidence={ECO:0000250|UniProtKB:P18163};
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:P18163};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19714;
CC Evidence={ECO:0000250|UniProtKB:P18163};
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:0000250|UniProtKB:P18163};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21381;
CC Evidence={ECO:0000250|UniProtKB:P18163};
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:P33121};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30752;
CC Evidence={ECO:0000250|UniProtKB:P33121};
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:0000250|UniProtKB:P18163};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47265;
CC Evidence={ECO:0000250|UniProtKB:P18163};
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:P18163};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52017;
CC Evidence={ECO:0000250|UniProtKB:P18163};
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:P18163};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52109;
CC Evidence={ECO:0000250|UniProtKB:P18163};
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:P18163};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52113;
CC Evidence={ECO:0000250|UniProtKB:P18163};
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:P18163};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52117;
CC Evidence={ECO:0000250|UniProtKB:P18163};
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:0000250|UniProtKB:P18163}.
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 -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; U15977; AAA52193.1; -; mRNA.
DR EMBL; AK004897; BAB23652.1; -; mRNA.
DR EMBL; AK145900; BAE26736.1; -; mRNA.
DR EMBL; AK149406; BAE28854.1; -; mRNA.
DR EMBL; AK152772; BAE31484.1; -; mRNA.
DR EMBL; AK153050; BAE31678.1; -; mRNA.
DR EMBL; AK161189; BAE36230.1; -; mRNA.
DR EMBL; AK168078; BAE40051.1; -; mRNA.
DR EMBL; BC056644; AAH56644.1; -; mRNA.
DR CCDS; CCDS22291.1; -.
DR RefSeq; NP_001289092.1; NM_001302163.1.
DR RefSeq; NP_032007.2; NM_007981.4.
DR RefSeq; XP_006509325.2; XM_006509262.3.
DR RefSeq; XP_006509327.1; XM_006509264.3.
DR RefSeq; XP_006509328.1; XM_006509265.2.
DR RefSeq; XP_006509329.1; XM_006509266.2.
DR RefSeq; XP_017168052.1; XM_017312563.1.
DR AlphaFoldDB; P41216; -.
DR SMR; P41216; -.
DR BioGRID; 199585; 12.
DR IntAct; P41216; 10.
DR STRING; 10090.ENSMUSP00000034046; -.
DR BindingDB; P41216; -.
DR ChEMBL; CHEMBL4680026; -.
DR CarbonylDB; P41216; -.
DR GlyGen; P41216; 1 site.
DR iPTMnet; P41216; -.
DR PhosphoSitePlus; P41216; -.
DR SwissPalm; P41216; -.
DR EPD; P41216; -.
DR jPOST; P41216; -.
DR MaxQB; P41216; -.
DR PaxDb; P41216; -.
DR PRIDE; P41216; -.
DR ProteomicsDB; 285656; -.
DR Antibodypedia; 1946; 310 antibodies from 35 providers.
DR DNASU; 14081; -.
DR Ensembl; ENSMUST00000034046; ENSMUSP00000034046; ENSMUSG00000018796.
DR Ensembl; ENSMUST00000110372; ENSMUSP00000106001; ENSMUSG00000018796.
DR GeneID; 14081; -.
DR KEGG; mmu:14081; -.
DR UCSC; uc009lqe.2; mouse.
DR CTD; 2180; -.
DR MGI; MGI:102797; Acsl1.
DR VEuPathDB; HostDB:ENSMUSG00000018796; -.
DR eggNOG; KOG1256; Eukaryota.
DR GeneTree; ENSGT00940000154508; -.
DR HOGENOM; CLU_000022_45_4_1; -.
DR InParanoid; P41216; -.
DR OrthoDB; 630541at2759; -.
DR PhylomeDB; P41216; -.
DR TreeFam; TF313877; -.
DR BRENDA; 6.2.1.3; 3474.
DR Reactome; R-MMU-2046105; Linoleic acid (LA) metabolism.
DR Reactome; R-MMU-2046106; alpha-linolenic acid (ALA) metabolism.
DR Reactome; R-MMU-75876; Synthesis of very long-chain fatty acyl-CoAs.
DR BioGRID-ORCS; 14081; 5 hits in 73 CRISPR screens.
DR ChiTaRS; Acsl1; mouse.
DR PRO; PR:P41216; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; P41216; protein.
DR Bgee; ENSMUSG00000018796; Expressed in brown adipose tissue and 285 other tissues.
DR ExpressionAtlas; P41216; baseline and differential.
DR Genevisible; P41216; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
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; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005778; C:peroxisomal membrane; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
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:0090434; F:oleoyl-CoA ligase activity; ISO:MGI.
DR GO; GO:0050197; F:phytanate-CoA ligase activity; ISS:UniProtKB.
DR GO; GO:0070251; F:pristanate-CoA ligase activity; IEA:RHEA.
DR GO; GO:0033211; P:adiponectin-activated signaling pathway; IMP:MGI.
DR GO; GO:0006631; P:fatty acid metabolic process; ISO:MGI.
DR GO; GO:0015908; P:fatty acid transport; ISO:MGI.
DR GO; GO:0008610; P:lipid 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:0035338; P:long-chain fatty-acyl-CoA biosynthetic process; ISO:MGI.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IMP:YuBioLab.
DR GO; GO:0010747; P:positive regulation of long-chain fatty acid import across plasma membrane; ISO:MGI.
DR GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; IMP:MGI.
DR GO; GO:0007584; P:response to nutrient; IEA:Ensembl.
DR GO; GO:0034201; P:response to oleic acid; IEA:Ensembl.
DR GO; GO:0014070; P:response to organic cyclic compound; IEA:Ensembl.
DR GO; GO:0010033; P:response to organic substance; ISO:MGI.
DR GO; GO:0019432; P:triglyceride biosynthetic process; ISO:MGI.
DR GO; GO:0000038; P:very long-chain fatty acid metabolic process; ISS:UniProtKB.
DR GO; GO:0042178; P:xenobiotic catabolic process; ISO:MGI.
DR CDD; cd05927; LC-FACS_euk; 1.
DR Gene3D; 3.40.50.12780; -; 1.
DR InterPro; IPR025110; AMP-bd_C.
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 Pfam; PF13193; AMP-binding_C; 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_0000193105"
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|Ref.4"
FT MOD_RES 9
FT /note="3'-nitrotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P18163"
FT MOD_RES 85
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P18163"
FT MOD_RES 86
FT /note="3'-nitrotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P18163"
FT MOD_RES 208
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 357
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 387
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 621
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 633
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P18163"
FT CARBOHYD 136
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000250"
FT CONFLICT 401..402
FT /note="EL -> DV (in Ref. 1; AAA52193)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 699 AA; 77951 MW; C8319972A764CCFA CRC64;
MEVHELFRYF RMPELIDIRQ YVRTLPTNTL MGFGAFAALT TFWYATRPKA LKPPCDLSMQ
SVEIAGTTDG IRRSAVLEDD KLLVYYYDDV RTMYDGFQRG IQVSNNGPCL GSRKPNQPYE
WISYKEVAEL AECIGSGLIQ KGFKPCSEQF IGLFSQNRPE WVIVEQGCFS YSMVVVPLYD
TLGADAITYI VNKAELSVIF ADKPEKAKLL LEGVENKLTP CLKIIVIMDS YGSDLVERGK
KCGVEIISLK ALEDLGRVNR VKPKPPEPED LAIICFTSGT TGNPKGAMIT HQNIINDCSG
FIKATESAFI ASTDDVLISF LPLAHMFETV VECVMLCHGA KIGFFQGDIR LLMDDLKVLQ
PTIFPVVPRL LNRMFDRIFG QANTSLKRWL LDFASKRKEA ELRSGIVRNN SLWDKLIFHK
IQSSLGGKVR LMITGAAPVS ATVLTFLRTA LGCQFYEGYG QTECTAGCCL SLPGDWTAGH
VGAPMPCNYV KLVDVEEMNY LASKGEGEVC VKGANVFKGY LKDPARTAEA LDKDGWLHTG
DIGKWLPNGT LKIIDRKKHI FKLAQGEYIA PEKIENIYLR SEAVAQVFVH GESLQAFLIA
VVVPDVESLP SWAQKRGLQG SFEELCRNKD INKAILDDLL KLGKEAGLKP FEQVKGIAVH
PELFSIDNGL LTPTLKAKRP ELRNYFRSQI DELYATIKI
