ACSL1_HUMAN
ID ACSL1_HUMAN Reviewed; 698 AA.
AC P33121; B7Z452; D3DP57; P41215; Q8N8V7; Q8TA99;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 201.
DE RecName: Full=Long-chain-fatty-acid--CoA ligase 1 {ECO:0000305};
DE EC=6.2.1.3 {ECO:0000269|PubMed:22633490, ECO:0000269|PubMed:24269233};
DE AltName: Full=Acyl-CoA synthetase 1;
DE Short=ACS1;
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=Long-chain acyl-CoA synthetase 2;
DE Short=LACS 2;
DE AltName: Full=Long-chain fatty acid-CoA ligase 2;
DE AltName: Full=Palmitoyl-CoA ligase 1;
DE AltName: Full=Palmitoyl-CoA ligase 2;
DE AltName: Full=Phytanate--CoA ligase;
DE EC=6.2.1.24 {ECO:0000250|UniProtKB:P18163};
GN Name=ACSL1 {ECO:0000312|HGNC:HGNC:3569};
GN Synonyms=FACL1, FACL2, LACS, LACS1, LACS2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Liver;
RX PubMed=1607358; DOI=10.1093/oxfordjournals.jbchem.a123707;
RA Abe T., Fujino T., Fukuyama R., Minoshima S., Shimizu N., Toh H.,
RA Suzuki H., Yamamoto T.;
RT "Human long-chain acyl-CoA synthetase: structure and chromosomal
RT location.";
RL J. Biochem. 111:123-128(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=8584017; DOI=10.1007/bf01076899;
RA Ghosh B., Barbosa E., Singh I.;
RT "Molecular cloning and sequencing of human palmitoyl-CoA ligase and its
RT tissue specific expression.";
RL Mol. Cell. Biochem. 151:77-81(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 395-698 (ISOFORM 2).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
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 [7]
RP PROTEIN SEQUENCE OF 1-8; 12-19; 341-349; 377-386; 562-572; 633-640 AND
RP 655-675, ACETYLATION AT MET-1, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=B-cell lymphoma;
RA Bienvenut W.V.;
RL Submitted (JUN-2005) to UniProtKB.
RN [8]
RP TISSUE SPECIFICITY.
RX PubMed=10548543; DOI=10.1042/bj3440135;
RA Malhotra K.T., Malhotra K., Lubin B.H., Kuypers F.A.;
RT "Identification and molecular characterization of acyl-CoA synthetase in
RT human red cells and erythroid precursor.";
RL Biochem. J. 344:135-143(1999).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=21242590; DOI=10.1194/jlr.m013292;
RA Golej D.L., Askari B., Kramer F., Barnhart S., Vivekanandan-Giri A.,
RA Pennathur S., Bornfeldt K.E.;
RT "Long-chain acyl-CoA synthetase 4 modulates prostaglandin E(2) release from
RT human arterial smooth muscle cells.";
RL J. Lipid Res. 52:782-793(2011).
RN [11]
RP CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=22633490; DOI=10.1016/j.molcel.2012.04.033;
RA Nakahara K., Ohkuni A., Kitamura T., Abe K., Naganuma T., Ohno Y.,
RA Zoeller R.A., Kihara A.;
RT "The Sjogren-Larsson syndrome gene encodes a hexadecenal dehydrogenase of
RT the sphingosine 1-phosphate degradation pathway.";
RL Mol. Cell 46:461-471(2012).
RN [12]
RP CATALYTIC ACTIVITY, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=24269233; DOI=10.1016/j.bbrc.2013.11.036;
RA Ohkuni A., Ohno Y., Kihara A.;
RT "Identification of acyl-CoA synthetases involved in the mammalian
RT sphingosine 1-phosphate metabolic pathway.";
RL Biochem. Biophys. Res. Commun. 442:195-201(2013).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-620, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
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:24269233, PubMed:22633490,
CC PubMed:21242590). Preferentially uses palmitoleate, oleate and
CC linoleate (PubMed:24269233). Preferentially activates arachidonate than
CC epoxyeicosatrienoic acids (EETs) or hydroxyeicosatrienoic acids (HETEs)
CC (By similarity). {ECO:0000250|UniProtKB:P18163,
CC ECO:0000269|PubMed:21242590, ECO:0000269|PubMed:22633490,
CC ECO:0000269|PubMed:24269233}.
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:22633490, ECO:0000269|PubMed:24269233};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15422;
CC Evidence={ECO:0000305|PubMed:22633490, ECO:0000305|PubMed:24269233};
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:0000269|PubMed:21242590,
CC ECO:0000269|PubMed:24269233};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30752;
CC Evidence={ECO:0000305|PubMed:21242590, ECO:0000305|PubMed:24269233};
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:0000269|PubMed:22633490, ECO:0000269|PubMed:24269233};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36140;
CC Evidence={ECO:0000305|PubMed:22633490, ECO:0000305|PubMed:24269233};
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:0000269|PubMed:21242590};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33608;
CC Evidence={ECO:0000305|PubMed:21242590};
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:0000269|PubMed:24269233}; Single-pass type III membrane protein
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P33121-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P33121-2; Sequence=VSP_009604;
CC Name=3;
CC IsoId=P33121-3; Sequence=VSP_054391;
CC -!- TISSUE SPECIFICITY: Highly expressed in liver, heart, skeletal muscle,
CC kidney and erythroid cells, and to a lesser extent in brain, lung,
CC placenta and pancreas. {ECO:0000269|PubMed:10548543}.
CC -!- DEVELOPMENTAL STAGE: Expressed during the early stages of erythroid
CC development while expression is very low in reticulocytes and young
CC erythrocytes.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing acceptor splice
CC site. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC04704.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; D10040; BAA00931.1; -; mRNA.
DR EMBL; L09229; AAB00959.1; -; mRNA.
DR EMBL; AK096117; BAC04704.1; ALT_INIT; mRNA.
DR EMBL; AK296826; BAH12438.1; -; mRNA.
DR EMBL; AC079257; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC084871; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471056; EAX04662.1; -; Genomic_DNA.
DR EMBL; CH471056; EAX04663.1; -; Genomic_DNA.
DR EMBL; CH471056; EAX04665.1; -; Genomic_DNA.
DR EMBL; BC026290; AAH26290.1; -; mRNA.
DR EMBL; BC050073; AAH50073.1; -; mRNA.
DR CCDS; CCDS3839.1; -. [P33121-1]
DR CCDS; CCDS68826.1; -. [P33121-3]
DR PIR; JX0202; JX0202.
DR RefSeq; NP_001273637.1; NM_001286708.1. [P33121-1]
DR RefSeq; NP_001273639.1; NM_001286710.1. [P33121-3]
DR RefSeq; NP_001273640.1; NM_001286711.1.
DR RefSeq; NP_001273641.1; NM_001286712.1.
DR RefSeq; NP_001986.2; NM_001995.3. [P33121-1]
DR RefSeq; XP_005262885.1; XM_005262828.1.
DR RefSeq; XP_005262886.1; XM_005262829.1.
DR RefSeq; XP_005262888.1; XM_005262831.1.
DR RefSeq; XP_011530044.1; XM_011531742.1.
DR RefSeq; XP_016863376.1; XM_017007887.1. [P33121-1]
DR RefSeq; XP_016863377.1; XM_017007888.1.
DR RefSeq; XP_016863378.1; XM_017007889.1.
DR AlphaFoldDB; P33121; -.
DR SMR; P33121; -.
DR BioGRID; 108476; 113.
DR IntAct; P33121; 9.
DR MINT; P33121; -.
DR STRING; 9606.ENSP00000422607; -.
DR BindingDB; P33121; -.
DR ChEMBL; CHEMBL4295746; -.
DR DrugBank; DB00131; Adenosine phosphate.
DR DrugBank; DB00171; ATP.
DR SwissLipids; SLP:000000199; -.
DR SwissLipids; SLP:000001468; -. [P33121-1]
DR GlyGen; P33121; 2 sites, 1 O-linked glycan (1 site).
DR iPTMnet; P33121; -.
DR PhosphoSitePlus; P33121; -.
DR SwissPalm; P33121; -.
DR BioMuta; ACSL1; -.
DR DMDM; 417241; -.
DR CPTAC; CPTAC-305; -.
DR CPTAC; CPTAC-306; -.
DR EPD; P33121; -.
DR jPOST; P33121; -.
DR MassIVE; P33121; -.
DR MaxQB; P33121; -.
DR PaxDb; P33121; -.
DR PeptideAtlas; P33121; -.
DR PRIDE; P33121; -.
DR ProteomicsDB; 54898; -. [P33121-1]
DR ProteomicsDB; 54899; -. [P33121-2]
DR ProteomicsDB; 6570; -.
DR Antibodypedia; 1946; 310 antibodies from 35 providers.
DR DNASU; 2180; -.
DR Ensembl; ENST00000281455.7; ENSP00000281455.2; ENSG00000151726.15. [P33121-1]
DR Ensembl; ENST00000504342.5; ENSP00000425006.1; ENSG00000151726.15. [P33121-1]
DR Ensembl; ENST00000513317.5; ENSP00000426150.1; ENSG00000151726.15. [P33121-3]
DR Ensembl; ENST00000515030.5; ENSP00000422607.1; ENSG00000151726.15. [P33121-1]
DR GeneID; 2180; -.
DR KEGG; hsa:2180; -.
DR MANE-Select; ENST00000281455.7; ENSP00000281455.2; NM_001995.5; NP_001986.2.
DR UCSC; uc003iwt.2; human. [P33121-1]
DR CTD; 2180; -.
DR DisGeNET; 2180; -.
DR GeneCards; ACSL1; -.
DR HGNC; HGNC:3569; ACSL1.
DR HPA; ENSG00000151726; Tissue enhanced (adipose tissue, liver, skeletal muscle).
DR MIM; 152425; gene.
DR neXtProt; NX_P33121; -.
DR OpenTargets; ENSG00000151726; -.
DR PharmGKB; PA27966; -.
DR VEuPathDB; HostDB:ENSG00000151726; -.
DR eggNOG; KOG1256; Eukaryota.
DR GeneTree; ENSGT00940000154508; -.
DR InParanoid; P33121; -.
DR OMA; RTTYEWT; -.
DR OrthoDB; 630541at2759; -.
DR PhylomeDB; P33121; -.
DR TreeFam; TF313877; -.
DR BioCyc; MetaCyc:HS07766-MON; -.
DR BRENDA; 6.2.1.3; 2681.
DR PathwayCommons; P33121; -.
DR Reactome; R-HSA-1989781; PPARA activates gene expression.
DR Reactome; R-HSA-2046105; Linoleic acid (LA) metabolism.
DR Reactome; R-HSA-2046106; alpha-linolenic acid (ALA) metabolism.
DR Reactome; R-HSA-75876; Synthesis of very long-chain fatty acyl-CoAs.
DR SignaLink; P33121; -.
DR SIGNOR; P33121; -.
DR BioGRID-ORCS; 2180; 15 hits in 1084 CRISPR screens.
DR ChiTaRS; ACSL1; human.
DR GeneWiki; ACSL1; -.
DR GenomeRNAi; 2180; -.
DR Pharos; P33121; Tbio.
DR PRO; PR:P33121; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; P33121; protein.
DR Bgee; ENSG00000151726; Expressed in right lobe of liver and 201 other tissues.
DR ExpressionAtlas; P33121; baseline and differential.
DR Genevisible; P33121; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005741; C:mitochondrial outer membrane; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005778; C:peroxisomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
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; IDA:UniProtKB.
DR GO; GO:0090434; F:oleoyl-CoA ligase activity; ISS:ARUK-UCL.
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; IEA:Ensembl.
DR GO; GO:0015908; P:fatty acid transport; IMP:ARUK-UCL.
DR GO; GO:0008610; P:lipid biosynthetic process; IDA:UniProtKB.
DR GO; GO:0044539; P:long-chain fatty acid import into cell; IDA:UniProtKB.
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; IBA:GO_Central.
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; ISS:ARUK-UCL.
DR GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; IEA:Ensembl.
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:0019432; P:triglyceride biosynthetic process; IEA:Ensembl.
DR GO; GO:0000038; P:very long-chain fatty acid metabolic process; IBA:GO_Central.
DR GO; GO:0042178; P:xenobiotic catabolic process; IEA:Ensembl.
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; Alternative splicing; ATP-binding; Direct protein sequencing;
KW Endoplasmic reticulum; Fatty acid metabolism; Glycoprotein; Ligase;
KW Lipid metabolism; Magnesium; Membrane; Microsome; Mitochondrion;
KW Mitochondrion outer membrane; Nitration; Nucleotide-binding; Peroxisome;
KW Phosphoprotein; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..698
FT /note="Long-chain-fatty-acid--CoA ligase 1"
FT /id="PRO_0000193104"
FT TRANSMEM 25..45
FT /note="Helical; Signal-anchor for type III membrane
FT protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 46..698
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|Ref.7"
FT MOD_RES 9
FT /note="3'-nitrotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P18163"
FT MOD_RES 84
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P18163"
FT MOD_RES 207
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P41216"
FT MOD_RES 356
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P41216"
FT MOD_RES 386
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P41216"
FT MOD_RES 620
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 632
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P18163"
FT CARBOHYD 135
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 306..331
FT /note="NTVNPCPDDTLISFLPLAHMFERVVE -> KALPLSASDTHISYLPLAHIYE
FT QLLK (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054391"
FT VAR_SEQ 508..517
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_009604"
FT CONFLICT 21..23
FT /note="YVR -> CV (in Ref. 2; AAB00959)"
FT /evidence="ECO:0000305"
FT CONFLICT 37..38
FT /note="AA -> SRR (in Ref. 2; AAB00959)"
FT /evidence="ECO:0000305"
FT CONFLICT 44..47
FT /note="YATR -> RPRH (in Ref. 2; AAB00959)"
FT /evidence="ECO:0000305"
FT CONFLICT 55..56
FT /note="CD -> WH (in Ref. 2; AAB00959)"
FT /evidence="ECO:0000305"
FT CONFLICT 229
FT /note="A -> S (in Ref. 2; AAB00959)"
FT /evidence="ECO:0000305"
FT CONFLICT 385
FT /note="L -> V (in Ref. 2; AAB00959)"
FT /evidence="ECO:0000305"
FT CONFLICT 400..401
FT /note="EL -> DV (in Ref. 2; AAB00959)"
FT /evidence="ECO:0000305"
FT CONFLICT 477
FT /note="A -> T (in Ref. 2; AAB00959)"
FT /evidence="ECO:0000305"
FT CONFLICT 492..494
FT /note="VDV -> GWQL (in Ref. 2; AAB00959)"
FT /evidence="ECO:0000305"
FT CONFLICT 502
FT /note="A -> S (in Ref. 2; AAB00959)"
FT /evidence="ECO:0000305"
FT CONFLICT 695
FT /note="T -> I (in Ref. 2; AAB00959)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 698 AA; 77943 MW; FD6669453589D362 CRC64;
MQAHELFRYF RMPELVDFRQ YVRTLPTNTL MGFGAFAALT TFWYATRPKP LKPPCDLSMQ
SVEVAGSGGA RRSALLDSDE PLVYFYDDVT TLYEGFQRGI QVSNNGPCLG SRKPDQPYEW
LSYKQVAELS ECIGSALIQK GFKTAPDQFI GIFAQNRPEW VIIEQGCFAY SMVIVPLYDT
LGNEAITYIV NKAELSLVFV DKPEKAKLLL EGVENKLIPG LKIIVVMDAY GSELVERGQR
CGVEVTSMKA MEDLGRANRR KPKPPAPEDL AVICFTSGTT GNPKGAMVTH RNIVSDCSAF
VKATENTVNP CPDDTLISFL PLAHMFERVV ECVMLCHGAK IGFFQGDIRL LMDDLKVLQP
TVFPVVPRLL NRMFDRIFGQ ANTTLKRWLL DFASKRKEAE LRSGIIRNNS LWDRLIFHKV
QSSLGGRVRL MVTGAAPVSA TVLTFLRAAL GCQFYEGYGQ TECTAGCCLT MPGDWTAGHV
GAPMPCNLIK LVDVEEMNYM AAEGEGEVCV KGPNVFQGYL KDPAKTAEAL DKDGWLHTGD
IGKWLPNGTL KIIDRKKHIF KLAQGEYIAP EKIENIYMRS EPVAQVFVHG ESLQAFLIAI
VVPDVETLCS WAQKRGFEGS FEELCRNKDV KKAILEDMVR LGKDSGLKPF EQVKGITLHP
ELFSIDNGLL TPTMKAKRPE LRNYFRSQID DLYSTIKV
