ACSL1_CAVPO
ID ACSL1_CAVPO Reviewed; 698 AA.
AC Q9JID6;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Long-chain-fatty-acid--CoA ligase 1 {ECO:0000250|UniProtKB:P33121};
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=Palmitoyl-CoA ligase;
DE AltName: Full=Phytanate--CoA ligase;
DE EC=6.2.1.24 {ECO:0000250|UniProtKB:P18163};
GN Name=ACSL1 {ECO:0000250|UniProtKB:P33121}; Synonyms=FACL1, LACS1;
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Sevoz C., Benoit E., Buronfosse T.;
RT "Molecular characterization and expression of guinea-pig acyl-CoA
RT synthetase 1.";
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
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; Evidence={ECO:0000250};
CC -!- ACTIVITY REGULATION: Inhibited at high temperature and by arachidonate.
CC {ECO:0000250|UniProtKB:P18163}.
CC -!- SUBCELLULAR LOCATION: Microsome membrane; Peripheral membrane protein.
CC Mitochondrion outer membrane {ECO:0000250}; Peripheral membrane protein
CC {ECO:0000250}. Peroxisome membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P33121}; Peripheral 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; AF236818; AAF91295.1; -; mRNA.
DR RefSeq; NP_001166379.1; NM_001172908.1.
DR AlphaFoldDB; Q9JID6; -.
DR SMR; Q9JID6; -.
DR STRING; 10141.ENSCPOP00000002483; -.
DR PRIDE; Q9JID6; -.
DR GeneID; 100135469; -.
DR KEGG; cpoc:100135469; -.
DR CTD; 2180; -.
DR eggNOG; KOG1256; Eukaryota.
DR InParanoid; Q9JID6; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005778; C:peroxisomal membrane; IEA:UniProtKB-SubCell.
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:0050197; F:phytanate-CoA ligase activity; ISS:UniProtKB.
DR GO; GO:0070251; F:pristanate-CoA ligase activity; IEA:RHEA.
DR GO; GO:0001676; P:long-chain fatty acid metabolic process; ISS:UniProtKB.
DR GO; GO:0000038; P:very long-chain fatty acid metabolic process; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW Acetylation; ATP-binding; Endoplasmic reticulum; Fatty acid metabolism;
KW Glycoprotein; Ligase; Lipid metabolism; Magnesium; Membrane; Microsome;
KW Mitochondrion; Mitochondrion outer membrane; Nitration; Nucleotide-binding;
KW Peroxisome; Phosphoprotein; Reference proteome.
FT CHAIN 1..698
FT /note="Long-chain-fatty-acid--CoA ligase 1"
FT /id="PRO_0000193103"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P33121"
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 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:0000250|UniProtKB:P33121"
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"
SQ SEQUENCE 698 AA; 77698 MW; CF8CB413209476AD CRC64;
MQAHELLQYF RLPELVDIRQ YVRTLPTNTL MGFGAFAALT TFWYATRPKA LKPPCDLSMQ
SVEVAGSDGA RRSTLLDSDE PLVYFYDDVR TLYDVFQRGI QVSNNGPCLG SRKPDQPYEW
LSYKQVEDLS ECIGSALLQK GFQASPDQFI GIFAQNRPEW VIIEQACFAY SMVVVPLYDT
LGADAITYIV NKAELSVIFA DKPEKARILL ESVENKLTPG LKIIVVMDSY GSELVEQGKK
CGVEVISLKA MEGLGRANRR KPKPPEPDDL AVICFTSGTT GNPKGAMITH KNVVSDCSAF
VKATEKALVL NASDIHISFL PLAHMYEQLL QCVMLCHGAK IGFFQGDIRL LMDDLKALQP
TIFPVVPRLL NRMFDRIFAQ ANTTVKRWLL DFASKRKEAE LRSGIIRNNS VWDKLIFHKI
QSSLGGKVRL MVTGAAPVSA TVLTFLRAAL GCQFYEGYGQ TECTAGCSLS VPGDWTAGHV
GAPMPCNFIK LVDVEEMNYM AAMGEGEVCV KGPNVFKGYL KDPAKTAEAL DKDGWLHTGD
IGKWLPNGTL KIIDRKKHIF KLAQGEYIAP EKIENIYVRS EPVAQVFVHG ESLQAFLIAI
VVPDAESLAS WARKRGFEGS FEELCRNKDV KKAILEDMVR IGKDSGLKSF EQVRGIALHP
ELFSVDNGLL TPTMKAKRPE LRNYFRSQID ELYSTIKV
