ACSL5_MOUSE
ID ACSL5_MOUSE Reviewed; 683 AA.
AC Q8JZR0;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Long-chain-fatty-acid--CoA ligase 5 {ECO:0000305};
DE EC=6.2.1.3 {ECO:0000250|UniProtKB:O88813};
DE AltName: Full=Arachidonate--CoA ligase {ECO:0000305};
DE EC=6.2.1.15 {ECO:0000250|UniProtKB:O88813};
DE AltName: Full=Long-chain acyl-CoA synthetase 5;
DE Short=LACS 5;
GN Name=Acsl5 {ECO:0000312|MGI:MGI:1919129}; Synonyms=Facl5;
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 [LARGE SCALE MRNA].
RC TISSUE=Mammary tumor;
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 [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, Liver, Lung, Pancreas, and Spleen;
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 [3]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-361, AND IDENTIFICATION BY MASS
RP 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). ACSL5 may activate
CC fatty acids from exogenous sources for the synthesis of triacylglycerol
CC destined for intracellular storage (By similarity). It was suggested
CC that it may also stimulate fatty acid oxidation (By similarity). At the
CC villus tip of the crypt-villus axis of the small intestine may
CC sensitize epithelial cells to apoptosis specifically triggered by the
CC death ligand TRAIL (By similarity). May have a role in the survival of
CC glioma cells (By similarity). Utilizes a wide range of saturated fatty
CC acids with a preference for C16-C18 unsaturated fatty acids (By
CC similarity). {ECO:0000250, ECO:0000250|UniProtKB:O88813}.
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:Q9ULC5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15422;
CC Evidence={ECO:0000250|UniProtKB:Q9ULC5};
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:O88813};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19714;
CC Evidence={ECO:0000250|UniProtKB:O88813};
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:Q9ULC5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30752;
CC Evidence={ECO:0000250|UniProtKB:Q9ULC5};
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:Q9ULC5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36140;
CC Evidence={ECO:0000250|UniProtKB:Q9ULC5};
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:O88813};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52117;
CC Evidence={ECO:0000250|UniProtKB:O88813};
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:O88813};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52113;
CC Evidence={ECO:0000250|UniProtKB:O88813};
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:O88813};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52109;
CC Evidence={ECO:0000250|UniProtKB:O88813};
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:O88813};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52017;
CC Evidence={ECO:0000250|UniProtKB:O88813};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=11,12-epoxy-(5Z,8Z,14Z)-eicosatrienoate + ATP + CoA = 11,12-
CC epoxy-(5Z,8Z,14Z)-eicosatrienoyl-CoA + AMP + diphosphate;
CC Xref=Rhea:RHEA:52012, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:76625, ChEBI:CHEBI:136115,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:O88813};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52013;
CC Evidence={ECO:0000250|UniProtKB:O88813};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q9ULC5}.
CC Endoplasmic reticulum {ECO:0000250|UniProtKB:Q9ULC5}. Mitochondrion
CC outer membrane {ECO:0000250}; Single-pass type III membrane protein
CC {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Single-
CC pass type III membrane protein {ECO:0000250}. Cell membrane
CC {ECO:0000250|UniProtKB:Q9ULC5}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; BC031544; AAH31544.1; -; mRNA.
DR CCDS; CCDS29908.1; -.
DR PIR; S49487; S49487.
DR RefSeq; NP_082252.1; NM_027976.2.
DR RefSeq; XP_006527241.1; XM_006527178.2.
DR AlphaFoldDB; Q8JZR0; -.
DR SMR; Q8JZR0; -.
DR BioGRID; 241124; 6.
DR STRING; 10090.ENSMUSP00000046585; -.
DR iPTMnet; Q8JZR0; -.
DR PhosphoSitePlus; Q8JZR0; -.
DR SwissPalm; Q8JZR0; -.
DR EPD; Q8JZR0; -.
DR jPOST; Q8JZR0; -.
DR MaxQB; Q8JZR0; -.
DR PaxDb; Q8JZR0; -.
DR PRIDE; Q8JZR0; -.
DR ProteomicsDB; 285660; -.
DR Antibodypedia; 31809; 280 antibodies from 34 providers.
DR DNASU; 433256; -.
DR Ensembl; ENSMUST00000043150; ENSMUSP00000046585; ENSMUSG00000024981.
DR GeneID; 433256; -.
DR KEGG; mmu:433256; -.
DR UCSC; uc008hxp.1; mouse.
DR CTD; 51703; -.
DR MGI; MGI:1919129; Acsl5.
DR VEuPathDB; HostDB:ENSMUSG00000024981; -.
DR eggNOG; KOG1256; Eukaryota.
DR GeneTree; ENSGT00940000156651; -.
DR HOGENOM; CLU_000022_45_4_1; -.
DR InParanoid; Q8JZR0; -.
DR OMA; PRIWTKF; -.
DR OrthoDB; 630541at2759; -.
DR PhylomeDB; Q8JZR0; -.
DR TreeFam; TF313877; -.
DR BRENDA; 6.2.1.3; 3474.
DR Reactome; R-MMU-75876; Synthesis of very long-chain fatty acyl-CoAs.
DR BioGRID-ORCS; 433256; 4 hits in 75 CRISPR screens.
DR ChiTaRS; Acsl5; mouse.
DR PRO; PR:Q8JZR0; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q8JZR0; protein.
DR Bgee; ENSMUSG00000024981; Expressed in small intestine Peyer's patch and 293 other tissues.
DR ExpressionAtlas; Q8JZR0; baseline and differential.
DR Genevisible; Q8JZR0; 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:0005743; C:mitochondrial inner membrane; HDA:MGI.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
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; IMP:UniProtKB.
DR GO; GO:0015908; P:fatty acid transport; ISO:MGI.
DR GO; GO:0008610; P:lipid biosynthetic process; IBA:GO_Central.
DR GO; GO:0001676; P:long-chain fatty acid metabolic process; IMP:UniProtKB.
DR GO; GO:0035338; P:long-chain fatty-acyl-CoA biosynthetic process; ISO:MGI.
DR GO; GO:0008654; P:phospholipid biosynthetic process; ISO:MGI.
DR GO; GO:0032000; P:positive regulation of fatty acid beta-oxidation; ISO:MGI.
DR GO; GO:0010747; P:positive regulation of long-chain fatty acid import across plasma membrane; ISO:MGI.
DR GO; GO:0010867; P:positive regulation of triglyceride biosynthetic process; ISO:MGI.
DR GO; GO:2001236; P:regulation of extrinsic apoptotic signaling pathway; ISO:MGI.
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; Cell membrane; Endoplasmic reticulum;
KW Fatty acid metabolism; Ligase; Lipid metabolism; Magnesium; Membrane;
KW Mitochondrion; Mitochondrion outer membrane; Nucleotide-binding;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..683
FT /note="Long-chain-fatty-acid--CoA ligase 5"
FT /id="PRO_0000193113"
FT TRANSMEM 12..32
FT /note="Helical; Signal-anchor for type III membrane
FT protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 33..683
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 361
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
SQ SEQUENCE 683 AA; 76206 MW; 734A1A5878741D70 CRC64;
MLFIFNFLFS PLPTPALICL LTFGTAIFLW LINRPQPVLP LIDLDNQSVG IEGGARRGAF
QKNNDLILYY FSDAKTLYEN FQRGLAVSDN GPCLGYRKPN QPYKWISYKQ VSDRAEYLGS
CLLHKGYKSS QDQFVGIFAQ NRPEWVISEL ACYTYSMVAV PLYDTLGTEA IIFVINRADI
PVVICDTPQK ATMLVENVEK GLTPGLKTII LMDPFDDDLM KRGEKCGVEM LSLHDAENIG
KENFKKPVPP KPEDLSVICF TSGTTGDPKG AMLTHENVVS NMAAFLKFLE PIFQPTSDDV
TISYLPLAHM FERLVQGILF SCGGKIGFFQ GDIRLLPDDM KALKPTVFPT VPRLLNRVYD
KVQNEAKTPL KKFLLNLAII SKFNEVKNGI IRRDSLWDKL VFSKIQGSLG GKVRLMITGA
APISTPVLTF FRAAMGCWVF EAYGQTECTG GCSITSPGDW TAGHVGTPVA CNFVKLEDVA
DMNYFSVNNE GEICIKGNNV FKGYLKDPEK TQEVLDKDGW LHTGDIGRWL PNGTLKIVDR
KKNIFKLAQG EYIAPEKIEN VYSRSRPVLQ VFVHGESLRS FLIGVVVPDP DSLPSFAAKI
GVKGSFEELC KNQCVKEAIL EDLQKIGKEG GLKSFEQVKS IFVHPEPFTI ENGLLTPTLK
AKRVELAKFF QTQIKSLYES IEE
