ID   ACSL4_RAT               Reviewed;         711 AA.
AC   O35547;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   31-JUL-2019, sequence version 2.
DT   24-JAN-2024, entry version 157.
DE   RecName: Full=Long-chain-fatty-acid--CoA ligase 4 {ECO:0000305};
DE            EC=6.2.1.3 {ECO:0000269|PubMed:23766516, ECO:0000269|PubMed:28209804, ECO:0000269|PubMed:9096315};
DE   AltName: Full=Arachidonate--CoA ligase {ECO:0000305};
DE            EC=6.2.1.15 {ECO:0000269|PubMed:28209804};
DE   AltName: Full=Long-chain acyl-CoA synthetase 4;
DE            Short=LACS 4;
GN   Name=Acsl4; Synonyms=Acs4, Facl4;
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], FUNCTION, AND CATALYTIC ACTIVITY (ISOFORM
RP   SHORT).
RC   STRAIN=Wistar; TISSUE=Liver;
RX   PubMed=9096315; DOI=10.1073/pnas.94.7.2880;
RA   Kang M., Fujino T., Sasano H., Minekura H., Yabuki N., Nagura H.,
RA   Iijima H., Yamamoto T.T.;
RT   "A novel arachidonate-preferring acyl-CoA synthetase is present in
RT   steroidogenic cells of the rat adrenal, ovary, and testis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 94:2880-2884(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-51 (ISOFORM LONG).
RA   Kube M., Klages S., Kuhl H., Thiel J., Beck A., Reinhardt R.;
RT   "Euratools EST.";
RL   Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
RN   [3]
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   [4]
RP   CATALYTIC ACTIVITY, FUNCTION, AND INDUCTION.
RX   PubMed=23766516; DOI=10.1074/jbc.m113.481077;
RA   Klett E.L., Chen S., Edin M.L., Li L.O., Ilkayeva O., Zeldin D.C.,
RA   Newgard C.B., Coleman R.A.;
RT   "Diminished acyl-CoA synthetase isoform 4 activity in INS 832/13 cells
RT   reduces cellular epoxyeicosatrienoic acid levels and results in impaired
RT   glucose-stimulated insulin secretion.";
RL   J. Biol. Chem. 288:21618-21629(2013).
RN   [5]
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   [6]
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-CoA for both synthesis of cellular lipids, and
CC       degradation via beta-oxidation (PubMed:28209804, PubMed:23766516,
CC       PubMed:9096315). Preferentially activates arachidonate and
CC       eicosapentaenoate as substrates (PubMed:9096315). Preferentially
CC       activates 8,9-EET > 14,15-EET > 5,6-EET > 11,12-EET (PubMed:23766516).
CC       Modulates glucose-stimulated insulin secretion by regulating the levels
CC       of unesterified EETs (PubMed:23766516). Modulates prostaglandin E2
CC       secretion (By similarity). {ECO:0000250|UniProtKB:O60488,
CC       ECO:0000269|PubMed:23766516, ECO:0000269|PubMed:28209804,
CC       ECO:0000269|PubMed:9096315}.
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:23766516, ECO:0000269|PubMed:28209804,
CC         ECO:0000269|PubMed:9096315};
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=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:0000305|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:0000305|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:0000305|PubMed:28209804};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5,6-epoxy-(8Z,11Z,14Z)-eicosatrienoate + ATP + CoA = 5,6-
CC         epoxy-(8Z,11Z,14Z)-eicosatrienoyl-CoA + AMP + diphosphate;
CC         Xref=Rhea:RHEA:52088, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:131992, ChEBI:CHEBI:136351,
CC         ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:23766516};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52089;
CC         Evidence={ECO:0000305|PubMed:23766516};
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:23766516,
CC         ECO:0000269|PubMed:28209804};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52017;
CC         Evidence={ECO:0000269|PubMed:23766516, ECO:0000269|PubMed:28209804};
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:0000269|PubMed:23766516,
CC         ECO:0000269|PubMed:28209804};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52013;
CC         Evidence={ECO:0000269|PubMed:23766516, ECO:0000269|PubMed:28209804};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=8,9-epoxy-(5Z,11Z,14Z)-eicosatrienoate + ATP + CoA = 8,9-
CC         epoxy-(5Z,11Z,14Z)-eicosatrienoyl-CoA + AMP + diphosphate;
CC         Xref=Rhea:RHEA:52008, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:84025, ChEBI:CHEBI:136107,
CC         ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:23766516,
CC         ECO:0000269|PubMed:28209804};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52009;
CC         Evidence={ECO:0000269|PubMed:23766516, ECO:0000269|PubMed:28209804};
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:O60488};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30752;
CC         Evidence={ECO:0000250|UniProtKB:O60488};
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:O60488};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36140;
CC         Evidence={ECO:0000250|UniProtKB:O60488};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- ACTIVITY REGULATION: Both triacsin C and rosiglitazone inhibit
CC       arachidonoyl-CoA ligase activity. {ECO:0000250|UniProtKB:O60488}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=34 uM for ATP {ECO:0000269|PubMed:15683247};
CC         KM=4.1 uM for CoA {ECO:0000269|PubMed:15683247};
CC         KM=5.4 uM for palmitate {ECO:0000269|PubMed:15683247};
CC         KM=19.5 uM for oleate {ECO:0000269|PubMed:15683247};
CC         KM=10 uM for arachidonate {ECO:0000269|PubMed:15683247};
CC         KM=4.5 uM for palmitate (when expressed in bacteria)
CC         {ECO:0000269|PubMed:28209804};
CC         KM=2.9 uM for stearate (when expressed in bacteria)
CC         {ECO:0000269|PubMed:28209804};
CC         KM=16.7 uM for oleate (when expressed in bacteria)
CC         {ECO:0000269|PubMed:28209804};
CC         KM=4 uM for linoleate (when expressed in bacteria)
CC         {ECO:0000269|PubMed:28209804};
CC         KM=11.4 uM for arachidonate (when expressed in bacteria)
CC         {ECO:0000269|PubMed:28209804};
CC         KM=24.8 uM for palmitate (when expressed in mammalian cell)
CC         {ECO:0000269|PubMed:28209804};
CC         KM=12.5 uM for stearate (when expressed in mammalian cell)
CC         {ECO:0000269|PubMed:28209804};
CC         KM=3.6 uM for oleate (when expressed in mammalian cell)
CC         {ECO:0000269|PubMed:28209804};
CC         KM=13.3 uM for linoleate (when expressed in mammalian cell)
CC         {ECO:0000269|PubMed:28209804};
CC         KM=7.5 uM for arachidonate (when expressed in mammalian cell)
CC         {ECO:0000269|PubMed:28209804};
CC         Vmax=2800 nmol/min/mg enzyme with palmitate as substrate
CC         {ECO:0000269|PubMed:15683247};
CC         Vmax=673 nmol/min/mg enzyme with oleate as substrate
CC         {ECO:0000269|PubMed:15683247};
CC         Vmax=4200 nmol/min/mg enzyme with arachidonate as substrate
CC         {ECO:0000269|PubMed:15683247};
CC         Vmax=4451 nmol/min/mg enzyme with palmitate as substrate (when
CC         expressed in bacteria) {ECO:0000269|PubMed:28209804};
CC         Vmax=2737 nmol/min/mg enzyme with stearate as substrate (when
CC         expressed in bacteria) {ECO:0000269|PubMed:28209804};
CC         Vmax=2366 nmol/min/mg enzyme with oleate as substrate (when expressed
CC         in bacteria) {ECO:0000269|PubMed:28209804};
CC         Vmax=1231 nmol/min/mg enzyme with linoleate as substrate (when
CC         expressed in bacteria) {ECO:0000269|PubMed:28209804};
CC         Vmax=7180 nmol/min/mg enzyme with arachidonate as substrate (when
CC         expressed in bacteria) {ECO:0000269|PubMed:28209804};
CC         Vmax=1990 nmol/min/mg enzyme with palmitate as substrate (when
CC         expressed in mammalian cell) {ECO:0000269|PubMed:28209804};
CC         Vmax=1240 nmol/min/mg enzyme with stearate as substrate (when
CC         expressed in mammalian cell) {ECO:0000269|PubMed:28209804};
CC         Vmax=466 nmol/min/mg enzyme with oleate as substrate (when expressed
CC         in mammalian cell) {ECO:0000269|PubMed:28209804};
CC         Vmax=1011 nmol/min/mg enzyme with linoleate as substrate (when
CC         expressed in mammalian cell) {ECO:0000269|PubMed:28209804};
CC         Vmax=4339 nmol/min/mg enzyme with arachidonate as substrate (when
CC         expressed in mammalian cell) {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:O60488}; Single-pass type III membrane protein
CC       {ECO:0000250}. Cell membrane {ECO:0000250|UniProtKB:O60488}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=Long;
CC         IsoId=O35547-1; Sequence=Displayed;
CC       Name=Short;
CC         IsoId=O35547-2; Sequence=VSP_060224;
CC   -!- INDUCTION: Expression is decreased by polyunsaturated fatty acid
CC       (PUFA). {ECO:0000269|PubMed:23766516}.
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; D85189; BAA22195.1; -; mRNA.
DR   EMBL; FM034112; -; NOT_ANNOTATED_CDS; mRNA.
DR   RefSeq; NP_446075.1; NM_053623.1. [O35547-2]
DR   RefSeq; XP_006257376.1; XM_006257314.3. [O35547-1]
DR   RefSeq; XP_006257377.1; XM_006257315.3. [O35547-2]
DR   RefSeq; XP_006257378.1; XM_006257316.2. [O35547-2]
DR   AlphaFoldDB; O35547; -.
DR   SMR; O35547; -.
DR   IntAct; O35547; 1.
DR   STRING; 10116.ENSRNOP00000026057; -.
DR   SwissLipids; SLP:000001679; -.
DR   PhosphoSitePlus; O35547; -.
DR   jPOST; O35547; -.
DR   PaxDb; 10116-ENSRNOP00000026057; -.
DR   Ensembl; ENSRNOT00000026057.7; ENSRNOP00000026057.5; ENSRNOG00000019180.7. [O35547-2]
DR   Ensembl; ENSRNOT00055042740; ENSRNOP00055034898; ENSRNOG00055024794. [O35547-1]
DR   Ensembl; ENSRNOT00060032631; ENSRNOP00060026634; ENSRNOG00060018877. [O35547-1]
DR   Ensembl; ENSRNOT00065045017; ENSRNOP00065036902; ENSRNOG00065026083. [O35547-1]
DR   GeneID; 113976; -.
DR   KEGG; rno:113976; -.
DR   AGR; RGD:69401; -.
DR   CTD; 2182; -.
DR   RGD; 69401; Acsl4.
DR   VEuPathDB; HostDB:ENSRNOG00000019180; -.
DR   eggNOG; KOG1180; Eukaryota.
DR   GeneTree; ENSGT00940000157427; -.
DR   HOGENOM; CLU_000022_45_2_1; -.
DR   InParanoid; O35547; -.
DR   OMA; KIFQWAA; -.
DR   OrthoDB; 443463at2759; -.
DR   PhylomeDB; O35547; -.
DR   TreeFam; TF314012; -.
DR   BRENDA; 6.2.1.3; 5301.
DR   Reactome; R-RNO-434313; Intracellular metabolism of fatty acids regulates insulin secretion.
DR   Reactome; R-RNO-75876; Synthesis of very long-chain fatty acyl-CoAs.
DR   SABIO-RK; O35547; -.
DR   PRO; PR:O35547; -.
DR   Proteomes; UP000002494; Chromosome X.
DR   Bgee; ENSRNOG00000019180; Expressed in Ammon's horn and 20 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005811; C:lipid droplet; ISO:RGD.
DR   GO; GO:0044233; C:mitochondria-associated endoplasmic reticulum membrane; ISO:RGD.
DR   GO; GO:0031966; C:mitochondrial membrane; IDA:RGD.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; ISO:RGD.
DR   GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR   GO; GO:0005778; C:peroxisomal membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005777; C:peroxisome; IDA:RGD.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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:0031957; F:very long-chain fatty acid-CoA ligase activity; ISO:RGD.
DR   GO; GO:0060996; P:dendritic spine development; IMP:RGD.
DR   GO; GO:0060136; P:embryonic process involved in female pregnancy; ISO:RGD.
DR   GO; GO:0006631; P:fatty acid metabolic process; IDA:RGD.
DR   GO; GO:0015908; P:fatty acid transport; IGI:RGD.
DR   GO; GO:0006629; P:lipid metabolic process; ISO:RGD.
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:0035336; P:long-chain fatty-acyl-CoA metabolic process; IBA:GO_Central.
DR   GO; GO:0030182; P:neuron differentiation; IBA:GO_Central.
DR   GO; GO:0032024; P:positive regulation of insulin secretion; IMP:UniProtKB.
DR   GO; GO:0070672; P:response to interleukin-15; IEP:RGD.
DR   GO; GO:0007584; P:response to nutrient; IEP:RGD.
DR   GO; GO:0019432; P:triglyceride biosynthetic process; IGI:RGD.
DR   CDD; cd17639; LC_FACS_euk1; 1.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR   InterPro; IPR045851; AMP-bd_C_sf.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR   InterPro; IPR042099; ANL_N_sf.
DR   PANTHER; PTHR43272; LONG-CHAIN-FATTY-ACID--COA LIGASE; 1.
DR   PANTHER; PTHR43272:SF22; LONG-CHAIN-FATTY-ACID--COA LIGASE 4; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
DR   Genevisible; O35547; RN.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Cell membrane; Endoplasmic reticulum;
KW   Fatty acid metabolism; Ligase; Lipid metabolism; Magnesium; Membrane;
KW   Microsome; Mitochondrion; Mitochondrion outer membrane; Nucleotide-binding;
KW   Peroxisome; Phosphoprotein; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..711
FT                   /note="Long-chain-fatty-acid--CoA ligase 4"
FT                   /id="PRO_0000193111"
FT   TRANSMEM        8..28
FT                   /note="Helical; Signal-anchor for type III membrane
FT                   protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        29..711
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   MOD_RES         447
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O60488"
FT   VAR_SEQ         1..41
FT                   /note="Missing (in isoform Short)"
FT                   /id="VSP_060224"
SQ   SEQUENCE   711 AA;  79065 MW;  75C7974109681FE8 CRC64;
     MKLKLNVLTI VLLPVHLLIT IYSALIFIPW YFLTNAKKKN AMAKRIKAKP TSDKPGSPYR
     SVTHFDSLAV IDIPGADTLD KLFDHAVAKF GKKDSLGTRE ILSEENEMQP NGKVFKKLIL
     GNYKWINYLE VNCRVNNFGS GLTALGLKPK NTIAIFCETR AEWMIAAQTC FKYNFPLVTL
     YATLGKEAVV HGLNESEASY LITSVELLES KLKAALLDIN CVKHIIYVDN KTINRAEYPE
     GLEIHSMQSV EELGSKPENS SIPPSRPTPS DMAIVMYTSG STGRPKGVMM HHSNLIAGMT
     GQCERIPGLG PKDTYIGYLP LAHVLELTAE ISCFTYGCRI GYSSPLTLSD QSSKIKKGSK
     GDCTVLKPTL MAAVPEIMDR IYKNVMSKVQ EMNYIQKTLF KIGYDYKLEQ IKKGYDAPLC
     NLILFKKVKA LLGGNVRMML SGGAPLSPQT HRFMNVCFCC PIGQGYGLTE SCGAGTVTEV
     TDYTTGRVGA PLICCEIKLK DWQEGGYTVH DKPNPRGEIV IGGQNISMGY FKNEEKTAED
     YSVDENGQRW FCTGDIGEFH PDGCLQIIDR KKDLVKLQAG EYVSLGKVEA ALKNCPLIDN
     ICAFAKSDQS YVISFVVPNQ KKLTLLAQQK GVEGSWVDIC NNPAMEAEIL KEIREAANAM
     KLERFEIPIK VRLSPEPWTP ETGLVTDAFK LKRKELKNHY LKDIERMYGG K
//