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Acsl1 acyl-CoA synthetase long-chain family member 1 [ Rattus norvegicus (Norway rat) ]

Gene ID: 25288, updated on 3-Apr-2024

Summary

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Official Symbol
Acsl1provided by RGD
Official Full Name
acyl-CoA synthetase long-chain family member 1provided by RGD
Primary source
RGD:2015
See related
Ensembl:ENSRNOG00000010633 AllianceGenome:RGD:2015
Gene type
protein coding
RefSeq status
PROVISIONAL
Organism
Rattus norvegicus
Lineage
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Rattus
Also known as
ACS; Acas; COAA; Facl2
Summary
Enables arachidonate-CoA ligase activity; oleoyl-CoA ligase activity; and phytanate-CoA ligase activity. Involved in several processes, including fatty acid metabolic process; long-chain fatty-acyl-CoA biosynthetic process; and positive regulation of long-chain fatty acid import across plasma membrane. Located in bounding membrane of organelle; endoplasmic reticulum; and plasma membrane. Biomarker of obesity. Orthologous to human ACSL1 (acyl-CoA synthetase long chain family member 1). [provided by Alliance of Genome Resources, Apr 2022]
Expression
Biased expression in Liver (RPKM 2227.9), Heart (RPKM 1039.3) and 6 other tissues See more
Orthologs
human mouse all
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Genomic context

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See Acsl1 in Genome Data Viewer
Location:
16q11
Exon count:
27
Annotation release Status Assembly Chr Location
RS_2024_02 current GRCr8 (GCF_036323735.1) 16 NC_086034.1 (52487870..52554110, complement)
RS_2023_06 previous assembly mRatBN7.2 (GCF_015227675.2) 16 NC_051351.1 (45755246..45821541, complement)
106 previous assembly Rnor_6.0 (GCF_000001895.5) 16 NC_005115.4 (48937456..49003898, complement)

Chromosome 16 - NC_086034.1Genomic Context describing neighboring genes Neighboring gene caspase 3 Neighboring gene primase and DNA directed polymerase Neighboring gene centromere protein U Neighboring gene uncharacterized LOC108348397 Neighboring gene uncharacterized LOC120097416 Neighboring gene small nucleolar RNA SNORA26

Genomic regions, transcripts, and products

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Go to nucleotide: Graphics FASTA GenBank

Expression

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  • Project title: A rat RNA-Seq transcriptomic BodyMap across 11 organs and 4 developmental stages
  • Description: 320 RNA samples isolated from 11 organs (adrenal gland, brain, heart, kidney, liver, lung, muscle, spleen, thymus, and testes or uterus) from both sexes of Fischer 344 rats across four developmental stages (2-, 6-, 21-, and 104-weeks-old)
  • BioProject: PRJNA238328
  • Publication: PMID 24510058
  • Analysis date: Mon Jun 6 17:44:12 2016

Bibliography

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Related articles in PubMed

  1. Post-translational modifications of rat liver mitochondrial outer membrane proteins identified by mass spectrometry. Distler AM, et al. Biochim Biophys Acta, 2007 May. PMID 17478130, Free PMC Article
  2. Effect of a hypolipidemic drug, Di (2-ethylhexyl) phthalate, on mRNA-expression associated fatty acid and acetate metabolism in rat tissues. Itsuki-Yoneda A, et al. Biosci Biotechnol Biochem, 2007 Feb. PMID 17284823
  3. Overexpression of rat long chain acyl-coa synthetase 1 alters fatty acid metabolism in rat primary hepatocytes. Li LO, et al. J Biol Chem, 2006 Dec 1. PMID 17028193
  4. Fatty acid handling protein expression in adipose tissue, fatty acid composition of adipose tissue and serum, and markers of insulin resistance. Gertow K, et al. Eur J Clin Nutr, 2006 Dec. PMID 16788709
  5. Effect of starvation on hepatic acyl-CoA synthetase, carnitine palmitoyltransferase-I, and acetyl-CoA carboxylase mRNA levels in rats. Ryu MH, et al. Nutrition, 2005 Apr. PMID 15811777

See all (43) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. MiR-34c promotes hepatic stellate cell activation and Liver Fibrogenesis by suppressing ACSL1 expression.
    Title: MiR-34c promotes hepatic stellate cell activation and Liver Fibrogenesis by suppressing ACSL1 expression.
  2. here we revealed that ACSs (Faa1 and Faa4 in yeast and ACSL1, ACSL4, ACSL5, ACSL6, and ACSVL4 in mammals) are involved in LCB uptake. In addition, we provided important insight into the molecular mechanism of LCFA transport
    Title: Long-chain bases of sphingolipids are transported into cells via the acyl-CoA synthetases.
  3. Acyl-CoA synthetase 1 deficiency alters cardiolipin species and impairs mitochondrial function
    Title: Acyl-CoA synthetase 1 deficiency alters cardiolipin species and impairs mitochondrial function.
  4. Acsl isozymes play distinct roles in the control of AA remodeling in rat fibroblasts: Acsl4 acts as the first step of enzyme for AA remodeling following IL-1beta stimulation, and Acsl1 is involved in the maintenance of some AA-containing PC species.
    Title: Role of long-chain acyl-coenzyme A synthetases in the regulation of arachidonic acid metabolism in interleukin 1β-stimulated rat fibroblasts.
  5. rat long chain acyl-coa synthetase 1 has a role in fatty acid metabolism in rat primary hepatocytes
    Title: Overexpression of rat long chain acyl-coa synthetase 1 alters fatty acid metabolism in rat primary hepatocytes.
  6. The fatty metabolism is stimulated in the CNS during a chronic pain state.
    Title: Up-regulation of fatty acid metabolizing-enzymes mRNA in rat spinal cord during persistent peripheral local inflammation.
  7. Long-chain acyl-CoenzymeA synthetase-2 expression is significantly upregulated in distinct regions of the frontal cortex in learned helpless rats relative to controls
    Title: Long-chain acyl-CoenzymeA synthetase-2 mRNA: increased cerebral cortex expression in an animal model of depression.
  8. Acyl-CoA synthetase 2 has a role in fatty acid internalization and neurite outgrowth
    Title: Acyl-CoA synthetase 2 overexpression enhances fatty acid internalization and neurite outgrowth.
Submit: New GeneRIF Correction

Pathways from PubChem

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Interactions

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Products Interactant Other Gene Complex Source Pubs Description

General gene information

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Markers

Homology

Gene Ontology Provided by RGD

Function Evidence Code Pubs
enables ATP binding IEA
Inferred from Electronic Annotation
more info
  
enables acetate-CoA ligase activity TAS
Traceable Author Statement
more info
 PubMed 
enables arachidonate-CoA ligase activity IBA
Inferred from Biological aspect of Ancestor
more info
  
enables arachidonate-CoA ligase activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables long-chain fatty acid-CoA ligase activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables long-chain fatty acid-CoA ligase activity IEA
Inferred from Electronic Annotation
more info
  
enables long-chain fatty acid-CoA ligase activity ISO
Inferred from Sequence Orthology
more info
  
enables oleoyl-CoA ligase activity IMP
Inferred from Mutant Phenotype
more info
 PubMed 
enables phytanate-CoA ligase activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables pristanate-CoA ligase activity IEA
Inferred from Electronic Annotation
more info
  
enables protein serine/threonine kinase activator activity ISO
Inferred from Sequence Orthology
more info
  
Process Evidence Code Pubs
acts_upstream_of_or_within adiponectin-activated signaling pathway ISO
Inferred from Sequence Orthology
more info
  
involved_in fatty acid metabolic process IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in fatty acid transport IGI
Inferred from Genetic Interaction
more info
 PubMed 
involved_in fatty acid transport ISO
Inferred from Sequence Orthology
more info
  
involved_in lipid biosynthetic process IEA
Inferred from Electronic Annotation
more info
  
involved_in lipid biosynthetic process ISO
Inferred from Sequence Orthology
more info
  
involved_in long-chain fatty acid import into cell IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in long-chain fatty acid import into cell ISO
Inferred from Sequence Orthology
more info
  
involved_in long-chain fatty acid metabolic process IBA
Inferred from Biological aspect of Ancestor
more info
  
involved_in long-chain fatty acid metabolic process IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in long-chain fatty acid metabolic process IEA
Inferred from Electronic Annotation
more info
  
involved_in long-chain fatty acid metabolic process ISO
Inferred from Sequence Orthology
more info
  
involved_in long-chain fatty acid metabolic process ISS
Inferred from Sequence or Structural Similarity
more info
  
involved_in long-chain fatty-acyl-CoA biosynthetic process IBA
Inferred from Biological aspect of Ancestor
more info
  
involved_in long-chain fatty-acyl-CoA biosynthetic process IGI
Inferred from Genetic Interaction
more info
 PubMed 
involved_in positive regulation of cold-induced thermogenesis ISO
Inferred from Sequence Orthology
more info
  
involved_in positive regulation of cold-induced thermogenesis ISS
Inferred from Sequence or Structural Similarity
more info
 PubMed 
involved_in positive regulation of long-chain fatty acid import across plasma membrane IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in response to nutrient IEP
Inferred from Expression Pattern
more info
 PubMed 
involved_in response to oleic acid IEP
Inferred from Expression Pattern
more info
 PubMed 
involved_in response to organic cyclic compound IEP
Inferred from Expression Pattern
more info
 PubMed 
involved_in response to organic substance IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in response to xenobiotic stimulus IEP
Inferred from Expression Pattern
more info
 PubMed 
involved_in triglyceride biosynthetic process IGI
Inferred from Genetic Interaction
more info
 PubMed 
involved_in very long-chain fatty acid metabolic process IBA
Inferred from Biological aspect of Ancestor
more info
  
involved_in very long-chain fatty acid metabolic process IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in xenobiotic catabolic process IDA
Inferred from Direct Assay
more info
 PubMed 
Component Evidence Code Pubs
is_active_in endoplasmic reticulum IBA
Inferred from Biological aspect of Ancestor
more info
  
located_in endoplasmic reticulum ISO
Inferred from Sequence Orthology
more info
  
located_in endoplasmic reticulum membrane IEA
Inferred from Electronic Annotation
more info
  
is_active_in membrane IBA
Inferred from Biological aspect of Ancestor
more info
  
located_in mitochondrial outer membrane IDA
Inferred from Direct Assay
more info
 PubMed 
located_in mitochondrial outer membrane IEA
Inferred from Electronic Annotation
more info
  
located_in mitochondrion IDA
Inferred from Direct Assay
more info
 PubMed 
located_in mitochondrion IMP
Inferred from Mutant Phenotype
more info
 PubMed 
located_in mitochondrion ISO
Inferred from Sequence Orthology
more info
  
located_in peroxisomal membrane IDA
Inferred from Direct Assay
more info
 PubMed 

General protein information

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Preferred Names
long-chain-fatty-acid--CoA ligase 1
Names
Acyl CoA synthetase, long chain
LACS 1
arachidonate--CoA ligase
fatty acid Coenzyme A ligase, long chain 2
long-chain acyl-CoA synthetase 1
long-chain-fatty-acid--CoA ligase, liver isozyme
phytanate--CoA ligase
NP_036952.1
XP_006253184.1
XP_006253185.1
XP_006253186.1
XP_006253187.1
XP_006253188.1
XP_006253189.1
XP_038950128.1
XP_063131127.1
XP_063131128.1
XP_063131129.1
XP_063131130.1
XP_063131132.1

NCBI Reference Sequences (RefSeq)

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RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

mRNA and Protein(s)

  1. NM_012820.2 → NP_036952.1  long-chain-fatty-acid--CoA ligase 1

    See identical proteins and their annotated locations for NP_036952.1

    Status: PROVISIONAL

    Source sequence(s)
    JAXUCZ010000016
    UniProtKB/Swiss-Prot
    P18163
    UniProtKB/TrEMBL
    A6JPN3, A6JPN4
    Conserved Domains (1) summary
    cd05927
    Location:117 → 695
    LC-FACS_euk; Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS)

RefSeqs of Annotated Genomes: GCF_036323735.1-RS_2024_02

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference GRCr8

Genomic

  1. NC_086034.1 Reference GRCr8

    Range
    52487870..52554110 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. XM_039094200.2 → XP_038950128.1  long-chain-fatty-acid--CoA ligase 1 isoform X2

    UniProtKB/TrEMBL
    A6JPN4
    Conserved Domains (1) summary
    cd05927
    Location:117 → 661
    LC-FACS_euk; Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS)

  2. XM_006253123.3 → XP_006253185.1  long-chain-fatty-acid--CoA ligase 1 isoform X1

    See identical proteins and their annotated locations for XP_006253185.1

    UniProtKB/Swiss-Prot
    P18163
    UniProtKB/TrEMBL
    A6JPN3, A6JPN4
    Related
    ENSRNOP00000014235.1
    Conserved Domains (1) summary
    cd05927
    Location:117 → 695
    LC-FACS_euk; Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS)

  3. XM_063275058.1 → XP_063131128.1  long-chain-fatty-acid--CoA ligase 1 isoform X2

  4. XM_006253122.3 → XP_006253184.1  long-chain-fatty-acid--CoA ligase 1 isoform X1

    See identical proteins and their annotated locations for XP_006253184.1

    UniProtKB/Swiss-Prot
    P18163
    UniProtKB/TrEMBL
    A6JPN3, A6JPN4
    Conserved Domains (1) summary
    cd05927
    Location:117 → 695
    LC-FACS_euk; Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS)

  5. XM_006253125.5 → XP_006253187.1  long-chain-fatty-acid--CoA ligase 1 isoform X1

    See identical proteins and their annotated locations for XP_006253187.1

    UniProtKB/Swiss-Prot
    P18163
    UniProtKB/TrEMBL
    A6JPN3, A6JPN4
    Conserved Domains (1) summary
    cd05927
    Location:117 → 695
    LC-FACS_euk; Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS)

  6. XM_063275060.1 → XP_063131130.1  long-chain-fatty-acid--CoA ligase 1 isoform X2

  7. XM_063275062.1 → XP_063131132.1  long-chain-fatty-acid--CoA ligase 1 isoform X3

    UniProtKB/TrEMBL
    A0A8L2R6L8

  8. XM_006253126.4 → XP_006253188.1  long-chain-fatty-acid--CoA ligase 1 isoform X1

    See identical proteins and their annotated locations for XP_006253188.1

    UniProtKB/Swiss-Prot
    P18163
    UniProtKB/TrEMBL
    A6JPN3, A6JPN4
    Conserved Domains (1) summary
    cd05927
    Location:117 → 695
    LC-FACS_euk; Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS)

  9. XM_006253127.1 → XP_006253189.1  long-chain-fatty-acid--CoA ligase 1 isoform X1

    See identical proteins and their annotated locations for XP_006253189.1

    UniProtKB/Swiss-Prot
    P18163
    UniProtKB/TrEMBL
    A6JPN3, A6JPN4
    Conserved Domains (1) summary
    cd05927
    Location:117 → 695
    LC-FACS_euk; Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS)

  10. XM_006253124.4 → XP_006253186.1  long-chain-fatty-acid--CoA ligase 1 isoform X1

    See identical proteins and their annotated locations for XP_006253186.1

    UniProtKB/Swiss-Prot
    P18163
    UniProtKB/TrEMBL
    A6JPN3, A6JPN4
    Conserved Domains (1) summary
    cd05927
    Location:117 → 695
    LC-FACS_euk; Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS)

  11. XM_063275059.1 → XP_063131129.1  long-chain-fatty-acid--CoA ligase 1 isoform X2

  12. XM_063275057.1 → XP_063131127.1  long-chain-fatty-acid--CoA ligase 1 isoform X1

    UniProtKB/Swiss-Prot
    P18163
    UniProtKB/TrEMBL
    A6JPN3
Nucleotide Protein Strain
Heading Accession and Version
Protein Accession Links
GenPept Link UniProtKB Link
P18163.1 GenPept UniProtKB/Swiss-Prot:P18163

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