ACSL3 acyl-CoA synthetase long chain family member 3 [Homo sapiens (human)] - Gene

Summary

Official Symbol: ACSL3provided by HGNC
Official Full Name: acyl-CoA synthetase long chain family member 3provided by HGNC
Primary source: HGNC:HGNC:3570
See related: Ensembl:ENSG00000123983 MIM:602371; AllianceGenome:HGNC:3570
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Homo sapiens
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo
Also known as: ACS3; FACL3; LACS3; LACS 3; PRO2194
Summary: The protein encoded by this gene is an isozyme of the long-chain fatty-acid-coenzyme A ligase family. Although differing in substrate specificity, subcellular localization, and tissue distribution, all isozymes of this family convert free long-chain fatty acids into fatty acyl-CoA esters, and thereby play a key role in lipid biosynthesis and fatty acid degradation. This isozyme is highly expressed in brain, and preferentially utilizes myristate, arachidonate, and eicosapentaenoate as substrates. The amino acid sequence of this isozyme is 92% identical to that of rat homolog. Two transcript variants encoding the same protein have been found for this gene. [provided by RefSeq, Jul 2008]
Expression: Ubiquitous expression in prostate (RPKM 44.8), brain (RPKM 31.0) and 24 other tissues See more
Orthologs: mouse all
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Genomic context

Location:: 2q36.1

Exon count:: 17

Annotation release	Status	Assembly	Chr	Location
RS_2024_08	current	GRCh38.p14 (GCF_000001405.40)	2	NC_000002.12 (222861036..222944639)
RS_2024_08	current	T2T-CHM13v2.0 (GCF_009914755.1)	2	NC_060926.1 (223346613..223427414)
RS_2024_09	previous assembly	GRCh37.p13 (GCF_000001405.25)	2	NC_000002.11 (223725754..223809357)

Chromosome 2 - NC_000002.12 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Expression

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See details

Project title: HPA RNA-seq normal tissues HPA RNA-seq normal tissues
Description: RNA-seq was performed of tissue samples from 95 human individuals representing 27 different tissues in order to determine tissue-specificity of all protein-coding genes
BioProject: PRJEB4337
Publication: PMID 24309898
Analysis date: Wed Apr 4 07:08:55 2018

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

[Research advances on the role of ACSL3 in the atherosclerosis].
Title: [Research advances on the role of ACSL3 in the atherosclerosis].
Activation of MAT2A-ACSL3 pathway protects cells from ferroptosis in gastric cancer.
Title: Activation of MAT2A-ACSL3 pathway protects cells from ferroptosis in gastric cancer.
Metabolic enzyme ACSL3 is a prognostic biomarker and correlates with anticancer effectiveness of statins in non-small cell lung cancer.
Title: Metabolic enzyme ACSL3 is a prognostic biomarker and correlates with anticancer effectiveness of statins in non-small cell lung cancer.
Immunohistochemical staining reveals differential expression of ACSL3 and ACSL4 in hepatocellular carcinoma and hepatic gastrointestinal metastases.
Title: Immunohistochemical staining reveals differential expression of ACSL3 and ACSL4 in hepatocellular carcinoma and hepatic gastrointestinal metastases.
The ACSL3-LPIAT1 signaling drives prostaglandin synthesis in non-small cell lung cancer.
Title: The ACSL3-LPIAT1 signaling drives prostaglandin synthesis in non-small cell lung cancer.
ACSL3 distribution closely overlapped with proteins involved in trafficking from the trans-Golgi network and endosomes. In contrast, the ACSL4 localisation pattern more closely followed that of calnexin which is an endoplasmic reticulum resident chaperone.
Title: The endogenous subcellular localisations of the long chain fatty acid-activating enzymes ACSL3 and ACSL4 in sarcoma and breast cancer cells.
Subcellular fractionation showed that at least 68% of ACSL3 remain at the ER even during extensive fatty acid supplementation. High resolution single molecule microscopy confirmed the abundance of cytoplasmic ACSL3 outside of LDs.
Title: The metabolic capacity of lipid droplet localized acyl-CoA synthetase 3 is not sufficient to support local triglyceride synthesis independent of the endoplasmic reticulum in A431 cells.
ACSL3 is essential for mutant KRAS lung cancer tumorigenesis in vivo and is highly expressed in human lung cancer
Title: Fatty Acid Oxidation Mediated by Acyl-CoA Synthetase Long Chain 3 Is Required for Mutant KRAS Lung Tumorigenesis.
Study shows that ACSL3 contributes to intratumoral steroidogenesis by modulating the steroidogenic genes and plays an important role in the growth of castration-resistant prostate cancer.
Title: ACSL3 promotes intratumoral steroidogenesis in prostate cancer cells.
ACLS4 and ACLS3 have roles in insulin secretion
Title: Characterization of Acyl-CoA synthetase isoforms in pancreatic beta cells: Gene silencing shows participation of ACSL3 and ACSL4 in insulin secretion.

Submit: New GeneRIF Correction See all GeneRIFs (23)

Phenotypes

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Find tests for this gene in the NIH Genetic Testing Registry (GTR)

Review eQTL and phenotype association data in this region using PheGenI

Variation

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See Variation Viewer (GRCh37.p13)

HIV-1 interactions

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Protein interactions

Protein	Gene	Interaction	Pubs
Envelope surface glycoprotein gp120	env	Tandem affinity purification and mass spectrometry analysis identify acyl-CoA synthetase long-chain family member 3 (ACSL3), HIV-1 Gag, Gag/Pol, gp120, and Nef incorporated into staufen1 RNP complexes isolated from HIV-1-expressing cells	PubMed
Gag-Pol	gag-pol	Tandem affinity purification and mass spectrometry analysis identify acyl-CoA synthetase long-chain family member 3 (ACSL3), HIV-1 Gag, Gag/Pol, gp120, and Nef incorporated into staufen1 RNP complexes isolated from HIV-1-expressing cells	PubMed
Nef	nef	Tandem affinity purification and mass spectrometry analysis identify acyl-CoA synthetase long-chain family member 3 (ACSL3), HIV-1 Gag, Gag/Pol, gp120, and Nef incorporated into staufen1 RNP complexes isolated from HIV-1-expressing cells	PubMed
Pr55(Gag)	gag	Tandem affinity purification and mass spectrometry analysis identify acyl-CoA synthetase long-chain family member 3 (ACSL3), HIV-1 Gag, Gag/Pol, gp120, and Nef incorporated into staufen1 RNP complexes isolated from HIV-1-expressing cells	PubMed
Vpu	vpu	HIV-1 Vpu is identified to have a physical interaction with acyl-CoA synthetase long-chain family member 3 (ACSL3) in human HEK293 and/or Jurkat cell lines by using affinity tagging and purification mass spectrometry analyses	PubMed

Go to the HIV-1, Human Interaction Database

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

RH80004 (e-PCR)
- UniSTS:91152

RH35858 (e-PCR)
- UniSTS:37920

ACSL3_3368 (e-PCR)
- UniSTS:468271

D2S130 (e-PCR)
- UniSTS:35887

A008B44 (e-PCR)
- UniSTS:43319

SHGC-36164 (e-PCR)
- UniSTS:11576

STS-N59230 (e-PCR)
- UniSTS:37948

D2S130 (e-PCR)
- UniSTS:7245

RH92846 (e-PCR)
- UniSTS:92259

RH69969 (e-PCR)
- UniSTS:55401

WI-21901 (e-PCR)
- UniSTS:43208

RH65698 (e-PCR)
- UniSTS:26327

Gene Ontology Provided by GOA

Function	Evidence Code	Pubs
enables ATP binding	IEA Inferred from Electronic Annotation more info
enables arachidonate-CoA ligase activity	ISS Inferred from Sequence or Structural Similarity more info
enables long-chain fatty acid-CoA ligase activity	IBA Inferred from Biological aspect of Ancestor more info
enables long-chain fatty acid-CoA ligase activity	IMP Inferred from Mutant Phenotype more info	PubMed
enables long-chain fatty acid-CoA ligase activity	ISS Inferred from Sequence or Structural Similarity more info
enables long-chain fatty acid-CoA ligase activity	TAS Traceable Author Statement more info
enables medium-chain fatty acid-CoA ligase activity	IEA Inferred from Electronic Annotation more info
enables palmitoyl-CoA ligase activity	TAS Traceable Author Statement more info
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables protein domain specific binding	IPI Inferred from Physical Interaction more info	PubMed
enables protein kinase binding	IPI Inferred from Physical Interaction more info	PubMed

Process	Evidence Code	Pubs
involved_in fatty acid metabolic process	TAS Traceable Author Statement more info
acts_upstream_of long-chain fatty acid import into cell	IDA Inferred from Direct Assay more info	PubMed
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	IMP Inferred from Mutant Phenotype more info	PubMed
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	TAS Traceable Author Statement more info
involved_in long-chain fatty-acyl-CoA metabolic process	IBA Inferred from Biological aspect of Ancestor more info
involved_in neuron differentiation	IBA Inferred from Biological aspect of Ancestor more info
involved_in positive regulation of Golgi to plasma membrane protein transport	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in positive regulation of phosphatidylcholine biosynthetic process	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in positive regulation of secretion	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in very-low-density lipoprotein particle assembly	IMP Inferred from Mutant Phenotype more info	PubMed

Component	Evidence Code	Pubs
located_in Golgi apparatus	IDA Inferred from Direct Assay more info	PubMed
is_active_in endoplasmic reticulum	IBA Inferred from Biological aspect of Ancestor more info
located_in endoplasmic reticulum	IDA Inferred from Direct Assay more info	PubMed
located_in endoplasmic reticulum membrane	TAS Traceable Author Statement more info
is_active_in lipid droplet	IBA Inferred from Biological aspect of Ancestor more info
located_in lipid droplet	IDA Inferred from Direct Assay more info	PubMed
located_in membrane	HDA more info	PubMed
located_in mitochondrial outer membrane	TAS Traceable Author Statement more info
located_in perinuclear region of cytoplasm	IDA Inferred from Direct Assay more info	PubMed
located_in peroxisomal membrane	IEA Inferred from Electronic Annotation more info
is_active_in plasma membrane	IBA Inferred from Biological aspect of Ancestor more info

General protein information

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Preferred Names: fatty acid CoA ligase Acsl3

Names: arachidonate--CoA ligase; fatty-acid-Coenzyme A ligase, long-chain 3; lignoceroyl-CoA synthase; long-chain acyl-CoA synthetase 3; long-chain-fatty-acid--CoA ligase 3; medium-chain acyl-CoA ligase Acsl3

NP_001341087.1

EC 6.2.1.15

EC 6.2.1.2

EC 6.2.1.3

NP_001341088.1

EC 6.2.1.15

EC 6.2.1.2

EC 6.2.1.3

NP_004448.2

EC 6.2.1.15

EC 6.2.1.2

EC 6.2.1.3

NP_976251.1

EC 6.2.1.15

EC 6.2.1.2

EC 6.2.1.3

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)

NM_001354158.2 → NP_001341087.1 fatty acid CoA ligase Acsl3

Status: REVIEWED

Source sequence(s)

AC013476, AC016712

Consensus CDS

CCDS2455.1

UniProtKB/Swiss-Prot

O95573, Q60I92, Q8IUM9

UniProtKB/TrEMBL

B2RBE0

Related

ENSP00000505793.1, ENST00000680395.1

Conserved Domains (1) summary

cl17068
Location:30 → 717

AFD_class_I; Adenylate forming domain, Class I superfamily
NM_001354159.2 → NP_001341088.1 fatty acid CoA ligase Acsl3

Status: REVIEWED

Source sequence(s)

AC013476, AC016712

Consensus CDS

CCDS2455.1

UniProtKB/Swiss-Prot

O95573, Q60I92, Q8IUM9

UniProtKB/TrEMBL

B2RBE0

Related

ENSP00000505400.1, ENST00000680251.1

Conserved Domains (1) summary

cl17068
Location:30 → 717

AFD_class_I; Adenylate forming domain, Class I superfamily
NM_004457.5 → NP_004448.2 fatty acid CoA ligase Acsl3

See identical proteins and their annotated locations for NP_004448.2

Status: REVIEWED

Source sequence(s)

AC013476, BC041692

Consensus CDS

CCDS2455.1

UniProtKB/Swiss-Prot

O95573, Q60I92, Q8IUM9

UniProtKB/TrEMBL

B2RBE0

Related

ENSP00000350012.3, ENST00000357430.8

Conserved Domains (1) summary

cl17068
Location:30 → 717

AFD_class_I; Adenylate forming domain, Class I superfamily
NM_203372.3 → NP_976251.1 fatty acid CoA ligase Acsl3

See identical proteins and their annotated locations for NP_976251.1

Status: REVIEWED

Source sequence(s)

AC013476, AC016712

Consensus CDS

CCDS2455.1

UniProtKB/Swiss-Prot

O95573, Q60I92, Q8IUM9

UniProtKB/TrEMBL

B2RBE0

Related

ENSP00000375918.3, ENST00000392066.7

Conserved Domains (1) summary

cl17068
Location:30 → 717

AFD_class_I; Adenylate forming domain, Class I superfamily