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O95573 (ACSL3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 127. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Long-chain-fatty-acid--CoA ligase 3

EC=6.2.1.3
Alternative name(s):
Long-chain acyl-CoA synthetase 3
Short name=LACS 3
Gene names
Name:ACSL3
Synonyms:ACS3, FACL3, LACS3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length720 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Acyl-CoA synthetases (ACSL) activates long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. ACSL3 mediates hepatic lipogenesis By similarity. Preferentially uses myristate, laurate, arachidonate and eicosapentaenoate as substrates By similarity. Has mainly an anabolic role in energy metabolism. Required for the incorporation of fatty acids into phosphatidylcholine, the major phospholipid located on the surface of VLDL (very low density lipoproteins). Ref.4

Catalytic activity

ATP + a long-chain fatty acid + CoA = AMP + diphosphate + an acyl-CoA.

Cofactor

Magnesium By similarity.

Subcellular location

Mitochondrion outer membrane; Single-pass type III membrane protein By similarity. Peroxisome membrane; Single-pass type III membrane protein By similarity. Microsome membrane; Single-pass type III membrane protein By similarity. Endoplasmic reticulum membrane; Single-pass type III membrane protein By similarity.

Sequence similarities

Belongs to the ATP-dependent AMP-binding enzyme family.

Ontologies

Keywords
   Biological processFatty acid metabolism
Lipid metabolism
   Cellular componentEndoplasmic reticulum
Membrane
Microsome
Mitochondrion
Mitochondrion outer membrane
Peroxisome
   Coding sequence diversityPolymorphism
   DomainSignal-anchor
Transmembrane
Transmembrane helix
   LigandATP-binding
Magnesium
Nucleotide-binding
   Molecular functionLigase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processbrain development

Inferred from electronic annotation. Source: Ensembl

fatty acid biosynthetic process

Inferred from electronic annotation. Source: Ensembl

long-chain fatty acid import

Inferred from direct assay PubMed 20219900. Source: UniProtKB

positive regulation of Golgi to plasma membrane protein transport

Inferred from mutant phenotype PubMed 20605918. Source: UniProtKB

positive regulation of phosphatidylcholine biosynthetic process

Inferred from mutant phenotype Ref.4. Source: UniProtKB

positive regulation of secretion

Inferred from mutant phenotype Ref.4. Source: UniProtKB

response to nutrient

Inferred from electronic annotation. Source: Ensembl

response to organic cyclic compound

Inferred from electronic annotation. Source: Ensembl

very-low-density lipoprotein particle assembly

Inferred from mutant phenotype Ref.4. Source: UniProtKB

   Cellular_componentGolgi apparatus

Inferred from direct assay PubMed 20605918. Source: UniProtKB

endoplasmic reticulum

Inferred from direct assay PubMed 14741744PubMed 20605918. Source: UniProtKB

endoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

lipid particle

Inferred from direct assay PubMed 14741744PubMed 21498505. Source: UniProtKB

mitochondrial outer membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

perinuclear region of cytoplasm

Inferred from direct assay PubMed 14741744PubMed 20605918. Source: UniProtKB

peroxisomal membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

long-chain fatty acid-CoA ligase activity

Inferred from mutant phenotype PubMed 20219900. Source: UniProtKB

protein domain specific binding

Inferred from physical interaction PubMed 20605918. Source: UniProtKB

protein kinase binding

Inferred from physical interaction PubMed 20605918. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 720720Long-chain-fatty-acid--CoA ligase 3
PRO_0000193107

Regions

Transmembrane21 – 4121Helical; Signal-anchor for type III membrane protein; Potential
Topological domain42 – 720679Cytoplasmic Potential

Amino acid modifications

Modified residue6831Phosphoserine Ref.5

Natural variations

Natural variant5511F → S. Ref.1 Ref.2
Corresponds to variant rs1046032 [ dbSNP | Ensembl ].
VAR_026716

Experimental info

Sequence conflict2461E → D in BAA37142. Ref.1
Sequence conflict2461E → D in BAB72074. Ref.2
Sequence conflict2461E → D in BAB72139. Ref.2

Sequences

Sequence LengthMass (Da)Tools
O95573 [UniParc].

Last modified October 3, 2006. Version 3.
Checksum: AAC4B0B4543EC8DD

FASTA72080,420
        10         20         30         40         50         60 
MNNHVSSKPS TMKLKHTINP ILLYFIHFLI SLYTILTYIP FYFFSESRQE KSNRIKAKPV 

        70         80         90        100        110        120 
NSKPDSAYRS VNSLDGLASV LYPGCDTLDK VFTYAKNKFK NKRLLGTREV LNEEDEVQPN 

       130        140        150        160        170        180 
GKIFKKVILG QYNWLSYEDV FVRAFNFGNG LQMLGQKPKT NIAIFCETRA EWMIAAQACF 

       190        200        210        220        230        240 
MYNFQLVTLY ATLGGPAIVH ALNETEVTNI ITSKELLQTK LKDIVSLVPR LRHIITVDGK 

       250        260        270        280        290        300 
PPTWSEFPKG IIVHTMAAVE ALGAKASMEN QPHSKPLPSD IAVIMYTSGS TGLPKGVMIS 

       310        320        330        340        350        360 
HSNIIAGITG MAERIPELGE EDVYIGYLPL AHVLELSAEL VCLSHGCRIG YSSPQTLADQ 

       370        380        390        400        410        420 
SSKIKKGSKG DTSMLKPTLM AAVPEIMDRI YKNVMNKVSE MSSFQRNLFI LAYNYKMEQI 

       430        440        450        460        470        480 
SKGRNTPLCD SFVFRKVRSL LGGNIRLLLC GGAPLSATTQ RFMNICFCCP VGQGYGLTES 

       490        500        510        520        530        540 
AGAGTISEVW DYNTGRVGAP LVCCEIKLKN WEEGGYFNTD KPHPRGEILI GGQSVTMGYY 

       550        560        570        580        590        600 
KNEAKTKADF FEDENGQRWL CTGDIGEFEP DGCLKIIDRK KDLVKLQAGE YVSLGKVEAA 

       610        620        630        640        650        660 
LKNLPLVDNI CAYANSYHSY VIGFVVPNQK ELTELARKKG LKGTWEELCN SCEMENEVLK 

       670        680        690        700        710        720 
VLSEAAISAS LEKFEIPVKI RLSPEPWTPE TGLVTDAFKL KRKELKTHYQ ADIERMYGRK 

« Hide

References

« Hide 'large scale' references
[1]"Human acyl-coenzyme A synthetase 3 cDNA and localization of its gene (ACS3) to chromosome band 2q34-q35."
Minekura H., Fujino T., Kang M.-J., Fujita T., Endo Y., Yamamoto T.T.
Genomics 42:180-181(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT SER-551.
Tissue: Placenta.
[2]"Genomic organization and transcription units of the human acyl-CoA synthetase 3 gene."
Minekura H., Kang M.-J., Inagaki Y., Suzuki H., Sato H., Fujino T., Yamamoto T.T.
Gene 278:185-192(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], VARIANT SER-551.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Pancreas.
[4]"Long chain acyl-CoA synthetase 3-mediated phosphatidylcholine synthesis is required for assembly of very low density lipoproteins in human hepatoma Huh7 cells."
Yao H., Ye J.
J. Biol. Chem. 283:849-854(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[5]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-683, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[6]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D89053 mRNA. Translation: BAA37142.1.
AB061712 mRNA. Translation: BAB72074.1.
AB061436 Genomic DNA. Translation: BAB72139.1.
BC041692 mRNA. Translation: AAH41692.1.
RefSeqNP_004448.2. NM_004457.3.
NP_976251.1. NM_203372.1.
UniGeneHs.655772.

3D structure databases

ProteinModelPortalO95573.
SMRO95573. Positions 122-641.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108477. 18 interactions.
IntActO95573. 11 interactions.
MINTMINT-4527745.
STRING9606.ENSP00000350012.

Chemistry

DrugBankDB00159. Icosapent.

PTM databases

PhosphoSiteO95573.

Proteomic databases

PaxDbO95573.
PeptideAtlasO95573.
PRIDEO95573.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000357430; ENSP00000350012; ENSG00000123983.
ENST00000392066; ENSP00000375918; ENSG00000123983.
GeneID2181.
KEGGhsa:2181.
UCSCuc002vni.3. human.

Organism-specific databases

CTD2181.
GeneCardsGC02P223725.
HGNCHGNC:3570. ACSL3.
HPAHPA011315.
MIM602371. gene.
neXtProtNX_O95573.
PharmGKBPA27967.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1022.
HOGENOMHOG000159459.
HOVERGENHBG106947.
InParanoidO95573.
KOK01897.
OMAVFMYAKN.
OrthoDBEOG7P2XRD.
PhylomeDBO95573.
TreeFamTF314012.

Enzyme and pathway databases

BioCycMetaCyc:HS04703-MONOMER.
BRENDA6.2.1.3. 2681.
ReactomeREACT_111217. Metabolism.

Gene expression databases

ArrayExpressO95573.
BgeeO95573.
CleanExHS_ACSL3.
GenevestigatorO95573.

Family and domain databases

InterProIPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamPF00501. AMP-binding. 1 hit.
[Graphical view]
PROSITEPS00455. AMP_BINDING. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiACSL3.
GenomeRNAi2181.
NextBio8805.
PROO95573.
SOURCESearch...

Entry information

Entry nameACSL3_HUMAN
AccessionPrimary (citable) accession number: O95573
Secondary accession number(s): Q60I92, Q8IUM9
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: October 3, 2006
Last modified: April 16, 2014
This is version 127 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM