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Q63151 (ACSL3_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 124. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·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):
Brain acyl-CoA synthetase II
Long-chain acyl-CoA synthetase 3
Short name=LACS 3
Gene names
Name:Acsl3
Synonyms:Acs3, Facl3
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

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 is required for the incorporation of fatty acids into phosphatidylcholine, the major phospholipid located on the surface of VLDL (very low density lipoproteins) By similarity. Has mainly an anabolic role in energy metabolism. Mediates hepatic lipogenesis. Preferentially uses myristate, laurate, arachidonate and eicosapentaenoate as substrates. Both isoforms exhibit the same level of activity. Ref.3

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.

Tissue specificity

Predominantly expressed in the brain, and to a much lesser extent, in lung, adrenal gland, kidney, small intestine, and adipose tissue but not detected in heart or liver.

Developmental stage

Detected 5 days after birth, increased to a maximal level at 15 days, and then decreased gradually to 10% of its maximum level in adult.

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 diversityAlternative initiation
   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 expression pattern Ref.1. Source: RGD

fatty acid biosynthetic process

Inferred from direct assay Ref.1. Source: RGD

fatty acid metabolic process

Traceable author statement Ref.1. Source: RGD

lipid metabolic process

Traceable author statement Ref.1. Source: RGD

long-chain fatty acid import

Inferred from electronic annotation. Source: Ensembl

long-chain fatty acid metabolic process

Inferred from direct assay Ref.1. Source: GOC

metabolic process

Traceable author statement Ref.1. Source: RGD

positive regulation of Golgi to plasma membrane protein transport

Inferred from electronic annotation. Source: Ensembl

positive regulation of phosphatidylcholine biosynthetic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of secretion

Inferred from electronic annotation. Source: Ensembl

response to nutrient

Inferred from expression pattern PubMed 16772660. Source: RGD

response to organic cyclic compound

Inferred from expression pattern PubMed 19025659. Source: RGD

very-low-density lipoprotein particle assembly

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentGolgi apparatus

Inferred from electronic annotation. Source: Ensembl

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 electronic annotation. Source: Ensembl

mitochondrial outer membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: Ensembl

peroxisomal membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

acetate-CoA ligase activity

Traceable author statement Ref.1. Source: RGD

long-chain fatty acid-CoA ligase activity

Inferred from direct assay Ref.1. Source: RGD

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative initiation. [Align] [Select]
Isoform Long (identifier: Q63151-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform Short (identifier: Q63151-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-11: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 720720Long-chain-fatty-acid--CoA ligase 3
PRO_0000001313

Regions

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

Amino acid modifications

Modified residue6831Phosphoserine By similarity

Natural variations

Alternative sequence1 – 1111Missing in isoform Short.
VSP_018649

Sequences

Sequence LengthMass (Da)Tools
Isoform Long [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 4D79FAEF25ADA527

FASTA72080,458
        10         20         30         40         50         60 
MNNHVSSTPS TMKLKQTIHP ILLYFIHFII SLYTILTYIP FYFLCESKQE KPNHIKAKPV 

        70         80         90        100        110        120 
SSKPDSAYRS VNSMDGLASV LYPGCDTLDK VFMYAKNKFK DKRLLGTREI LNEEDEIQPN 

       130        140        150        160        170        180 
GKVFKKVILG HYNWLSYEDV FIRALDFGNG LQMLGQKPKA NIAIFCETRA EWMIAAQACF 

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

       250        260        270        280        290        300 
PPTWSEFPKG VIVHTMAAVQ ALGVKADVDK KAHSKPLPSD IAVIMYTSGS TGIPKGVMIS 

       310        320        330        340        350        360 
HSNIIASITG MARRIPRLGE EDVYIGYLPL AHVLELSAEL VCLSHGCRIG YSSPQTLADQ 

       370        380        390        400        410        420 
SSKIKKGSKG DTSVLKPTLM AAVPEIMDRI YKNVMNKVNE MSAFQRNLFI LAYNYKMEQI 

       430        440        450        460        470        480 
SKGCSTPLCD RFVFRNVRRL LGGNIRVLLC GGAPLSATTQ RFMNICFCCP VGQGYGLTES 

       490        500        510        520        530        540 
TGAGTITEVW DYNTGRVGAP LVCCEIKLKN WEEGGYFNTD KPHPRGEILI GGQNVTMGYY 

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

       610        620        630        640        650        660 
LKNLPLIDNI CAYANSYHSY VIGFVVPNQK ELTELARTKG FNGTWEELCN SSEMENEVLK 

       670        680        690        700        710        720 
VLSEAAISAS LEKFEIPLKI RLSPDPWTPE TGLVTDAFKL KRKELKTHYQ ADIERMYGRK 

« Hide

Isoform Short [UniParc].

Checksum: FD6262C2D2794D6A
Show »

FASTA70979,302

References

[1]"Molecular characterization and expression of rat acyl-CoA synthetase 3."
Fujino T., Kang M.-J., Suzuki H., Iijima H., Yamamoto T.T.
J. Biol. Chem. 271:16748-16752(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION.
Strain: Wistar.
Tissue: Brain.
[2]"Alternative translation initiation generates acyl-CoA synthetase 3 isoforms with heterogeneous amino termini."
Fujino T., Kang M.-J., Minekura H., Suzuki H., Yamamoto T.T.
J. Biochem. 122:212-216(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE INITIATION.
[3]"Suppression of long chain acyl-CoA synthetase 3 (ACSL3) decreases hepatic de novo fatty acid synthesis through decreased transcriptional activity."
Bu S.Y., Mashek M.T., Mashek D.G.
J. Biol. Chem. 284:30474-30483(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D30666 mRNA. Translation: BAA06340.1.
RefSeqNP_476448.1. NM_057107.1. [Q63151-1]
XP_006245191.1. XM_006245129.1. [Q63151-1]
UniGeneRn.54820.

3D structure databases

ProteinModelPortalQ63151.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ63151. 1 interaction.
STRING10116.ENSRNOP00000020161.

Proteomic databases

PaxDbQ63151.
PRIDEQ63151.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000020161; ENSRNOP00000020161; ENSRNOG00000014718. [Q63151-1]
GeneID114024.
KEGGrno:114024.
UCSCRGD:70552. rat. [Q63151-1]

Organism-specific databases

CTD2181.
RGD70552. Acsl3.

Phylogenomic databases

eggNOGCOG1022.
GeneTreeENSGT00690000102168.
HOGENOMHOG000159459.
HOVERGENHBG106947.
InParanoidQ63151.
KOK01897.
OMACDRFIFR.
OrthoDBEOG7P2XRD.
PhylomeDBQ63151.
TreeFamTF314012.

Enzyme and pathway databases

BRENDA6.2.1.3. 5301.

Gene expression databases

GenevestigatorQ63151.

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

NextBio618179.
PROQ63151.

Entry information

Entry nameACSL3_RAT
AccessionPrimary (citable) accession number: Q63151
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: November 1, 1996
Last modified: July 9, 2014
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families