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Reviewed, UniProtKB/Swiss-Prot Q63151 (ACSL3_RAT)

Last modified January 19, 2010. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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
    Brain acyl-CoA synthetase II
Gene names
Name: Acsl3
Synonyms: Acs3, Facl3
OrganismRattus norvegicus (Rat)
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 carboxylic 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.

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

Amino acid modifications

Modified residue5931Phosphoserine By similarity
Modified residue6831Phosphoserine By similarity
Modified residue6881Phosphothreonine 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.

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: 8663269] [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: 9276691] [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: 19737935] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D30666 mRNA. Translation: BAA06340.1.
IPIIPI00205908.
IPI00760128.
RefSeqNP_476448.1.
UniGeneRn.54820

3D structure databases

SMRQ63151. Positions 132-711.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ63151.

Genome annotation databases

EnsemblENSRNOT00000020161; ENSRNOP00000020161; ENSRNOG00000014718; Rattus norvegicus. [Genome view]
GeneID114024.
KEGGrno:114024.
NMPDRfig|10116.3.peg.30313.
UCSCNM_057107. rat.

Organism-specific databases

CTD114024.
RGD70552. Acsl3.

Phylogenomic databases

eggNOGroNOG09303.
HOVERGENQ63151.
InParanoidQ63151.
OMANQIKAKP.
OrthoDBEOG9Z0DRH.
PhylomeDBQ63151.

Enzyme and pathway databases

BRENDA6.2.1.3. 248.

Gene expression databases

ArrayExpressQ63151.
GenevestigatorQ63151.
GermOnlineENSRNOG00000014718. Rattus norvegicus.

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 Resources

NextBio618179.

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: January 19, 2010
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents