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Protein

Long-chain-fatty-acid--CoA ligase 3

Gene

Acsl3

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.By similarity1 Publication

Catalytic activityi

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

Cofactori

Mg2+By similarity

Kineticsi

  1. KM=402 µM for ATP1 Publication
  2. KM=3.0 µM for CoA1 Publication
  3. KM=4.3 µM for palmitate1 Publication
  4. KM=5.1 µM for oleate1 Publication
  5. KM=8.9 µM for arachidonate1 Publication
  1. Vmax=2306 nmol/min/mg enzyme with palmitate as substrate1 Publication
  2. Vmax=2399 nmol/min/mg enzyme with oleate as substrate1 Publication
  3. Vmax=4022 nmol/min/mg enzyme with arachidonate as substrate1 Publication

GO - Molecular functioni

  • acetate-CoA ligase activity Source: RGD
  • ATP binding Source: UniProtKB-KW
  • long-chain fatty acid-CoA ligase activity Source: RGD

GO - Biological processi

  • brain development Source: RGD
  • fatty acid biosynthetic process Source: RGD
  • fatty acid metabolic process Source: RGD
  • lipid metabolic process Source: RGD
  • long-chain fatty acid import Source: Ensembl
  • long-chain fatty acid metabolic process Source: GOC
  • metabolic process Source: RGD
  • positive regulation of Golgi to plasma membrane protein transport Source: Ensembl
  • positive regulation of phosphatidylcholine biosynthetic process Source: Ensembl
  • positive regulation of secretion Source: Ensembl
  • response to nutrient Source: RGD
  • response to organic cyclic compound Source: RGD
  • very-low-density lipoprotein particle assembly Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Keywords - Ligandi

ATP-binding, Magnesium, Nucleotide-binding

Enzyme and pathway databases

BRENDAi6.2.1.3. 5301.
ReactomeiREACT_346713. Synthesis of very long-chain fatty acyl-CoAs.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Acsl3
Synonyms:Acs3, Facl3
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Chromosome 9

Organism-specific databases

RGDi70552. Acsl3.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei21 – 4121Helical; Signal-anchor for type III membrane proteinSequence AnalysisAdd
BLAST
Topological domaini42 – 720679CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Microsome, Mitochondrion, Mitochondrion outer membrane, Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 720720Long-chain-fatty-acid--CoA ligase 3PRO_0000001313Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei683 – 6831PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ63151.
PRIDEiQ63151.

Expressioni

Tissue specificityi

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 stagei

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.

Gene expression databases

GenevisibleiQ63151. RN.

Interactioni

Protein-protein interaction databases

IntActiQ63151. 1 interaction.
STRINGi10116.ENSRNOP00000020161.

Structurei

3D structure databases

ProteinModelPortaliQ63151.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1022.
GeneTreeiENSGT00690000102168.
HOGENOMiHOG000159459.
HOVERGENiHBG106947.
InParanoidiQ63151.
KOiK01897.
OMAiYTTPLCD.
OrthoDBiEOG7P2XRD.
PhylomeDBiQ63151.
TreeFamiTF314012.

Family and domain databases

InterProiIPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamiPF00501. AMP-binding. 1 hit.
[Graphical view]
PROSITEiPS00455. AMP_BINDING. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative initiation. AlignAdd to basket

Isoform Long (identifier: Q63151-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MNNHVSSTPS TMKLKQTIHP ILLYFIHFII SLYTILTYIP FYFLCESKQE
60 70 80 90 100
KPNHIKAKPV SSKPDSAYRS VNSMDGLASV LYPGCDTLDK VFMYAKNKFK
110 120 130 140 150
DKRLLGTREI LNEEDEIQPN GKVFKKVILG HYNWLSYEDV FIRALDFGNG
160 170 180 190 200
LQMLGQKPKA NIAIFCETRA EWMIAAQACF MYNFQLVTLY ATLGGPAIVH
210 220 230 240 250
GLNETEVTNI ITSKELLQTK LKDIVSLVPR LRHIITVDGK PPTWSEFPKG
260 270 280 290 300
VIVHTMAAVQ ALGVKADVDK KAHSKPLPSD IAVIMYTSGS TGIPKGVMIS
310 320 330 340 350
HSNIIASITG MARRIPRLGE EDVYIGYLPL AHVLELSAEL VCLSHGCRIG
360 370 380 390 400
YSSPQTLADQ SSKIKKGSKG DTSVLKPTLM AAVPEIMDRI YKNVMNKVNE
410 420 430 440 450
MSAFQRNLFI LAYNYKMEQI SKGCSTPLCD RFVFRNVRRL LGGNIRVLLC
460 470 480 490 500
GGAPLSATTQ RFMNICFCCP VGQGYGLTES TGAGTITEVW DYNTGRVGAP
510 520 530 540 550
LVCCEIKLKN WEEGGYFNTD KPHPRGEILI GGQNVTMGYY KNEAKTKADF
560 570 580 590 600
FEDENGQRWL CTGDIGEFDP DGCLKIIDRK KDLVKLQAGE YVSLGKVEAA
610 620 630 640 650
LKNLPLIDNI CAYANSYHSY VIGFVVPNQK ELTELARTKG FNGTWEELCN
660 670 680 690 700
SSEMENEVLK VLSEAAISAS LEKFEIPLKI RLSPDPWTPE TGLVTDAFKL
710 720
KRKELKTHYQ ADIERMYGRK
Length:720
Mass (Da):80,458
Last modified:November 1, 1996 - v1
Checksum:i4D79FAEF25ADA527
GO
Isoform Short (identifier: Q63151-2) [UniParc]FASTAAdd to basket

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

Show »
Length:709
Mass (Da):79,302
Checksum:iFD6262C2D2794D6A
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 1111Missing in isoform Short. CuratedVSP_018649Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D30666 mRNA. Translation: BAA06340.1.
RefSeqiNP_476448.1. NM_057107.1. [Q63151-1]
UniGeneiRn.54820.

Genome annotation databases

EnsembliENSRNOT00000020161; ENSRNOP00000020161; ENSRNOG00000014718. [Q63151-1]
GeneIDi114024.
KEGGirno:114024.
UCSCiRGD:70552. rat. [Q63151-1]

Keywords - Coding sequence diversityi

Alternative initiation

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D30666 mRNA. Translation: BAA06340.1.
RefSeqiNP_476448.1. NM_057107.1. [Q63151-1]
UniGeneiRn.54820.

3D structure databases

ProteinModelPortaliQ63151.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ63151. 1 interaction.
STRINGi10116.ENSRNOP00000020161.

Proteomic databases

PaxDbiQ63151.
PRIDEiQ63151.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000020161; ENSRNOP00000020161; ENSRNOG00000014718. [Q63151-1]
GeneIDi114024.
KEGGirno:114024.
UCSCiRGD:70552. rat. [Q63151-1]

Organism-specific databases

CTDi2181.
RGDi70552. Acsl3.

Phylogenomic databases

eggNOGiCOG1022.
GeneTreeiENSGT00690000102168.
HOGENOMiHOG000159459.
HOVERGENiHBG106947.
InParanoidiQ63151.
KOiK01897.
OMAiYTTPLCD.
OrthoDBiEOG7P2XRD.
PhylomeDBiQ63151.
TreeFamiTF314012.

Enzyme and pathway databases

BRENDAi6.2.1.3. 5301.
ReactomeiREACT_346713. Synthesis of very long-chain fatty acyl-CoAs.

Miscellaneous databases

NextBioi618179.
PROiQ63151.

Gene expression databases

GenevisibleiQ63151. RN.

Family and domain databases

InterProiIPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamiPF00501. AMP-binding. 1 hit.
[Graphical view]
PROSITEiPS00455. AMP_BINDING. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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. "Characterization of recombinant long-chain rat acyl-CoA synthetase isoforms 3 and 6: identification of a novel variant of isoform 6."
    Van Horn C.G., Caviglia J.M., Li L.O., Wang S., Granger D.A., Coleman R.A.
    Biochemistry 44:1635-1642(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: BIOPHYSICOCHEMICAL PROPERTIES.
    Tissue: Brain.
  4. "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.

Entry informationi

Entry nameiACSL3_RAT
AccessioniPrimary (citable) accession number: Q63151
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: November 1, 1996
Last modified: July 22, 2015
This is version 132 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

5 rat isozymes encoded by different genes have been described. ACSL6 corresponds to isozyme 2 (ACS2).1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.