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Protein

Long-chain-fatty-acid--CoA ligase 1

Gene

Acsl1

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

Functioni

Activation of long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. Preferentially uses oleate, arachidonate, eicosapentaenoate and docosahexaenoate as substrates.

Catalytic activityi

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

Cofactori

Kineticsi

  1. KM=649 µM for ATP1 Publication
  2. KM=6.4 µM for CoA1 Publication
  3. KM=5.0 µM for palmitate1 Publication

Vmax=1695 nmol/min/mg enzyme with palmitate as substrate1 Publication

GO - Molecular functioni

  1. acetate-CoA ligase activity Source: RGD
  2. ATP binding Source: UniProtKB-KW
  3. long-chain fatty acid-CoA ligase activity Source: UniProtKB

GO - Biological processi

  1. adiponectin-activated signaling pathway Source: Ensembl
  2. fatty acid metabolic process Source: RGD
  3. fatty acid transport Source: RGD
  4. lipid biosynthetic process Source: Ensembl
  5. lipid metabolic process Source: RGD
  6. long-chain fatty acid import Source: Ensembl
  7. positive regulation of protein serine/threonine kinase activity Source: Ensembl
  8. response to drug Source: RGD
  9. response to nutrient Source: RGD
  10. response to oleic acid Source: RGD
  11. response to organic cyclic compound Source: RGD
  12. response to organic substance Source: RGD
  13. triglyceride metabolic process Source: RGD
  14. xenobiotic catabolic process Source: RGD
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

BioCyciMetaCyc:MONOMER-14442.
BRENDAi6.2.1.3. 5301.
ReactomeiREACT_285313. PPARA activates gene expression.
REACT_288124. Linoleic acid (LA) metabolism.
REACT_298905. alpha-linolenic acid (ALA) metabolism.
REACT_346713. Synthesis of very long-chain fatty acyl-CoAs.
SABIO-RKP18163.

Names & Taxonomyi

Protein namesi
Recommended name:
Long-chain-fatty-acid--CoA ligase 1 (EC:6.2.1.3)
Alternative name(s):
Long-chain acyl-CoA synthetase 1
Short name:
LACS 1
Long-chain-fatty-acid--CoA ligase, liver isozyme
Gene namesi
Name:Acsl1
Synonyms:Acs1, Acsl2, Facl2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Chromosome 16

Organism-specific databases

RGDi2015. Acsl1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei25 – 4521Helical; Signal-anchor for type III membrane proteinSequence AnalysisAdd
BLAST
Topological domaini46 – 699654CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum Source: RGD
  2. endoplasmic reticulum membrane Source: UniProtKB-SubCell
  3. integral component of membrane Source: UniProtKB-KW
  4. mitochondrial outer membrane Source: RGD
  5. peroxisomal membrane Source: HGNC
  6. plasma membrane Source: RGD
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 – 699699Long-chain-fatty-acid--CoA ligase 1PRO_0000193106Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei9 – 91Nitrated tyrosine1 Publication
Modified residuei85 – 851Phosphotyrosine1 Publication
Modified residuei86 – 861Nitrated tyrosine1 Publication
Glycosylationi136 – 1361O-linked (GlcNAc)1 Publication
Modified residuei208 – 2081N6-acetyllysineBy similarity
Modified residuei357 – 3571N6-acetyllysineBy similarity
Modified residuei387 – 3871N6-acetyllysineBy similarity
Modified residuei621 – 6211PhosphoserineBy similarity
Modified residuei633 – 6331N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation, Glycoprotein, Nitration, Phosphoprotein

Proteomic databases

PaxDbiP18163.
PRIDEiP18163.

PTM databases

PhosphoSiteiP18163.

Expressioni

Tissue specificityi

Liver, heart, epididymal adipose and to a lesser extent brain, small intestine and lung.

Developmental stagei

Levels remain constant during development.

Inductioni

By high fat and high carbohydrate diets.

Gene expression databases

GenevestigatoriP18163.

Interactioni

Protein-protein interaction databases

IntActiP18163. 28 interactions.
MINTiMINT-4570488.
STRINGi10116.ENSRNOP00000014235.

Structurei

3D structure databases

ProteinModelPortaliP18163.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1022.
GeneTreeiENSGT00690000101725.
HOGENOMiHOG000159459.
HOVERGENiHBG050452.
InParanoidiP18163.
KOiK01897.
OMAiQENKCLT.
OrthoDBiEOG71CFKN.
PhylomeDBiP18163.
TreeFamiTF313877.

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]

Sequencei

Sequence statusi: Complete.

P18163-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEVHELFRYF RMPELIDIRQ YVRTLPTNTL MGFGAFAALT TFWYATRPKA
60 70 80 90 100
LKPPCDLSMQ SVEVTGTTEG VRRSAVLEDD KLLLYYYDDV RTMYDGFQRG
110 120 130 140 150
IQVSNDGPCL GSRKPNQPYE WISYKQVAEM AECIGSALIQ KGFKPCSEQF
160 170 180 190 200
IGIFSQNRPE WVTIEQGCFT YSMVVVPLYD TLGTDAITYI VNKAELSVIF
210 220 230 240 250
ADKPEKAKLL LEGVENKLTP CLKIIVIMDS YDNDLVERGQ KCGVEIIGLK
260 270 280 290 300
ALEDLGRVNR TKPKPPEPED LAIICFTSGT TGNPKGAMVT HQNIMNDCSG
310 320 330 340 350
FIKATESAFI ASPEDVLISF LPLAHMFETV VECVMLCHGA KIGFFQGDIR
360 370 380 390 400
LLMDDLKVLQ PTIFPVVPRL LNRMFDRIFG QANTSVKRWL LDFASKRKEA
410 420 430 440 450
ELRSGIVRNN SLWDKLIFHK IQSSLGGKVR LMITGAAPVS ATVLTFLRAA
460 470 480 490 500
LGCQFYEGYG QTECTAGCCL SLPGDWTAGH VGAPMPCNYI KLVDVEDMNY
510 520 530 540 550
QAAKGEGEVC VKGANVFKGY LKDPARTAEA LDKDGWLHTG DIGKWLPNGT
560 570 580 590 600
LKIIDRKKHI FKLAQGEYIA PEKIENIYLR SEAVAQVFVH GESLQAFLIA
610 620 630 640 650
IVVPDVEILP SWAQKRGFQG SFEELCRNKD INKAILEDMV KLGKNAGLKP
660 670 680 690
FEQVKGIAVH PELFSIDNGL LTPTLKAKRP ELRNYFRSQI DELYSTIKI
Length:699
Mass (Da):78,179
Last modified:November 1, 1990 - v1
Checksum:i6E1EACE0EAE8A85C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D90109 mRNA. Translation: BAA14136.1.
PIRiA36275.
RefSeqiNP_036952.1. NM_012820.1.
XP_006253184.1. XM_006253122.1.
XP_006253185.1. XM_006253123.1.
XP_006253186.1. XM_006253124.2.
XP_006253187.1. XM_006253125.2.
XP_006253188.1. XM_006253126.1.
XP_006253189.1. XM_006253127.1.
XP_008769476.1. XM_008771254.1.
UniGeneiRn.6215.

Genome annotation databases

EnsembliENSRNOT00000014235; ENSRNOP00000014235; ENSRNOG00000010633.
GeneIDi25288.
KEGGirno:25288.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D90109 mRNA. Translation: BAA14136.1.
PIRiA36275.
RefSeqiNP_036952.1. NM_012820.1.
XP_006253184.1. XM_006253122.1.
XP_006253185.1. XM_006253123.1.
XP_006253186.1. XM_006253124.2.
XP_006253187.1. XM_006253125.2.
XP_006253188.1. XM_006253126.1.
XP_006253189.1. XM_006253127.1.
XP_008769476.1. XM_008771254.1.
UniGeneiRn.6215.

3D structure databases

ProteinModelPortaliP18163.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP18163. 28 interactions.
MINTiMINT-4570488.
STRINGi10116.ENSRNOP00000014235.

PTM databases

PhosphoSiteiP18163.

Proteomic databases

PaxDbiP18163.
PRIDEiP18163.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000014235; ENSRNOP00000014235; ENSRNOG00000010633.
GeneIDi25288.
KEGGirno:25288.

Organism-specific databases

CTDi2180.
RGDi2015. Acsl1.

Phylogenomic databases

eggNOGiCOG1022.
GeneTreeiENSGT00690000101725.
HOGENOMiHOG000159459.
HOVERGENiHBG050452.
InParanoidiP18163.
KOiK01897.
OMAiQENKCLT.
OrthoDBiEOG71CFKN.
PhylomeDBiP18163.
TreeFamiTF313877.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-14442.
BRENDAi6.2.1.3. 5301.
ReactomeiREACT_285313. PPARA activates gene expression.
REACT_288124. Linoleic acid (LA) metabolism.
REACT_298905. alpha-linolenic acid (ALA) metabolism.
REACT_346713. Synthesis of very long-chain fatty acyl-CoAs.
SABIO-RKP18163.

Miscellaneous databases

NextBioi606025.
PROiP18163.

Gene expression databases

GenevestigatoriP18163.

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. "Structure and regulation of rat long-chain acyl-CoA synthetase."
    Suzuki H., Kawarabayasi Y., Kondo J., Abe T., Nishikawa K., Kimura S., Hashimoto T., Yamamoto T.
    J. Biol. Chem. 265:8681-8685(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    Strain: Wistar.
    Tissue: Liver.
  2. "Post-translational modifications of rat liver mitochondrial outer membrane proteins identified by mass spectrometry."
    Distler A.M., Kerner J., Hoppel C.L.
    Biochim. Biophys. Acta 1774:628-636(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-19; 82-91 AND 628-641, ACETYLATION AT MET-1 AND LYS-633, NITRATION AT TYR-9 AND TYR-86, PHOSPHORYLATION AT TYR-85, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Liver.
  3. "Biochemical studies of two rat acyl-CoA synthetases, ACS1 and ACS2."
    Iijima H., Fujino T., Minekura H., Suzuki H., Kang M.-J., Yamamoto T.T.
    Eur. J. Biochem. 242:186-190(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  4. "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.
  5. "Discovery and confirmation of O-GlcNAcylated proteins in rat liver mitochondria by combination of mass spectrometry and immunological methods."
    Cao W., Cao J., Huang J., Yao J., Yan G., Xu H., Yang P.
    PLoS ONE 8:E76399-E76399(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT SER-136.

Entry informationi

Entry nameiACSL1_RAT
AccessioniPrimary (citable) accession number: P18163
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: April 1, 2015
This is version 129 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, Direct protein sequencing, 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.