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P18163 (ACSL1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 121. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Acsl1
Synonyms:Acs1, Acsl2, Facl2
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length699 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

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

Cofactor

Magnesium.

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

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

Developmental stage

Levels remain constant during development.

Induction

By high fat and high carbohydrate diets.

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
   DomainSignal-anchor
Transmembrane
Transmembrane helix
   LigandATP-binding
Magnesium
Nucleotide-binding
   Molecular functionLigase
   PTMAcetylation
Nitration
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processadiponectin-activated signaling pathway

Inferred from electronic annotation. Source: Ensembl

fatty acid metabolic process

Inferred from mutant phenotype PubMed 17028193. Source: RGD

fatty acid transport

Inferred from genetic interaction PubMed 16466685. Source: RGD

lipid biosynthetic process

Inferred from electronic annotation. Source: Ensembl

lipid metabolic process

Traceable author statement Ref.1. Source: RGD

long-chain fatty acid import

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein serine/threonine kinase activity

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from expression pattern PubMed 16428347PubMed 17284823. Source: RGD

response to nutrient

Inferred from expression pattern PubMed 15811777. Source: RGD

response to oleic acid

Inferred from expression pattern PubMed 16428347. Source: RGD

response to organic cyclic compound

Inferred from expression pattern PubMed 10777552. Source: RGD

response to organic substance

Inferred from direct assay PubMed 11319222. Source: RGD

triglyceride metabolic process

Inferred from genetic interaction PubMed 16466685. Source: RGD

xenobiotic catabolic process

Inferred from direct assay PubMed 10725307. Source: RGD

   Cellular_componentendoplasmic reticulum

Inferred from direct assay PubMed 11319232PubMed 12147264. Source: RGD

endoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

mitochondrial outer membrane

Inferred from direct assay Ref.2. Source: RGD

peroxisomal membrane

Inferred from direct assay PubMed 14561759. Source: HGNC

plasma membrane

Inferred from direct assay PubMed 15601973. Source: RGD

   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 PubMed 10198260. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 699699Long-chain-fatty-acid--CoA ligase 1
PRO_0000193106

Regions

Transmembrane25 – 4521Helical; Signal-anchor for type III membrane protein; Potential
Topological domain46 – 699654Cytoplasmic Potential

Amino acid modifications

Modified residue11N-acetylmethionine Ref.2
Modified residue91Nitrated tyrosine Ref.2
Modified residue851Phosphotyrosine Ref.2
Modified residue861Nitrated tyrosine Ref.2
Modified residue2081N6-acetyllysine By similarity
Modified residue3571N6-acetyllysine By similarity
Modified residue3871N6-acetyllysine By similarity
Modified residue6211Phosphoserine By similarity
Modified residue6331N6-acetyllysine Ref.2

Sequences

Sequence LengthMass (Da)Tools
P18163 [UniParc].

Last modified November 1, 1990. Version 1.
Checksum: 6E1EACE0EAE8A85C

FASTA69978,179
        10         20         30         40         50         60 
MEVHELFRYF RMPELIDIRQ YVRTLPTNTL MGFGAFAALT TFWYATRPKA LKPPCDLSMQ 

        70         80         90        100        110        120 
SVEVTGTTEG VRRSAVLEDD KLLLYYYDDV RTMYDGFQRG IQVSNDGPCL GSRKPNQPYE 

       130        140        150        160        170        180 
WISYKQVAEM AECIGSALIQ KGFKPCSEQF IGIFSQNRPE WVTIEQGCFT YSMVVVPLYD 

       190        200        210        220        230        240 
TLGTDAITYI VNKAELSVIF ADKPEKAKLL LEGVENKLTP CLKIIVIMDS YDNDLVERGQ 

       250        260        270        280        290        300 
KCGVEIIGLK ALEDLGRVNR TKPKPPEPED LAIICFTSGT TGNPKGAMVT HQNIMNDCSG 

       310        320        330        340        350        360 
FIKATESAFI ASPEDVLISF LPLAHMFETV VECVMLCHGA KIGFFQGDIR LLMDDLKVLQ 

       370        380        390        400        410        420 
PTIFPVVPRL LNRMFDRIFG QANTSVKRWL LDFASKRKEA ELRSGIVRNN SLWDKLIFHK 

       430        440        450        460        470        480 
IQSSLGGKVR LMITGAAPVS ATVLTFLRAA LGCQFYEGYG QTECTAGCCL SLPGDWTAGH 

       490        500        510        520        530        540 
VGAPMPCNYI KLVDVEDMNY QAAKGEGEVC VKGANVFKGY LKDPARTAEA LDKDGWLHTG 

       550        560        570        580        590        600 
DIGKWLPNGT LKIIDRKKHI FKLAQGEYIA PEKIENIYLR SEAVAQVFVH GESLQAFLIA 

       610        620        630        640        650        660 
IVVPDVEILP SWAQKRGFQG SFEELCRNKD INKAILEDMV KLGKNAGLKP FEQVKGIAVH 

       670        680        690 
PELFSIDNGL LTPTLKAKRP ELRNYFRSQI DELYSTIKI 

« Hide

References

[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D90109 mRNA. Translation: BAA14136.1.
PIRA36275.
RefSeqNP_036952.1. NM_012820.1.
XP_006253184.1. XM_006253122.1.
XP_006253185.1. XM_006253123.1.
XP_006253186.1. XM_006253124.1.
XP_006253187.1. XM_006253125.1.
XP_006253188.1. XM_006253126.1.
XP_006253189.1. XM_006253127.1.
UniGeneRn.6215.

3D structure databases

ProteinModelPortalP18163.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP18163. 28 interactions.
MINTMINT-4570488.
STRING10116.ENSRNOP00000014235.

PTM databases

PhosphoSiteP18163.

Proteomic databases

PaxDbP18163.
PRIDEP18163.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000014235; ENSRNOP00000014235; ENSRNOG00000010633.
GeneID25288.
KEGGrno:25288.

Organism-specific databases

CTD2180.
RGD2015. Acsl1.

Phylogenomic databases

eggNOGCOG1022.
GeneTreeENSGT00690000101725.
HOGENOMHOG000159459.
HOVERGENHBG050452.
InParanoidP18163.
KOK01897.
OMAAKCPIVE.
OrthoDBEOG71CFKN.
PhylomeDBP18163.
TreeFamTF313877.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-14442.
BRENDA6.2.1.3. 5301.
SABIO-RKP18163.

Gene expression databases

GenevestigatorP18163.

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

NextBio606025.
PROP18163.

Entry information

Entry nameACSL1_RAT
AccessionPrimary (citable) accession number: P18163
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: April 16, 2014
This is version 121 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