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O88813 (ACSL5_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 94. 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 5

EC=6.2.1.3
Alternative name(s):
Long-chain acyl-CoA synthetase 5
Short name=LACS 5
Gene names
Name:Acsl5
Synonyms:Acs5, Facl5
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length683 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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. ACSL5 may sensitize epithelial cells to apoptosis specifically triggered by the death ligand TRAIL at the villus tip of the crypt-villus axis of the small intestine By similarity. May have a role in the survival of glioma cells By similarity. May activate fatty acids from exogenous sources for the synthesis of triacylglycerol destined for intracellular storage. It was suggested that it may also stimulate fatty acid oxidation. Utilizes a wide range of saturated fatty acids with a preference for C16-C18 unsaturated fatty acids. Ref.1 Ref.2 Ref.3

Catalytic activity

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

Subcellular location

Mitochondrion. Endoplasmic reticulum. Mitochondrion outer membrane; Single-pass type III membrane protein By similarity. Endoplasmic reticulum membrane; Single-pass type III membrane protein By similarity Ref.2.

Tissue specificity

Expressed most abundantly in the small intestine, and to a much lesser extent in the lung, liver, adrenal gland, adipose tissue and kidney. Ref.1

Induction

Expression decreases in response to fast and increases after high sucrose diet. Ref.2

Sequence similarities

Belongs to the ATP-dependent AMP-binding enzyme family.

Ontologies

Keywords
   Biological processFatty acid metabolism
Lipid metabolism
   Cellular componentEndoplasmic reticulum
Membrane
Mitochondrion
Mitochondrion outer membrane
   DomainSignal-anchor
Transmembrane
Transmembrane helix
   LigandATP-binding
Magnesium
Nucleotide-binding
   Molecular functionLigase
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular response to insulin stimulus

Inferred from expression pattern PubMed 16198472. Source: RGD

fatty acid metabolic process

Traceable author statement Ref.1. Source: RGD

fatty acid transport

Inferred from genetic interaction PubMed 14711823. Source: RGD

long-chain fatty acid metabolic process

Inferred from direct assay Ref.1. Source: GOC

phospholipid biosynthetic process

Inferred from genetic interaction PubMed 14711823. Source: RGD

positive regulation of fatty acid beta-oxidation

Inferred from genetic interaction PubMed 14711823. Source: RGD

positive regulation of plasma membrane long-chain fatty acid transport

Inferred from direct assay Ref.2. Source: RGD

positive regulation of triglyceride biosynthetic process

Inferred from direct assay Ref.2. Source: RGD

response to cholesterol

Inferred from expression pattern Ref.1. Source: RGD

response to glucose

Inferred from expression pattern PubMed 16198472. Source: RGD

response to nutrient

Inferred from expression pattern PubMed 16772660. Source: RGD

response to sucrose

Inferred from expression pattern Ref.1. Source: RGD

   Cellular_componentendoplasmic 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 electronic annotation. Source: UniProtKB-SubCell

mitochondrion

Inferred from direct assay PubMed 12147264. Source: RGD

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

long-chain fatty acid-CoA ligase activity

Inferred from direct assay Ref.1. Source: RGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 683683Long-chain-fatty-acid--CoA ligase 5
PRO_0000193114

Regions

Transmembrane12 – 3221Helical; Signal-anchor for type III membrane protein; Potential
Topological domain33 – 683651Cytoplasmic Potential

Amino acid modifications

Modified residue3611N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
O88813 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: D4EC2A58FD29040C

FASTA68376,405
        10         20         30         40         50         60 
MLFIFNFLFS PLPTPALICL LTFGTAIFLW LINRPQPVLP LIDLDNQSVG IEGGARRGAF 

        70         80         90        100        110        120 
QKNNDLILYY FSDAKTLYEV FQRGLAVSDN GPCLGYRKPN QPYKWISYKQ VSDRAEYLGS 

       130        140        150        160        170        180 
CLLHKGYKPS QDQFIGIFAQ NRPEWVISEL ACYTYSMVAV PLYDTLGAEA IIYVINRADI 

       190        200        210        220        230        240 
SVVICDTPQK ATMLIENVEK DLTPGLKTVI LMDPFDDDLM KRGEKCGIEM LSLHDAENLG 

       250        260        270        280        290        300 
KENFKKPMPP NPEDLSVICF TSGTTGDPKG AMLTHQNIVS NMAAFLKFLE PIFQPTPEDV 

       310        320        330        340        350        360 
TISYLPLAHM FERLVQGVIF SCGGKIGFFQ GDIRLLPDDM KALKPTVFPT VPRLLNRVYD 

       370        380        390        400        410        420 
KVQNEAKTPL KKFLLNLAII SKFNEVRNGI IRRNSLWDKL VFSKIQSSLG GKVRLMITGA 

       430        440        450        460        470        480 
APISTPVLTF FRAAMGCWVF EAYGQTECTA GCSITSPGDW TAGHVGTPVS CNFVKLEDVA 

       490        500        510        520        530        540 
DMNYFSVNNE GEICIKGNNV FKGYLKDPEK TQEVLDKDGW LHTGDIGRWL PNGTLKIIDR 

       550        560        570        580        590        600 
KKNIFKLAQG EYIAPEKIEN VYSRSRPILQ VFVHGESLRS FLIGVVVPDP ESLPSFAAKI 

       610        620        630        640        650        660 
GVKGSFEELC QNQCVKKAIL EDLQKVGKEG GLKSFEQVKS IFVHPEPFSI ENGLLTPTLK 

       670        680 
AKRVELAKFF QTQIKSLYES IEE 

« Hide

References

[1]"A novel acyl-CoA synthetase, ACS5, expressed in intestinal epithelial cells and proliferating preadipocytes."
Oikawa E., Iijima H., Suzuki T., Sasano H., Sato H., Kamataki A., Nagura H., Kang M.-J., Fujino T., Suzuki H., Yamamoto T.T.
J. Biochem. 124:679-685(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
[2]"Rat long chain acyl-CoA synthetase 5 increases fatty acid uptake and partitioning to cellular triacylglycerol in McArdle-RH7777 cells."
Mashek D.G., McKenzie M.A., Van Horn C.G., Coleman R.A.
J. Biol. Chem. 281:945-950(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INDUCTION.
[3]"Transcriptional activation of hepatic ACSL3 and ACSL5 by oncostatin m reduces hypertriglyceridemia through enhanced beta-oxidation."
Zhou Y., Abidi P., Kim A., Chen W., Huang T.-T., Kraemer F.B., Liu J.
Arterioscler. Thromb. Vasc. Biol. 27:2198-2205(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB012933 mRNA. Translation: BAA33581.1.
PIRJE0262.
RefSeqNP_446059.1. NM_053607.1.
UniGeneRn.105862.

3D structure databases

ProteinModelPortalO88813.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-4567115.
STRING10116.ENSRNOP00000022126.

Proteomic databases

PaxDbO88813.
PRIDEO88813.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID94340.
KEGGrno:94340.
UCSCRGD:69402. rat.

Organism-specific databases

CTD51703.
RGD69402. Acsl5.

Phylogenomic databases

eggNOGCOG1022.
HOGENOMHOG000159459.
HOVERGENHBG050452.
KOK01897.
PhylomeDBO88813.

Enzyme and pathway databases

BRENDA6.2.1.3. 5301.
SABIO-RKO88813.

Gene expression databases

GenevestigatorO88813.

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

NextBio617929.

Entry information

Entry nameACSL5_RAT
AccessionPrimary (citable) accession number: O88813
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: November 1, 1998
Last modified: April 16, 2014
This is version 94 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