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P33124 (ACSL6_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 115. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Long-chain-fatty-acid--CoA ligase 6

EC=6.2.1.3
Alternative name(s):
Long-chain acyl-CoA synthetase 6
Short name=LACS 6
Long-chain-fatty-acid--CoA ligase, brain isozyme
Gene names
Name:Acsl6
Synonyms:Acs2, Facl6
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length697 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. Plays an important role in fatty acid metabolism in brain and the acyl-CoAs produced may be utilized exclusively for the synthesis of the brain lipid.

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

Expressed predominantly in brain and, to a much lesser extent, in heart and adrenal.

Developmental stage

Detected 5 days after birth, and increased in a coordinate fashion during the development of brain, and the amount did not decrease when myelination was completed.

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
   Coding sequence diversityAlternative splicing
   DomainSignal-anchor
Transmembrane
Transmembrane helix
   LigandATP-binding
Magnesium
Nucleotide-binding
   Molecular functionLigase
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcellular response to insulin stimulus

Inferred from expression pattern PubMed 16428347. Source: RGD

fatty acid transport

Inferred from genetic interaction PubMed 16466685. Source: RGD

long-chain fatty acid metabolic process

Inferred from direct assay Ref.3. Source: RGD

neuroblast proliferation

Inferred from electronic annotation. Source: Ensembl

neuron development

Inferred from expression pattern PubMed 16848632. Source: RGD

phospholipid biosynthetic process

Inferred from mutant phenotype PubMed 15655248. Source: RGD

positive regulation of neuron projection development

Inferred from mutant phenotype PubMed 15051725. Source: RGD

positive regulation of plasma membrane long-chain fatty acid transport

Inferred from mutant phenotype PubMed 15655248. Source: RGD

positive regulation of triglyceride biosynthetic process

Inferred from genetic interaction PubMed 16466685. Source: RGD

response to gravity

Inferred from expression pattern PubMed 16848632. Source: RGD

response to hypoxia

Inferred from expression pattern PubMed 15942958. Source: RGD

response to nutrient

Inferred from expression pattern PubMed 16772660. Source: RGD

response to steroid hormone

Inferred from expression pattern PubMed 11118002. Source: RGD

triglyceride metabolic process

Inferred from genetic interaction PubMed 16466685. 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

nucleus

Inferred from direct assay PubMed 15942958. Source: RGD

peroxisomal membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

long-chain fatty acid-CoA ligase activity

Inferred from direct assay Ref.3. Source: RGD

protein homodimerization activity

Inferred from direct assay PubMed 20429931PubMed 20429931. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P33124-1)

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 2 (identifier: P33124-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MLTFFLVSGGSLWLFAEIALSLLEKM

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 697697Long-chain-fatty-acid--CoA ligase 6
PRO_0000193117

Regions

Transmembrane25 – 4521Helical; Signal-anchor for type III membrane protein; Potential
Topological domain46 – 697652Cytoplasmic Potential

Natural variations

Alternative sequence11M → MLTFFLVSGGSLWLFAEIAL SLLEKM in isoform 2.
VSP_037825

Experimental info

Sequence conflict5581H → D in AAB19809. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 1, 1993. Version 1.
Checksum: 0B0CA7EFD653E2BE

FASTA69778,180
        10         20         30         40         50         60 
MQTQEILRIL RLPELSDLGQ FFRSLSATTL VSMGALAAIL AYWLTHRPKA LQPPCNLLMQ 

        70         80         90        100        110        120 
SEEVEDSGGA RRSVIGDCTQ LLTHYYDDAR TMYQVFRRGL SISGNGPCLG FRKPEQPYQW 

       130        140        150        160        170        180 
LSYQEVAKRA EFLGSGLLQH DCKVGTEQFI GVFAQNRPEW IIAELACYTY SMVVVPLYDT 

       190        200        210        220        230        240 
LGPGSIRYII NTADICTVIV DKPHKAILLL EHVERKETPG LKLVILMEPF DDALRERGKK 

       250        260        270        280        290        300 
CGVDIKSMQA IEDSGQENHR VPVPPRPDDL SIVCFTSGTT GNPKGAMLTH GNVVADFSGF 

       310        320        330        340        350        360 
LKVTESQWAP TCADVHFSYL PLAHMFERMV QSVVYCHGGR VGFFQGDIRL LSDDMKALRP 

       370        380        390        400        410        420 
TIFPVVPRLL NRMYDKIFHQ ADTSLKRWLL EFAAKRKQAE VRSGIIRNNS IWDELFFNKI 

       430        440        450        460        470        480 
QASLGGHVRM IVTGAAPASP TVLGFLRAAL GCQVYEGYGQ TECTAGCTFT TPGDWTSGHV 

       490        500        510        520        530        540 
GAPLPCNHIK LVDAEELNYW TSKGEGEICV KGPNVFKGYL KDEDRTKEAL DSDGWLHTGD 

       550        560        570        580        590        600 
IGKWLPEGTL KIIDRKKHIF KLAQGEYVAP EKIENIYIRS EPVAQIYVHG DSLKAFLVGI 

       610        620        630        640        650        660 
VVPDPEVMPC WAQKKGIEGN YQELCKSKEL KKAILDDMVM LGKESGLHSF EQVKAIYIHC 

       670        680        690 
DMFSVQNGLL TPTLKAKRPE LREYFKKQIE ELYSISM 

« Hide

Isoform 2 [UniParc].

Checksum: 3E3F54AAFDF059F8
Show »

FASTA72280,949

References

« Hide 'large scale' references
[1]"Molecular cloning and sequencing of cDNA encoding the phosphatidylinositol kinase from rat brain."
Yamakawa A., Nishizawa M., Fujiwara K.T., Kawai S., Kawasaki H., Suzuki K., Takenawa T.
J. Biol. Chem. 266:17580-17583(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 491-503; 544-551; 573-579 AND 633-636.
Tissue: Brain.
[2]Erratum
Yamakawa A., Nishizawa M., Fujiwara K.T., Kawai S., Kawasaki H., Suzuki K., Takenawa T.
J. Biol. Chem. 267:25620-25620(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: RETRACTION.
[3]"Cloning and functional expression of a novel long-chain acyl-CoA synthetase expressed in brain."
Fujino T., Yamamoto T.
J. Biochem. 111:197-203(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Strain: Wistar.
Tissue: Brain.
[4]"Amgen rat EST program."
Amgen EST program
Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-160 (ISOFORM 2).
Tissue: Spinal ganglion.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
S56508 mRNA. Translation: AAB19809.2.
D10041 mRNA. Translation: BAA00932.1.
CB582512 mRNA. No translation available.
PIRJX0205.
RefSeqNP_570095.1. NM_130739.1.
UniGeneRn.33697.

3D structure databases

ProteinModelPortalP33124.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-4564901.

PTM databases

PhosphoSiteP33124.

Proteomic databases

PaxDbP33124.
PRIDEP33124.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000030760; ENSRNOP00000033248; ENSRNOG00000026745. [P33124-1]
ENSRNOT00000058817; ENSRNOP00000055608; ENSRNOG00000026745. [P33124-2]
GeneID117243.
KEGGrno:117243.
UCSCRGD:69403. rat. [P33124-1]

Organism-specific databases

CTD23305.
RGD69403. Acsl6.

Phylogenomic databases

eggNOGCOG1022.
GeneTreeENSGT00690000101725.
HOGENOMHOG000159459.
HOVERGENHBG050452.
KOK01897.
OMAMFERMVQ.
OrthoDBEOG71CFKN.
PhylomeDBP33124.

Enzyme and pathway databases

BRENDA6.2.1.3. 5301.

Gene expression databases

ArrayExpressP33124.
GenevestigatorP33124.

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

NextBio620076.

Entry information

Entry nameACSL6_RAT
AccessionPrimary (citable) accession number: P33124
Secondary accession number(s): Q63835
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: April 16, 2014
This is version 115 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