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Reviewed, UniProtKB/Swiss-Prot P33124 (ACSL6_RAT)

Last modified January 19, 2010. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

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Protein attributes

Sequence length697 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

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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 carboxylic 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.

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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
   LigandATP-binding
Magnesium
Nucleotide-binding
   Molecular functionLigase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processcellular response to insulin stimulus

Inferred from expression pattern. Source: RGD

fatty acid transport

Inferred from genetic interaction. Source: RGD

long-chain fatty acid metabolic process Ref.3

Inferred from direct assay. Source: RGD

phospholipid biosynthetic process

Inferred from mutant phenotype. Source: RGD

positive regulation of neuron projection development

Inferred from mutant phenotype. Source: RGD

positive regulation of plasma membrane long-chain fatty acid transport

Inferred from mutant phenotype. Source: RGD

response to hypoxia

Inferred from expression pattern. Source: RGD

response to nutrient

Inferred from expression pattern. Source: RGD

response to steroid hormone stimulus

Inferred from expression pattern. Source: RGD

triglyceride metabolic process

Inferred from genetic interaction. Source: RGD

   Cellular componentendoplasmic reticulum

Inferred from electronic annotation. Source: UniProtKB-KW

integral to membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

microsome

Inferred from electronic annotation. Source: UniProtKB-KW

mitochondrial outer membrane

Inferred from electronic annotation. Source: UniProtKB-KW

nucleus

Inferred from direct assay. Source: RGD

peroxisome

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

long-chain-fatty-acid-CoA ligase activity Ref.3

Inferred from direct assay. Source: RGD

magnesium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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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

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

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

Regions

Transmembrane25 – 4521Signal-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

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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.

Checksum: 3E3F54AAFDF059F8
Show »

FASTA72280,949

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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: 1654331] [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: 1460058] [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: 1569043] [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.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		S56508 mRNA. Translation: AAB19809.2.
D10041 mRNA. Translation: BAA00932.1.
CB582512 mRNA. No translation available.
IPIIPI00324041.
IPI00776455.
PIRJX0205.
RefSeqNP_570095.1.
UniGeneRn.33697

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGP33124.

Proteomic databases

PRIDEP33124.

Genome annotation databases

EnsemblENSRNOT00000030760; ENSRNOP00000033248; ENSRNOG00000026745; Rattus norvegicus. [Genome view]
GeneID117243.
KEGGrno:117243.
UCSCNM_130739. rat.

Organism-specific databases

CTD117243.
RGD69403. Acsl6.

Phylogenomic databases

eggNOGroNOG07192.
HOVERGENP33124.
PhylomeDBP33124.

Enzyme and pathway databases

BRENDA6.2.1.3. 248.

Gene expression databases

ArrayExpressP33124.
GenevestigatorP33124.
GermOnlineENSRNOG00000026745. Rattus norvegicus.

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 Resources

NextBio620076.

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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: January 19, 2010
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents