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O35547 (ACSL4_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 99. 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 4

EC=6.2.1.3
Alternative name(s):
Long-chain acyl-CoA synthetase 4
Short name=LACS 4
Gene names
Name:Acsl4
Synonyms:Acs4, Facl4
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length670 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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

Catalytic activity

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

Cofactor

Magnesium By similarity.

Sequence similarities

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

Ontologies

Keywords
   Biological processFatty acid metabolism
Lipid metabolism
   LigandATP-binding
Magnesium
Nucleotide-binding
   Molecular functionLigase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processdendritic spine development

Inferred from mutant phenotype PubMed 19166906. Source: RGD

embryonic process involved in female pregnancy

Inferred from electronic annotation. Source: Ensembl

fatty acid metabolic process

Traceable author statement Ref.1. Source: RGD

fatty acid transport

Inferred from genetic interaction PubMed 16466685. Source: RGD

lipid biosynthetic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of prostaglandin secretion

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell growth

Inferred from electronic annotation. Source: Ensembl

response to interleukin-15

Inferred from expression pattern PubMed 18239634. Source: RGD

response to nutrient

Inferred from expression pattern PubMed 16772660. Source: RGD

triglyceride metabolic process

Inferred from genetic interaction PubMed 16466685. Source: RGD

   Cellular_componentlipid particle

Inferred from electronic annotation. Source: Ensembl

mitochondrial membrane

Inferred from direct assay PubMed 12147264. Source: RGD

neuronal cell body

Inferred from direct assay PubMed 19166906. Source: RGD

peroxisome

Inferred from direct assay PubMed 12147264. Source: RGD

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

arachidonate-CoA ligase activity

Inferred from electronic annotation. Source: Ensembl

long-chain fatty acid-CoA ligase activity

Inferred from direct assay Ref.1. Source: RGD

very long-chain fatty acid-CoA ligase activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 670670Long-chain-fatty-acid--CoA ligase 4
PRO_0000193111

Sequences

Sequence LengthMass (Da)Tools
O35547 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: B7D290973B650CB6

FASTA67074,327
        10         20         30         40         50         60 
MAKRIKAKPT SDKPGSPYRS VTHFDSLAVI DIPGADTLDK LFDHAVAKFG KKDSLGTREI 

        70         80         90        100        110        120 
LSEENEMQPN GKVFKKLILG NYKWINYLEV NCRVNNFGSG LTALGLKPKN TIAIFCETRA 

       130        140        150        160        170        180 
EWMIAAQTCF KYNFPLVTLY ATLGKEAVVH GLNESEASYL ITSVELLESK LKAALLDINC 

       190        200        210        220        230        240 
VKHIIYVDNK TINRAEYPEG LEIHSMQSVE ELGSKPENSS IPPSRPTPSD MAIVMYTSGS 

       250        260        270        280        290        300 
TGRPKGVMMH HSNLIAGMTG QCERIPGLGP KDTYIGYLPL AHVLELTAEI SCFTYGCRIG 

       310        320        330        340        350        360 
YSSPLTLSDQ SSKIKKGSKG DCTVLKPTLM AAVPEIMDRI YKNVMSKVQE MNYIQKTLFK 

       370        380        390        400        410        420 
IGYDYKLEQI KKGYDAPLCN LILFKKVKAL LGGNVRMMLS GGAPLSPQTH RFMNVCFCCP 

       430        440        450        460        470        480 
IGQGYGLTES CGAGTVTEVT DYTTGRVGAP LICCEIKLKD WQEGGYTVHD KPNPRGEIVI 

       490        500        510        520        530        540 
GGQNISMGYF KNEEKTAEDY SVDENGQRWF CTGDIGEFHP DGCLQIIDRK KDLVKLQAGE 

       550        560        570        580        590        600 
YVSLGKVEAA LKNCPLIDNI CAFAKSDQSY VISFVVPNQK KLTLLAQQKG VEGSWVDICN 

       610        620        630        640        650        660 
NPAMEAEILK EIREAANAMK LERFEIPIKV RLSPEPWTPE TGLVTDAFKL KRKELKNHYL 

       670 
KDIERMYGGK 

« Hide

References

[1]"A novel arachidonate-preferring acyl-CoA synthetase is present in steroidogenic cells of the rat adrenal, ovary, and testis."
Kang M., Fujino T., Sasano H., Minekura H., Yabuki N., Nagura H., Iijima H., Yamamoto T.T.
Proc. Natl. Acad. Sci. U.S.A. 94:2880-2884(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Wistar.
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D85189 mRNA. Translation: BAA22195.1.
RefSeqNP_446075.1. NM_053623.1.
XP_006257377.1. XM_006257315.1.
XP_006257378.1. XM_006257316.1.
XP_006257379.1. XM_006257317.1.
UniGeneRn.87821.

3D structure databases

ProteinModelPortalO35547.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-4567100.
STRING10116.ENSRNOP00000026057.

Proteomic databases

PaxDbO35547.
PRIDEO35547.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000026057; ENSRNOP00000026057; ENSRNOG00000019180.
GeneID113976.
KEGGrno:113976.

Organism-specific databases

CTD2182.
RGD69401. Acsl4.

Phylogenomic databases

eggNOGCOG1022.
GeneTreeENSGT00690000102168.
HOGENOMHOG000159459.
HOVERGENHBG106947.
InParanoidO35547.
KOK01897.
OMANAMKLER.
OrthoDBEOG7P2XRD.
PhylomeDBO35547.
TreeFamTF314012.

Enzyme and pathway databases

BRENDA6.2.1.3. 5301.
SABIO-RKO35547.

Gene expression databases

GenevestigatorO35547.

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

NextBio618117.

Entry information

Entry nameACSL4_RAT
AccessionPrimary (citable) accession number: O35547
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: January 1, 1998
Last modified: April 16, 2014
This is version 99 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