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Protein

Long-chain-fatty-acid--CoA ligase 4

Gene

Acsl4

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

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

Cofactori

Mg2+By similarity

Kineticsi

  1. KM=34 µM for ATP1 Publication
  2. KM=4.1 µM for CoA1 Publication
  3. KM=5.4 µM for palmitate1 Publication
  4. KM=19.5 µM for oleate1 Publication
  5. KM=10 µM for arachidonate1 Publication
  1. Vmax=2800 nmol/min/mg enzyme with palmitate as substrate1 Publication
  2. Vmax=673 nmol/min/mg enzyme with oleate as substrate1 Publication
  3. Vmax=4200 nmol/min/mg enzyme with arachidonate as substrate1 Publication

GO - Molecular functioni

GO - Biological processi

  • dendritic spine development Source: RGD
  • embryonic process involved in female pregnancy Source: Ensembl
  • fatty acid metabolic process Source: RGD
  • fatty acid transport Source: RGD
  • lipid biosynthetic process Source: Ensembl
  • long-chain fatty acid metabolic process Source: GOC
  • negative regulation of prostaglandin secretion Source: Ensembl
  • positive regulation of cell growth Source: Ensembl
  • response to interleukin-15 Source: RGD
  • response to nutrient Source: RGD
  • triglyceride metabolic process Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Keywords - Ligandi

ATP-binding, Magnesium, Nucleotide-binding

Enzyme and pathway databases

BRENDAi6.2.1.3. 5301.
ReactomeiREACT_346713. Synthesis of very long-chain fatty acyl-CoAs.
SABIO-RKO35547.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Acsl4
Synonyms:Acs4, Facl4
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Chromosome X

Organism-specific databases

RGDi69401. Acsl4.

Subcellular locationi

GO - Cellular componenti

  • ER-mitochondrion membrane contact site Source: Ensembl
  • extracellular exosome Source: Ensembl
  • lipid particle Source: Ensembl
  • mitochondrial membrane Source: RGD
  • neuronal cell body Source: RGD
  • peroxisome Source: RGD
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 670670Long-chain-fatty-acid--CoA ligase 4PRO_0000193111Add
BLAST

Proteomic databases

PaxDbiO35547.
PRIDEiO35547.

Expressioni

Gene expression databases

GenevisibleiO35547. RN.

Interactioni

Protein-protein interaction databases

MINTiMINT-4567100.
STRINGi10116.ENSRNOP00000026057.

Structurei

3D structure databases

ProteinModelPortaliO35547.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1022.
GeneTreeiENSGT00690000102168.
HOGENOMiHOG000159459.
HOVERGENiHBG106947.
InParanoidiO35547.
KOiK01897.
OMAiNAMKLER.
OrthoDBiEOG7P2XRD.
PhylomeDBiO35547.
TreeFamiTF314012.

Family and domain databases

InterProiIPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamiPF00501. AMP-binding. 1 hit.
[Graphical view]
PROSITEiPS00455. AMP_BINDING. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O35547-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKRIKAKPT SDKPGSPYRS VTHFDSLAVI DIPGADTLDK LFDHAVAKFG
60 70 80 90 100
KKDSLGTREI LSEENEMQPN GKVFKKLILG NYKWINYLEV NCRVNNFGSG
110 120 130 140 150
LTALGLKPKN TIAIFCETRA EWMIAAQTCF KYNFPLVTLY ATLGKEAVVH
160 170 180 190 200
GLNESEASYL ITSVELLESK LKAALLDINC VKHIIYVDNK TINRAEYPEG
210 220 230 240 250
LEIHSMQSVE ELGSKPENSS IPPSRPTPSD MAIVMYTSGS TGRPKGVMMH
260 270 280 290 300
HSNLIAGMTG QCERIPGLGP KDTYIGYLPL AHVLELTAEI SCFTYGCRIG
310 320 330 340 350
YSSPLTLSDQ SSKIKKGSKG DCTVLKPTLM AAVPEIMDRI YKNVMSKVQE
360 370 380 390 400
MNYIQKTLFK IGYDYKLEQI KKGYDAPLCN LILFKKVKAL LGGNVRMMLS
410 420 430 440 450
GGAPLSPQTH RFMNVCFCCP IGQGYGLTES CGAGTVTEVT DYTTGRVGAP
460 470 480 490 500
LICCEIKLKD WQEGGYTVHD KPNPRGEIVI GGQNISMGYF KNEEKTAEDY
510 520 530 540 550
SVDENGQRWF CTGDIGEFHP DGCLQIIDRK KDLVKLQAGE YVSLGKVEAA
560 570 580 590 600
LKNCPLIDNI CAFAKSDQSY VISFVVPNQK KLTLLAQQKG VEGSWVDICN
610 620 630 640 650
NPAMEAEILK EIREAANAMK LERFEIPIKV RLSPEPWTPE TGLVTDAFKL
660 670
KRKELKNHYL KDIERMYGGK
Length:670
Mass (Da):74,327
Last modified:January 1, 1998 - v1
Checksum:iB7D290973B650CB6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D85189 mRNA. Translation: BAA22195.1.
RefSeqiNP_446075.1. NM_053623.1.
XP_006257377.1. XM_006257315.2.
XP_006257378.1. XM_006257316.2.
UniGeneiRn.87821.

Genome annotation databases

EnsembliENSRNOT00000026057; ENSRNOP00000026057; ENSRNOG00000019180.
GeneIDi113976.
KEGGirno:113976.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D85189 mRNA. Translation: BAA22195.1.
RefSeqiNP_446075.1. NM_053623.1.
XP_006257377.1. XM_006257315.2.
XP_006257378.1. XM_006257316.2.
UniGeneiRn.87821.

3D structure databases

ProteinModelPortaliO35547.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-4567100.
STRINGi10116.ENSRNOP00000026057.

Proteomic databases

PaxDbiO35547.
PRIDEiO35547.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000026057; ENSRNOP00000026057; ENSRNOG00000019180.
GeneIDi113976.
KEGGirno:113976.

Organism-specific databases

CTDi2182.
RGDi69401. Acsl4.

Phylogenomic databases

eggNOGiCOG1022.
GeneTreeiENSGT00690000102168.
HOGENOMiHOG000159459.
HOVERGENiHBG106947.
InParanoidiO35547.
KOiK01897.
OMAiNAMKLER.
OrthoDBiEOG7P2XRD.
PhylomeDBiO35547.
TreeFamiTF314012.

Enzyme and pathway databases

BRENDAi6.2.1.3. 5301.
ReactomeiREACT_346713. Synthesis of very long-chain fatty acyl-CoAs.
SABIO-RKO35547.

Miscellaneous databases

NextBioi618117.
PROiO35547.

Gene expression databases

GenevisibleiO35547. RN.

Family and domain databases

InterProiIPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamiPF00501. AMP-binding. 1 hit.
[Graphical view]
PROSITEiPS00455. AMP_BINDING. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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.
  2. "Characterization of recombinant long-chain rat acyl-CoA synthetase isoforms 3 and 6: identification of a novel variant of isoform 6."
    Van Horn C.G., Caviglia J.M., Li L.O., Wang S., Granger D.A., Coleman R.A.
    Biochemistry 44:1635-1642(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: BIOPHYSICOCHEMICAL PROPERTIES.
    Tissue: Brain.

Entry informationi

Entry nameiACSL4_RAT
AccessioniPrimary (citable) accession number: O35547
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: January 1, 1998
Last modified: June 24, 2015
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

5 rat isozymes encoded by different genes have been described. ACSL6 corresponds to isozyme 2 (ACS2).1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.