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O88813

- ACSL5_RAT

UniProt

O88813 - ACSL5_RAT

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Protein

Long-chain-fatty-acid--CoA ligase 5

Gene

Acsl5

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

Functioni

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.By similarity3 Publications

Catalytic activityi

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

Kineticsi

  1. KM=666 µM for ATP1 Publication
  2. KM=2.4 µM for CoA1 Publication
  3. KM=8.6 µM for palmitate1 Publication

Vmax=130 nmol/min/mg enzyme with palmitate as substrate1 Publication

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. long-chain fatty acid-CoA ligase activity Source: RGD

GO - Biological processi

  1. cellular response to insulin stimulus Source: RGD
  2. fatty acid metabolic process Source: RGD
  3. fatty acid transport Source: RGD
  4. long-chain fatty acid metabolic process Source: GOC
  5. phospholipid biosynthetic process Source: RGD
  6. positive regulation of fatty acid beta-oxidation Source: RGD
  7. positive regulation of plasma membrane long-chain fatty acid transport Source: RGD
  8. positive regulation of triglyceride biosynthetic process Source: RGD
  9. response to cholesterol Source: RGD
  10. response to glucose Source: RGD
  11. response to nutrient Source: RGD
  12. response to sucrose 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.
SABIO-RKO88813.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Acsl5
Synonyms:Acs5, Facl5
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi69402. Acsl5.

Subcellular locationi

Mitochondrion 1 Publication. Endoplasmic reticulum 1 Publication. Mitochondrion outer membrane By similarity; Single-pass type III membrane protein By similarity. Endoplasmic reticulum membrane By similarity; Single-pass type III membrane protein By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei12 – 3221Helical; Signal-anchor for type III membrane proteinSequence AnalysisAdd
BLAST
Topological domaini33 – 683651CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum Source: UniProtKB-KW
  2. integral component of membrane Source: UniProtKB-KW
  3. mitochondrial outer membrane Source: UniProtKB-KW
  4. mitochondrion Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Mitochondrion, Mitochondrion outer membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 683683Long-chain-fatty-acid--CoA ligase 5PRO_0000193114Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei361 – 3611N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiO88813.
PRIDEiO88813.

Expressioni

Tissue specificityi

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

Inductioni

Expression decreases in response to fast and increases after high sucrose diet.1 Publication

Gene expression databases

GenevestigatoriO88813.

Interactioni

Protein-protein interaction databases

MINTiMINT-4567115.
STRINGi10116.ENSRNOP00000022126.

Structurei

3D structure databases

ProteinModelPortaliO88813.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1022.
HOGENOMiHOG000159459.
HOVERGENiHBG050452.
InParanoidiO88813.
KOiK01897.
PhylomeDBiO88813.

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.

O88813-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLFIFNFLFS PLPTPALICL LTFGTAIFLW LINRPQPVLP LIDLDNQSVG
60 70 80 90 100
IEGGARRGAF QKNNDLILYY FSDAKTLYEV FQRGLAVSDN GPCLGYRKPN
110 120 130 140 150
QPYKWISYKQ VSDRAEYLGS CLLHKGYKPS QDQFIGIFAQ NRPEWVISEL
160 170 180 190 200
ACYTYSMVAV PLYDTLGAEA IIYVINRADI SVVICDTPQK ATMLIENVEK
210 220 230 240 250
DLTPGLKTVI LMDPFDDDLM KRGEKCGIEM LSLHDAENLG KENFKKPMPP
260 270 280 290 300
NPEDLSVICF TSGTTGDPKG AMLTHQNIVS NMAAFLKFLE PIFQPTPEDV
310 320 330 340 350
TISYLPLAHM FERLVQGVIF SCGGKIGFFQ GDIRLLPDDM KALKPTVFPT
360 370 380 390 400
VPRLLNRVYD KVQNEAKTPL KKFLLNLAII SKFNEVRNGI IRRNSLWDKL
410 420 430 440 450
VFSKIQSSLG GKVRLMITGA APISTPVLTF FRAAMGCWVF EAYGQTECTA
460 470 480 490 500
GCSITSPGDW TAGHVGTPVS CNFVKLEDVA DMNYFSVNNE GEICIKGNNV
510 520 530 540 550
FKGYLKDPEK TQEVLDKDGW LHTGDIGRWL PNGTLKIIDR KKNIFKLAQG
560 570 580 590 600
EYIAPEKIEN VYSRSRPILQ VFVHGESLRS FLIGVVVPDP ESLPSFAAKI
610 620 630 640 650
GVKGSFEELC QNQCVKKAIL EDLQKVGKEG GLKSFEQVKS IFVHPEPFSI
660 670 680
ENGLLTPTLK AKRVELAKFF QTQIKSLYES IEE
Length:683
Mass (Da):76,405
Last modified:November 1, 1998 - v1
Checksum:iD4EC2A58FD29040C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB012933 mRNA. Translation: BAA33581.1.
PIRiJE0262.
RefSeqiNP_446059.1. NM_053607.1.
UniGeneiRn.105862.

Genome annotation databases

GeneIDi94340.
KEGGirno:94340.
UCSCiRGD:69402. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB012933 mRNA. Translation: BAA33581.1 .
PIRi JE0262.
RefSeqi NP_446059.1. NM_053607.1.
UniGenei Rn.105862.

3D structure databases

ProteinModelPortali O88813.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

MINTi MINT-4567115.
STRINGi 10116.ENSRNOP00000022126.

Proteomic databases

PaxDbi O88813.
PRIDEi O88813.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 94340.
KEGGi rno:94340.
UCSCi RGD:69402. rat.

Organism-specific databases

CTDi 51703.
RGDi 69402. Acsl5.

Phylogenomic databases

eggNOGi COG1022.
HOGENOMi HOG000159459.
HOVERGENi HBG050452.
InParanoidi O88813.
KOi K01897.
PhylomeDBi O88813.

Enzyme and pathway databases

BRENDAi 6.2.1.3. 5301.
SABIO-RK O88813.

Miscellaneous databases

NextBioi 617929.

Gene expression databases

Genevestigatori O88813.

Family and domain databases

InterProi IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view ]
Pfami PF00501. AMP-binding. 1 hit.
[Graphical view ]
PROSITEi PS00455. AMP_BINDING. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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. "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.
  3. "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.
  4. "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.

Entry informationi

Entry nameiACSL5_RAT
AccessioniPrimary (citable) accession number: O88813
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: November 1, 1998
Last modified: November 26, 2014
This is version 98 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