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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, Acs5, Facl5
Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at transcript 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.3 Publications

Catalytic activityi

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

GO - Molecular functioni

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

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei12 – 3221Helical; Signal-anchor for type III membrane protein; Reviewed prediction
Add
BLAST
Topological domaini33 – 683651Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum membrane Source: UniProtKB-SubCell
  2. integral component of membrane Source: UniProtKB-KW
  3. mitochondrial outer membrane Source: UniProtKB-SubCell
  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 5
PRO_0000193114Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei361 – 3611N6-acetyllysine By 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.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1022.
HOGENOMiHOG000159459.
HOVERGENiHBG050452.
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

MLFIFNFLFS PLPTPALICL LTFGTAIFLW LINRPQPVLP LIDLDNQSVG    50
IEGGARRGAF QKNNDLILYY FSDAKTLYEV FQRGLAVSDN GPCLGYRKPN 100
QPYKWISYKQ VSDRAEYLGS CLLHKGYKPS QDQFIGIFAQ NRPEWVISEL 150
ACYTYSMVAV PLYDTLGAEA IIYVINRADI SVVICDTPQK ATMLIENVEK 200
DLTPGLKTVI LMDPFDDDLM KRGEKCGIEM LSLHDAENLG KENFKKPMPP 250
NPEDLSVICF TSGTTGDPKG AMLTHQNIVS NMAAFLKFLE PIFQPTPEDV 300
TISYLPLAHM FERLVQGVIF SCGGKIGFFQ GDIRLLPDDM KALKPTVFPT 350
VPRLLNRVYD KVQNEAKTPL KKFLLNLAII SKFNEVRNGI IRRNSLWDKL 400
VFSKIQSSLG GKVRLMITGA APISTPVLTF FRAAMGCWVF EAYGQTECTA 450
GCSITSPGDW TAGHVGTPVS CNFVKLEDVA DMNYFSVNNE GEICIKGNNV 500
FKGYLKDPEK TQEVLDKDGW LHTGDIGRWL PNGTLKIIDR KKNIFKLAQG 550
EYIAPEKIEN VYSRSRPILQ VFVHGESLRS FLIGVVVPDP ESLPSFAAKI 600
GVKGSFEELC QNQCVKKAIL EDLQKVGKEG GLKSFEQVKS IFVHPEPFSI 650
ENGLLTPTLK AKRVELAKFF QTQIKSLYES IEE 683
Length:683
Mass (Da):76,405
Last modified:November 1, 1998 - v1
Checksum:iD4EC2A58FD29040C
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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...

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.
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. "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.
  3. "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: July 9, 2014
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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