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O88813

- ACSL5_RAT

UniProt

O88813 - ACSL5_RAT

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 transcript leveli
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    • History
      Entry version 96 (01 Oct 2014)
      Sequence version 1 (01 Nov 1998)
      Previous versions | rss
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    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.

    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

    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

    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

    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...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini33 – 683651CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

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

    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

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    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...
    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.
    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: October 1, 2014
    This is version 96 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