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Q63151

- ACSL3_RAT

UniProt

Q63151 - ACSL3_RAT

Protein

Long-chain-fatty-acid--CoA ligase 3

Gene

Acsl3

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 125 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      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. ACSL3 is required for the incorporation of fatty acids into phosphatidylcholine, the major phospholipid located on the surface of VLDL (very low density lipoproteins) By similarity. Has mainly an anabolic role in energy metabolism. Mediates hepatic lipogenesis. Preferentially uses myristate, laurate, arachidonate and eicosapentaenoate as substrates. Both isoforms exhibit the same level of activity.By similarity1 Publication

    Catalytic activityi

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

    Cofactori

    Magnesium.By similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. brain development Source: RGD
    2. fatty acid biosynthetic process Source: RGD
    3. fatty acid metabolic process Source: RGD
    4. lipid metabolic process Source: RGD
    5. long-chain fatty acid import Source: Ensembl
    6. long-chain fatty acid metabolic process Source: GOC
    7. metabolic process Source: RGD
    8. positive regulation of Golgi to plasma membrane protein transport Source: Ensembl
    9. positive regulation of phosphatidylcholine biosynthetic process Source: Ensembl
    10. positive regulation of secretion Source: Ensembl
    11. response to nutrient Source: RGD
    12. response to organic cyclic compound Source: RGD
    13. very-low-density lipoprotein particle assembly Source: Ensembl

    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.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Long-chain-fatty-acid--CoA ligase 3 (EC:6.2.1.3)
    Alternative name(s):
    Brain acyl-CoA synthetase II
    Long-chain acyl-CoA synthetase 3
    Short name:
    LACS 3
    Gene namesi
    Name:Acsl3
    Synonyms:Acs3, Facl3
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 9

    Organism-specific databases

    RGDi70552. Acsl3.

    Subcellular locationi

    GO - Cellular componenti

    1. endoplasmic reticulum membrane Source: UniProtKB-SubCell
    2. Golgi apparatus Source: Ensembl
    3. integral component of membrane Source: UniProtKB-KW
    4. lipid particle Source: Ensembl
    5. mitochondrial outer membrane Source: UniProtKB-SubCell
    6. perinuclear region of cytoplasm Source: Ensembl
    7. peroxisomal membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane, Microsome, Mitochondrion, Mitochondrion outer membrane, Peroxisome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 720720Long-chain-fatty-acid--CoA ligase 3PRO_0000001313Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei683 – 6831PhosphoserineBy similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiQ63151.
    PRIDEiQ63151.

    Expressioni

    Tissue specificityi

    Predominantly expressed in the brain, and to a much lesser extent, in lung, adrenal gland, kidney, small intestine, and adipose tissue but not detected in heart or liver.

    Developmental stagei

    Detected 5 days after birth, increased to a maximal level at 15 days, and then decreased gradually to 10% of its maximum level in adult.

    Gene expression databases

    GenevestigatoriQ63151.

    Interactioni

    Protein-protein interaction databases

    IntActiQ63151. 1 interaction.
    STRINGi10116.ENSRNOP00000020161.

    Structurei

    3D structure databases

    ProteinModelPortaliQ63151.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini42 – 720679CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei21 – 4121Helical; Signal-anchor for type III membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG1022.
    GeneTreeiENSGT00690000102168.
    HOGENOMiHOG000159459.
    HOVERGENiHBG106947.
    InParanoidiQ63151.
    KOiK01897.
    OMAiCDRFIFR.
    OrthoDBiEOG7P2XRD.
    PhylomeDBiQ63151.
    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]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative initiation. Align

    Isoform Long (identifier: Q63151-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MNNHVSSTPS TMKLKQTIHP ILLYFIHFII SLYTILTYIP FYFLCESKQE    50
    KPNHIKAKPV SSKPDSAYRS VNSMDGLASV LYPGCDTLDK VFMYAKNKFK 100
    DKRLLGTREI LNEEDEIQPN GKVFKKVILG HYNWLSYEDV FIRALDFGNG 150
    LQMLGQKPKA NIAIFCETRA EWMIAAQACF MYNFQLVTLY ATLGGPAIVH 200
    GLNETEVTNI ITSKELLQTK LKDIVSLVPR LRHIITVDGK PPTWSEFPKG 250
    VIVHTMAAVQ ALGVKADVDK KAHSKPLPSD IAVIMYTSGS TGIPKGVMIS 300
    HSNIIASITG MARRIPRLGE EDVYIGYLPL AHVLELSAEL VCLSHGCRIG 350
    YSSPQTLADQ SSKIKKGSKG DTSVLKPTLM AAVPEIMDRI YKNVMNKVNE 400
    MSAFQRNLFI LAYNYKMEQI SKGCSTPLCD RFVFRNVRRL LGGNIRVLLC 450
    GGAPLSATTQ RFMNICFCCP VGQGYGLTES TGAGTITEVW DYNTGRVGAP 500
    LVCCEIKLKN WEEGGYFNTD KPHPRGEILI GGQNVTMGYY KNEAKTKADF 550
    FEDENGQRWL CTGDIGEFDP DGCLKIIDRK KDLVKLQAGE YVSLGKVEAA 600
    LKNLPLIDNI CAYANSYHSY VIGFVVPNQK ELTELARTKG FNGTWEELCN 650
    SSEMENEVLK VLSEAAISAS LEKFEIPLKI RLSPDPWTPE TGLVTDAFKL 700
    KRKELKTHYQ ADIERMYGRK 720
    Length:720
    Mass (Da):80,458
    Last modified:November 1, 1996 - v1
    Checksum:i4D79FAEF25ADA527
    GO
    Isoform Short (identifier: Q63151-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-11: Missing.

    Show »
    Length:709
    Mass (Da):79,302
    Checksum:iFD6262C2D2794D6A
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 1111Missing in isoform Short. CuratedVSP_018649Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D30666 mRNA. Translation: BAA06340.1.
    RefSeqiNP_476448.1. NM_057107.1. [Q63151-1]
    XP_006245191.1. XM_006245129.1. [Q63151-1]
    UniGeneiRn.54820.

    Genome annotation databases

    EnsembliENSRNOT00000020161; ENSRNOP00000020161; ENSRNOG00000014718. [Q63151-1]
    GeneIDi114024.
    KEGGirno:114024.
    UCSCiRGD:70552. rat. [Q63151-1]

    Keywords - Coding sequence diversityi

    Alternative initiation

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D30666 mRNA. Translation: BAA06340.1 .
    RefSeqi NP_476448.1. NM_057107.1. [Q63151-1 ]
    XP_006245191.1. XM_006245129.1. [Q63151-1 ]
    UniGenei Rn.54820.

    3D structure databases

    ProteinModelPortali Q63151.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q63151. 1 interaction.
    STRINGi 10116.ENSRNOP00000020161.

    Proteomic databases

    PaxDbi Q63151.
    PRIDEi Q63151.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000020161 ; ENSRNOP00000020161 ; ENSRNOG00000014718 . [Q63151-1 ]
    GeneIDi 114024.
    KEGGi rno:114024.
    UCSCi RGD:70552. rat. [Q63151-1 ]

    Organism-specific databases

    CTDi 2181.
    RGDi 70552. Acsl3.

    Phylogenomic databases

    eggNOGi COG1022.
    GeneTreei ENSGT00690000102168.
    HOGENOMi HOG000159459.
    HOVERGENi HBG106947.
    InParanoidi Q63151.
    KOi K01897.
    OMAi CDRFIFR.
    OrthoDBi EOG7P2XRD.
    PhylomeDBi Q63151.
    TreeFami TF314012.

    Enzyme and pathway databases

    BRENDAi 6.2.1.3. 5301.

    Miscellaneous databases

    NextBioi 618179.
    PROi Q63151.

    Gene expression databases

    Genevestigatori Q63151.

    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. "Molecular characterization and expression of rat acyl-CoA synthetase 3."
      Fujino T., Kang M.-J., Suzuki H., Iijima H., Yamamoto T.T.
      J. Biol. Chem. 271:16748-16752(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION.
      Strain: Wistar.
      Tissue: Brain.
    2. "Alternative translation initiation generates acyl-CoA synthetase 3 isoforms with heterogeneous amino termini."
      Fujino T., Kang M.-J., Minekura H., Suzuki H., Yamamoto T.T.
      J. Biochem. 122:212-216(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE INITIATION.
    3. "Suppression of long chain acyl-CoA synthetase 3 (ACSL3) decreases hepatic de novo fatty acid synthesis through decreased transcriptional activity."
      Bu S.Y., Mashek M.T., Mashek D.G.
      J. Biol. Chem. 284:30474-30483(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.

    Entry informationi

    Entry nameiACSL3_RAT
    AccessioniPrimary (citable) accession number: Q63151
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 27, 2001
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 125 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