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P18163

- ACSL1_RAT

UniProt

P18163 - ACSL1_RAT

Protein

Long-chain-fatty-acid--CoA ligase 1

Gene

Acsl1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 124 (01 Oct 2014)
      Sequence version 1 (01 Nov 1990)
      Previous versions | rss
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    Functioni

    Activation of long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. Preferentially uses oleate, arachidonate, eicosapentaenoate and docosahexaenoate as substrates.

    Catalytic activityi

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

    Cofactori

    Magnesium.

    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: UniProtKB

    GO - Biological processi

    1. adiponectin-activated signaling pathway Source: Ensembl
    2. fatty acid metabolic process Source: RGD
    3. fatty acid transport Source: RGD
    4. lipid biosynthetic process Source: Ensembl
    5. lipid metabolic process Source: RGD
    6. long-chain fatty acid import Source: Ensembl
    7. positive regulation of protein serine/threonine kinase activity Source: Ensembl
    8. response to drug Source: RGD
    9. response to nutrient Source: RGD
    10. response to oleic acid Source: RGD
    11. response to organic cyclic compound Source: RGD
    12. response to organic substance Source: RGD
    13. triglyceride metabolic process Source: RGD
    14. xenobiotic catabolic process 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

    BioCyciMetaCyc:MONOMER-14442.
    BRENDAi6.2.1.3. 5301.
    ReactomeiREACT_196408. PPARA activates gene expression.
    REACT_198818. alpha-linolenic acid (ALA) metabolism.
    REACT_198820. Linoleic acid (LA) metabolism.
    SABIO-RKP18163.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Long-chain-fatty-acid--CoA ligase 1 (EC:6.2.1.3)
    Alternative name(s):
    Long-chain acyl-CoA synthetase 1
    Short name:
    LACS 1
    Long-chain-fatty-acid--CoA ligase, liver isozyme
    Gene namesi
    Name:Acsl1
    Synonyms:Acs1, Acsl2, Facl2
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 16

    Organism-specific databases

    RGDi2015. Acsl1.

    Subcellular locationi

    GO - Cellular componenti

    1. endoplasmic reticulum Source: RGD
    2. endoplasmic reticulum membrane Source: UniProtKB-SubCell
    3. integral component of membrane Source: UniProtKB-KW
    4. mitochondrial outer membrane Source: RGD
    5. peroxisomal membrane Source: HGNC
    6. plasma membrane Source: RGD

    Keywords - Cellular componenti

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

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 699699Long-chain-fatty-acid--CoA ligase 1PRO_0000193106Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei9 – 91Nitrated tyrosine1 Publication
    Modified residuei85 – 851Phosphotyrosine1 Publication
    Modified residuei86 – 861Nitrated tyrosine1 Publication
    Glycosylationi136 – 1361O-linked (GlcNAc)1 Publication
    Modified residuei208 – 2081N6-acetyllysineBy similarity
    Modified residuei357 – 3571N6-acetyllysineBy similarity
    Modified residuei387 – 3871N6-acetyllysineBy similarity
    Modified residuei621 – 6211PhosphoserineBy similarity
    Modified residuei633 – 6331N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation, Glycoprotein, Nitration, Phosphoprotein

    Proteomic databases

    PaxDbiP18163.
    PRIDEiP18163.

    PTM databases

    PhosphoSiteiP18163.

    Expressioni

    Tissue specificityi

    Liver, heart, epididymal adipose and to a lesser extent brain, small intestine and lung.

    Developmental stagei

    Levels remain constant during development.

    Inductioni

    By high fat and high carbohydrate diets.

    Gene expression databases

    GenevestigatoriP18163.

    Interactioni

    Protein-protein interaction databases

    IntActiP18163. 28 interactions.
    MINTiMINT-4570488.
    STRINGi10116.ENSRNOP00000014235.

    Structurei

    3D structure databases

    ProteinModelPortaliP18163.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini46 – 699654CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei25 – 4521Helical; Signal-anchor for type III membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG1022.
    GeneTreeiENSGT00690000101725.
    HOGENOMiHOG000159459.
    HOVERGENiHBG050452.
    InParanoidiP18163.
    KOiK01897.
    OMAiWDRLIFH.
    OrthoDBiEOG71CFKN.
    PhylomeDBiP18163.
    TreeFamiTF313877.

    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.

    P18163-1 [UniParc]FASTAAdd to Basket

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    MEVHELFRYF RMPELIDIRQ YVRTLPTNTL MGFGAFAALT TFWYATRPKA    50
    LKPPCDLSMQ SVEVTGTTEG VRRSAVLEDD KLLLYYYDDV RTMYDGFQRG 100
    IQVSNDGPCL GSRKPNQPYE WISYKQVAEM AECIGSALIQ KGFKPCSEQF 150
    IGIFSQNRPE WVTIEQGCFT YSMVVVPLYD TLGTDAITYI VNKAELSVIF 200
    ADKPEKAKLL LEGVENKLTP CLKIIVIMDS YDNDLVERGQ KCGVEIIGLK 250
    ALEDLGRVNR TKPKPPEPED LAIICFTSGT TGNPKGAMVT HQNIMNDCSG 300
    FIKATESAFI ASPEDVLISF LPLAHMFETV VECVMLCHGA KIGFFQGDIR 350
    LLMDDLKVLQ PTIFPVVPRL LNRMFDRIFG QANTSVKRWL LDFASKRKEA 400
    ELRSGIVRNN SLWDKLIFHK IQSSLGGKVR LMITGAAPVS ATVLTFLRAA 450
    LGCQFYEGYG QTECTAGCCL SLPGDWTAGH VGAPMPCNYI KLVDVEDMNY 500
    QAAKGEGEVC VKGANVFKGY LKDPARTAEA LDKDGWLHTG DIGKWLPNGT 550
    LKIIDRKKHI FKLAQGEYIA PEKIENIYLR SEAVAQVFVH GESLQAFLIA 600
    IVVPDVEILP SWAQKRGFQG SFEELCRNKD INKAILEDMV KLGKNAGLKP 650
    FEQVKGIAVH PELFSIDNGL LTPTLKAKRP ELRNYFRSQI DELYSTIKI 699
    Length:699
    Mass (Da):78,179
    Last modified:November 1, 1990 - v1
    Checksum:i6E1EACE0EAE8A85C
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D90109 mRNA. Translation: BAA14136.1.
    PIRiA36275.
    RefSeqiNP_036952.1. NM_012820.1.
    XP_006253184.1. XM_006253122.1.
    XP_006253185.1. XM_006253123.1.
    XP_006253186.1. XM_006253124.1.
    XP_006253187.1. XM_006253125.1.
    XP_006253188.1. XM_006253126.1.
    XP_006253189.1. XM_006253127.1.
    UniGeneiRn.6215.

    Genome annotation databases

    EnsembliENSRNOT00000014235; ENSRNOP00000014235; ENSRNOG00000010633.
    GeneIDi25288.
    KEGGirno:25288.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D90109 mRNA. Translation: BAA14136.1 .
    PIRi A36275.
    RefSeqi NP_036952.1. NM_012820.1.
    XP_006253184.1. XM_006253122.1.
    XP_006253185.1. XM_006253123.1.
    XP_006253186.1. XM_006253124.1.
    XP_006253187.1. XM_006253125.1.
    XP_006253188.1. XM_006253126.1.
    XP_006253189.1. XM_006253127.1.
    UniGenei Rn.6215.

    3D structure databases

    ProteinModelPortali P18163.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P18163. 28 interactions.
    MINTi MINT-4570488.
    STRINGi 10116.ENSRNOP00000014235.

    PTM databases

    PhosphoSitei P18163.

    Proteomic databases

    PaxDbi P18163.
    PRIDEi P18163.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000014235 ; ENSRNOP00000014235 ; ENSRNOG00000010633 .
    GeneIDi 25288.
    KEGGi rno:25288.

    Organism-specific databases

    CTDi 2180.
    RGDi 2015. Acsl1.

    Phylogenomic databases

    eggNOGi COG1022.
    GeneTreei ENSGT00690000101725.
    HOGENOMi HOG000159459.
    HOVERGENi HBG050452.
    InParanoidi P18163.
    KOi K01897.
    OMAi WDRLIFH.
    OrthoDBi EOG71CFKN.
    PhylomeDBi P18163.
    TreeFami TF313877.

    Enzyme and pathway databases

    BioCyci MetaCyc:MONOMER-14442.
    BRENDAi 6.2.1.3. 5301.
    Reactomei REACT_196408. PPARA activates gene expression.
    REACT_198818. alpha-linolenic acid (ALA) metabolism.
    REACT_198820. Linoleic acid (LA) metabolism.
    SABIO-RK P18163.

    Miscellaneous databases

    NextBioi 606025.
    PROi P18163.

    Gene expression databases

    Genevestigatori P18163.

    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. "Structure and regulation of rat long-chain acyl-CoA synthetase."
      Suzuki H., Kawarabayasi Y., Kondo J., Abe T., Nishikawa K., Kimura S., Hashimoto T., Yamamoto T.
      J. Biol. Chem. 265:8681-8685(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
      Strain: Wistar.
      Tissue: Liver.
    2. "Post-translational modifications of rat liver mitochondrial outer membrane proteins identified by mass spectrometry."
      Distler A.M., Kerner J., Hoppel C.L.
      Biochim. Biophys. Acta 1774:628-636(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-19; 82-91 AND 628-641, ACETYLATION AT MET-1 AND LYS-633, NITRATION AT TYR-9 AND TYR-86, PHOSPHORYLATION AT TYR-85, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Liver.
    3. "Biochemical studies of two rat acyl-CoA synthetases, ACS1 and ACS2."
      Iijima H., Fujino T., Minekura H., Suzuki H., Kang M.-J., Yamamoto T.T.
      Eur. J. Biochem. 242:186-190(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    4. "Discovery and confirmation of O-GlcNAcylated proteins in rat liver mitochondria by combination of mass spectrometry and immunological methods."
      Cao W., Cao J., Huang J., Yao J., Yan G., Xu H., Yang P.
      PLoS ONE 8:E76399-E76399(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION AT SER-136.

    Entry informationi

    Entry nameiACSL1_RAT
    AccessioniPrimary (citable) accession number: P18163
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1990
    Last sequence update: November 1, 1990
    Last modified: October 1, 2014
    This is version 124 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, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3