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Q9CZW4

- ACSL3_MOUSE

UniProt

Q9CZW4 - ACSL3_MOUSE

Protein

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

Gene

Acsl3

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 106 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      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 has mainly an anabolic role in energy metabolism By similarity. Required for the incorporation of fatty acids into phosphatidylcholine, the major phospholipid located on the surface of VLDL (very low density lipoproteins) By similarity. Mediates hepatic lipogenesis By similarity. Preferentially uses myristate, laurate, arachidonate and eicosapentaenoate as substrates By similarity.By similarity

    Catalytic activityi

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

    Cofactori

    Magnesium.By similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. brain development Source: Ensembl
    2. fatty acid biosynthetic process Source: Ensembl
    3. long-chain fatty acid import Source: Ensembl
    4. positive regulation of Golgi to plasma membrane protein transport Source: Ensembl
    5. positive regulation of phosphatidylcholine biosynthetic process Source: Ensembl
    6. positive regulation of secretion Source: Ensembl
    7. response to nutrient Source: Ensembl
    8. response to organic cyclic compound Source: Ensembl
    9. 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. 3474.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Long-chain-fatty-acid--CoA ligase 3 (EC:6.2.1.3)
    Alternative name(s):
    Long-chain acyl-CoA synthetase 3
    Short name:
    LACS 3
    Gene namesi
    Name:Acsl3
    Synonyms:Acs3, Facl3
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 1

    Organism-specific databases

    MGIiMGI:1921455. 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_0000193108Add
    BLAST

    Amino acid modifications

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

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9CZW4.
    PaxDbiQ9CZW4.
    PRIDEiQ9CZW4.

    PTM databases

    PhosphoSiteiQ9CZW4.

    Expressioni

    Inductioni

    High expression in ob/ob mice (obese) and mice fed at high sucrose diet.1 Publication

    Gene expression databases

    ArrayExpressiQ9CZW4.
    BgeeiQ9CZW4.
    GenevestigatoriQ9CZW4.

    Interactioni

    Protein-protein interaction databases

    IntActiQ9CZW4. 1 interaction.
    MINTiMINT-4117014.
    STRINGi10090.ENSMUSP00000121695.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9CZW4.
    SMRiQ9CZW4. Positions 135-664.
    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.
    InParanoidiQ8K1J7.
    KOiK01897.
    OMAiCDRFIFR.
    OrthoDBiEOG7P2XRD.
    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]

    Sequencei

    Sequence statusi: Complete.

    Q9CZW4-1 [UniParc]FASTAAdd to Basket

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    MNNHVSSTPS TMKLKQTINP ILLYFIHFII SLYTILTYIP FYFLCESKQE    50
    KPNQIKAKPV SSKPDSAYRS INSVDGLASV LYPGCDTLDK VFMYAKNKFK 100
    NKRLLGTREI LNEEDEIQPN GKIFKKVILG HYNWLSYEDV FIRALDFGNG 150
    LQMLGQKPKA NIAIFCETRA EWMIAAQACF MYNFQLVTLY ATLGGPAIVH 200
    GLNETEVTNI ITSKELLQTK LKDIVSLVPR LRHIITVDGK PPTWSEFPKG 250
    VIVHTMAAVQ ALGVKANVEK KAHSKPLPSD IAVIMYTSGS TGIPKGVMIS 300
    HSNIIASITG MARRIPRLGE EDVYIGYLPL AHVLELSAEL VCLSHGCRIG 350
    YSSPQTLADQ SSKIKKGSKG DTSVLKPTLM AAVPEIMDRI YKNVMNKVNE 400
    MSAFQRNLFI LAYNYKMEQI SKGCSTPLCD RFVFRNVRRL LGGNIRLLLC 450
    GGAPLSATTQ RFMNICFCCP VGQGYGLTES TGAGTITEVW DYNTGRVGAP 500
    LVCCEIKLKN WEEGGYFNTD KPHPRGEILI GGQNVTMGYY KNEAKTKTDF 550
    FEDENGQRWL CTGDIGEFDP DGCLKIIDRK KDLVKLQAGE YVSLGKVEAA 600
    LKNLPLIDNI CAYANSYHSY VIGFVVPNQK ELTELARTKG FKGTWEELCN 650
    SSEMENEVLK VLSEAAISAS LEKFEIPLKI RLSPDPWTPE TGLVTDAFKL 700
    KRKELKTHYQ ADIERMYGRK 720
    Length:720
    Mass (Da):80,492
    Last modified:July 27, 2011 - v2
    Checksum:i27F9CCA6961B5BA0
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti223 – 2231D → E in BAB28022. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK012088 mRNA. Translation: BAB28022.1.
    AK161708 mRNA. Translation: BAE36543.1.
    CH466548 Genomic DNA. Translation: EDL00440.1.
    CH466548 Genomic DNA. Translation: EDL00441.1.
    BC031529 mRNA. Translation: AAH31529.1.
    CCDSiCCDS15087.1.
    RefSeqiNP_001028778.2. NM_001033606.2.
    NP_001129694.1. NM_001136222.1.
    NP_083093.2. NM_028817.3.
    UniGeneiMm.276016.

    Genome annotation databases

    EnsembliENSMUST00000035779; ENSMUSP00000045291; ENSMUSG00000032883.
    ENSMUST00000142704; ENSMUSP00000121695; ENSMUSG00000032883.
    GeneIDi74205.
    KEGGimmu:74205.
    UCSCiuc007bqo.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK012088 mRNA. Translation: BAB28022.1 .
    AK161708 mRNA. Translation: BAE36543.1 .
    CH466548 Genomic DNA. Translation: EDL00440.1 .
    CH466548 Genomic DNA. Translation: EDL00441.1 .
    BC031529 mRNA. Translation: AAH31529.1 .
    CCDSi CCDS15087.1.
    RefSeqi NP_001028778.2. NM_001033606.2.
    NP_001129694.1. NM_001136222.1.
    NP_083093.2. NM_028817.3.
    UniGenei Mm.276016.

    3D structure databases

    ProteinModelPortali Q9CZW4.
    SMRi Q9CZW4. Positions 135-664.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q9CZW4. 1 interaction.
    MINTi MINT-4117014.
    STRINGi 10090.ENSMUSP00000121695.

    PTM databases

    PhosphoSitei Q9CZW4.

    Proteomic databases

    MaxQBi Q9CZW4.
    PaxDbi Q9CZW4.
    PRIDEi Q9CZW4.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000035779 ; ENSMUSP00000045291 ; ENSMUSG00000032883 .
    ENSMUST00000142704 ; ENSMUSP00000121695 ; ENSMUSG00000032883 .
    GeneIDi 74205.
    KEGGi mmu:74205.
    UCSCi uc007bqo.2. mouse.

    Organism-specific databases

    CTDi 2181.
    MGIi MGI:1921455. Acsl3.

    Phylogenomic databases

    eggNOGi COG1022.
    GeneTreei ENSGT00690000102168.
    HOGENOMi HOG000159459.
    HOVERGENi HBG106947.
    InParanoidi Q8K1J7.
    KOi K01897.
    OMAi CDRFIFR.
    OrthoDBi EOG7P2XRD.
    TreeFami TF314012.

    Enzyme and pathway databases

    BRENDAi 6.2.1.3. 3474.

    Miscellaneous databases

    NextBioi 340106.
    PROi Q9CZW4.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9CZW4.
    Bgeei Q9CZW4.
    Genevestigatori Q9CZW4.

    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. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Embryo.
    2. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Czech II.
      Tissue: Mammary tumor.
    4. "Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
      Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
      Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Brain.
    5. "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: INDUCTION.

    Entry informationi

    Entry nameiACSL3_MOUSE
    AccessioniPrimary (citable) accession number: Q9CZW4
    Secondary accession number(s): Q8K1J7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 2, 2002
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 106 of the entry and version 2 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. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3