Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

O95573

- ACSL3_HUMAN

UniProt

O95573 - ACSL3_HUMAN

Protein

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

Gene

ACSL3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 131 (01 Oct 2014)
      Sequence version 3 (03 Oct 2006)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Acyl-CoA synthetases (ACSL) activates long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. ACSL3 mediates hepatic lipogenesis By similarity. Preferentially uses myristate, laurate, arachidonate and eicosapentaenoate as substrates By similarity. Has mainly an anabolic role in energy metabolism. Required for the incorporation of fatty acids into phosphatidylcholine, the major phospholipid located on the surface of VLDL (very low density lipoproteins).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. ATP binding Source: UniProtKB-KW
    2. long-chain fatty acid-CoA ligase activity Source: UniProtKB
    3. protein domain specific binding Source: UniProtKB
    4. protein kinase binding Source: UniProtKB

    GO - Biological processi

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

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Fatty acid metabolism, Lipid metabolism

    Keywords - Ligandi

    ATP-binding, Magnesium, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:HS04703-MONOMER.
    BRENDAi6.2.1.3. 2681.
    ReactomeiREACT_380. Synthesis of very long-chain fatty acyl-CoAs.

    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, LACS3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:3570. ACSL3.

    Subcellular locationi

    GO - Cellular componenti

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

    Keywords - Cellular componenti

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

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA27967.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 720720Long-chain-fatty-acid--CoA ligase 3PRO_0000193107Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei683 – 6831Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiO95573.
    PaxDbiO95573.
    PeptideAtlasiO95573.
    PRIDEiO95573.

    PTM databases

    PhosphoSiteiO95573.

    Expressioni

    Gene expression databases

    ArrayExpressiO95573.
    BgeeiO95573.
    CleanExiHS_ACSL3.
    GenevestigatoriO95573.

    Organism-specific databases

    HPAiHPA011315.

    Interactioni

    Protein-protein interaction databases

    BioGridi108477. 17 interactions.
    IntActiO95573. 11 interactions.
    MINTiMINT-4527745.
    STRINGi9606.ENSP00000350012.

    Structurei

    3D structure databases

    ProteinModelPortaliO95573.
    SMRiO95573. Positions 122-641.
    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.
    HOGENOMiHOG000159459.
    HOVERGENiHBG106947.
    InParanoidiO95573.
    KOiK01897.
    OMAiCDRFIFR.
    OrthoDBiEOG7P2XRD.
    PhylomeDBiO95573.
    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.

    O95573-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNNHVSSKPS TMKLKHTINP ILLYFIHFLI SLYTILTYIP FYFFSESRQE    50
    KSNRIKAKPV NSKPDSAYRS VNSLDGLASV LYPGCDTLDK VFTYAKNKFK 100
    NKRLLGTREV LNEEDEVQPN GKIFKKVILG QYNWLSYEDV FVRAFNFGNG 150
    LQMLGQKPKT NIAIFCETRA EWMIAAQACF MYNFQLVTLY ATLGGPAIVH 200
    ALNETEVTNI ITSKELLQTK LKDIVSLVPR LRHIITVDGK PPTWSEFPKG 250
    IIVHTMAAVE ALGAKASMEN QPHSKPLPSD IAVIMYTSGS TGLPKGVMIS 300
    HSNIIAGITG MAERIPELGE EDVYIGYLPL AHVLELSAEL VCLSHGCRIG 350
    YSSPQTLADQ SSKIKKGSKG DTSMLKPTLM AAVPEIMDRI YKNVMNKVSE 400
    MSSFQRNLFI LAYNYKMEQI SKGRNTPLCD SFVFRKVRSL LGGNIRLLLC 450
    GGAPLSATTQ RFMNICFCCP VGQGYGLTES AGAGTISEVW DYNTGRVGAP 500
    LVCCEIKLKN WEEGGYFNTD KPHPRGEILI GGQSVTMGYY KNEAKTKADF 550
    FEDENGQRWL CTGDIGEFEP DGCLKIIDRK KDLVKLQAGE YVSLGKVEAA 600
    LKNLPLVDNI CAYANSYHSY VIGFVVPNQK ELTELARKKG LKGTWEELCN 650
    SCEMENEVLK VLSEAAISAS LEKFEIPVKI RLSPEPWTPE TGLVTDAFKL 700
    KRKELKTHYQ ADIERMYGRK 720
    Length:720
    Mass (Da):80,420
    Last modified:October 3, 2006 - v3
    Checksum:iAAC4B0B4543EC8DD
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti246 – 2461E → D in BAA37142. (PubMed:9177793)Curated
    Sequence conflicti246 – 2461E → D in BAB72074. (PubMed:11707336)Curated
    Sequence conflicti246 – 2461E → D in BAB72139. (PubMed:11707336)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti551 – 5511F → S.2 Publications
    Corresponds to variant rs1046032 [ dbSNP | Ensembl ].
    VAR_026716

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D89053 mRNA. Translation: BAA37142.1.
    AB061712 mRNA. Translation: BAB72074.1.
    AB061436 Genomic DNA. Translation: BAB72139.1.
    BC041692 mRNA. Translation: AAH41692.1.
    CCDSiCCDS2455.1.
    RefSeqiNP_004448.2. NM_004457.3.
    NP_976251.1. NM_203372.1.
    UniGeneiHs.655772.

    Genome annotation databases

    EnsembliENST00000357430; ENSP00000350012; ENSG00000123983.
    ENST00000392066; ENSP00000375918; ENSG00000123983.
    GeneIDi2181.
    KEGGihsa:2181.
    UCSCiuc002vni.3. human.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D89053 mRNA. Translation: BAA37142.1 .
    AB061712 mRNA. Translation: BAB72074.1 .
    AB061436 Genomic DNA. Translation: BAB72139.1 .
    BC041692 mRNA. Translation: AAH41692.1 .
    CCDSi CCDS2455.1.
    RefSeqi NP_004448.2. NM_004457.3.
    NP_976251.1. NM_203372.1.
    UniGenei Hs.655772.

    3D structure databases

    ProteinModelPortali O95573.
    SMRi O95573. Positions 122-641.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108477. 17 interactions.
    IntActi O95573. 11 interactions.
    MINTi MINT-4527745.
    STRINGi 9606.ENSP00000350012.

    Chemistry

    DrugBanki DB00159. Icosapent.

    PTM databases

    PhosphoSitei O95573.

    Proteomic databases

    MaxQBi O95573.
    PaxDbi O95573.
    PeptideAtlasi O95573.
    PRIDEi O95573.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000357430 ; ENSP00000350012 ; ENSG00000123983 .
    ENST00000392066 ; ENSP00000375918 ; ENSG00000123983 .
    GeneIDi 2181.
    KEGGi hsa:2181.
    UCSCi uc002vni.3. human.

    Organism-specific databases

    CTDi 2181.
    GeneCardsi GC02P223725.
    HGNCi HGNC:3570. ACSL3.
    HPAi HPA011315.
    MIMi 602371. gene.
    neXtProti NX_O95573.
    PharmGKBi PA27967.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1022.
    HOGENOMi HOG000159459.
    HOVERGENi HBG106947.
    InParanoidi O95573.
    KOi K01897.
    OMAi CDRFIFR.
    OrthoDBi EOG7P2XRD.
    PhylomeDBi O95573.
    TreeFami TF314012.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS04703-MONOMER.
    BRENDAi 6.2.1.3. 2681.
    Reactomei REACT_380. Synthesis of very long-chain fatty acyl-CoAs.

    Miscellaneous databases

    GeneWikii ACSL3.
    GenomeRNAii 2181.
    NextBioi 8805.
    PROi O95573.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O95573.
    Bgeei O95573.
    CleanExi HS_ACSL3.
    Genevestigatori O95573.

    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. "Human acyl-coenzyme A synthetase 3 cDNA and localization of its gene (ACS3) to chromosome band 2q34-q35."
      Minekura H., Fujino T., Kang M.-J., Fujita T., Endo Y., Yamamoto T.T.
      Genomics 42:180-181(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT SER-551.
      Tissue: Placenta.
    2. "Genomic organization and transcription units of the human acyl-CoA synthetase 3 gene."
      Minekura H., Kang M.-J., Inagaki Y., Suzuki H., Sato H., Fujino T., Yamamoto T.T.
      Gene 278:185-192(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], VARIANT SER-551.
    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].
      Tissue: Pancreas.
    4. "Long chain acyl-CoA synthetase 3-mediated phosphatidylcholine synthesis is required for assembly of very low density lipoproteins in human hepatoma Huh7 cells."
      Yao H., Ye J.
      J. Biol. Chem. 283:849-854(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    5. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-683, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiACSL3_HUMAN
    AccessioniPrimary (citable) accession number: O95573
    Secondary accession number(s): Q60I92, Q8IUM9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 27, 2001
    Last sequence update: October 3, 2006
    Last modified: October 1, 2014
    This is version 131 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3