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Q5R668

- ACSL3_PONAB

UniProt

Q5R668 - ACSL3_PONAB

Protein

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

Gene

ACSL3

Organism
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 59 (01 Oct 2014)
      Sequence version 2 (13 Jun 2006)
      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

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Fatty acid metabolism, Lipid metabolism

    Keywords - Ligandi

    ATP-binding, Magnesium, Nucleotide-binding

    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
    OrganismiPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
    Taxonomic identifieri9601 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo
    ProteomesiUP000001595: Unplaced

    Subcellular locationi

    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. 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_0000240276Add
    BLAST

    Amino acid modifications

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

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PRIDEiQ5R668.

    Structurei

    3D structure databases

    ProteinModelPortaliQ5R668.
    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

    HOVERGENiHBG106947.
    InParanoidiQ5R668.
    KOiK01897.

    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.

    Q5R668-1 [UniParc]FASTAAdd to Basket

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    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 SKGRNTPLCN SFVFRKVRSL LGGNIRLLLC 450
    GGAPLSATTQ RFMNICFCCP VGQGYGLTES AGAGTISEVW DYNTGRVGAP 500
    LVCCEIKLKN WEEGGYFNTD KPHPRGEILI GGQIVTMGYY 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):80,445
    Last modified:June 13, 2006 - v2
    Checksum:iC5E83CFBD6904101
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti104 – 1041L → P in CAH91520. 1 PublicationCurated
    Sequence conflicti112 – 1121N → S in CAH93302. 1 PublicationCurated
    Sequence conflicti117 – 1171V → I in CAH93302. 1 PublicationCurated
    Sequence conflicti210 – 2101I → T in CAH91520. 1 PublicationCurated
    Sequence conflicti270 – 2701N → D in CAH93302. 1 PublicationCurated
    Sequence conflicti386 – 3861I → T in CAH92748. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR859345 mRNA. Translation: CAH91520.1.
    CR860628 mRNA. Translation: CAH92748.1.
    CR861232 mRNA. Translation: CAH93302.1.
    RefSeqiNP_001127581.1. NM_001134109.1.
    NP_001128901.1. NM_001135429.1.
    UniGeneiPab.19655.

    Genome annotation databases

    GeneIDi100174659.
    100189843.
    KEGGipon:100174659.
    pon:100189843.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR859345 mRNA. Translation: CAH91520.1 .
    CR860628 mRNA. Translation: CAH92748.1 .
    CR861232 mRNA. Translation: CAH93302.1 .
    RefSeqi NP_001127581.1. NM_001134109.1.
    NP_001128901.1. NM_001135429.1.
    UniGenei Pab.19655.

    3D structure databases

    ProteinModelPortali Q5R668.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi Q5R668.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 100174659.
    100189843.
    KEGGi pon:100174659.
    pon:100189843.

    Organism-specific databases

    CTDi 2181.

    Phylogenomic databases

    HOVERGENi HBG106947.
    InParanoidi Q5R668.
    KOi K01897.

    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 German cDNA consortium
      Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain cortex.

    Entry informationi

    Entry nameiACSL3_PONAB
    AccessioniPrimary (citable) accession number: Q5R668
    Secondary accession number(s): Q5R4L4, Q5R9P0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 13, 2006
    Last sequence update: June 13, 2006
    Last modified: October 1, 2014
    This is version 59 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3