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O46647

- LIPL_NEOVI

UniProt

O46647 - LIPL_NEOVI

Protein

Lipoprotein lipase

Gene

LPL

Organism
Neovison vison (American mink) (Mustela vison)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 90 (01 Oct 2014)
      Sequence version 1 (01 Jun 1998)
      Previous versions | rss
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    Functioni

    The primary function of this lipase is the hydrolysis of triglycerides of circulating chylomicrons and very low density lipoproteins (VLDL). Binding to heparin sulfate proteogylcans at the cell surface is vital to the function. The apolipoprotein, APOC2, acts as a coactivator of LPL activity in the presence of lipids on the luminal surface of vascular endothelium By similarity.By similarity

    Catalytic activityi

    Triacylglycerol + H2O = diacylglycerol + a carboxylate.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei159 – 1591NucleophileBy similarity
    Active sitei183 – 1831Charge relay systemPROSITE-ProRule annotation
    Active sitei268 – 2681Charge relay systemPROSITE-ProRule annotation

    GO - Molecular functioni

    1. heparin binding Source: UniProtKB-KW
    2. lipoprotein lipase activity Source: UniProtKB-EC

    GO - Biological processi

    1. lipid catabolic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Lipid degradation, Lipid metabolism

    Keywords - Ligandi

    Heparin-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Lipoprotein lipase (EC:3.1.1.34)
    Short name:
    LPL
    Gene namesi
    Name:LPL
    OrganismiNeovison vison (American mink) (Mustela vison)
    Taxonomic identifieri452646 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaMustelidaeMustelinaeNeovison

    Subcellular locationi

    Cell membrane By similarity; Lipid-anchorGPI-anchor By similarity. Secreted By similarity
    Note: Locates to the plasma membrane of microvilli of hepatocytes with triacyl-glycerol-rich lipoproteins (TRL). Some of the bound LPL is then internalized and located inside non-coated endocytic vesicles By similarity.By similarity

    GO - Cellular componenti

    1. anchored component of membrane Source: UniProtKB-KW
    2. chylomicron Source: UniProtKB-KW
    3. plasma membrane Source: UniProtKB-SubCell
    4. very-low-density lipoprotein particle Source: UniProtKB-KW

    Keywords - Cellular componenti

    Cell membrane, Chylomicron, Membrane, Secreted, VLDL

    Pathology & Biotechi

    Involvement in diseasei

    Defects in LPL are a cause of chylomicronemia syndrome, also known as type I hyperlipoproteinemia.1 Publication

    Keywords - Diseasei

    Disease mutation, Hyperlipidemia

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2727By similarityAdd
    BLAST
    Chaini28 – 475448Lipoprotein lipasePRO_0000017777Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi54 ↔ 67PROSITE-ProRule annotation
    Glycosylationi70 – 701N-linked (GlcNAc...)Sequence Analysis
    Modified residuei121 – 1211Nitrated tyrosineBy similarity
    Modified residuei191 – 1911Nitrated tyrosineBy similarity
    Disulfide bondi243 ↔ 266PROSITE-ProRule annotation
    Disulfide bondi291 ↔ 310PROSITE-ProRule annotation
    Disulfide bondi302 ↔ 305PROSITE-ProRule annotation
    Modified residuei343 – 3431Nitrated tyrosineBy similarity
    Glycosylationi386 – 3861N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi445 ↔ 465PROSITE-ProRule annotation

    Post-translational modificationi

    Tyrosine nitration after lipopolysaccharide (LPS) challenge down-regulates the lipase activity.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein, Nitration

    Interactioni

    Subunit structurei

    Homodimer By similarity. Interacts with APOC2; the interaction activates LPL activity in the presence of lipids. Interacts with GPIHBP1 By similarity.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliO46647.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini341 – 464124PLATPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni346 – 44196Heparin-bindingBy similarityAdd
    BLAST

    Sequence similaritiesi

    Belongs to the AB hydrolase superfamily. Lipase family.Curated
    Contains 1 PLAT domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Phylogenomic databases

    HOVERGENiHBG002259.

    Family and domain databases

    Gene3Di2.60.60.20. 1 hit.
    3.40.50.1820. 1 hit.
    InterProiIPR029058. AB_hydrolase.
    IPR000734. Lipase.
    IPR008976. Lipase_LipOase.
    IPR013818. Lipase_N.
    IPR002330. Lipo_Lipase.
    IPR016272. Lipoprotein_lipase_LIPH.
    IPR001024. PLAT/LH2_dom.
    [Graphical view]
    PANTHERiPTHR11610. PTHR11610. 1 hit.
    PTHR11610:SF3. PTHR11610:SF3. 1 hit.
    PfamiPF00151. Lipase. 1 hit.
    PF01477. PLAT. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000865. Lipoprotein_lipase_LIPH. 1 hit.
    PRINTSiPR00822. LIPOLIPASE.
    PR00821. TAGLIPASE.
    SMARTiSM00308. LH2. 1 hit.
    [Graphical view]
    SUPFAMiSSF49723. SSF49723. 1 hit.
    SSF53474. SSF53474. 1 hit.
    TIGRFAMsiTIGR03230. lipo_lipase. 1 hit.
    PROSITEiPS00120. LIPASE_SER. 1 hit.
    PS50095. PLAT. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    O46647-1 [UniParc]FASTAAdd to Basket

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    MESKALLLVA LGMWFQSLTA TRGGVAAADR GGDFIDIESK FALRTPEDTA    50
    EDTCHLIPGV TESVANCHFN HSSKTFVVIH GWTVTGMYES WVPKLVAALY 100
    KREPDSNVIV VDWLSRAQQH YPVSAGYTKL VGKDVAKFIN WMAEEFHYPL 150
    DNVHLLGYSL GAHAAGIAGS LTNKKVNRIT GLDPAGPNFE YAEAPSRLSP 200
    DDADFVDVLH TFTRGSPGRS IGIQKPVGHV DIYPNGGTFQ PGCNIGEAIR 250
    VIAERGLGDV DQLVKCSHER SIHLFIDSLL NEENPSKAYR CNSKEAFEKG 300
    LCLSCRKNRC NNLGYEINKV RAKRSSKMYL KTRSQMPYKV FHYQVKIHFS 350
    GTESDTQTNQ AFEISLYGTV AESENIPFTL PEVSANKTYS FLIYTEVDIG 400
    ELLMLKLKWK SDSYFSWSDW WSSPGFAIEK IRVKAGETQK KVIFCSREKV 450
    SHLQKGKASV VFVKCHDKSL NKKSG 475
    Length:475
    Mass (Da):52,968
    Last modified:June 1, 1998 - v1
    Checksum:i2F2DBF0090F0FB7C
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti241 – 2411P → L in chylomicronemia syndrome; no lipase activity. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ223493 Genomic DNA. Translation: CAA11411.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ223493 Genomic DNA. Translation: CAA11411.1 .

    3D structure databases

    ProteinModelPortali O46647.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    HOVERGENi HBG002259.

    Family and domain databases

    Gene3Di 2.60.60.20. 1 hit.
    3.40.50.1820. 1 hit.
    InterProi IPR029058. AB_hydrolase.
    IPR000734. Lipase.
    IPR008976. Lipase_LipOase.
    IPR013818. Lipase_N.
    IPR002330. Lipo_Lipase.
    IPR016272. Lipoprotein_lipase_LIPH.
    IPR001024. PLAT/LH2_dom.
    [Graphical view ]
    PANTHERi PTHR11610. PTHR11610. 1 hit.
    PTHR11610:SF3. PTHR11610:SF3. 1 hit.
    Pfami PF00151. Lipase. 1 hit.
    PF01477. PLAT. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000865. Lipoprotein_lipase_LIPH. 1 hit.
    PRINTSi PR00822. LIPOLIPASE.
    PR00821. TAGLIPASE.
    SMARTi SM00308. LH2. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49723. SSF49723. 1 hit.
    SSF53474. SSF53474. 1 hit.
    TIGRFAMsi TIGR03230. lipo_lipase. 1 hit.
    PROSITEi PS00120. LIPASE_SER. 1 hit.
    PS50095. PLAT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A mutation in the lipoprotein lipase gene associated with hyperlipoproteinemia type I in mink: studies on lipid and lipase levels in heterozygotes."
      Lindberg A., Nordstoga K., Christophersen B., Savonen R., van Tol A., Olivecrona G.
      Int. J. Mol. Med. 1:529-538(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT CHYLOMICRONEMIA SYNDROME LEU-241.
      Tissue: Heart.

    Entry informationi

    Entry nameiLIPL_NEOVI
    AccessioniPrimary (citable) accession number: O46647
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: June 1, 1998
    Last modified: October 1, 2014
    This is version 90 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3