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Q06000

- LIPL_RAT

UniProt

Q06000 - LIPL_RAT

Protein

Lipoprotein lipase

Gene

Lpl

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 Feb 1994)
      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: RGD
    3. triglyceride binding Source: RGD

    GO - Biological processi

    1. lipid catabolic process Source: RGD
    2. positive regulation of cholesterol storage Source: Ensembl
    3. positive regulation of macrophage derived foam cell differentiation Source: Ensembl
    4. positive regulation of sequestering of triglyceride Source: Ensembl
    5. response to cold Source: RGD
    6. response to drug Source: RGD
    7. triglyceride biosynthetic process Source: RGD
    8. triglyceride catabolic process Source: Ensembl
    9. triglyceride homeostasis Source: Ensembl

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Lipid degradation, Lipid metabolism

    Keywords - Ligandi

    Heparin-binding

    Enzyme and pathway databases

    BRENDAi3.1.1.34. 5301.
    ReactomeiREACT_199015. Retinoid metabolism and transport.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Lipoprotein lipase (EC:3.1.1.34)
    Short name:
    LPL
    Gene namesi
    Name:Lpl
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 16

    Organism-specific databases

    RGDi3017. Lpl.

    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. cell surface Source: Ensembl
    3. chylomicron Source: UniProtKB-KW
    4. extracellular matrix Source: RGD
    5. plasma membrane Source: UniProtKB-SubCell
    6. very-low-density lipoprotein particle Source: UniProtKB-KW

    Keywords - Cellular componenti

    Cell membrane, Chylomicron, Membrane, Secreted, VLDL

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2727By similarityAdd
    BLAST
    Chaini28 – 474447Lipoprotein lipasePRO_0000017779Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi54 ↔ 67PROSITE-ProRule annotation
    Glycosylationi70 – 701N-linked (GlcNAc...)Sequence Analysis
    Modified residuei121 – 1211Nitrated tyrosine1 Publication
    Modified residuei191 – 1911Nitrated tyrosine1 Publication
    Disulfide bondi243 ↔ 266PROSITE-ProRule annotation
    Disulfide bondi291 ↔ 310PROSITE-ProRule annotation
    Disulfide bondi302 ↔ 305PROSITE-ProRule annotation
    Modified residuei343 – 3431Nitrated tyrosine1 Publication
    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.1 Publication

    Keywords - PTMi

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

    Proteomic databases

    PaxDbiQ06000.
    PRIDEiQ06000.

    Expressioni

    Inductioni

    Induced by insulin. Inhibited by isoproterenol.1 Publication

    Gene expression databases

    GenevestigatoriQ06000.

    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

    Protein-protein interaction databases

    STRINGi10116.ENSRNOP00000016543.

    Structurei

    3D structure databases

    ProteinModelPortaliQ06000.
    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

    eggNOGiNOG40923.
    GeneTreeiENSGT00750000117234.
    HOGENOMiHOG000038553.
    HOVERGENiHBG002259.
    InParanoidiQ06000.
    KOiK01059.
    OMAiESVANCH.
    OrthoDBiEOG757CX5.
    PhylomeDBiQ06000.
    TreeFamiTF324997.

    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.

    Q06000-1 [UniParc]FASTAAdd to Basket

    « Hide

    MESKALLLVA LGVWLQSLTA FRGGVAAADG GRDFSDIESK FALRTPEDTA    50
    EDTCHLIPGL ADSVSNCHFN HSSKTFVVIH GWTVTGMYES WVPKLVAALY 100
    KREPDSNVIV VDWLYRAQQH YPVSAGYTKL VGNDVARFIN WLEEEFNYPL 150
    DNVHLLGYSL GAHAAGVAGS LTNKKVNRIT GLDPAGPNFE YAEAPSRLSP 200
    DDADFVDVLH TFTRGSPGRS IGIQKPVGHV DIYPNGGTFQ PGCNIGEAIR 250
    VIAEKGLGDV DQLVKCSHER SIHLFIDSLL NEENPSKAYR CNSKEAFEKG 300
    LCLSCRKNRC NNVGYEINKV RAKRSSKMYL KTRSQMPYKV FHYQVKIHFS 350
    GTENDKQNNQ AFEISLYGTV AESENIPFTL PEVATNKTYS FLIYTEVDIG 400
    ELLMMKLKWK NDSYFRWSDW WSSPSFVIEK IRVKAGETQK KVIFCAREKV 450
    SHLQKGKDAA VFVKCHDKSL KKSG 474
    Length:474
    Mass (Da):53,082
    Last modified:February 1, 1994 - v1
    Checksum:iF4F6F4BCCA4F1626
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti336 – 3361M → V no nucleotide entry (PubMed:2233752)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L03294 mRNA. Translation: AAA41534.1.
    BC081836 mRNA. Translation: AAH81836.1.
    PIRiJH0790.
    RefSeqiNP_036730.1. NM_012598.2.
    UniGeneiRn.3834.

    Genome annotation databases

    EnsembliENSRNOT00000016543; ENSRNOP00000016543; ENSRNOG00000012181.
    GeneIDi24539.
    KEGGirno:24539.
    UCSCiRGD:3017. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L03294 mRNA. Translation: AAA41534.1 .
    BC081836 mRNA. Translation: AAH81836.1 .
    PIRi JH0790.
    RefSeqi NP_036730.1. NM_012598.2.
    UniGenei Rn.3834.

    3D structure databases

    ProteinModelPortali Q06000.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10116.ENSRNOP00000016543.

    Chemistry

    BindingDBi Q06000.
    ChEMBLi CHEMBL5906.

    Proteomic databases

    PaxDbi Q06000.
    PRIDEi Q06000.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000016543 ; ENSRNOP00000016543 ; ENSRNOG00000012181 .
    GeneIDi 24539.
    KEGGi rno:24539.
    UCSCi RGD:3017. rat.

    Organism-specific databases

    CTDi 4023.
    RGDi 3017. Lpl.

    Phylogenomic databases

    eggNOGi NOG40923.
    GeneTreei ENSGT00750000117234.
    HOGENOMi HOG000038553.
    HOVERGENi HBG002259.
    InParanoidi Q06000.
    KOi K01059.
    OMAi ESVANCH.
    OrthoDBi EOG757CX5.
    PhylomeDBi Q06000.
    TreeFami TF324997.

    Enzyme and pathway databases

    BRENDAi 3.1.1.34. 5301.
    Reactomei REACT_199015. Retinoid metabolism and transport.

    Miscellaneous databases

    NextBioi 603620.
    PROi Q06000.

    Gene expression databases

    Genevestigatori Q06000.

    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. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: Sprague-Dawley.
      Tissue: Testis.
    2. "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: Kidney.
    3. "Lipoprotein lipase gene expression in rat adipocytes is regulated by isoproterenol and insulin through different mechanisms."
      Raynolds M.V., Awald P.D., Gordon D.F., Gutierrez-Hartmann A., Rule D.C., Wood W.M., Eckel R.H.
      Mol. Endocrinol. 4:1416-1422(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 336-474, INDUCTION.
      Tissue: Heart.
    4. "Lipoprotein lipase is nitrated in vivo after lipopolysaccharide challenge."
      Casanovas A., Carrascal M., Abian J., Lopez-Tejero M.D., Llobera M.
      Free Radic. Biol. Med. 47:1553-1560(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: NITRATION AT TYR-121; TYR-191 AND TYR-343, IDENTIFICATION BY MASS SPECTROMETRY.
    5. "Discovery of lipoprotein lipase pI isoforms and contributions to their characterization."
      Casanovas A., Carrascal M., Abian J., Lopez-Tejero M.D., Llobera M.
      J. Proteomics 72:1031-1039(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, GLYCOSYLATION.

    Entry informationi

    Entry nameiLIPL_RAT
    AccessioniPrimary (citable) accession number: Q06000
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1994
    Last sequence update: February 1, 1994
    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, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3