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P11151

- LIPL_BOVIN

UniProt

P11151 - LIPL_BOVIN

Protein

Lipoprotein lipase

Gene

LPL

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 122 (01 Oct 2014)
      Sequence version 2 (12 Dec 2006)
      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.

    Catalytic activityi

    Triacylglycerol + H2O = diacylglycerol + a carboxylate.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei162 – 1621NucleophileBy similarity
    Active sitei186 – 1861Charge relay systemPROSITE-ProRule annotation
    Active sitei271 – 2711Charge relay systemPROSITE-ProRule annotation

    GO - Molecular functioni

    1. apolipoprotein binding Source: BHF-UCL
    2. heparin binding Source: UniProtKB-KW
    3. lipoprotein lipase activity Source: BHF-UCL
    4. phospholipase activity Source: BHF-UCL
    5. protein binding Source: IntAct
    6. triglyceride lipase activity Source: BHF-UCL

    GO - Biological processi

    1. fatty acid biosynthetic process Source: BHF-UCL
    2. phospholipid metabolic process Source: BHF-UCL
    3. positive regulation of cholesterol storage Source: Ensembl
    4. positive regulation of macrophage derived foam cell differentiation Source: Ensembl
    5. positive regulation of sequestering of triglyceride Source: Ensembl
    6. triglyceride catabolic process Source: BHF-UCL
    7. triglyceride homeostasis Source: Ensembl
    8. triglyceride metabolic process Source: BHF-UCL
    9. very-low-density lipoprotein particle remodeling Source: BHF-UCL

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Lipid degradation, Lipid metabolism

    Keywords - Ligandi

    Heparin-binding

    Enzyme and pathway databases

    BRENDAi3.1.1.34. 908.
    ReactomeiREACT_204227. Retinoid metabolism and transport.
    REACT_206940. Chylomicron-mediated lipid transport.
    REACT_220799. Transcriptional regulation of white adipocyte differentiation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Lipoprotein lipase (EC:3.1.1.34)
    Short name:
    LPL
    Gene namesi
    Name:LPL
    OrganismiBos taurus (Bovine)
    Taxonomic identifieri9913 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
    ProteomesiUP000009136: Chromosome 8

    Subcellular locationi

    Cell membrane; Lipid-anchorGPI-anchor. Secreted
    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.

    GO - Cellular componenti

    1. anchored component of membrane Source: UniProtKB-KW
    2. cell surface Source: Ensembl
    3. chylomicron Source: UniProtKB-KW
    4. plasma membrane Source: UniProtKB-SubCell
    5. 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 – 28282 PublicationsAdd
    BLAST
    Chaini29 – 478450Lipoprotein lipasePRO_0000017772Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi57 ↔ 701 PublicationPROSITE-ProRule annotation
    Glycosylationi73 – 731N-linked (GlcNAc...)
    Modified residuei124 – 1241Nitrated tyrosineBy similarity
    Modified residuei194 – 1941Nitrated tyrosineBy similarity
    Disulfide bondi246 ↔ 2691 PublicationPROSITE-ProRule annotation
    Disulfide bondi294 ↔ 3131 PublicationPROSITE-ProRule annotation
    Disulfide bondi305 ↔ 3081 PublicationPROSITE-ProRule annotation
    Modified residuei346 – 3461Nitrated tyrosineBy similarity
    Glycosylationi389 – 3891N-linked (GlcNAc...)
    Disulfide bondi448 ↔ 4681 PublicationPROSITE-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

    Proteomic databases

    PaxDbiP11151.
    PRIDEiP11151.

    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

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    SORT1Q995236EBI-8794090,EBI-1057058From a different organism.

    Protein-protein interaction databases

    BioGridi158237. 1 interaction.
    IntActiP11151. 2 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliP11151.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini344 – 467124PLATPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni349 – 44496Heparin-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.
    InParanoidiP11151.
    KOiK01059.
    OMAiESVANCH.
    OrthoDBiEOG757CX5.
    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.

    P11151-1 [UniParc]FASTAAdd to Basket

    « Hide

    MESKALLLLA LSVCLQSLTV SRGGLVAADR ITGGKDFRDI ESKFALRTPE    50
    DTAEDTCHLI PGVTESVANC HFNHSSKTFV VIHGWTVTGM YESWVPKLVA 100
    ALYKREPDSN VIVVDWLSRA QQHYPVSAGY TKLVGQDVAK FMNWMADEFN 150
    YPLGNVHLLG YSLGAHAAGI AGSLTNKKVN RITGLDPAGP NFEYAEAPSR 200
    LSPDDADFVD VLHTFTRGSP GRSIGIQKPV GHVDIYPNGG TFQPGCNIGE 250
    ALRVIAERGL GDVDQLVKCS HERSVHLFID SLLNEENPSK AYRCNSKEAF 300
    EKGLCLSCRK NRCNNMGYEI NKVRAKRSSK MYLKTRSQMP YKVFHYQVKI 350
    HFSGTESNTY TNQAFEISLY GTVAESENIP FTLPEVSTNK TYSFLLYTEV 400
    DIGELLMLKL KWISDSYFSW SNWWSSPGFD IGKIRVKAGE TQKKVIFCSR 450
    EKMSYLQKGK SPVIFVKCHD KSLNRKSG 478
    Length:478
    Mass (Da):53,378
    Last modified:December 12, 2006 - v2
    Checksum:i06FDD429DD194A1F
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC118091 mRNA. Translation: AAI18092.1.
    M16966 mRNA. Translation: AAA30624.1.
    PIRiA27053.
    RefSeqiNP_001068588.1. NM_001075120.1.
    UniGeneiBt.5387.

    Genome annotation databases

    EnsembliENSBTAT00000017086; ENSBTAP00000017086; ENSBTAG00000012855.
    GeneIDi280843.
    KEGGibta:280843.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC118091 mRNA. Translation: AAI18092.1 .
    M16966 mRNA. Translation: AAA30624.1 .
    PIRi A27053.
    RefSeqi NP_001068588.1. NM_001075120.1.
    UniGenei Bt.5387.

    3D structure databases

    ProteinModelPortali P11151.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 158237. 1 interaction.
    IntActi P11151. 2 interactions.

    Chemistry

    ChEMBLi CHEMBL3064.

    Proteomic databases

    PaxDbi P11151.
    PRIDEi P11151.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSBTAT00000017086 ; ENSBTAP00000017086 ; ENSBTAG00000012855 .
    GeneIDi 280843.
    KEGGi bta:280843.

    Organism-specific databases

    CTDi 4023.

    Phylogenomic databases

    eggNOGi NOG40923.
    GeneTreei ENSGT00750000117234.
    HOGENOMi HOG000038553.
    HOVERGENi HBG002259.
    InParanoidi P11151.
    KOi K01059.
    OMAi ESVANCH.
    OrthoDBi EOG757CX5.
    TreeFami TF324997.

    Enzyme and pathway databases

    BRENDAi 3.1.1.34. 908.
    Reactomei REACT_204227. Retinoid metabolism and transport.
    REACT_206940. Chylomicron-mediated lipid transport.
    REACT_220799. Transcriptional regulation of white adipocyte differentiation.

    Miscellaneous databases

    NextBioi 20804991.

    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. NIH - Mammalian Gene Collection (MGC) project
      Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Hereford.
      Tissue: Uterus.
    2. "Molecular cloning and sequence of a cDNA coding for bovine lipoprotein lipase."
      Senda M., Oka K., Brown W.V., Qasba P.K., Furuichi Y.
      Proc. Natl. Acad. Sci. U.S.A. 84:4369-4373(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 29-478.
    3. "Structure of bovine milk lipoprotein lipase."
      Yang C.-Y., Gu Z.-W., Yang H.-X., Rohde M.F., Gotto A.M. Jr., Pownall H.J.
      J. Biol. Chem. 264:16822-16827(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 29-478, DISULFIDE BONDS.
      Tissue: Mammary gland.
    4. "Lipoprotein lipases from cow, guinea-pig and man. Structural characterization and identification of protease-sensitive internal regions."
      Bengtsson-Olivecrona G., Olivecrona T., Joernvall H.
      Eur. J. Biochem. 161:281-288(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 29-55.
    5. "Metabolism of endothelial cell-bound lipoprotein lipase. Evidence for heparan sulfate proteoglycan-mediated internalization and recycling."
      Saxena U., Klein M.G., Goldberg I.J.
      J. Biol. Chem. 265:12880-12886(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: HEPARIN BINDING, SUBCELLULAR LOCATION.
    6. "Binding and intracellular trafficking of lipoprotein lipase and triacylglycerol-rich lipoproteins by liver cells."
      Casaroli-Marano R.P., Garcia R., Vilella E., Olivecrona G., Reina M., Vilaro S.
      J. Lipid Res. 39:789-806(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    7. "Apolipoprotein C-II39-62 activates lipoprotein lipase by direct lipid-independent binding."
      MacPhee C.E., Hatters D.M., Sawyer W.H., Howlett G.J.
      Biochemistry 39:3433-3440(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH APOC2, ENZYME ACTIVITY.

    Entry informationi

    Entry nameiLIPL_BOVIN
    AccessioniPrimary (citable) accession number: P11151
    Secondary accession number(s): Q17R03
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: December 12, 2006
    Last modified: October 1, 2014
    This is version 122 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, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3