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P11153

- LIPL_CAVPO

UniProt

P11153 - LIPL_CAVPO

Protein

Lipoprotein lipase

Gene

LPL

Organism
Cavia porcellus (Guinea pig)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 111 (01 Oct 2014)
      Sequence version 1 (01 Jul 1989)
      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 sitei149 – 1491NucleophileBy similarity
    Active sitei173 – 1731Charge relay systemPROSITE-ProRule annotation
    Active sitei258 – 2581Charge 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
    OrganismiCavia porcellus (Guinea pig)
    Taxonomic identifieri10141 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaHystricognathiCaviidaeCavia
    ProteomesiUP000005447: Unplaced

    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

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1717Sequence AnalysisAdd
    BLAST
    Chaini18 – 465448Lipoprotein lipasePRO_0000017773Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi44 ↔ 57PROSITE-ProRule annotation
    Glycosylationi60 – 601N-linked (GlcNAc...)Sequence Analysis
    Modified residuei111 – 1111Nitrated tyrosineBy similarity
    Modified residuei181 – 1811Nitrated tyrosineBy similarity
    Disulfide bondi233 ↔ 256PROSITE-ProRule annotation
    Disulfide bondi281 ↔ 300PROSITE-ProRule annotation
    Disulfide bondi292 ↔ 295PROSITE-ProRule annotation
    Modified residuei333 – 3331Nitrated tyrosineBy similarity
    Glycosylationi376 – 3761N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi435 ↔ 455PROSITE-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

    Expressioni

    Tissue specificityi

    High level of expression in expression in adipocytes, heart muscle and mammary gland.1 Publication

    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

    STRINGi10141.ENSCPOP00000003655.

    Structurei

    3D structure databases

    ProteinModelPortaliP11153.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini331 – 454124PLATPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni336 – 43196Heparin-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.
    HOGENOMiHOG000038553.
    HOVERGENiHBG002259.
    InParanoidiP11153.

    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.

    P11153-1 [UniParc]FASTAAdd to Basket

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    MNIDRKILNK ALAKEKVANC QKDYTDIESK FARRTPENTV EDTCHLIPGV    50
    TESVANCHFN HSSKTFMVIH GWTVTGMYES WVPKLVAALY KREPDSNVIV 100
    VDWLRRAQHH YPESADYTKL VGEDVARFIN WMEDEFKYSV DNVHLLGYSL 150
    GAHAAGVAGS RTNTKVSRIT GLDPAGPNFE YAEATSRLSP DDAQFVDVLH 200
    TFTRGSPGRS IGIQKPVGHV DIYPNGGSFQ PGCNIQDALR VISQKGFGDM 250
    DQLVKCSHER SIHLFIDSLL NEENPSKAYR CNSKEAFEKG LCLSCRKNRC 300
    NNVGYEINKV RAKRSSKMYL KTRSQMPYKV FHYQVKIYFS GTETTTYTNQ 350
    AFEISLYGTV AESENIPFTL PEVSANNTYS FLIYTEVDIG ELLMLKLKWI 400
    TESYFSWSSW WGRPTFTIEK IRVKAGETQK KIVFCSREKV SKLQKGKEAP 450
    VFVKCHDKSL NKKSG 465
    Length:465
    Mass (Da):52,781
    Last modified:July 1, 1989 - v1
    Checksum:iE2515F36BEFD5F10
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M15483 mRNA. Translation: AAA37046.1.
    M33381
    , M33377, M33378, M33379, M33380 Genomic DNA. Translation: AAA37039.1.
    PIRiJS0398. A27330.
    RefSeqiNP_001166449.1. NM_001172978.1.

    Genome annotation databases

    GeneIDi100135570.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M15483 mRNA. Translation: AAA37046.1 .
    M33381
    , M33377 , M33378 , M33379 , M33380 Genomic DNA. Translation: AAA37039.1 .
    PIRi JS0398. A27330.
    RefSeqi NP_001166449.1. NM_001172978.1.

    3D structure databases

    ProteinModelPortali P11153.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10141.ENSCPOP00000003655.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 100135570.

    Organism-specific databases

    CTDi 4023.

    Phylogenomic databases

    eggNOGi NOG40923.
    HOGENOMi HOG000038553.
    HOVERGENi HBG002259.
    InParanoidi P11153.

    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. "Molecular cloning and sequence analysis of cDNA encoding lipoprotein lipase of guinea pig."
      Enerbaeck S., Semb H., Bengtsson-Olivecrona G., Carlsson P., Hermansson M.-L., Olivecrona T., Bjursell G.
      Gene 58:1-12(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    2. "Genomic organization of the region encoding guinea pig lipoprotein lipase; evidence for exon fusion and unconventional splicing."
      Enerbaeck S., Bjursell G.
      Gene 84:391-397(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

    Entry informationi

    Entry nameiLIPL_CAVPO
    AccessioniPrimary (citable) accession number: P11153
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: July 1, 1989
    Last modified: October 1, 2014
    This is version 111 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