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P11602

- LIPL_CHICK

UniProt

P11602 - LIPL_CHICK

Protein

Lipoprotein lipase

Gene

LPL

Organism
Gallus gallus (Chicken)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 117 (01 Oct 2014)
      Sequence version 1 (01 Oct 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 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. positive regulation of cholesterol storage Source: Ensembl
    2. positive regulation of macrophage derived foam cell differentiation Source: Ensembl
    3. positive regulation of sequestering of triglyceride Source: Ensembl
    4. triglyceride catabolic process Source: Ensembl
    5. triglyceride homeostasis Source: Ensembl

    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
    OrganismiGallus gallus (Chicken)
    Taxonomic identifieri9031 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus
    ProteomesiUP000000539: Chromosome Z

    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. plasma membrane Source: UniProtKB-SubCell
    5. very-low-density lipoprotein particle Source: UniProtKB-KW

    Keywords - Cellular componenti

    Cell membrane, Chylomicron, Membrane, Secreted, VLDL

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi306 – 3061R → Q: Some loss of heparin-binding ability; when associated with Q-307 and Q-309. 1 Publication
    Mutagenesisi307 – 3071K → Q: Some loss of heparin-binding ability; when associated with Q-306 and Q-309. 1 Publication
    Mutagenesisi309 – 3091R → Q: Some loss of heparin-binding ability; when associated with Q-306 and Q-307. 1 Publication
    Mutagenesisi346 – 3461K → N: Reduced heparin-binding ability and some decrease in specific enzymatic activity. 1 Publication
    Mutagenesisi430 – 4301R → N: Reduced heparin-binding ability and some reduction in specific enzymatic activity. Almost complete loss of heparin binding and greatly reduced specific enzymatic activity; when associated with N-432 and N-434. 1 Publication
    Mutagenesisi432 – 4321R → N: Reduced heparin-binding ability. Almost complete loss of heparin binding and greatly reduced specific enzymatic activity; when associated with N-430 and N-434. 1 Publication
    Mutagenesisi434 – 4341K → N: Reduced heparin-binding ability. Almost complete loss of heparin binding and greatly reduced specific enzymatic activity; when associated with N-430 and N-432. 1 Publication
    Mutagenesisi440 – 4401K → N: No change in heparin-binding activity nor in specific enzymatic activity. Reduced heparin-binding activity and decreased specific enzymatic activity; when associated with N-441. 1 Publication
    Mutagenesisi441 – 4411K → N: Reduced heparin-binding activity and decreased specific enzymatic activity. No further reduction of heparin-binding nor of specific enzymatic activity; when associated with N-440. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2525Add
    BLAST
    Chaini26 – 490465Lipoprotein lipase1 PublicationPRO_0000017782Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi54 ↔ 67PROSITE-ProRule annotation
    Glycosylationi70 – 701N-linked (GlcNAc...) (complex)1 Publication
    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
    Glycosylationi354 – 3541N-linked (GlcNAc...)1 Publication
    Glycosylationi386 – 3861N-linked (GlcNAc...)1 Publication
    Disulfide bondi445 ↔ 465PROSITE-ProRule annotation

    Post-translational modificationi

    N-glycan at Asn-70 is a triantennary complex oligosaccharide containing sialic acid, galactose, mannose, and N-acetylglucosamine, the reducing GlcNAc being sulfated at C6.
    Tyrosine nitration after lipopolysaccharide (LPS) challenge down-regulates the lipase activity.By similarity

    Keywords - PTMi

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

    Proteomic databases

    PaxDbiP11602.

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    STRINGi9031.ENSGALP00000036979.

    Structurei

    3D structure databases

    ProteinModelPortaliP11602.
    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-bindingAdd
    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.
    InParanoidiP11602.
    KOiK01059.
    PhylomeDBiP11602.

    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.

    P11602-1 [UniParc]FASTAAdd to Basket

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    MERGRGMGKT ALLAVLCLCL RGAAGSDPEA EMNFEGIESK FSLRTPAEPD    50
    EDVCYLVPGQ MDSLAQCNFN HTSKTFVVIH GWTVTGMYES WVPKLVDALY 100
    KREPDSNVIV VDWLVRAQQH YPVSAAYTKL VGKDVAMFID WMEEKFNYPL 150
    NNVHLLGYSL GAHAAGIAGS LTKKKVNRIT GLDPAGPTFE YADAPIRLSP 200
    DDADFVDVLH TYTRGSPDRS IGIQKPVGHI DIYPNGGGFQ PGCNLGEALR 250
    LIAEKGFSDV DQLVKCSHER SIHLFIDSLL YEEKPSMAYR CNTKEAFEKG 300
    LCLSCRKNRC NNLGYKVNRV RTKRNTKMYL KTRAQMPYKV FHYQVKIHFF 350
    GKTNVTKVDQ PFLISLYGTL DESENIPFTL PEVSSNKTFS FLIYTEVDIG 400
    DLLMLKLQWE KDTFFSWSDW WTPFAFTIQR VRVKSGETQK KVVFCSRDGS 450
    SRLGKGEEAA IFVKCLEQPV SRKRGGAKKA SKENSAHESA 490
    Length:490
    Mass (Da):55,132
    Last modified:October 1, 1989 - v1
    Checksum:iC014D23363E81FF3
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti377 – 3771P → A in CAA43037. (PubMed:1730055)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X14670 mRNA. Translation: CAA32800.1.
    X60547 Genomic DNA. Translation: CAA43037.1.
    PIRiS04331.
    RefSeqiNP_990613.1. NM_205282.1.
    UniGeneiGga.1152.

    Genome annotation databases

    EnsembliENSGALT00000037774; ENSGALP00000036979; ENSGALG00000015425.
    GeneIDi396219.
    KEGGigga:396219.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X14670 mRNA. Translation: CAA32800.1 .
    X60547 Genomic DNA. Translation: CAA43037.1 .
    PIRi S04331.
    RefSeqi NP_990613.1. NM_205282.1.
    UniGenei Gga.1152.

    3D structure databases

    ProteinModelPortali P11602.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9031.ENSGALP00000036979.

    Proteomic databases

    PaxDbi P11602.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSGALT00000037774 ; ENSGALP00000036979 ; ENSGALG00000015425 .
    GeneIDi 396219.
    KEGGi gga:396219.

    Organism-specific databases

    CTDi 4023.

    Phylogenomic databases

    eggNOGi NOG40923.
    GeneTreei ENSGT00750000117234.
    HOGENOMi HOG000038553.
    HOVERGENi HBG002259.
    InParanoidi P11602.
    KOi K01059.
    PhylomeDBi P11602.

    Miscellaneous databases

    NextBioi 20816271.
    PROi P11602.

    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. "Avian adipose lipoprotein lipase: cDNA sequence and reciprocal regulation of mRNA levels in adipose and heart."
      Cooper D.A., Stein J.C., Strieleman P.J., Bensadoun A.
      Biochim. Biophys. Acta 1008:92-101(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: White leghorn.
      Tissue: Adipose tissue.
    2. "The structure and complete nucleotide sequence of the avian lipoprotein lipase gene."
      Cooper D.A., Lu S.C., Viswanath R., Freiman R.N., Bensadoun A.
      Biochim. Biophys. Acta 1129:166-171(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: White leghorn.
    3. "Occurrence of sulfate in an asparagine-linked complex oligosaccharide of chicken adipose lipoprotein lipase."
      Hoogewerf A.J., Bensadoun A.
      J. Biol. Chem. 266:1048-1057(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION AT ASN-70; ASN-354 AND ASN-386, STRUCTURE OF CARBOHYDRATES.
    4. "Identification of a heparin-binding domain in the distal carboxyl-terminal region of lipoprotein lipase by site-directed mutagenesis."
      Sendak R.A., Bensadoun A.
      J. Lipid Res. 39:1310-1315(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: HEPARIN-BINDING DOMAIN, MUTAGENESIS OF ARG-306; LYS-307; ARG-309; LYS-346; ARG-430; ARG-432; LYS-434; LYS-440 AND LYS-441.

    Entry informationi

    Entry nameiLIPL_CHICK
    AccessioniPrimary (citable) accession number: P11602
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1989
    Last sequence update: October 1, 1989
    Last modified: October 1, 2014
    This is version 117 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