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Q29524

- LIPL_SHEEP

UniProt

Q29524 - LIPL_SHEEP

Protein

Lipoprotein lipase

Gene

LPL

Organism
Ovis aries (Sheep)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 96 (01 Oct 2014)
      Sequence version 1 (01 Nov 1997)
      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 sitei162 – 1621Nucleophile
    Active sitei186 – 1861Charge relay system
    Active sitei271 – 2711Charge relay system

    GO - Molecular functioni

    1. heparin binding Source: UniProtKB-KW
    2. lipoprotein lipase activity Source: UniProtKB-EC
    3. protein binding Source: BHF-UCL

    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
    OrganismiOvis aries (Sheep)
    Taxonomic identifieri9940 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeCaprinaeOvis
    ProteomesiUP000002356: Chromosome 2

    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

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2727Sequence AnalysisAdd
    BLAST
    Chaini28 – 478451Lipoprotein lipasePRO_0000017781Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi57 ↔ 70PROSITE-ProRule annotation
    Glycosylationi73 – 731N-linked (GlcNAc...)Sequence Analysis
    Modified residuei124 – 1241Nitrated tyrosineBy similarity
    Modified residuei194 – 1941Nitrated tyrosineBy similarity
    Disulfide bondi246 ↔ 269PROSITE-ProRule annotation
    Disulfide bondi294 ↔ 313PROSITE-ProRule annotation
    Disulfide bondi305 ↔ 308PROSITE-ProRule annotation
    Modified residuei346 – 3461Nitrated tyrosineBy similarity
    Glycosylationi389 – 3891N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi448 ↔ 468PROSITE-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

    ProteinModelPortaliQ29524.
    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

    GeneTreeiENSGT00750000117234.
    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.

    Q29524-1 [UniParc]FASTAAdd to Basket

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    MESKVLLLLA LSVWLQSLTV SRGGLVAADR ITRGKDFRDI 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):53,588
    Last modified:November 1, 1997 - v1
    Checksum:i10F41EE1FFB9C882
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X68308 mRNA. Translation: CAA48384.1.
    PIRiS29846.
    RefSeqiNP_001009394.1. NM_001009394.1.
    UniGeneiOar.459.

    Genome annotation databases

    EnsembliENSOART00000011666; ENSOARP00000011504; ENSOARG00000010719.
    GeneIDi443408.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X68308 mRNA. Translation: CAA48384.1 .
    PIRi S29846.
    RefSeqi NP_001009394.1. NM_001009394.1.
    UniGenei Oar.459.

    3D structure databases

    ProteinModelPortali Q29524.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSOART00000011666 ; ENSOARP00000011504 ; ENSOARG00000010719 .
    GeneIDi 443408.

    Organism-specific databases

    CTDi 4023.

    Phylogenomic databases

    GeneTreei ENSGT00750000117234.
    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. "Cloning and sequencing of a full length cDNA encoding ovine lipoprotein lipase."
      Edwards W.D., Daniels S.W., Page R.A., Volpe C.P., Kille P., Sweeney G.E., Cryer A.
      Biochim. Biophys. Acta 1172:167-170(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: Welsh Mountain/Dorset.
      Tissue: Adipose tissue.

    Entry informationi

    Entry nameiLIPL_SHEEP
    AccessioniPrimary (citable) accession number: Q29524
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 96 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