Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P49923

- LIPL_PIG

UniProt

P49923 - LIPL_PIG

Protein

Lipoprotein lipase

Gene

LPL

Organism
Sus scrofa (Pig)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 97 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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 – 1621NucleophileBy similarity
    Active sitei186 – 1861Charge relay systemPROSITE-ProRule annotation
    Active sitei271 – 2711Charge 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
    OrganismiSus scrofa (Pig)
    Taxonomic identifieri9823 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
    ProteomesiUP000008227: 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 – 2727By similarityAdd
    BLAST
    Chaini28 – 478451Lipoprotein lipasePRO_0000017780Add
    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

    Proteomic databases

    PaxDbiP49923.

    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

    ProteinModelPortaliP49923.
    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.
    HOGENOMiHOG000038553.
    HOVERGENiHBG002259.
    KOiK01059.

    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.

    P49923-1 [UniParc]FASTAAdd to Basket

    « Hide

    MESKALLLVA LSVWLQSLIV SREGLATADR ISGGRDFTDI ESKFALRTPE    50
    DTVEDTCHLI PGVTESVANC HFNHSSKTFV VIHGWTVTGM YESWVPKLVA 100
    ALYKREPDSN VIVVDWLSRA QQHYPISAGY TKLVGQDVAT FIDWMAVEFS 150
    YPPNNVHLLG YSLGAHAAGI AGSLTKKKVN RITGLDPAGP NFEYAEAPSR 200
    LSPDDADFVD VLHTFTRGSP GRSIGIQKPV GHVDIYPNGG TFQPGCNIGE 250
    AIRVIAERGL GDVDQLVKCS HERSIHLFID SLLNEENPSK AYRCNSKEAF 300
    EKGLCLSCRK NRCNNLGYEI NKVRAKRSSK MYLKTRAQMP YKVFHYQVKM 350
    RFSGTESDTH TNQAFEISLY GTVAESENIP FTLPEVSTNK TYSFLIYTEV 400
    DIGELLMLKL KWVSDSYFSW SNWWSSPGFA IEKIRVKAGE TQKKVIFCSR 450
    EKKSHLQKGK SSVVFVKCHD KSLNRKSG 478
    Length:478
    Mass (Da):53,455
    Last modified:October 1, 1996 - v1
    Checksum:iD0500324117261E3
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X62984 mRNA. Translation: CAA44725.1.
    PIRiI47146. S18158.
    RefSeqiNP_999451.1. NM_214286.1.
    UniGeneiSsc.95883.

    Genome annotation databases

    GeneIDi397537.
    KEGGissc:397537.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X62984 mRNA. Translation: CAA44725.1 .
    PIRi I47146. S18158.
    RefSeqi NP_999451.1. NM_214286.1.
    UniGenei Ssc.95883.

    3D structure databases

    ProteinModelPortali P49923.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PaxDbi P49923.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 397537.
    KEGGi ssc:397537.

    Organism-specific databases

    CTDi 4023.

    Phylogenomic databases

    eggNOGi NOG40923.
    HOGENOMi HOG000038553.
    HOVERGENi HBG002259.
    KOi K01059.

    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. "Isolation and sequencing of porcine lipoprotein lipase cDNA and its use in multiallelic restriction fragment length polymorphism detection."
      Harbitz I., Kristensen T., Kran S., Davies W.
      Anim. Genet. 23:517-522(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: Norwegian Landrace.
      Tissue: Skeletal muscle.

    Entry informationi

    Entry nameiLIPL_PIG
    AccessioniPrimary (citable) accession number: P49923
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 97 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