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P11152

- LIPL_MOUSE

UniProt

P11152 - LIPL_MOUSE

Protein

Lipoprotein lipase

Gene

Lpl

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 148 (01 Oct 2014)
      Sequence version 3 (27 Jul 2011)
      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: MGI
    3. protein binding Source: MGI
    4. triglyceride binding Source: Ensembl
    5. triglyceride lipase activity Source: BHF-UCL

    GO - Biological processi

    1. positive regulation of cholesterol storage Source: Ensembl
    2. positive regulation of macrophage derived foam cell differentiation Source: BHF-UCL
    3. positive regulation of sequestering of triglyceride Source: Ensembl
    4. response to cold Source: Ensembl
    5. response to drug Source: Ensembl
    6. triglyceride biosynthetic process Source: Ensembl
    7. triglyceride catabolic process Source: BHF-UCL
    8. triglyceride homeostasis Source: Ensembl

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Lipid degradation, Lipid metabolism

    Keywords - Ligandi

    Heparin-binding

    Enzyme and pathway databases

    BRENDAi3.1.1.34. 3474.
    ReactomeiREACT_198569. Retinoid metabolism and transport.
    REACT_216017. Chylomicron-mediated lipid transport.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Lipoprotein lipase (EC:3.1.1.34)
    Short name:
    LPL
    Gene namesi
    Name:Lpl
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 8

    Organism-specific databases

    MGIiMGI:96820. Lpl.

    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: BHF-UCL
    3. chylomicron Source: UniProtKB-KW
    4. extracellular matrix Source: Ensembl
    5. extracellular space Source: BHF-UCL
    6. plasma membrane Source: UniProtKB-SubCell
    7. 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 – 474447Lipoprotein lipasePRO_0000017776Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi54 ↔ 67PROSITE-ProRule annotation
    Glycosylationi70 – 701N-linked (GlcNAc...)Sequence Analysis
    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
    Glycosylationi386 – 3861N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi445 ↔ 465PROSITE-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

    MaxQBiP11152.
    PaxDbiP11152.
    PRIDEiP11152.

    PTM databases

    PhosphoSiteiP11152.

    Expressioni

    Tissue specificityi

    Expressed in liver, epididymal fat, heart, psoas muscle, lactating mammary gland, adrenal, lung, and ovary. Highest levels in heart and adrenal gland.1 Publication

    Developmental stagei

    Maximum expression in adipose tissue during early development. In heart, low levels 6 days before birth increasing 278-fold as animals reach adulthood.1 Publication

    Gene expression databases

    ArrayExpressiP11152.
    BgeeiP11152.
    CleanExiMM_LPL.
    GenevestigatoriP11152.

    Interactioni

    Subunit structurei

    Homodimer By similarity. Interacts with APOC2; the interaction activates LPL activity in the presence of lipids By similarity. Interacts with GPIHBP1.By similarity1 Publication

    Protein-protein interaction databases

    IntActiP11152. 1 interaction.

    Structurei

    3D structure databases

    ProteinModelPortaliP11152.
    SMRiP11152. Positions 36-450.
    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-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.
    InParanoidiQ542L4.
    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.

    P11152-1 [UniParc]FASTAAdd to Basket

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    MESKALLLVV LGVWLQSLTA FRGGVAAADA GRDFSDIESK FALRTPEDTA    50
    EDTCHLIPGL ADSVSNCHFN HSSKTFVVIH GWTVTGMYES WVPKLVAALY 100
    KREPDSNVIV VDWLYRAQQH YPVSAGYTKL VGNDVARFIN WMEEEFNYPL 150
    DNVHLLGYSL GAHAAGVAGS LTNKKVNRIT GLDPAGPNFE YAEAPSRLSP 200
    DDADFVDVLH TFTRGSPGRS IGIQKPVGHV DIYPNGGTFQ PGCNIGEAIR 250
    VIAERGLGDV DQLVKCSHER SIHLFIDSLL NEENPSKAYR CNSKEAFEKG 300
    LCLSCRKNRC NNLGYEINKV RAKRSSKMYL KTRSQMPYKV FHYQVKIHFS 350
    GTEDGKQHNQ AFEISLYGTV AESENIPFTL PEVSTNKTYS FLIYTEVDIG 400
    ELLMMKLKWI SDSYFSWPDW WSSPSFVIER IRVKAGETQK KVIFCAREKV 450
    SHLQKGKDSA VFVKCHDKSL KKSG 474
    Length:474
    Mass (Da):53,109
    Last modified:July 27, 2011 - v3
    Checksum:iE5895C98B7AE16CD
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti129 – 1291K → Y no nucleotide entry (PubMed:2723548)Curated
    Sequence conflicti147 – 1471N → K in AAA39441. (PubMed:1765386)Curated
    Sequence conflicti354 – 3541D → N no nucleotide entry (PubMed:2723548)Curated
    Sequence conflicti410 – 4101I → M no nucleotide entry (PubMed:2723548)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M60847
    , M60838, M60839, M60840, M60842, M60843, M60844, M60845, M60846 Genomic DNA. Translation: AAA39441.1.
    AK002645 mRNA. Translation: BAB22256.1.
    AK017272 mRNA. No translation available.
    AK045064 mRNA. Translation: BAC32204.1.
    AK086023 mRNA. Translation: BAC39594.1.
    AK150355 mRNA. Translation: BAE29491.1.
    AK150375 mRNA. Translation: BAE29507.1.
    AK150457 mRNA. Translation: BAE29577.1.
    AK150488 mRNA. Translation: BAE29604.1.
    AK150505 mRNA. Translation: BAE29618.1.
    AK150593 mRNA. Translation: BAE29686.1.
    AK150672 mRNA. Translation: BAE29754.1.
    AK151006 mRNA. Translation: BAE30029.1.
    AK151093 mRNA. Translation: BAE30105.1.
    AK151105 mRNA. Translation: BAE30115.1.
    AK151369 mRNA. Translation: BAE30343.1.
    AK151434 mRNA. Translation: BAE30397.1.
    AK151521 mRNA. Translation: BAE30470.1.
    AK151540 mRNA. Translation: BAE30486.1.
    AK151563 mRNA. Translation: BAE30505.1.
    AK151630 mRNA. Translation: BAE30564.1.
    AK151679 mRNA. Translation: BAE30604.1.
    AK151727 mRNA. Translation: BAE30645.1.
    AK151772 mRNA. Translation: BAE30678.1.
    AK151801 mRNA. Translation: BAE30701.1.
    AK151828 mRNA. Translation: BAE30723.1.
    AK151866 mRNA. Translation: BAE30754.1.
    AK151870 mRNA. Translation: BAE30758.1.
    AK151872 mRNA. Translation: BAE30760.1.
    AK151893 mRNA. Translation: BAE30777.1.
    AK152014 mRNA. Translation: BAE30876.1.
    AK152035 mRNA. Translation: BAE30894.1.
    AK152049 mRNA. Translation: BAE30905.1.
    AK152053 mRNA. Translation: BAE30909.1.
    AK152079 mRNA. Translation: BAE30930.1.
    AK152350 mRNA. Translation: BAE31144.1.
    AK152657 mRNA. Translation: BAE31394.1.
    AK153148 mRNA. Translation: BAE31758.1.
    AK153242 mRNA. Translation: BAE31834.1.
    AK153425 mRNA. Translation: BAE31984.1.
    AK159268 mRNA. Translation: BAE34947.1.
    AK170486 mRNA. Translation: BAE41828.1.
    BC003305 mRNA. Translation: AAH03305.1.
    M65258 mRNA. Translation: AAA39442.1.
    J03302 mRNA. Translation: AAA39440.1.
    M63335 Genomic DNA. Translation: AAC04464.1.
    CCDSiCCDS40357.1.
    PIRiA40570.
    RefSeqiNP_032535.2. NM_008509.2.
    UniGeneiMm.1514.

    Genome annotation databases

    EnsembliENSMUST00000015712; ENSMUSP00000015712; ENSMUSG00000015568.
    ENSMUST00000168401; ENSMUSP00000132259; ENSMUSG00000015568.
    GeneIDi16956.
    KEGGimmu:16956.
    UCSCiuc009lwq.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M60847
    , M60838 , M60839 , M60840 , M60842 , M60843 , M60844 , M60845 , M60846 Genomic DNA. Translation: AAA39441.1 .
    AK002645 mRNA. Translation: BAB22256.1 .
    AK017272 mRNA. No translation available.
    AK045064 mRNA. Translation: BAC32204.1 .
    AK086023 mRNA. Translation: BAC39594.1 .
    AK150355 mRNA. Translation: BAE29491.1 .
    AK150375 mRNA. Translation: BAE29507.1 .
    AK150457 mRNA. Translation: BAE29577.1 .
    AK150488 mRNA. Translation: BAE29604.1 .
    AK150505 mRNA. Translation: BAE29618.1 .
    AK150593 mRNA. Translation: BAE29686.1 .
    AK150672 mRNA. Translation: BAE29754.1 .
    AK151006 mRNA. Translation: BAE30029.1 .
    AK151093 mRNA. Translation: BAE30105.1 .
    AK151105 mRNA. Translation: BAE30115.1 .
    AK151369 mRNA. Translation: BAE30343.1 .
    AK151434 mRNA. Translation: BAE30397.1 .
    AK151521 mRNA. Translation: BAE30470.1 .
    AK151540 mRNA. Translation: BAE30486.1 .
    AK151563 mRNA. Translation: BAE30505.1 .
    AK151630 mRNA. Translation: BAE30564.1 .
    AK151679 mRNA. Translation: BAE30604.1 .
    AK151727 mRNA. Translation: BAE30645.1 .
    AK151772 mRNA. Translation: BAE30678.1 .
    AK151801 mRNA. Translation: BAE30701.1 .
    AK151828 mRNA. Translation: BAE30723.1 .
    AK151866 mRNA. Translation: BAE30754.1 .
    AK151870 mRNA. Translation: BAE30758.1 .
    AK151872 mRNA. Translation: BAE30760.1 .
    AK151893 mRNA. Translation: BAE30777.1 .
    AK152014 mRNA. Translation: BAE30876.1 .
    AK152035 mRNA. Translation: BAE30894.1 .
    AK152049 mRNA. Translation: BAE30905.1 .
    AK152053 mRNA. Translation: BAE30909.1 .
    AK152079 mRNA. Translation: BAE30930.1 .
    AK152350 mRNA. Translation: BAE31144.1 .
    AK152657 mRNA. Translation: BAE31394.1 .
    AK153148 mRNA. Translation: BAE31758.1 .
    AK153242 mRNA. Translation: BAE31834.1 .
    AK153425 mRNA. Translation: BAE31984.1 .
    AK159268 mRNA. Translation: BAE34947.1 .
    AK170486 mRNA. Translation: BAE41828.1 .
    BC003305 mRNA. Translation: AAH03305.1 .
    M65258 mRNA. Translation: AAA39442.1 .
    J03302 mRNA. Translation: AAA39440.1 .
    M63335 Genomic DNA. Translation: AAC04464.1 .
    CCDSi CCDS40357.1.
    PIRi A40570.
    RefSeqi NP_032535.2. NM_008509.2.
    UniGenei Mm.1514.

    3D structure databases

    ProteinModelPortali P11152.
    SMRi P11152. Positions 36-450.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P11152. 1 interaction.

    PTM databases

    PhosphoSitei P11152.

    Proteomic databases

    MaxQBi P11152.
    PaxDbi P11152.
    PRIDEi P11152.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000015712 ; ENSMUSP00000015712 ; ENSMUSG00000015568 .
    ENSMUST00000168401 ; ENSMUSP00000132259 ; ENSMUSG00000015568 .
    GeneIDi 16956.
    KEGGi mmu:16956.
    UCSCi uc009lwq.1. mouse.

    Organism-specific databases

    CTDi 4023.
    MGIi MGI:96820. Lpl.

    Phylogenomic databases

    eggNOGi NOG40923.
    GeneTreei ENSGT00750000117234.
    HOGENOMi HOG000038553.
    HOVERGENi HBG002259.
    InParanoidi Q542L4.
    KOi K01059.
    OMAi ESVANCH.
    OrthoDBi EOG757CX5.
    TreeFami TF324997.

    Enzyme and pathway databases

    BRENDAi 3.1.1.34. 3474.
    Reactomei REACT_198569. Retinoid metabolism and transport.
    REACT_216017. Chylomicron-mediated lipid transport.

    Miscellaneous databases

    ChiTaRSi LPL. mouse.
    NextBioi 291008.
    PROi P11152.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P11152.
    Bgeei P11152.
    CleanExi MM_LPL.
    Genevestigatori P11152.

    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. "Lipoprotein lipase and hepatic lipase mRNA tissue specific expression, developmental regulation, and evolution."
      Semenkovich C.F., Chen S.H., Wims M., Luo C.C., Li W.H., Chan L.
      J. Lipid Res. 30:423-431(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
      Tissue: Macrophage.
    2. "The structure of the mouse lipoprotein lipase gene: a B1 repetitive element is inserted into the 3' untranslated region of the mRNA."
      Zechner R., Newman T.C., Steiner E., Breslow J.L.
      Genomics 11:62-76(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J and NOD.
      Tissue: Bone marrow, Embryo, Head, Heart and Kidney.
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    5. "Adipogenesis in a myeloid supporting bone marrow stromal cell line."
      Gimble J.M., Hua X., Youkhana K., Bass H.W., Medina K., Sullivan M., Greenberger J.S., Wang C.S.
      J. Cell. Biochem. 50:73-82(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-183.
    6. "Cloning and characterization of the promoter of the murine lipoprotein lipase-encoding gene: structural and functional analysis."
      Hua X., Enerbaeck S., Hudson J., Youkhana K., Gimble J.M.
      Gene 107:247-258(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-29.
      Strain: BALB/c.
      Tissue: Liver.
    7. "The sequence of cDNA encoding lipoprotein lipase. A member of a lipase gene family."
      Kirchgessner T.G., Svenson K.L., Lusis A.J., Schotz M.C.
      J. Biol. Chem. 262:8463-8466(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 9-474.
    8. "Glycosylphosphatidylinositol-anchored high-density lipoprotein-binding protein 1 plays a critical role in the lipolytic processing of chylomicrons."
      Beigneux A.P., Davies B.S.J., Gin P., Weinstein M.M., Farber E., Qiao X., Peale F., Bunting S., Walzem R.L., Wong J.S., Blaner W.S., Ding Z.-M., Melford K., Wongsiriroj N., Shu X., de Sauvage F., Ryan R.O., Fong L.G., Bensadoun A., Young S.G.
      Cell Metab. 5:279-291(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GPIHBP1.

    Entry informationi

    Entry nameiLIPL_MOUSE
    AccessioniPrimary (citable) accession number: P11152
    Secondary accession number(s): Q05956
    , Q542L4, Q9D3M9, Q9DCM8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 148 of the entry and version 3 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. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3