Sequence Detail

ID/Version

P11152 Q9DCM8 Q542L4 Q05956 Q9D3M9 (UniProt | EBI)

Last sequence update: 2011-07-27
Last annotation update: 2024-03-27

Sequence description from provider

RecName: Full=Lipoprotein lipase; Short=LPL; EC=3.1.1.34 {ECO:0000269|PubMed:8675619};AltName: Full=Phospholipase A1; EC=3.1.1.32 {ECO:0000250|UniProtKB:P06858};Flags: Precursor;

Provider

SWISS-PROT

Sequence

Polypeptide 474 aa

Source

Organism mouse

See UniProt | EBI for source

Annotated genes and markers

Follow the symbol links to get more information on the GO terms, expression assays, orthologs, phenotypic alleles, and other information for the genes or markers below.

Type	Symbol	Name	GO Terms	Expression Assays	Orthologs	Phenotypic Alleles
Gene	Lpl	lipoprotein lipase	76	123	3	12

Sequence references in MGI

J:705 Hua XX, et al., Cloning and characterization of the promoter of the murine lipoprotein lipase-encoding gene: structural and functional analysis. Gene. 1991 Nov 15;107(2):247-58
J:8759 Kirchgessner TG, et al., The sequence of cDNA encoding lipoprotein lipase. A member of a lipase gene family. J Biol Chem. 1987 Jun 25;262(18):8463-6
J:11573 Zechner R, et al., The structure of the mouse lipoprotein lipase gene: a B1 repetitive element is inserted into the 3' untranslated region of the mRNA. Genomics. 1991 Sep;11(1):62-76
J:30062 Weinstock PH, et al., Severe hypertriglyceridemia, reduced high density lipoprotein, and neonatal death in lipoprotein lipase knockout mice. Mild hypertriglyceridemia with impaired very low density lipoprotein clearance in heterozygotes. J Clin Invest. 1995 Dec;96(6):2555-68
J:99680 The FANTOM Consortium and RIKEN Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group), The Transcriptional Landscape of the Mammalian Genome. Science. 2005;309(5740):1559-1563
J:129764 Beigneux AP, et al., Glycosylphosphatidylinositol-anchored high-density lipoprotein-binding protein 1 plays a critical role in the lipolytic processing of chylomicrons. Cell Metab. 2007 Apr;5(4):279-91
J:162997 Davies BS, et al., GPIHBP1 is responsible for the entry of lipoprotein lipase into capillaries. Cell Metab. 2010 Jul 4;12(1):42-52
J:214777 Goulbourne CN, et al., The GPIHBP1-LPL complex is responsible for the margination of triglyceride-rich lipoproteins in capillaries. Cell Metab. 2014 May 6;19(5):849-60
J:215786 Sha H, et al., The ER-associated degradation adaptor protein Sel1L regulates LPL secretion and lipid metabolism. Cell Metab. 2014 Sep 2;20(3):458-70
J:237922 Allan CM, et al., Mobility of "HSPG-bound" LPL explains how LPL is able to reach GPIHBP1 on capillaries. J Lipid Res. 2017 Jan;58(1):216-225
J:292518 Huttlin EL, et al., A tissue-specific atlas of mouse protein phosphorylation and expression. Cell. 2010 Dec 23;143(7):1174-89