Homo sapiens Protein: LPL
Summary
InnateDB Protein IDBP-9634.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol LPL
Protein Name lipoprotein lipase
Synonyms HDLCQ11; LIPD;
Species Homo sapiens
Ensembl Protein ENSP00000309757
InnateDB Gene IDBG-9632 (LPL)
Protein Structure
UniProt Annotation
Function 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). {ECO:0000250}.
Subcellular Localization Cell membrane {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}. Secreted {ECO:0000250}. 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). {ECO:0000250}.
Disease Associations Lipoprotein lipase deficiency (LPL deficiency) [MIM:238600]: Recessive disorder usually manifesting in childhood. On a normal diet, patients often present with abdominal pain, hepatosplenomegaly, lipemia retinalis, eruptive xanthomata, and massive hypertriglyceridemia, sometimes complicated with acute pancreatitis. {ECO:0000269PubMed:10660334, ECO:0000269PubMed:10787434, ECO:0000269PubMed:11068186, ECO:0000269PubMed:11099402, ECO:0000269PubMed:11134145, ECO:0000269PubMed:11441134, ECO:0000269PubMed:12204001, ECO:0000269PubMed:12641539, ECO:0000269PubMed:12966036, ECO:0000269PubMed:1400331, ECO:0000269PubMed:1479292, ECO:0000269PubMed:14984478, ECO:0000269PubMed:15185149, ECO:0000269PubMed:1521525, ECO:0000269PubMed:15256764, ECO:0000269PubMed:15877202, ECO:0000269PubMed:1598907, ECO:0000269PubMed:1619366, ECO:0000269PubMed:1639392, ECO:0000269PubMed:1674945, ECO:0000269PubMed:1702428, ECO:0000269PubMed:1730727, ECO:0000269PubMed:1752947, ECO:0000269PubMed:1907278, ECO:0000269PubMed:1969408, ECO:0000269PubMed:1975597, ECO:0000269PubMed:2010533, ECO:0000269PubMed:2038366, ECO:0000269PubMed:2110364, ECO:0000269PubMed:2121025, ECO:0000269PubMed:7647785, ECO:0000269PubMed:7806969, ECO:0000269PubMed:7906986, ECO:0000269PubMed:7912254, ECO:0000269PubMed:7999071, ECO:0000269PubMed:8077845, ECO:0000269PubMed:8096693, ECO:0000269PubMed:8135797, ECO:0000269PubMed:8288243, ECO:0000269PubMed:8301230, ECO:0000269PubMed:8325986, ECO:0000269PubMed:8486765, ECO:0000269PubMed:8728326, ECO:0000269PubMed:8778602, ECO:0000269PubMed:8858123, ECO:0000269PubMed:8872057, ECO:0000269PubMed:8956048, ECO:0000269PubMed:8956052, ECO:0000269PubMed:9279761, ECO:0000269PubMed:9298816, ECO:0000269PubMed:9498099, ECO:0000269PubMed:9662394, ECO:0000269PubMed:9714430, ECO:0000269PubMed:9719626}. Note=The disease is caused by mutations affecting the gene represented in this entry.
Tissue Specificity
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 23 experimentally validated interaction(s) in this database.
Experimentally validated
Total 23 [view]
Protein-Protein 21 [view]
Protein-DNA 2 [view]
Protein-RNA 0
DNA-DNA 0
RNA-RNA 0
DNA-RNA 0
Gene Ontology

Molecular Function
Accession GO Term
GO:0004465 lipoprotein lipase activity
GO:0004620 phospholipase activity
GO:0004806 triglyceride lipase activity
GO:0005102 receptor binding
GO:0005515 protein binding
GO:0008201 heparin binding
GO:0017129 triglyceride binding
GO:0034185 apolipoprotein binding
GO:0052689 carboxylic ester hydrolase activity
Biological Process
GO:0001523 retinoid metabolic process
GO:0006629 lipid metabolic process
GO:0006633 fatty acid biosynthetic process
GO:0006641 triglyceride metabolic process
GO:0006644 phospholipid metabolic process
GO:0007603 phototransduction, visible light
GO:0009409 response to cold
GO:0010744 positive regulation of macrophage derived foam cell differentiation
GO:0010886 positive regulation of cholesterol storage
GO:0010890 positive regulation of sequestering of triglyceride
GO:0016042 lipid catabolic process
GO:0019432 triglyceride biosynthetic process
GO:0019433 triglyceride catabolic process
GO:0034371 chylomicron remodeling
GO:0034372 very-low-density lipoprotein particle remodeling
GO:0042157 lipoprotein metabolic process
GO:0042493 response to drug
GO:0044281 small molecule metabolic process
GO:0070328 triglyceride homeostasis
Cellular Component
GO:0005576 extracellular region
GO:0005615 extracellular space
GO:0005886 plasma membrane
GO:0009986 cell surface
GO:0031012 extracellular matrix
GO:0031225 anchored component of membrane
GO:0034361 very-low-density lipoprotein particle
GO:0042627 chylomicron
GO:0070062 extracellular vesicular exosome
Protein Structure and Domains
PDB ID
InterPro IPR000734 Lipase
IPR001024 PLAT/LH2 domain
IPR002330 Lipoprotein lipase
IPR008976 Lipase/lipooxygenase, PLAT/LH2
IPR013818 Lipase, N-terminal
IPR016272 Lipoprotein lipase, LIPH
IPR029058 Alpha/Beta hydrolase fold
PFAM PF01477
PF00151
PRINTS PR00821
PR00822
PIRSF PIRSF000865
SMART SM00308
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt P06858
PhosphoSite PhosphoSite-P06858
TrEMBL Q71UV2
UniProt Splice Variant
Entrez Gene 4023
UniGene Hs.619595
RefSeq NP_000228
HUGO HGNC:6677
OMIM 609708
CCDS CCDS6012
HPRD 01999
IMGT
EMBL AC100802 AC107964 AF050163 AK312311 BC011353 BT006726 CH471080 DQ083390 M15856 M76722 S76076 S76077 X14390 X54516 X68111
GenPept AAA59528 AAB20999 AAB21000 AAB59536 AAC61679 AAH11353 AAP35372 AAY85371 BAG35236 CAA32564 CAA38372 CAA48230 EAW63764