UniProtKB - P11152 (LIPL_MOUSE)
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Protein
Lipoprotein lipase
Gene
Lpl
Organism
Mus musculus (Mouse)
Status
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
Catalytic activityi
Triacylglycerol + H2O = diacylglycerol + a carboxylate.By similarity
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 159 | NucleophileBy similarity | 1 | |
Active sitei | 183 | Charge relay systemPROSITE-ProRule annotation | 1 | |
Active sitei | 268 | Charge relay systemPROSITE-ProRule annotation | 1 |
GO - Molecular functioni
- apolipoprotein binding Source: MGI
- heparin binding Source: UniProtKB
- lipoprotein lipase activity Source: MGI
- receptor binding Source: MGI
- triglyceride binding Source: Ensembl
- triglyceride lipase activity Source: BHF-UCL
GO - Biological processi
- cholesterol homeostasis Source: MGI
- fatty acid biosynthetic process Source: MGI
- low-density lipoprotein particle mediated signaling Source: MGI
- positive regulation of chemokine secretion Source: MGI
- positive regulation of cholesterol storage Source: MGI
- positive regulation of macrophage derived foam cell differentiation Source: BHF-UCL
- positive regulation of sequestering of triglyceride Source: MGI
- response to cold Source: Ensembl
- response to drug Source: Ensembl
- triglyceride biosynthetic process Source: UniProtKB
- triglyceride catabolic process Source: BHF-UCL
- triglyceride homeostasis Source: MGI
- very-low-density lipoprotein particle remodeling Source: MGI
Keywordsi
Molecular function | Heparin-binding, Hydrolase |
Biological process | Lipid degradation, Lipid metabolism |
Enzyme and pathway databases
BRENDAi | 3.1.1.34 3474 |
Reactomei | R-MMU-8963889 Assembly of active LPL and LIPC lipase complexes R-MMU-8963901 Chylomicron remodeling R-MMU-975634 Retinoid metabolism and transport |
Protein family/group databases
ESTHERi | mouse-lipli Lipoprotein_Lipase |
Names & Taxonomyi
Protein namesi | |
Gene namesi | Name:Lpl |
Organismi | Mus musculus (Mouse) |
Taxonomic identifieri | 10090 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus |
Proteomesi |
|
Organism-specific databases
MGIi | MGI:96820 Lpl |
Subcellular locationi
Keywords - Cellular componenti
Cell membrane, Chylomicron, Membrane, Secreted, VLDLPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 27 | Sequence analysisAdd BLAST | 27 | |
ChainiPRO_0000017776 | 28 – 474 | Lipoprotein lipaseAdd BLAST | 447 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Disulfide bondi | 54 ↔ 67 | PROSITE-ProRule annotation | ||
Glycosylationi | 70 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Modified residuei | 121 | Nitrated tyrosineBy similarity | 1 | |
Modified residuei | 191 | Nitrated tyrosineBy similarity | 1 | |
Disulfide bondi | 243 ↔ 266 | PROSITE-ProRule annotation | ||
Disulfide bondi | 291 ↔ 310 | PROSITE-ProRule annotation | ||
Disulfide bondi | 302 ↔ 305 | PROSITE-ProRule annotation | ||
Modified residuei | 343 | Nitrated tyrosineBy similarity | 1 | |
Glycosylationi | 386 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 445 ↔ 465 | PROSITE-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, NitrationProteomic databases
MaxQBi | P11152 |
PaxDbi | P11152 |
PeptideAtlasi | P11152 |
PRIDEi | P11152 |
PTM databases
iPTMneti | P11152 |
PhosphoSitePlusi | P11152 |
SwissPalmi | P11152 |
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
Bgeei | ENSMUSG00000015568 |
CleanExi | MM_LPL |
Genevisiblei | P11152 MM |
Interactioni
Subunit structurei
Homodimer (PubMed:25066055). Interacts with APOC2; the interaction activates LPL activity in the presence of lipids (By similarity). Interacts with GPIHBP1 (PubMed:17403372). Interacts with LMF1 and SEL1L (PubMed:25066055).By similarity2 Publications
GO - Molecular functioni
- apolipoprotein binding Source: MGI
- receptor binding Source: MGI
Protein-protein interaction databases
IntActi | P11152 2 interactors. |
STRINGi | 10090.ENSMUSP00000015712 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 341 – 464 | PLATPROSITE-ProRule annotationAdd BLAST | 124 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 346 – 441 | Heparin-bindingBy similarityAdd BLAST | 96 |
Sequence similaritiesi
Keywords - Domaini
SignalPhylogenomic databases
eggNOGi | ENOG410IJUA Eukaryota ENOG4111GMM LUCA |
GeneTreei | ENSGT00760000119069 |
HOGENOMi | HOG000038553 |
HOVERGENi | HBG002259 |
InParanoidi | P11152 |
KOi | K01059 |
OMAi | HYQVKIH |
OrthoDBi | EOG091G052B |
TreeFami | TF324997 |
Family and domain databases
CDDi | cd00707 Pancreat_lipase_like, 1 hit |
Gene3Di | 3.40.50.18201 hit |
InterProi | View protein in InterPro IPR029058 AB_hydrolase IPR013818 Lipase/vitellogenin IPR016272 Lipase_LIPH IPR033906 Lipase_N IPR002330 Lipo_Lipase IPR001024 PLAT/LH2_dom IPR036392 PLAT/LH2_dom_sf IPR000734 TAG_lipase |
PANTHERi | PTHR11610 PTHR11610, 1 hit PTHR11610:SF3 PTHR11610:SF3, 1 hit |
Pfami | View protein in Pfam PF00151 Lipase, 1 hit PF01477 PLAT, 1 hit |
PIRSFi | PIRSF000865 Lipoprotein_lipase_LIPH, 1 hit |
PRINTSi | PR00822 LIPOLIPASE PR00821 TAGLIPASE |
SMARTi | View protein in SMART SM00308 LH2, 1 hit |
SUPFAMi | SSF49723 SSF49723, 1 hit SSF53474 SSF53474, 1 hit |
TIGRFAMsi | TIGR03230 lipo_lipase, 1 hit |
PROSITEi | View protein in PROSITE PS00120 LIPASE_SER, 1 hit PS50095 PLAT, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
P11152-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MESKALLLVV LGVWLQSLTA FRGGVAAADA GRDFSDIESK FALRTPEDTA
60 70 80 90 100
EDTCHLIPGL ADSVSNCHFN HSSKTFVVIH GWTVTGMYES WVPKLVAALY
110 120 130 140 150
KREPDSNVIV VDWLYRAQQH YPVSAGYTKL VGNDVARFIN WMEEEFNYPL
160 170 180 190 200
DNVHLLGYSL GAHAAGVAGS LTNKKVNRIT GLDPAGPNFE YAEAPSRLSP
210 220 230 240 250
DDADFVDVLH TFTRGSPGRS IGIQKPVGHV DIYPNGGTFQ PGCNIGEAIR
260 270 280 290 300
VIAERGLGDV DQLVKCSHER SIHLFIDSLL NEENPSKAYR CNSKEAFEKG
310 320 330 340 350
LCLSCRKNRC NNLGYEINKV RAKRSSKMYL KTRSQMPYKV FHYQVKIHFS
360 370 380 390 400
GTEDGKQHNQ AFEISLYGTV AESENIPFTL PEVSTNKTYS FLIYTEVDIG
410 420 430 440 450
ELLMMKLKWI SDSYFSWPDW WSSPSFVIER IRVKAGETQK KVIFCAREKV
460 470
SHLQKGKDSA VFVKCHDKSL KKSG
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 129 | K → Y no nucleotide entry (PubMed:2723548).Curated | 1 | |
Sequence conflicti | 147 | N → K in AAA39441 (PubMed:1765386).Curated | 1 | |
Sequence conflicti | 354 | D → N no nucleotide entry (PubMed:2723548).Curated | 1 | |
Sequence conflicti | 410 | I → M no nucleotide entry (PubMed:2723548).Curated | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M60847 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 |
Genome annotation databases
Ensembli | ENSMUST00000015712; ENSMUSP00000015712; ENSMUSG00000015568 ENSMUST00000168401; ENSMUSP00000132259; ENSMUSG00000015568 |
GeneIDi | 16956 |
KEGGi | mmu:16956 |
UCSCi | uc009lwq.1 mouse |
Similar proteinsi
Entry informationi
Entry namei | LIPL_MOUSE | |
Accessioni | P11152Primary (citable) accession number: P11152 Secondary accession number(s): Q05956 Q9DCM8 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 1, 1989 |
Last sequence update: | July 27, 2011 | |
Last modified: | March 28, 2018 | |
This is version 175 of the entry and version 3 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |