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Protein

Lipoprotein lipase

Gene

Lpl

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

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 keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei159NucleophileBy similarity1
Active sitei183Charge relay systemPROSITE-ProRule annotation1
Active sitei268Charge relay systemPROSITE-ProRule annotation1

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

Keywordsi

Molecular functionHeparin-binding, Hydrolase
Biological processLipid degradation, Lipid metabolism

Enzyme and pathway databases

BRENDAi3.1.1.34 3474
ReactomeiR-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

ESTHERimouse-lipli Lipoprotein_Lipase

Names & Taxonomyi

Protein namesi
Recommended name:
Lipoprotein lipase (EC:3.1.1.34By similarity)
Short name:
LPL
Gene namesi
Name:Lpl
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:96820 Lpl

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Chylomicron, Membrane, Secreted, VLDL

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 27Sequence analysisAdd BLAST27
ChainiPRO_000001777628 – 474Lipoprotein lipaseAdd BLAST447

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi54 ↔ 67PROSITE-ProRule annotation
Glycosylationi70N-linked (GlcNAc...) asparagineSequence analysis1
Modified residuei121Nitrated tyrosineBy similarity1
Modified residuei191Nitrated tyrosineBy similarity1
Disulfide bondi243 ↔ 266PROSITE-ProRule annotation
Disulfide bondi291 ↔ 310PROSITE-ProRule annotation
Disulfide bondi302 ↔ 305PROSITE-ProRule annotation
Modified residuei343Nitrated tyrosineBy similarity1
Glycosylationi386N-linked (GlcNAc...) asparagineSequence analysis1
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
PeptideAtlasiP11152
PRIDEiP11152

PTM databases

iPTMnetiP11152
PhosphoSitePlusiP11152
SwissPalmiP11152

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

BgeeiENSMUSG00000015568
CleanExiMM_LPL
GenevisibleiP11152 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

Protein-protein interaction databases

IntActiP11152 2 interactors.
STRINGi10090.ENSMUSP00000015712

Structurei

3D structure databases

ProteinModelPortaliP11152
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini341 – 464PLATPROSITE-ProRule annotationAdd BLAST124

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni346 – 441Heparin-bindingBy similarityAdd BLAST96

Sequence similaritiesi

Belongs to the AB hydrolase superfamily. Lipase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IJUA Eukaryota
ENOG4111GMM LUCA
GeneTreeiENSGT00760000119069
HOGENOMiHOG000038553
HOVERGENiHBG002259
InParanoidiP11152
KOiK01059
OMAiHYQVKIH
OrthoDBiEOG091G052B
TreeFamiTF324997

Family and domain databases

CDDicd00707 Pancreat_lipase_like, 1 hit
Gene3Di3.40.50.18201 hit
InterProiView 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
PANTHERiPTHR11610 PTHR11610, 1 hit
PTHR11610:SF3 PTHR11610:SF3, 1 hit
PfamiView protein in Pfam
PF00151 Lipase, 1 hit
PF01477 PLAT, 1 hit
PIRSFiPIRSF000865 Lipoprotein_lipase_LIPH, 1 hit
PRINTSiPR00822 LIPOLIPASE
PR00821 TAGLIPASE
SMARTiView protein in SMART
SM00308 LH2, 1 hit
SUPFAMiSSF49723 SSF49723, 1 hit
SSF53474 SSF53474, 1 hit
TIGRFAMsiTIGR03230 lipo_lipase, 1 hit
PROSITEiView protein in PROSITE
PS00120 LIPASE_SER, 1 hit
PS50095 PLAT, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P11152-1 [UniParc]FASTAAdd to basket

« Hide

        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
Length:474
Mass (Da):53,109
Last modified:July 27, 2011 - v3
Checksum:iE5895C98B7AE16CD
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti129K → Y no nucleotide entry (PubMed:2723548).Curated1
Sequence conflicti147N → K in AAA39441 (PubMed:1765386).Curated1
Sequence conflicti354D → N no nucleotide entry (PubMed:2723548).Curated1
Sequence conflicti410I → M no nucleotide entry (PubMed:2723548).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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

Similar proteinsi

Entry informationi

Entry nameiLIPL_MOUSE
AccessioniPrimary (citable) accession number: P11152
Secondary accession number(s): Q05956
, Q542L4, Q9D3M9, Q9DCM8
Entry historyiIntegrated 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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome