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Protein

Lipoprotein lipase

Gene

Lpl

Organism
Rattus norvegicus (Rat)
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: RGD
  • heparin binding Source: UniProtKB
  • lipoprotein lipase activity Source: CACAO
  • receptor binding Source: RGD
  • triglyceride binding Source: RGD
  • triglyceride lipase activity Source: RGD

GO - Biological processi

Keywordsi

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

Enzyme and pathway databases

BRENDAi3.1.1.34 5301
ReactomeiR-RNO-8963889 Assembly of active LPL and LIPC lipase complexes
R-RNO-8963901 Chylomicron remodeling
R-RNO-975634 Retinoid metabolism and transport

Protein family/group databases

ESTHERiratno-lipli Lipoprotein_Lipase

Names & Taxonomyi

Protein namesi
Recommended name:
Lipoprotein lipase (EC:3.1.1.34By similarity)
Short name:
LPL
Gene namesi
Name:Lpl
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 16

Organism-specific databases

RGDi3017 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

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL5906

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 27By similarityAdd BLAST27
ChainiPRO_000001777928 – 474Lipoprotein lipaseAdd BLAST447

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi54 ↔ 67PROSITE-ProRule annotation
Glycosylationi70N-linked (GlcNAc...) asparagineSequence analysis1
Modified residuei121Nitrated tyrosine1 Publication1
Modified residuei191Nitrated tyrosine1 Publication1
Disulfide bondi243 ↔ 266PROSITE-ProRule annotation
Disulfide bondi291 ↔ 310PROSITE-ProRule annotation
Disulfide bondi302 ↔ 305PROSITE-ProRule annotation
Modified residuei343Nitrated tyrosine1 Publication1
Glycosylationi386N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi445 ↔ 465PROSITE-ProRule annotation

Post-translational modificationi

Tyrosine nitration after lipopolysaccharide (LPS) challenge down-regulates the lipase activity.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein, Nitration

Proteomic databases

PaxDbiQ06000
PRIDEiQ06000

Expressioni

Inductioni

Induced by insulin. Inhibited by isoproterenol.1 Publication

Gene expression databases

BgeeiENSRNOG00000012181
GenevisibleiQ06000 RN

Interactioni

Subunit structurei

Homodimer (By similarity). Interacts with APOC2; the interaction activates LPL activity in the presence of lipids (By similarity). Interacts with GPIHBP1. Interacts with LMF1 and SEL1L (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000016543

Chemistry databases

BindingDBiQ06000

Structurei

3D structure databases

ProteinModelPortaliQ06000
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
InParanoidiQ06000
KOiK01059
OMAiHYQVKIH
OrthoDBiEOG091G052B
PhylomeDBiQ06000
TreeFamiTF324997

Family and domain databases

CDDicd00707 Pancreat_lipase_like, 1 hit
Gene3Di3.40.50.1820, 1 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.

Q06000-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MESKALLLVA LGVWLQSLTA FRGGVAAADG GRDFSDIESK FALRTPEDTA
60 70 80 90 100
EDTCHLIPGL ADSVSNCHFN HSSKTFVVIH GWTVTGMYES WVPKLVAALY
110 120 130 140 150
KREPDSNVIV VDWLYRAQQH YPVSAGYTKL VGNDVARFIN WLEEEFNYPL
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
VIAEKGLGDV DQLVKCSHER SIHLFIDSLL NEENPSKAYR CNSKEAFEKG
310 320 330 340 350
LCLSCRKNRC NNVGYEINKV RAKRSSKMYL KTRSQMPYKV FHYQVKIHFS
360 370 380 390 400
GTENDKQNNQ AFEISLYGTV AESENIPFTL PEVATNKTYS FLIYTEVDIG
410 420 430 440 450
ELLMMKLKWK NDSYFRWSDW WSSPSFVIEK IRVKAGETQK KVIFCAREKV
460 470
SHLQKGKDAA VFVKCHDKSL KKSG
Length:474
Mass (Da):53,082
Last modified:February 1, 1994 - v1
Checksum:iF4F6F4BCCA4F1626
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti336M → V no nucleotide entry (PubMed:2233752).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L03294 mRNA Translation: AAA41534.1
BC081836 mRNA Translation: AAH81836.1
PIRiJH0790
RefSeqiNP_036730.1, NM_012598.2
UniGeneiRn.3834

Genome annotation databases

EnsembliENSRNOT00000016543; ENSRNOP00000016543; ENSRNOG00000012181
GeneIDi24539
KEGGirno:24539
UCSCiRGD:3017 rat

Similar proteinsi

Entry informationi

Entry nameiLIPL_RAT
AccessioniPrimary (citable) accession number: Q06000
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: March 28, 2018
This is version 146 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health