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Protein

Lipoprotein lipase

Gene

LPL

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei162NucleophileBy similarity1
Active sitei186Charge relay systemPROSITE-ProRule annotation1
Active sitei271Charge relay systemPROSITE-ProRule annotation1

GO - Molecular functioni

  • apolipoprotein binding Source: BHF-UCL
  • heparin binding Source: UniProtKB
  • lipoprotein lipase activity Source: BHF-UCL
  • phospholipase activity Source: BHF-UCL
  • receptor 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. 908.
ReactomeiR-BTA-8963889. Assembly of active LPL and LIPC lipase complexes.

Protein family/group databases

ESTHERibovin-lipli. Lipoprotein_Lipase.

Names & Taxonomyi

Protein namesi
Recommended name:
Lipoprotein lipase (EC:3.1.1.341 Publication)
Short name:
LPL
Gene namesi
Name:LPL
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 8

Subcellular locationi

  • Cell membrane; Lipid-anchorGPI-anchor
  • Secreted

  • 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.

GO - Cellular componenti

Keywords - Cellular componenti

Cell membrane, Chylomicron, Membrane, Secreted, VLDL

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL3064.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 282 PublicationsAdd BLAST28
ChainiPRO_000001777229 – 478Lipoprotein lipaseAdd BLAST450

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi57 ↔ 70PROSITE-ProRule annotation1 Publication
Glycosylationi73N-linked (GlcNAc...) asparagine1
Modified residuei124Nitrated tyrosineBy similarity1
Modified residuei194Nitrated tyrosineBy similarity1
Disulfide bondi246 ↔ 269PROSITE-ProRule annotation1 Publication
Disulfide bondi294 ↔ 313PROSITE-ProRule annotation1 Publication
Disulfide bondi305 ↔ 308PROSITE-ProRule annotation1 Publication
Modified residuei346Nitrated tyrosineBy similarity1
Glycosylationi389N-linked (GlcNAc...) asparagine1
Disulfide bondi448 ↔ 468PROSITE-ProRule annotation1 Publication

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

PaxDbiP11151.
PeptideAtlasiP11151.
PRIDEiP11151.

Expressioni

Gene expression databases

BgeeiENSBTAG00000012855.

Interactioni

Subunit structurei

Homodimer (By similarity). Interacts with APOC2; the interaction activates LPL activity in the presence of lipids (PubMed:10727238). Interacts with GPIHBP1. Interacts with LMF1 and SEL1L (By similarity).By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
SORT1Q995236EBI-8794090,EBI-1057058From Homo sapiens.

GO - Molecular functioni

  • apolipoprotein binding Source: BHF-UCL
  • receptor binding Source: Ensembl

Protein-protein interaction databases

BioGridi158237. 1 interactor.
DIPiDIP-61310N.
IntActiP11151. 3 interactors.
STRINGi9913.ENSBTAP00000017086.

Structurei

3D structure databases

ProteinModelPortaliP11151.
SMRiP11151.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini344 – 467PLATPROSITE-ProRule annotationAdd BLAST124

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni349 – 444Heparin-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.
InParanoidiP11151.
KOiK01059.
OMAiFHYQVKI.
OrthoDBiEOG091G052B.
TreeFamiTF324997.

Family and domain databases

CDDicd00707. Pancreat_lipase_like. 1 hit.
Gene3Di2.60.60.20. 1 hit.
3.40.50.1820. 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.
IPR000734. TAG_lipase.
PANTHERiPTHR11610. PTHR11610. 1 hit.
PTHR11610:SF122. PTHR11610:SF122. 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.

P11151-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MESKALLLLA LSVCLQSLTV SRGGLVAADR ITGGKDFRDI ESKFALRTPE
60 70 80 90 100
DTAEDTCHLI PGVTESVANC HFNHSSKTFV VIHGWTVTGM YESWVPKLVA
110 120 130 140 150
ALYKREPDSN VIVVDWLSRA QQHYPVSAGY TKLVGQDVAK FMNWMADEFN
160 170 180 190 200
YPLGNVHLLG YSLGAHAAGI AGSLTNKKVN RITGLDPAGP NFEYAEAPSR
210 220 230 240 250
LSPDDADFVD VLHTFTRGSP GRSIGIQKPV GHVDIYPNGG TFQPGCNIGE
260 270 280 290 300
ALRVIAERGL GDVDQLVKCS HERSVHLFID SLLNEENPSK AYRCNSKEAF
310 320 330 340 350
EKGLCLSCRK NRCNNMGYEI NKVRAKRSSK MYLKTRSQMP YKVFHYQVKI
360 370 380 390 400
HFSGTESNTY TNQAFEISLY GTVAESENIP FTLPEVSTNK TYSFLLYTEV
410 420 430 440 450
DIGELLMLKL KWISDSYFSW SNWWSSPGFD IGKIRVKAGE TQKKVIFCSR
460 470
EKMSYLQKGK SPVIFVKCHD KSLNRKSG
Length:478
Mass (Da):53,378
Last modified:December 12, 2006 - v2
Checksum:i06FDD429DD194A1F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC118091 mRNA. Translation: AAI18092.1.
M16966 mRNA. Translation: AAA30624.1.
PIRiA27053.
RefSeqiNP_001068588.1. NM_001075120.1.
UniGeneiBt.5387.

Genome annotation databases

EnsembliENSBTAT00000017086; ENSBTAP00000017086; ENSBTAG00000012855.
GeneIDi280843.
KEGGibta:280843.

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.

Entry informationi

Entry nameiLIPL_BOVIN
AccessioniPrimary (citable) accession number: P11151
Secondary accession number(s): Q17R03
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: December 12, 2006
Last modified: June 7, 2017
This is version 144 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families