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P11151 (LIPL_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 119. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Lipoprotein lipase

Short name=LPL
EC=3.1.1.34
Gene names
Name:LPL
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length478 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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.

Catalytic activity

Triacylglycerol + H2O = diacylglycerol + a carboxylate. Ref.7

Subunit structure

Homodimer By similarity. Interacts with APOC2; the interaction activates LPL activity in the presence of lipids. Interacts with GPIHBP1 By similarity. Ref.7

Subcellular location

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. Ref.5 Ref.6

Post-translational modification

Tyrosine nitration after lipopolysaccharide (LPS) challenge down-regulates the lipase activity By similarity.

Sequence similarities

Belongs to the AB hydrolase superfamily. Lipase family.

Contains 1 PLAT domain.

Ontologies

Keywords
   Biological processLipid degradation
Lipid metabolism
   Cellular componentCell membrane
Chylomicron
Membrane
Secreted
VLDL
   DomainSignal
   LigandHeparin-binding
   Molecular functionHydrolase
   PTMDisulfide bond
Glycoprotein
GPI-anchor
Lipoprotein
Nitration
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processfatty acid biosynthetic process

Inferred from direct assay PubMed 18635818. Source: BHF-UCL

phospholipid metabolic process

Inferred from direct assay Ref.7. Source: BHF-UCL

positive regulation of cholesterol storage

Inferred from electronic annotation. Source: Ensembl

positive regulation of macrophage derived foam cell differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of sequestering of triglyceride

Inferred from electronic annotation. Source: Ensembl

triglyceride catabolic process

Inferred from direct assay PubMed 18635818. Source: BHF-UCL

triglyceride homeostasis

Inferred from electronic annotation. Source: Ensembl

triglyceride metabolic process

Inferred from direct assay Ref.7. Source: BHF-UCL

very-low-density lipoprotein particle remodeling

Inferred from direct assay PubMed 18635818. Source: BHF-UCL

   Cellular_componentanchored component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

cell surface

Inferred from electronic annotation. Source: Ensembl

chylomicron

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

very-low-density lipoprotein particle

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionapolipoprotein binding

Inferred from physical interaction Ref.7. Source: BHF-UCL

heparin binding

Inferred from electronic annotation. Source: UniProtKB-KW

lipoprotein lipase activity

Inferred from direct assay Ref.7PubMed 18635818. Source: BHF-UCL

phospholipase activity

Inferred from direct assay Ref.7. Source: BHF-UCL

triglyceride lipase activity

Inferred from direct assay Ref.7. Source: BHF-UCL

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

SORT1Q995236EBI-8794090,EBI-1057058From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2828 Ref.3 Ref.4
Chain29 – 478450Lipoprotein lipase
PRO_0000017772

Regions

Domain344 – 467124PLAT
Region349 – 44496Heparin-binding By similarity

Sites

Active site1621Nucleophile By similarity
Active site1861Charge relay system By similarity
Active site2711Charge relay system By similarity

Amino acid modifications

Modified residue1241Nitrated tyrosine By similarity
Modified residue1941Nitrated tyrosine By similarity
Modified residue3461Nitrated tyrosine By similarity
Glycosylation731N-linked (GlcNAc...)
Glycosylation3891N-linked (GlcNAc...)
Disulfide bond57 ↔ 70 Ref.3
Disulfide bond246 ↔ 269 Ref.3
Disulfide bond294 ↔ 313 Ref.3
Disulfide bond305 ↔ 308 Ref.3
Disulfide bond448 ↔ 468 Ref.3

Sequences

Sequence LengthMass (Da)Tools
P11151 [UniParc].

Last modified December 12, 2006. Version 2.
Checksum: 06FDD429DD194A1F

FASTA47853,378
        10         20         30         40         50         60 
MESKALLLLA LSVCLQSLTV SRGGLVAADR ITGGKDFRDI ESKFALRTPE DTAEDTCHLI 

        70         80         90        100        110        120 
PGVTESVANC HFNHSSKTFV VIHGWTVTGM YESWVPKLVA ALYKREPDSN VIVVDWLSRA 

       130        140        150        160        170        180 
QQHYPVSAGY TKLVGQDVAK FMNWMADEFN YPLGNVHLLG YSLGAHAAGI AGSLTNKKVN 

       190        200        210        220        230        240 
RITGLDPAGP NFEYAEAPSR LSPDDADFVD VLHTFTRGSP GRSIGIQKPV GHVDIYPNGG 

       250        260        270        280        290        300 
TFQPGCNIGE ALRVIAERGL GDVDQLVKCS HERSVHLFID SLLNEENPSK AYRCNSKEAF 

       310        320        330        340        350        360 
EKGLCLSCRK NRCNNMGYEI NKVRAKRSSK MYLKTRSQMP YKVFHYQVKI HFSGTESNTY 

       370        380        390        400        410        420 
TNQAFEISLY GTVAESENIP FTLPEVSTNK TYSFLLYTEV DIGELLMLKL KWISDSYFSW 

       430        440        450        460        470 
SNWWSSPGFD IGKIRVKAGE TQKKVIFCSR EKMSYLQKGK SPVIFVKCHD KSLNRKSG 

« Hide

References

« Hide 'large scale' references
[1]NIH - Mammalian Gene Collection (MGC) project
Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Hereford.
Tissue: Uterus.
[2]"Molecular cloning and sequence of a cDNA coding for bovine lipoprotein lipase."
Senda M., Oka K., Brown W.V., Qasba P.K., Furuichi Y.
Proc. Natl. Acad. Sci. U.S.A. 84:4369-4373(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 29-478.
[3]"Structure of bovine milk lipoprotein lipase."
Yang C.-Y., Gu Z.-W., Yang H.-X., Rohde M.F., Gotto A.M. Jr., Pownall H.J.
J. Biol. Chem. 264:16822-16827(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 29-478, DISULFIDE BONDS.
Tissue: Mammary gland.
[4]"Lipoprotein lipases from cow, guinea-pig and man. Structural characterization and identification of protease-sensitive internal regions."
Bengtsson-Olivecrona G., Olivecrona T., Joernvall H.
Eur. J. Biochem. 161:281-288(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 29-55.
[5]"Metabolism of endothelial cell-bound lipoprotein lipase. Evidence for heparan sulfate proteoglycan-mediated internalization and recycling."
Saxena U., Klein M.G., Goldberg I.J.
J. Biol. Chem. 265:12880-12886(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: HEPARIN BINDING, SUBCELLULAR LOCATION.
[6]"Binding and intracellular trafficking of lipoprotein lipase and triacylglycerol-rich lipoproteins by liver cells."
Casaroli-Marano R.P., Garcia R., Vilella E., Olivecrona G., Reina M., Vilaro S.
J. Lipid Res. 39:789-806(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[7]"Apolipoprotein C-II39-62 activates lipoprotein lipase by direct lipid-independent binding."
MacPhee C.E., Hatters D.M., Sawyer W.H., Howlett G.J.
Biochemistry 39:3433-3440(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH APOC2, ENZYME ACTIVITY.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC118091 mRNA. Translation: AAI18092.1.
M16966 mRNA. Translation: AAA30624.1.
PIRA27053.
RefSeqNP_001068588.1. NM_001075120.1.
UniGeneBt.5387.

3D structure databases

ProteinModelPortalP11151.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid158237. 1 interaction.
IntActP11151. 2 interactions.

Chemistry

ChEMBLCHEMBL3064.

Proteomic databases

PaxDbP11151.
PRIDEP11151.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000017086; ENSBTAP00000017086; ENSBTAG00000012855.
GeneID280843.
KEGGbta:280843.

Organism-specific databases

CTD4023.

Phylogenomic databases

eggNOGNOG40923.
GeneTreeENSGT00750000117234.
HOGENOMHOG000038553.
HOVERGENHBG002259.
InParanoidP11151.
KOK01059.
OMAESVANCH.
OrthoDBEOG757CX5.
TreeFamTF324997.

Enzyme and pathway databases

BRENDA3.1.1.34. 908.

Family and domain databases

Gene3D2.60.60.20. 1 hit.
InterProIPR000734. Lipase.
IPR008976. Lipase_LipOase.
IPR013818. Lipase_N.
IPR002330. Lipo_Lipase.
IPR016272. Lipoprotein_lipase_LIPH.
IPR001024. PLAT/LH2_dom.
[Graphical view]
PANTHERPTHR11610. PTHR11610. 1 hit.
PTHR11610:SF3. PTHR11610:SF3. 1 hit.
PfamPF00151. Lipase. 1 hit.
PF01477. PLAT. 1 hit.
[Graphical view]
PIRSFPIRSF000865. Lipoprotein_lipase_LIPH. 1 hit.
PRINTSPR00822. LIPOLIPASE.
PR00821. TAGLIPASE.
SMARTSM00308. LH2. 1 hit.
[Graphical view]
SUPFAMSSF49723. SSF49723. 1 hit.
TIGRFAMsTIGR03230. lipo_lipase. 1 hit.
PROSITEPS00120. LIPASE_SER. 1 hit.
PS50095. PLAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20804991.

Entry information

Entry nameLIPL_BOVIN
AccessionPrimary (citable) accession number: P11151
Secondary accession number(s): Q17R03
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: December 12, 2006
Last modified: April 16, 2014
This is version 119 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families