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Q06000 (LIPL_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 122. 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·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
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length474 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 By similarity.

Catalytic activity

Triacylglycerol + H2O = diacylglycerol + a carboxylate.

Subunit structure

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

Subcellular location

Cell membrane By similarity; Lipid-anchorGPI-anchor By similarity. Secreted By similarity. 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 By similarity.

Induction

Induced by insulin. Inhibited by isoproterenol. Ref.3

Post-translational modification

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

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
Reference proteome
Gene Ontology (GO)
   Biological_processlipid catabolic process

Inferred from direct assay PubMed 12551943. Source: RGD

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

response to cold

Inferred from expression pattern PubMed 18722549. Source: RGD

response to drug

Inferred from expression pattern PubMed 11016888. Source: RGD

triglyceride biosynthetic process

Inferred from mutant phenotype PubMed 11788374. Source: RGD

triglyceride catabolic process

Inferred from electronic annotation. Source: Ensembl

triglyceride homeostasis

Inferred from electronic annotation. Source: Ensembl

   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

extracellular matrix

Inferred from direct assay PubMed 12551943. Source: RGD

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

very-low-density lipoprotein particle

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionheparin binding

Inferred from electronic annotation. Source: UniProtKB-KW

lipoprotein lipase activity

Inferred from direct assay PubMed 11788374PubMed 12551943. Source: RGD

triglyceride binding

Inferred from direct assay PubMed 12551943. Source: RGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727 By similarity
Chain28 – 474447Lipoprotein lipase
PRO_0000017779

Regions

Domain341 – 464124PLAT
Region346 – 44196Heparin-binding By similarity

Sites

Active site1591Nucleophile By similarity
Active site1831Charge relay system By similarity
Active site2681Charge relay system By similarity

Amino acid modifications

Modified residue1211Nitrated tyrosine Ref.4
Modified residue1911Nitrated tyrosine Ref.4
Modified residue3431Nitrated tyrosine Ref.4
Glycosylation701N-linked (GlcNAc...) Potential
Glycosylation3861N-linked (GlcNAc...) Potential
Disulfide bond54 ↔ 67 By similarity
Disulfide bond243 ↔ 266 By similarity
Disulfide bond291 ↔ 310 By similarity
Disulfide bond302 ↔ 305 By similarity
Disulfide bond445 ↔ 465 By similarity

Experimental info

Sequence conflict3361M → V no nucleotide entry Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q06000 [UniParc].

Last modified February 1, 1994. Version 1.
Checksum: F4F6F4BCCA4F1626

FASTA47453,082
        10         20         30         40         50         60 
MESKALLLVA LGVWLQSLTA FRGGVAAADG GRDFSDIESK FALRTPEDTA EDTCHLIPGL 

        70         80         90        100        110        120 
ADSVSNCHFN HSSKTFVVIH GWTVTGMYES WVPKLVAALY KREPDSNVIV VDWLYRAQQH 

       130        140        150        160        170        180 
YPVSAGYTKL VGNDVARFIN WLEEEFNYPL DNVHLLGYSL GAHAAGVAGS LTNKKVNRIT 

       190        200        210        220        230        240 
GLDPAGPNFE YAEAPSRLSP DDADFVDVLH TFTRGSPGRS IGIQKPVGHV DIYPNGGTFQ 

       250        260        270        280        290        300 
PGCNIGEAIR VIAEKGLGDV DQLVKCSHER SIHLFIDSLL NEENPSKAYR CNSKEAFEKG 

       310        320        330        340        350        360 
LCLSCRKNRC NNVGYEINKV RAKRSSKMYL KTRSQMPYKV FHYQVKIHFS GTENDKQNNQ 

       370        380        390        400        410        420 
AFEISLYGTV AESENIPFTL PEVATNKTYS FLIYTEVDIG ELLMMKLKWK NDSYFRWSDW 

       430        440        450        460        470 
WSSPSFVIEK IRVKAGETQK KVIFCAREKV SHLQKGKDAA VFVKCHDKSL KKSG 

« Hide

References

« Hide 'large scale' references
[1]"Sequence of rat lipoprotein lipase-encoding cDNA."
Brault D., Noe L., Etienne J., Hamelin J., Raisonnier A., Souli A., Chuat J.-C., Dugail I., Quignard-Boulange A., Lavau M., Galibert F.
Gene 121:237-246(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Sprague-Dawley.
Tissue: Testis.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.
[3]"Lipoprotein lipase gene expression in rat adipocytes is regulated by isoproterenol and insulin through different mechanisms."
Raynolds M.V., Awald P.D., Gordon D.F., Gutierrez-Hartmann A., Rule D.C., Wood W.M., Eckel R.H.
Mol. Endocrinol. 4:1416-1422(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 336-474, INDUCTION.
Tissue: Heart.
[4]"Lipoprotein lipase is nitrated in vivo after lipopolysaccharide challenge."
Casanovas A., Carrascal M., Abian J., Lopez-Tejero M.D., Llobera M.
Free Radic. Biol. Med. 47:1553-1560(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NITRATION AT TYR-121; TYR-191 AND TYR-343, IDENTIFICATION BY MASS SPECTROMETRY.
[5]"Discovery of lipoprotein lipase pI isoforms and contributions to their characterization."
Casanovas A., Carrascal M., Abian J., Lopez-Tejero M.D., Llobera M.
J. Proteomics 72:1031-1039(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, GLYCOSYLATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L03294 mRNA. Translation: AAA41534.1.
BC081836 mRNA. Translation: AAH81836.1.
PIRJH0790.
RefSeqNP_036730.1. NM_012598.2.
UniGeneRn.3834.

3D structure databases

ProteinModelPortalQ06000.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000016543.

Chemistry

BindingDBQ06000.
ChEMBLCHEMBL5906.

Proteomic databases

PaxDbQ06000.
PRIDEQ06000.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000016543; ENSRNOP00000016543; ENSRNOG00000012181.
GeneID24539.
KEGGrno:24539.
UCSCRGD:3017. rat.

Organism-specific databases

CTD4023.
RGD3017. Lpl.

Phylogenomic databases

eggNOGNOG40923.
GeneTreeENSGT00750000117234.
HOGENOMHOG000038553.
HOVERGENHBG002259.
InParanoidQ06000.
KOK01059.
OMAESVANCH.
OrthoDBEOG757CX5.
PhylomeDBQ06000.
TreeFamTF324997.

Enzyme and pathway databases

BRENDA3.1.1.34. 5301.

Gene expression databases

GenevestigatorQ06000.

Family and domain databases

Gene3D2.60.60.20. 1 hit.
3.40.50.1820. 1 hit.
InterProIPR029058. AB_hydrolase.
IPR000734. 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.
SSF53474. SSF53474. 1 hit.
TIGRFAMsTIGR03230. lipo_lipase. 1 hit.
PROSITEPS00120. LIPASE_SER. 1 hit.
PS50095. PLAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio603620.
PROQ06000.

Entry information

Entry nameLIPL_RAT
AccessionPrimary (citable) accession number: Q06000
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: July 9, 2014
This is version 122 of the entry and version 1 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