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P11153 (LIPL_CAVPO) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 110. 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
OrganismCavia porcellus (Guinea pig) [Reference proteome]
Taxonomic identifier10141 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaHystricognathiCaviidaeCavia

Protein attributes

Sequence length465 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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.

Tissue specificity

High level of expression in expression in adipocytes, heart muscle and mammary gland. Ref.1

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Potential
Chain18 – 465448Lipoprotein lipase
PRO_0000017773

Regions

Domain331 – 454124PLAT
Region336 – 43196Heparin-binding By similarity

Sites

Active site1491Nucleophile By similarity
Active site1731Charge relay system By similarity
Active site2581Charge relay system By similarity

Amino acid modifications

Modified residue1111Nitrated tyrosine By similarity
Modified residue1811Nitrated tyrosine By similarity
Modified residue3331Nitrated tyrosine By similarity
Glycosylation601N-linked (GlcNAc...) Potential
Glycosylation3761N-linked (GlcNAc...) Potential
Disulfide bond44 ↔ 57 By similarity
Disulfide bond233 ↔ 256 By similarity
Disulfide bond281 ↔ 300 By similarity
Disulfide bond292 ↔ 295 By similarity
Disulfide bond435 ↔ 455 By similarity

Sequences

Sequence LengthMass (Da)Tools
P11153 [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: E2515F36BEFD5F10

FASTA46552,781
        10         20         30         40         50         60 
MNIDRKILNK ALAKEKVANC QKDYTDIESK FARRTPENTV EDTCHLIPGV TESVANCHFN 

        70         80         90        100        110        120 
HSSKTFMVIH GWTVTGMYES WVPKLVAALY KREPDSNVIV VDWLRRAQHH YPESADYTKL 

       130        140        150        160        170        180 
VGEDVARFIN WMEDEFKYSV DNVHLLGYSL GAHAAGVAGS RTNTKVSRIT GLDPAGPNFE 

       190        200        210        220        230        240 
YAEATSRLSP DDAQFVDVLH TFTRGSPGRS IGIQKPVGHV DIYPNGGSFQ PGCNIQDALR 

       250        260        270        280        290        300 
VISQKGFGDM DQLVKCSHER SIHLFIDSLL NEENPSKAYR CNSKEAFEKG LCLSCRKNRC 

       310        320        330        340        350        360 
NNVGYEINKV RAKRSSKMYL KTRSQMPYKV FHYQVKIYFS GTETTTYTNQ AFEISLYGTV 

       370        380        390        400        410        420 
AESENIPFTL PEVSANNTYS FLIYTEVDIG ELLMLKLKWI TESYFSWSSW WGRPTFTIEK 

       430        440        450        460 
IRVKAGETQK KIVFCSREKV SKLQKGKEAP VFVKCHDKSL NKKSG 

« Hide

References

[1]"Molecular cloning and sequence analysis of cDNA encoding lipoprotein lipase of guinea pig."
Enerbaeck S., Semb H., Bengtsson-Olivecrona G., Carlsson P., Hermansson M.-L., Olivecrona T., Bjursell G.
Gene 58:1-12(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
[2]"Genomic organization of the region encoding guinea pig lipoprotein lipase; evidence for exon fusion and unconventional splicing."
Enerbaeck S., Bjursell G.
Gene 84:391-397(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M15483 mRNA. Translation: AAA37046.1.
M33381 expand/collapse EMBL AC list , M33377, M33378, M33379, M33380 Genomic DNA. Translation: AAA37039.1.
PIRA27330. JS0398.
RefSeqNP_001166449.1. NM_001172978.1.

3D structure databases

ProteinModelPortalP11153.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10141.ENSCPOP00000003655.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100135570.

Organism-specific databases

CTD4023.

Phylogenomic databases

eggNOGNOG40923.
HOGENOMHOG000038553.
HOVERGENHBG002259.
InParanoidP11153.

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...

Entry information

Entry nameLIPL_CAVPO
AccessionPrimary (citable) accession number: P11153
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: June 11, 2014
This is version 110 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