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P55031 (LIPL_FELCA) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 95. 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
OrganismFelis catus (Cat) (Felis silvestris catus) [Reference proteome]
Taxonomic identifier9685 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraFeliformiaFelidaeFelinaeFelis

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 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.

Post-translational modification

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

Involvement in disease

Defects in LPL are a cause of chylomicronemia syndrome, also known as type I hyperlipoproteinemia. Animals exhibit reduced body mass, growth rates, and increased stillbirth rates.

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 – 2323 Potential
Chain24 – 478455Lipoprotein lipase
PRO_0000017774

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...) Potential
Glycosylation3891N-linked (GlcNAc...) Potential
Disulfide bond57 ↔ 70 By similarity
Disulfide bond246 ↔ 269 By similarity
Disulfide bond294 ↔ 313 By similarity
Disulfide bond305 ↔ 308 By similarity
Disulfide bond448 ↔ 468 By similarity

Natural variations

Natural variant4351R → G in chylomicronemia syndrome. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P55031 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: F57014446127E8C9

FASTA47853,668
        10         20         30         40         50         60 
MESKTLFLMA LGIWLQSLTT TRGWVAADDR ITGGRDFIDI ESKFALRTPE DIAEDTCHLI 

        70         80         90        100        110        120 
PGVTESVANC HFNHTSKTFV VIHGWTVTGM YESWVPKLVA APYKREPDSN VIVVDWLSRA 

       130        140        150        160        170        180 
QQHYPVSAGY TKLVGKDVAK FINWMAEEFH YPLDNVHLLG YSLGAHAAGI AGSLTNKKVN 

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

       250        260        270        280        290        300 
TFQPGCNIGE AIRVIAERGL GDVDQLVKCS HERSIHLFID SLLNEENPSK AYRCNSKEAF 

       310        320        330        340        350        360 
EKGLCLSCRK NRCNNLGYEI NKVRAKRSSK MYLKTRSQMP YKVFHYQVKI HFSGTESDTQ 

       370        380        390        400        410        420 
TNQVFEISLY GTVAESENIP FTLPEISANK TYSFLIYTEV DIGELLMLKL KWKSDSYFSW 

       430        440        450        460        470 
SDWWSSPGFT IEKIRVKAGE TQKKVIFCSR EKVSHLQKGK ASVVFVKCHD KSLNKKSG 

« Hide

References

[1]"A mutation in the lipoprotein lipase gene is the molecular basis of chylomicronemia in a colony of domestic cats."
Ginzinger D.G., Lewis M.E.S., Ma Y., Jones B.R., Liu G., Jones S.D.
J. Clin. Invest. 97:1257-1266(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT CHYLOMICRONEMIA SYNDROME GLY-435.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U42725 mRNA. Translation: AAB03848.1.
RefSeqNP_001036032.1. NM_001042567.1.

3D structure databases

ProteinModelPortalP55031.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9685.ENSFCAP00000011284.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID727696.
KEGGfca:727696.

Organism-specific databases

CTD4023.

Phylogenomic databases

eggNOGNOG40923.
HOVERGENHBG002259.
KOK01059.

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_FELCA
AccessionPrimary (citable) accession number: P55031
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: June 11, 2014
This is version 95 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