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Reviewed, UniProtKB/Swiss-Prot P55031 (LIPL_FELCA)

Last modified October 13, 2009. Version 72. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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)
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). The enzyme functions in the presence of apolipoprotein C-2 on the luminal surface of vascular endothelium.

Catalytic activity

Triacylglycerol + H2O = diacylglycerol + a carboxylate.

Subunit structure

Homodimer. Interacts with apolipoprotein C-2. Interacts with GPIHBP1.

Subcellular location

Cell membrane; Lipid-anchorGPI-anchor.

Involvement in disease

Defects in LPL are a cause of chylomicronemia syndrome, also known as type I hyperlipoproteinemia.

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
Region322 – 33413Heparin-binding Potential

Sites

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

Amino acid modifications

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
P55031-1 [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: 8636438] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT CHYLOMICRONEMIA SYNDROME GLY-435.

Cross-references

Sequence databases

U42725 mRNA. Translation: AAB03848.1.
RefSeqNP_001036032.1.

3D structure databases

HSSPHSSP built from PDB template 1RP1 based on UniProtKB P06857.
ModBaseSearch...

Protein-protein interaction databases

STRINGP55031.

Genome annotation databases

GeneID727696.

Organism-specific databases

CTD727696.

Phylogenomic databases

HOVERGENP55031.

Enzyme and pathway databases

BRENDA3.1.1.34. 273949.

Family and domain databases

InterProIPR000734. Lipase.
IPR013818. Lipase_N.
IPR008262. Lipase_Ser_AS.
IPR002330. Lipo_Lipase.
IPR001024. LipOase_LH2.
IPR016272. Lipoprotein_lipase_LIPH.
[Graphical view]
PANTHERPTHR11610. Lipase. 1 hit.
PTHR11610:SF3. Lipase_lipo. 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]
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: October 13, 2009
This is version 72 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents