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O46647 (LIPL_NEOVI) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Lipoprotein lipase

Short name=LPL
EC=3.1.1.34
Gene names
Name:LPL
OrganismNeovison vison (American mink) (Mustela vison)
Taxonomic identifier452646 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaMustelidaeMustelinaeNeovison

Protein attributes

Sequence length475 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.

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 – 2727 By similarity
Chain28 – 475448Lipoprotein lipase
PRO_0000017777

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 By similarity
Modified residue1911Nitrated tyrosine By similarity
Modified residue3431Nitrated tyrosine By similarity
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

Natural variations

Natural variant2411P → L in chylomicronemia syndrome; no lipase activity. Ref.1

Sequences

Sequence LengthMass (Da)Tools
O46647 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: 2F2DBF0090F0FB7C

FASTA47552,968
        10         20         30         40         50         60 
MESKALLLVA LGMWFQSLTA TRGGVAAADR GGDFIDIESK FALRTPEDTA EDTCHLIPGV 

        70         80         90        100        110        120 
TESVANCHFN HSSKTFVVIH GWTVTGMYES WVPKLVAALY KREPDSNVIV VDWLSRAQQH 

       130        140        150        160        170        180 
YPVSAGYTKL VGKDVAKFIN WMAEEFHYPL DNVHLLGYSL GAHAAGIAGS LTNKKVNRIT 

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

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

       310        320        330        340        350        360 
LCLSCRKNRC NNLGYEINKV RAKRSSKMYL KTRSQMPYKV FHYQVKIHFS GTESDTQTNQ 

       370        380        390        400        410        420 
AFEISLYGTV AESENIPFTL PEVSANKTYS FLIYTEVDIG ELLMLKLKWK SDSYFSWSDW 

       430        440        450        460        470 
WSSPGFAIEK IRVKAGETQK KVIFCSREKV SHLQKGKASV VFVKCHDKSL NKKSG 

« Hide

References

[1]"A mutation in the lipoprotein lipase gene associated with hyperlipoproteinemia type I in mink: studies on lipid and lipase levels in heterozygotes."
Lindberg A., Nordstoga K., Christophersen B., Savonen R., van Tol A., Olivecrona G.
Int. J. Mol. Med. 1:529-538(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT CHYLOMICRONEMIA SYNDROME LEU-241.
Tissue: Heart.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ223493 Genomic DNA. Translation: CAA11411.1.

3D structure databases

ProteinModelPortalO46647.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG002259.

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...

Entry information

Entry nameLIPL_NEOVI
AccessionPrimary (citable) accession number: O46647
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: June 1, 1998
Last modified: February 19, 2014
This is version 88 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