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Q29524 (LIPL_SHEEP) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 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
OrganismOvis aries (Sheep) [Reference proteome]
Taxonomic identifier9940 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeCaprinaeOvis

Protein attributes

Sequence length478 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.

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.

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_processpositive 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

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

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 electronic annotation. Source: UniProtKB-EC

protein binding

Inferred from physical interaction PubMed 17403372. Source: BHF-UCL

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727 Potential
Chain28 – 478451Lipoprotein lipase
PRO_0000017781

Regions

Domain344 – 467124PLAT
Region349 – 44496Heparin-binding By similarity

Sites

Active site1621Nucleophile
Active site1861Charge relay system
Active site2711Charge relay system

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

Sequences

Sequence LengthMass (Da)Tools
Q29524 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: 10F41EE1FFB9C882

FASTA47853,588
        10         20         30         40         50         60 
MESKVLLLLA LSVWLQSLTV SRGGLVAADR ITRGKDFRDI ESKFALRTPE DTAEDTCHLI 

        70         80         90        100        110        120 
PGVTESVANC HFNHSSKTFV VIHGWTVTGM YESWVPKLVA ALYKREPDSN VIVVDWLSRA 

       130        140        150        160        170        180 
QQHYPVSAGY TKLVGQDVAK FMNWMADEFN YPLGNVHLLG YSLGAHAAGI AGSLTNKKVN 

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

       250        260        270        280        290        300 
TFQPGCNIGE ALRVIAERGL GDVDQLVKCS HERSVHLFID SLLNEENPSK AYRCNSKEAF 

       310        320        330        340        350        360 
EKGLCLSCRK NRCNNMGYEI NKVRAKRSSK MYLKTRSQMP YKVFHYQVKI HFSGTESNTY 

       370        380        390        400        410        420 
TNQAFEISLY GTVAESENIP FTLPEVSTNK TYSFLLYTEV DIGELLMLKL KWISDSYFSW 

       430        440        450        460        470 
SNWWSSPGFD IGKIRVKAGE TQKKVIFCSR EKMSYLQKGK SPVIFVKCHD KSLNRKSG 

« Hide

References

[1]"Cloning and sequencing of a full length cDNA encoding ovine lipoprotein lipase."
Edwards W.D., Daniels S.W., Page R.A., Volpe C.P., Kille P., Sweeney G.E., Cryer A.
Biochim. Biophys. Acta 1172:167-170(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Welsh Mountain/Dorset.
Tissue: Adipose tissue.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X68308 mRNA. Translation: CAA48384.1.
PIRS29846.
RefSeqNP_001009394.1. NM_001009394.1.
UniGeneOar.459.

3D structure databases

ProteinModelPortalQ29524.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSOART00000011666; ENSOARP00000011504; ENSOARG00000010719.
GeneID443408.

Organism-specific databases

CTD4023.

Phylogenomic databases

GeneTreeENSGT00750000117234.
HOVERGENHBG002259.

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_SHEEP
AccessionPrimary (citable) accession number: Q29524
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: July 9, 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