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P49923 (LIPL_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 91. 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
OrganismSus scrofa (Pig) [Reference proteome]
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

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-anchor › GPI-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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727 By similarity
Chain28 – 478451Lipoprotein lipase
PRO_0000017780

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

Sequences

Sequence LengthMass (Da)Tools
P49923 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: D0500324117261E3

FASTA47853,455
        10         20         30         40         50         60 
MESKALLLVA LSVWLQSLIV SREGLATADR ISGGRDFTDI ESKFALRTPE DTVEDTCHLI 

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

       130        140        150        160        170        180 
QQHYPISAGY TKLVGQDVAT FIDWMAVEFS YPPNNVHLLG YSLGAHAAGI AGSLTKKKVN 

       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 MYLKTRAQMP YKVFHYQVKM RFSGTESDTH 

       370        380        390        400        410        420 
TNQAFEISLY GTVAESENIP FTLPEVSTNK TYSFLIYTEV DIGELLMLKL KWVSDSYFSW 

       430        440        450        460        470 
SNWWSSPGFA IEKIRVKAGE TQKKVIFCSR EKKSHLQKGK SSVVFVKCHD KSLNRKSG

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References

[1]"Isolation and sequencing of porcine lipoprotein lipase cDNA and its use in multiallelic restriction fragment length polymorphism detection."
Harbitz I., Kristensen T., Kran S., Davies W.
Anim. Genet. 23:517-522(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Norwegian Landrace.
Tissue: Skeletal muscle.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X62984 mRNA. Translation: CAA44725.1.
PIRS18158. I47146.
RefSeqNP_999451.1. NM_214286.1.
UniGeneSsc.95883.

3D structure databases

ProteinModelPortalP49923.
ModBaseSearch...

Proteomic databases

PaxDbP49923.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID397537.
KEGGssc:397537.

Organism-specific databases

CTD4023.

Phylogenomic databases

eggNOGNOG40923.
HOGENOMHOG000038553.
HOVERGENHBG002259.
KOK01059.
OrthoDBEOG480HWP.

Family and domain databases

Gene3D2.60.60.20. 1 hit.
InterProIPR000734. Lipase.
IPR008976. Lipase_LipOase.
IPR013818. Lipase_N.
IPR002330. Lipo_Lipase.
IPR001024. LipOase_LH2.
IPR016272. Lipoprotein_lipase_LIPH.
[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. Lipase_LipOase. 1 hit.
TIGRFAMsTIGR03230. lipo_lipase. 1 hit.
PROSITEPS00120. LIPASE_SER. 1 hit.
PS50095. PLAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameLIPL_PIG
AccessionPrimary (citable) accession number: P49923
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: April 3, 2013
This is version 91 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

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