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Reviewed, UniProtKB/Swiss-Prot Q29524 (LIPL_SHEEP)

Last modified February 9, 2010. Version 74. 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
OrganismOvis aries (Sheep)
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). 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.

Post-translational modification

Tyrosine nitrated in vivo after lipopolysaccharide (LPS) challenge, which down-regulates lipoprotein 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 Potential
Chain28 – 478451Lipoprotein lipase
PRO_0000017781

Regions

Domain344 – 467124PLAT
Region322 – 33413Heparin-binding Potential

Sites

Active site1621Nucleophile
Active site1861Charge relay system
Active site2711Charge relay system

Amino acid modifications

Modified residue1241Nitrated tyrosine By similarity
Modified residue1301Nitrated tyrosine By similarity
Modified residue3181Nitrated 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
Q29524-1 [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 

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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: 8439555] [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.
UniGeneOar.13297

3D structure databases

SMRQ29524. Positions 38-454.
ModBaseSearch...

Genome annotation databases

GeneID443408.

Organism-specific databases

CTD443408.

Phylogenomic databases

HOVERGENQ29524.

Enzyme and pathway databases

BRENDA3.1.1.34. 271.

Family and domain databases

InterProIPR000734. Lipase.
IPR008976. Lipase_LipOase.
IPR013818. Lipase_N.
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_SHEEP
AccessionPrimary (citable) accession number: Q29524
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: February 9, 2010
This is version 74 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