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Reviewed, UniProtKB/Swiss-Prot P11151 (LIPL_BOVIN)

Last modified November 3, 2009. Version 87. 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

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Names and origin

Protein namesRecommended name:
    Lipoprotein lipase
      Short name=LPL
    EC=3.1.1.34
Gene names
Name: LPL
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

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Protein attributes

Sequence length478 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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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-anchor › GPI-anchor.

Sequence similarities

Belongs to the AB hydrolase superfamily. Lipase family.

Contains 1 PLAT domain.

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Ontologies

Keywords
   Biological processLipid degradation
   Cellular componentCell membrane
Chylomicron
Membrane
VLDL
   DomainSignal
   LigandHeparin-binding
   Molecular functionHydrolase
   PTMDisulfide bond
GPI-anchor
Glycoprotein
Lipoprotein
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processfatty acid biosynthetic process

Inferred from direct assay. Source: UniProtKB

phospholipid metabolic process

Inferred from direct assay. Source: UniProtKB

triglyceride catabolic process

Inferred from direct assay. Source: UniProtKB

very-low-density lipoprotein particle remodeling

Inferred from direct assay. Source: UniProtKB

   Cellular componentanchored to membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

chylomicron

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-KW

very-low-density lipoprotein particle

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionapolipoprotein binding

Inferred from physical interaction. Source: UniProtKB

heparin binding

Inferred from electronic annotation. Source: UniProtKB-KW

lipoprotein lipase activity

Inferred from direct assay. Source: UniProtKB

phospholipase activity

Inferred from direct assay. Source: UniProtKB

phospholipid binding

Inferred by curator. Source: UniProtKB

triglyceride binding

Inferred by curator. Source: UniProtKB

triglyceride lipase activity

Inferred from direct assay. Source: UniProtKB

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2828 Ref.3 Ref.4
Chain29 – 478450Lipoprotein lipase
PRO_0000017772

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...)
Glycosylation3891N-linked (GlcNAc...)
Disulfide bond57 ↔ 70 Ref.3
Disulfide bond246 ↔ 269 Ref.3
Disulfide bond294 ↔ 313 Ref.3
Disulfide bond305 ↔ 308 Ref.3
Disulfide bond448 ↔ 468 Ref.3

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Sequences

Sequence LengthMass (Da)Tools
P11151-1 [UniParc].

Last modified December 12, 2006. Version 2.
Checksum: 06FDD429DD194A1F

FASTA47853,378
        10         20         30         40         50         60 
MESKALLLLA LSVCLQSLTV SRGGLVAADR ITGGKDFRDI 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

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References

« Hide 'large scale' references
[1]NIH - Mammalian Gene Collection (MGC) project
Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Hereford.
Tissue: Uterus.
[2]"Molecular cloning and sequence of a cDNA coding for bovine lipoprotein lipase."
Senda M., Oka K., Brown W.V., Qasba P.K., Furuichi Y.
Proc. Natl. Acad. Sci. U.S.A. 84:4369-4373(1987) [PubMed: 2885834] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 29-478.
[3]"Structure of bovine milk lipoprotein lipase."
Yang C.-Y., Gu Z.-W., Yang H.-X., Rohde M.F., Gotto A.M. Jr., Pownall H.J.
J. Biol. Chem. 264:16822-16827(1989) [PubMed: 2674142] [Abstract]
Cited for: PROTEIN SEQUENCE OF 29-478, DISULFIDE BONDS.
[4]"Lipoprotein lipases from cow, guinea-pig and man. Structural characterization and identification of protease-sensitive internal regions."
Bengtsson-Olivecrona G., Olivecrona T., Joernvall H.
Eur. J. Biochem. 161:281-288(1986) [PubMed: 3536511] [Abstract]
Cited for: PROTEIN SEQUENCE OF 29-55.

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Cross-references

Sequence databases

BC118091 mRNA. Translation: AAI18092.1.
M16966 mRNA. Translation: AAA30624.1.
IPIIPI00692291.
PIRA27053.
RefSeqNP_001068588.1.
UniGeneBt.5387

3D structure databases

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

Protein-protein interaction databases

STRINGP11151.

Genome annotation databases

EnsemblENSBTAT00000017086; ENSBTAP00000017086; ENSBTAG00000012855; Bos taurus. [Genome view]
GeneID280843.
KEGGbta:280843.

Organism-specific databases

CTD280843.

Phylogenomic databases

HOVERGENP11151.
OMATVTGMYE.

Enzyme and pathway databases

BRENDA3.1.1.34. 251.

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]
Gene3DG3DSA:2.60.60.20. Lipase_LipOase. 1 hit.
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...

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Entry information

Entry nameLIPL_BOVIN
AccessionPrimary (citable) accession number: P11151
Secondary accession number(s): Q17R03
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: December 12, 2006
Last modified: November 3, 2009
This is version 87 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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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