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P11151

- LIPL_BOVIN

UniProt

P11151 - LIPL_BOVIN

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Protein

Lipoprotein lipase

Gene
LPL
Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.

Catalytic activityi

Triacylglycerol + H2O = diacylglycerol + a carboxylate.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei162 – 1621Nucleophile By similarity
Active sitei186 – 1861Charge relay system By similarity
Active sitei271 – 2711Charge relay system By similarity

GO - Molecular functioni

  1. apolipoprotein binding Source: BHF-UCL
  2. heparin binding Source: UniProtKB-KW
  3. lipoprotein lipase activity Source: BHF-UCL
  4. phospholipase activity Source: BHF-UCL
  5. protein binding Source: IntAct
  6. triglyceride lipase activity Source: BHF-UCL

GO - Biological processi

  1. fatty acid biosynthetic process Source: BHF-UCL
  2. phospholipid metabolic process Source: BHF-UCL
  3. positive regulation of cholesterol storage Source: Ensembl
  4. positive regulation of macrophage derived foam cell differentiation Source: Ensembl
  5. positive regulation of sequestering of triglyceride Source: Ensembl
  6. triglyceride catabolic process Source: BHF-UCL
  7. triglyceride homeostasis Source: Ensembl
  8. triglyceride metabolic process Source: BHF-UCL
  9. very-low-density lipoprotein particle remodeling Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Keywords - Ligandi

Heparin-binding

Enzyme and pathway databases

BRENDAi3.1.1.34. 908.
ReactomeiREACT_204227. Retinoid metabolism and transport.
REACT_206940. Chylomicron-mediated lipid transport.
REACT_220799. Transcriptional regulation of white adipocyte differentiation.

Names & Taxonomyi

Protein namesi
Recommended name:
Lipoprotein lipase (EC:3.1.1.34)
Short name:
LPL
Gene namesi
Name:LPL
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136: Chromosome 8

Subcellular locationi

Cell membrane; Lipid-anchorGPI-anchor. Secreted
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.2 Publications

GO - Cellular componenti

  1. anchored component of membrane Source: UniProtKB-KW
  2. cell surface Source: Ensembl
  3. chylomicron Source: UniProtKB-KW
  4. plasma membrane Source: UniProtKB-SubCell
  5. very-low-density lipoprotein particle Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Chylomicron, Membrane, Secreted, VLDL

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 28282 PublicationsAdd
BLAST
Chaini29 – 478450Lipoprotein lipasePRO_0000017772Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi57 ↔ 701 Publication
Glycosylationi73 – 731N-linked (GlcNAc...)
Modified residuei124 – 1241Nitrated tyrosine By similarity
Modified residuei194 – 1941Nitrated tyrosine By similarity
Disulfide bondi246 ↔ 2691 Publication
Disulfide bondi294 ↔ 3131 Publication
Disulfide bondi305 ↔ 3081 Publication
Modified residuei346 – 3461Nitrated tyrosine By similarity
Glycosylationi389 – 3891N-linked (GlcNAc...)
Disulfide bondi448 ↔ 4681 Publication

Post-translational modificationi

Tyrosine nitration after lipopolysaccharide (LPS) challenge down-regulates the lipase activity By similarity.

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein, Nitration

Proteomic databases

PaxDbiP11151.
PRIDEiP11151.

Interactioni

Subunit structurei

Homodimer By similarity. Interacts with APOC2; the interaction activates LPL activity in the presence of lipids. Interacts with GPIHBP1 By similarity.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
SORT1Q995236EBI-8794090,EBI-1057058From a different organism.

Protein-protein interaction databases

BioGridi158237. 1 interaction.
IntActiP11151. 2 interactions.

Structurei

3D structure databases

ProteinModelPortaliP11151.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini344 – 467124PLATAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni349 – 44496Heparin-binding By similarityAdd
BLAST

Sequence similaritiesi

Contains 1 PLAT domain.

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG40923.
GeneTreeiENSGT00750000117234.
HOGENOMiHOG000038553.
HOVERGENiHBG002259.
InParanoidiP11151.
KOiK01059.
OMAiESVANCH.
OrthoDBiEOG757CX5.
TreeFamiTF324997.

Family and domain databases

Gene3Di2.60.60.20. 1 hit.
3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR000734. Lipase.
IPR008976. Lipase_LipOase.
IPR013818. Lipase_N.
IPR002330. Lipo_Lipase.
IPR016272. Lipoprotein_lipase_LIPH.
IPR001024. PLAT/LH2_dom.
[Graphical view]
PANTHERiPTHR11610. PTHR11610. 1 hit.
PTHR11610:SF3. PTHR11610:SF3. 1 hit.
PfamiPF00151. Lipase. 1 hit.
PF01477. PLAT. 1 hit.
[Graphical view]
PIRSFiPIRSF000865. Lipoprotein_lipase_LIPH. 1 hit.
PRINTSiPR00822. LIPOLIPASE.
PR00821. TAGLIPASE.
SMARTiSM00308. LH2. 1 hit.
[Graphical view]
SUPFAMiSSF49723. SSF49723. 1 hit.
SSF53474. SSF53474. 1 hit.
TIGRFAMsiTIGR03230. lipo_lipase. 1 hit.
PROSITEiPS00120. LIPASE_SER. 1 hit.
PS50095. PLAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P11151-1 [UniParc]FASTAAdd to Basket

« Hide

MESKALLLLA LSVCLQSLTV SRGGLVAADR ITGGKDFRDI ESKFALRTPE    50
DTAEDTCHLI PGVTESVANC HFNHSSKTFV VIHGWTVTGM YESWVPKLVA 100
ALYKREPDSN VIVVDWLSRA QQHYPVSAGY TKLVGQDVAK FMNWMADEFN 150
YPLGNVHLLG YSLGAHAAGI AGSLTNKKVN RITGLDPAGP NFEYAEAPSR 200
LSPDDADFVD VLHTFTRGSP GRSIGIQKPV GHVDIYPNGG TFQPGCNIGE 250
ALRVIAERGL GDVDQLVKCS HERSVHLFID SLLNEENPSK AYRCNSKEAF 300
EKGLCLSCRK NRCNNMGYEI NKVRAKRSSK MYLKTRSQMP YKVFHYQVKI 350
HFSGTESNTY TNQAFEISLY GTVAESENIP FTLPEVSTNK TYSFLLYTEV 400
DIGELLMLKL KWISDSYFSW SNWWSSPGFD IGKIRVKAGE TQKKVIFCSR 450
EKMSYLQKGK SPVIFVKCHD KSLNRKSG 478
Length:478
Mass (Da):53,378
Last modified:December 12, 2006 - v2
Checksum:i06FDD429DD194A1F
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BC118091 mRNA. Translation: AAI18092.1.
M16966 mRNA. Translation: AAA30624.1.
PIRiA27053.
RefSeqiNP_001068588.1. NM_001075120.1.
UniGeneiBt.5387.

Genome annotation databases

EnsembliENSBTAT00000017086; ENSBTAP00000017086; ENSBTAG00000012855.
GeneIDi280843.
KEGGibta:280843.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BC118091 mRNA. Translation: AAI18092.1 .
M16966 mRNA. Translation: AAA30624.1 .
PIRi A27053.
RefSeqi NP_001068588.1. NM_001075120.1.
UniGenei Bt.5387.

3D structure databases

ProteinModelPortali P11151.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 158237. 1 interaction.
IntActi P11151. 2 interactions.

Chemistry

ChEMBLi CHEMBL3064.

Proteomic databases

PaxDbi P11151.
PRIDEi P11151.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSBTAT00000017086 ; ENSBTAP00000017086 ; ENSBTAG00000012855 .
GeneIDi 280843.
KEGGi bta:280843.

Organism-specific databases

CTDi 4023.

Phylogenomic databases

eggNOGi NOG40923.
GeneTreei ENSGT00750000117234.
HOGENOMi HOG000038553.
HOVERGENi HBG002259.
InParanoidi P11151.
KOi K01059.
OMAi ESVANCH.
OrthoDBi EOG757CX5.
TreeFami TF324997.

Enzyme and pathway databases

BRENDAi 3.1.1.34. 908.
Reactomei REACT_204227. Retinoid metabolism and transport.
REACT_206940. Chylomicron-mediated lipid transport.
REACT_220799. Transcriptional regulation of white adipocyte differentiation.

Miscellaneous databases

NextBioi 20804991.

Family and domain databases

Gene3Di 2.60.60.20. 1 hit.
3.40.50.1820. 1 hit.
InterProi IPR029058. AB_hydrolase.
IPR000734. Lipase.
IPR008976. Lipase_LipOase.
IPR013818. Lipase_N.
IPR002330. Lipo_Lipase.
IPR016272. Lipoprotein_lipase_LIPH.
IPR001024. PLAT/LH2_dom.
[Graphical view ]
PANTHERi PTHR11610. PTHR11610. 1 hit.
PTHR11610:SF3. PTHR11610:SF3. 1 hit.
Pfami PF00151. Lipase. 1 hit.
PF01477. PLAT. 1 hit.
[Graphical view ]
PIRSFi PIRSF000865. Lipoprotein_lipase_LIPH. 1 hit.
PRINTSi PR00822. LIPOLIPASE.
PR00821. TAGLIPASE.
SMARTi SM00308. LH2. 1 hit.
[Graphical view ]
SUPFAMi SSF49723. SSF49723. 1 hit.
SSF53474. SSF53474. 1 hit.
TIGRFAMsi TIGR03230. lipo_lipase. 1 hit.
PROSITEi PS00120. LIPASE_SER. 1 hit.
PS50095. PLAT. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 29-478, DISULFIDE BONDS.
    Tissue: Mammary gland.
  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] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 29-55.
  5. "Metabolism of endothelial cell-bound lipoprotein lipase. Evidence for heparan sulfate proteoglycan-mediated internalization and recycling."
    Saxena U., Klein M.G., Goldberg I.J.
    J. Biol. Chem. 265:12880-12886(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: HEPARIN BINDING, SUBCELLULAR LOCATION.
  6. "Binding and intracellular trafficking of lipoprotein lipase and triacylglycerol-rich lipoproteins by liver cells."
    Casaroli-Marano R.P., Garcia R., Vilella E., Olivecrona G., Reina M., Vilaro S.
    J. Lipid Res. 39:789-806(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  7. "Apolipoprotein C-II39-62 activates lipoprotein lipase by direct lipid-independent binding."
    MacPhee C.E., Hatters D.M., Sawyer W.H., Howlett G.J.
    Biochemistry 39:3433-3440(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH APOC2, ENZYME ACTIVITY.

Entry informationi

Entry nameiLIPL_BOVIN
AccessioniPrimary (citable) accession number: P11151
Secondary accession number(s): Q17R03
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: December 12, 2006
Last modified: September 3, 2014
This is version 121 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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