Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P11151

- LIPL_BOVIN

UniProt

P11151 - LIPL_BOVIN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

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 – 1621NucleophileBy similarity
Active sitei186 – 1861Charge relay systemPROSITE-ProRule annotation
Active sitei271 – 2711Charge relay systemPROSITE-ProRule annotation

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. 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.

GO - Cellular componenti

  1. anchored component of membrane Source: UniProtKB-KW
  2. cell surface Source: Ensembl
  3. chylomicron Source: UniProtKB-KW
  4. extracellular vesicular exosome Source: Ensembl
  5. plasma membrane Source: UniProtKB-KW
  6. 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 PublicationPROSITE-ProRule annotation
Glycosylationi73 – 731N-linked (GlcNAc...)
Modified residuei124 – 1241Nitrated tyrosineBy similarity
Modified residuei194 – 1941Nitrated tyrosineBy similarity
Disulfide bondi246 ↔ 2691 PublicationPROSITE-ProRule annotation
Disulfide bondi294 ↔ 3131 PublicationPROSITE-ProRule annotation
Disulfide bondi305 ↔ 3081 PublicationPROSITE-ProRule annotation
Modified residuei346 – 3461Nitrated tyrosineBy similarity
Glycosylationi389 – 3891N-linked (GlcNAc...)
Disulfide bondi448 ↔ 4681 PublicationPROSITE-ProRule annotation

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).By similarity

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.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini344 – 467124PLATPROSITE-ProRule annotationAdd
BLAST

Region

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

Sequence similaritiesi

Belongs to the AB hydrolase superfamily. Lipase family.Curated
Contains 1 PLAT domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG40923.
GeneTreeiENSGT00760000119069.
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

        10         20         30         40         50
MESKALLLLA LSVCLQSLTV SRGGLVAADR ITGGKDFRDI ESKFALRTPE
60 70 80 90 100
DTAEDTCHLI PGVTESVANC HFNHSSKTFV VIHGWTVTGM YESWVPKLVA
110 120 130 140 150
ALYKREPDSN VIVVDWLSRA QQHYPVSAGY TKLVGQDVAK FMNWMADEFN
160 170 180 190 200
YPLGNVHLLG YSLGAHAAGI AGSLTNKKVN RITGLDPAGP NFEYAEAPSR
210 220 230 240 250
LSPDDADFVD VLHTFTRGSP GRSIGIQKPV GHVDIYPNGG TFQPGCNIGE
260 270 280 290 300
ALRVIAERGL GDVDQLVKCS HERSVHLFID SLLNEENPSK AYRCNSKEAF
310 320 330 340 350
EKGLCLSCRK NRCNNMGYEI NKVRAKRSSK MYLKTRSQMP YKVFHYQVKI
360 370 380 390 400
HFSGTESNTY TNQAFEISLY GTVAESENIP FTLPEVSTNK TYSFLLYTEV
410 420 430 440 450
DIGELLMLKL KWISDSYFSW SNWWSSPGFD IGKIRVKAGE TQKKVIFCSR
460 470
EKMSYLQKGK SPVIFVKCHD KSLNRKSG
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 ENSGT00760000119069.
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: October 29, 2014
This is version 123 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