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Q06000

- LIPL_RAT

UniProt

Q06000 - LIPL_RAT

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Protein

Lipoprotein lipase

Gene

Lpl

Organism
Rattus norvegicus (Rat)
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 (By similarity).By similarity

Catalytic activityi

Triacylglycerol + H2O = diacylglycerol + a carboxylate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei159 – 1591NucleophileBy similarity
Active sitei183 – 1831Charge relay systemPROSITE-ProRule annotation
Active sitei268 – 2681Charge relay systemPROSITE-ProRule annotation

GO - Molecular functioni

  1. heparin binding Source: UniProtKB-KW
  2. lipoprotein lipase activity Source: RGD
  3. triglyceride binding Source: RGD

GO - Biological processi

  1. lipid catabolic process Source: RGD
  2. positive regulation of cholesterol storage Source: Ensembl
  3. positive regulation of macrophage derived foam cell differentiation Source: Ensembl
  4. positive regulation of sequestering of triglyceride Source: Ensembl
  5. response to cold Source: RGD
  6. response to drug Source: RGD
  7. triglyceride biosynthetic process Source: RGD
  8. triglyceride catabolic process Source: Ensembl
  9. triglyceride homeostasis Source: Ensembl
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. 5301.
ReactomeiREACT_199015. Retinoid metabolism and transport.
REACT_250929. Chylomicron-mediated lipid transport.
REACT_260360. 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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 16

Organism-specific databases

RGDi3017. Lpl.

Subcellular locationi

Cell membrane By similarity; Lipid-anchorGPI-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).By similarity

GO - Cellular componenti

  1. anchored component of membrane Source: UniProtKB-KW
  2. cell surface Source: Ensembl
  3. chylomicron Source: UniProtKB-KW
  4. extracellular matrix Source: RGD
  5. extracellular vesicular exosome Source: Ensembl
  6. plasma membrane Source: UniProtKB-KW
  7. 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 – 2727By similarityAdd
BLAST
Chaini28 – 474447Lipoprotein lipasePRO_0000017779Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi54 ↔ 67PROSITE-ProRule annotation
Glycosylationi70 – 701N-linked (GlcNAc...)Sequence Analysis
Modified residuei121 – 1211Nitrated tyrosine1 Publication
Modified residuei191 – 1911Nitrated tyrosine1 Publication
Disulfide bondi243 ↔ 266PROSITE-ProRule annotation
Disulfide bondi291 ↔ 310PROSITE-ProRule annotation
Disulfide bondi302 ↔ 305PROSITE-ProRule annotation
Modified residuei343 – 3431Nitrated tyrosine1 Publication
Glycosylationi386 – 3861N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi445 ↔ 465PROSITE-ProRule annotation

Post-translational modificationi

Tyrosine nitration after lipopolysaccharide (LPS) challenge down-regulates the lipase activity.1 Publication

Keywords - PTMi

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

Proteomic databases

PaxDbiQ06000.
PRIDEiQ06000.

Expressioni

Inductioni

Induced by insulin. Inhibited by isoproterenol.1 Publication

Gene expression databases

GenevestigatoriQ06000.

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

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000016543.

Structurei

3D structure databases

ProteinModelPortaliQ06000.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini341 – 464124PLATPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni346 – 44196Heparin-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.
InParanoidiQ06000.
KOiK01059.
OMAiESVANCH.
OrthoDBiEOG757CX5.
PhylomeDBiQ06000.
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.

Q06000-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MESKALLLVA LGVWLQSLTA FRGGVAAADG GRDFSDIESK FALRTPEDTA
60 70 80 90 100
EDTCHLIPGL ADSVSNCHFN HSSKTFVVIH GWTVTGMYES WVPKLVAALY
110 120 130 140 150
KREPDSNVIV VDWLYRAQQH YPVSAGYTKL VGNDVARFIN WLEEEFNYPL
160 170 180 190 200
DNVHLLGYSL GAHAAGVAGS LTNKKVNRIT GLDPAGPNFE YAEAPSRLSP
210 220 230 240 250
DDADFVDVLH TFTRGSPGRS IGIQKPVGHV DIYPNGGTFQ PGCNIGEAIR
260 270 280 290 300
VIAEKGLGDV DQLVKCSHER SIHLFIDSLL NEENPSKAYR CNSKEAFEKG
310 320 330 340 350
LCLSCRKNRC NNVGYEINKV RAKRSSKMYL KTRSQMPYKV FHYQVKIHFS
360 370 380 390 400
GTENDKQNNQ AFEISLYGTV AESENIPFTL PEVATNKTYS FLIYTEVDIG
410 420 430 440 450
ELLMMKLKWK NDSYFRWSDW WSSPSFVIEK IRVKAGETQK KVIFCAREKV
460 470
SHLQKGKDAA VFVKCHDKSL KKSG
Length:474
Mass (Da):53,082
Last modified:February 1, 1994 - v1
Checksum:iF4F6F4BCCA4F1626
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti336 – 3361M → V no nucleotide entry (PubMed:2233752)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L03294 mRNA. Translation: AAA41534.1.
BC081836 mRNA. Translation: AAH81836.1.
PIRiJH0790.
RefSeqiNP_036730.1. NM_012598.2.
UniGeneiRn.3834.

Genome annotation databases

EnsembliENSRNOT00000016543; ENSRNOP00000016543; ENSRNOG00000012181.
GeneIDi24539.
KEGGirno:24539.
UCSCiRGD:3017. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L03294 mRNA. Translation: AAA41534.1 .
BC081836 mRNA. Translation: AAH81836.1 .
PIRi JH0790.
RefSeqi NP_036730.1. NM_012598.2.
UniGenei Rn.3834.

3D structure databases

ProteinModelPortali Q06000.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10116.ENSRNOP00000016543.

Chemistry

BindingDBi Q06000.
ChEMBLi CHEMBL5906.

Proteomic databases

PaxDbi Q06000.
PRIDEi Q06000.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000016543 ; ENSRNOP00000016543 ; ENSRNOG00000012181 .
GeneIDi 24539.
KEGGi rno:24539.
UCSCi RGD:3017. rat.

Organism-specific databases

CTDi 4023.
RGDi 3017. Lpl.

Phylogenomic databases

eggNOGi NOG40923.
GeneTreei ENSGT00760000119069.
HOGENOMi HOG000038553.
HOVERGENi HBG002259.
InParanoidi Q06000.
KOi K01059.
OMAi ESVANCH.
OrthoDBi EOG757CX5.
PhylomeDBi Q06000.
TreeFami TF324997.

Enzyme and pathway databases

BRENDAi 3.1.1.34. 5301.
Reactomei REACT_199015. Retinoid metabolism and transport.
REACT_250929. Chylomicron-mediated lipid transport.
REACT_260360. Transcriptional regulation of white adipocyte differentiation.

Miscellaneous databases

NextBioi 603620.
PROi Q06000.

Gene expression databases

Genevestigatori Q06000.

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. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Testis.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Kidney.
  3. "Lipoprotein lipase gene expression in rat adipocytes is regulated by isoproterenol and insulin through different mechanisms."
    Raynolds M.V., Awald P.D., Gordon D.F., Gutierrez-Hartmann A., Rule D.C., Wood W.M., Eckel R.H.
    Mol. Endocrinol. 4:1416-1422(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 336-474, INDUCTION.
    Tissue: Heart.
  4. "Lipoprotein lipase is nitrated in vivo after lipopolysaccharide challenge."
    Casanovas A., Carrascal M., Abian J., Lopez-Tejero M.D., Llobera M.
    Free Radic. Biol. Med. 47:1553-1560(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NITRATION AT TYR-121; TYR-191 AND TYR-343, IDENTIFICATION BY MASS SPECTROMETRY.
  5. "Discovery of lipoprotein lipase pI isoforms and contributions to their characterization."
    Casanovas A., Carrascal M., Abian J., Lopez-Tejero M.D., Llobera M.
    J. Proteomics 72:1031-1039(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, GLYCOSYLATION.

Entry informationi

Entry nameiLIPL_RAT
AccessioniPrimary (citable) accession number: Q06000
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: November 26, 2014
This is version 126 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3