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Protein

Lipoprotein lipase

Gene

Lpl

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: 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.By similarity

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

  • heparin binding Source: UniProtKB
  • lipoprotein lipase activity Source: CACAO
  • triglyceride binding Source: RGD

GO - Biological processi

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.
ReactomeiR-RNO-174800. Chylomicron-mediated lipid transport.
R-RNO-975634. Retinoid metabolism and transport.

Protein family/group databases

ESTHERiratno-lipli. Lipoprotein_Lipase.

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
Proteomesi
  • UP000002494 Componenti: 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

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Chylomicron, Membrane, Secreted, VLDL

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL5906.

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

BgeeiENSRNOG00000012181.
GenevisibleiQ06000. RN.

Interactioni

Subunit structurei

Homodimer (By similarity). Interacts with APOC2; the interaction activates LPL activity in the presence of lipids (By similarity). Interacts with GPIHBP1. Interacts with LMF1 and SEL1L (By similarity).By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000016543.

Chemistry

BindingDBiQ06000.

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

eggNOGiENOG410IJUA. Eukaryota.
ENOG4111GMM. LUCA.
GeneTreeiENSGT00760000119069.
HOGENOMiHOG000038553.
HOVERGENiHBG002259.
InParanoidiQ06000.
KOiK01059.
OMAiESVANCH.
OrthoDBiEOG091G052B.
PhylomeDBiQ06000.
TreeFamiTF324997.

Family and domain databases

Gene3Di2.60.60.20. 1 hit.
3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR016272. Lipase_LIPH.
IPR013818. Lipase_N.
IPR002330. Lipo_Lipase.
IPR001024. PLAT/LH2_dom.
IPR000734. TAG_lipase.
[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.
PIRiJH0790.
RefSeqiNP_036730.1. NM_012598.2.
UniGeneiRn.3834.

3D structure databases

ProteinModelPortaliQ06000.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000016543.

Chemistry

BindingDBiQ06000.
ChEMBLiCHEMBL5906.

Protein family/group databases

ESTHERiratno-lipli. Lipoprotein_Lipase.

Proteomic databases

PaxDbiQ06000.
PRIDEiQ06000.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi4023.
RGDi3017. Lpl.

Phylogenomic databases

eggNOGiENOG410IJUA. Eukaryota.
ENOG4111GMM. LUCA.
GeneTreeiENSGT00760000119069.
HOGENOMiHOG000038553.
HOVERGENiHBG002259.
InParanoidiQ06000.
KOiK01059.
OMAiESVANCH.
OrthoDBiEOG091G052B.
PhylomeDBiQ06000.
TreeFamiTF324997.

Enzyme and pathway databases

BRENDAi3.1.1.34. 5301.
ReactomeiR-RNO-174800. Chylomicron-mediated lipid transport.
R-RNO-975634. Retinoid metabolism and transport.

Miscellaneous databases

PROiQ06000.

Gene expression databases

BgeeiENSRNOG00000012181.
GenevisibleiQ06000. RN.

Family and domain databases

Gene3Di2.60.60.20. 1 hit.
3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR016272. Lipase_LIPH.
IPR013818. Lipase_N.
IPR002330. Lipo_Lipase.
IPR001024. PLAT/LH2_dom.
IPR000734. TAG_lipase.
[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]
ProtoNetiSearch...

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: September 7, 2016
This is version 137 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.