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Protein

Lipoprotein lipase

Gene

LPL

Organism
Gallus gallus (Chicken)
Status
Reviewed-Annotation score: -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

Catalytic activityi

Triacylglycerol + H2O = diacylglycerol + a carboxylate.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei159NucleophileBy similarity1
Active sitei183Charge relay systemPROSITE-ProRule annotation1
Active sitei268Charge relay systemPROSITE-ProRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHeparin-binding, Hydrolase
Biological processLipid degradation, Lipid metabolism

Enzyme and pathway databases

ReactomeiR-GGA-8963889 Assembly of active LPL and LIPC lipase complexes

Protein family/group databases

ESTHERichick-lipli Lipoprotein_Lipase

Names & Taxonomyi

Protein namesi
Recommended name:
Lipoprotein lipase (EC:3.1.1.34By similarity)
Short name:
LPL
Gene namesi
Name:LPL
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
Proteomesi
  • UP000000539 Componenti: Chromosome Z

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Chylomicron, Membrane, Secreted, VLDL

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi306R → Q: Some loss of heparin-binding ability; when associated with Q-307 and Q-309. 1 Publication1
Mutagenesisi307K → Q: Some loss of heparin-binding ability; when associated with Q-306 and Q-309. 1 Publication1
Mutagenesisi309R → Q: Some loss of heparin-binding ability; when associated with Q-306 and Q-307. 1 Publication1
Mutagenesisi346K → N: Reduced heparin-binding ability and some decrease in specific enzymatic activity. 1 Publication1
Mutagenesisi430R → N: Reduced heparin-binding ability and some reduction in specific enzymatic activity. Almost complete loss of heparin binding and greatly reduced specific enzymatic activity; when associated with N-432 and N-434. 1 Publication1
Mutagenesisi432R → N: Reduced heparin-binding ability. Almost complete loss of heparin binding and greatly reduced specific enzymatic activity; when associated with N-430 and N-434. 1 Publication1
Mutagenesisi434K → N: Reduced heparin-binding ability. Almost complete loss of heparin binding and greatly reduced specific enzymatic activity; when associated with N-430 and N-432. 1 Publication1
Mutagenesisi440K → N: No change in heparin-binding activity nor in specific enzymatic activity. Reduced heparin-binding activity and decreased specific enzymatic activity; when associated with N-441. 1 Publication1
Mutagenesisi441K → N: Reduced heparin-binding activity and decreased specific enzymatic activity. No further reduction of heparin-binding nor of specific enzymatic activity; when associated with N-440. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 25Add BLAST25
ChainiPRO_000001778226 – 490Lipoprotein lipase1 PublicationAdd BLAST465

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi54 ↔ 67PROSITE-ProRule annotation
Glycosylationi70N-linked (GlcNAc...) (complex) asparagine1 Publication1
Modified residuei121Nitrated tyrosineBy similarity1
Modified residuei191Nitrated tyrosineBy similarity1
Disulfide bondi243 ↔ 266PROSITE-ProRule annotation
Disulfide bondi291 ↔ 310PROSITE-ProRule annotation
Disulfide bondi302 ↔ 305PROSITE-ProRule annotation
Modified residuei343Nitrated tyrosineBy similarity1
Glycosylationi354N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi386N-linked (GlcNAc...) asparagine1 Publication1
Disulfide bondi445 ↔ 465PROSITE-ProRule annotation

Post-translational modificationi

N-glycan at Asn-70 is a triantennary complex oligosaccharide containing sialic acid, galactose, mannose, and N-acetylglucosamine, the reducing GlcNAc being sulfated at C6.1 Publication
Tyrosine nitration after lipopolysaccharide (LPS) challenge down-regulates the lipase activity.By similarity

Keywords - PTMi

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

Proteomic databases

PaxDbiP11602

PTM databases

iPTMnetiP11602

Expressioni

Gene expression databases

BgeeiENSGALG00000015425

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

GO - Molecular functioni

Protein-protein interaction databases

STRINGi9031.ENSGALP00000036979

Structurei

3D structure databases

ProteinModelPortaliP11602
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini341 – 464PLATPROSITE-ProRule annotationAdd BLAST124

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni346 – 441Heparin-bindingAdd BLAST96

Sequence similaritiesi

Belongs to the AB hydrolase superfamily. Lipase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IJUA Eukaryota
ENOG4111GMM LUCA
GeneTreeiENSGT00760000119069
HOGENOMiHOG000038553
HOVERGENiHBG002259
InParanoidiP11602
KOiK01059
OMAiHYQVKIH
OrthoDBiEOG091G052B
PhylomeDBiP11602

Family and domain databases

CDDicd00707 Pancreat_lipase_like, 1 hit
Gene3Di3.40.50.1820, 1 hit
InterProiView protein in InterPro
IPR029058 AB_hydrolase
IPR013818 Lipase/vitellogenin
IPR016272 Lipase_LIPH
IPR033906 Lipase_N
IPR002330 Lipo_Lipase
IPR001024 PLAT/LH2_dom
IPR036392 PLAT/LH2_dom_sf
IPR000734 TAG_lipase
PANTHERiPTHR11610 PTHR11610, 1 hit
PTHR11610:SF3 PTHR11610:SF3, 1 hit
PfamiView protein in Pfam
PF00151 Lipase, 1 hit
PF01477 PLAT, 1 hit
PIRSFiPIRSF000865 Lipoprotein_lipase_LIPH, 1 hit
PRINTSiPR00822 LIPOLIPASE
PR00821 TAGLIPASE
SMARTiView protein in SMART
SM00308 LH2, 1 hit
SUPFAMiSSF49723 SSF49723, 1 hit
SSF53474 SSF53474, 1 hit
TIGRFAMsiTIGR03230 lipo_lipase, 1 hit
PROSITEiView protein in PROSITE
PS00120 LIPASE_SER, 1 hit
PS50095 PLAT, 1 hit

Sequencei

Sequence statusi: Complete.

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

P11602-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MERGRGMGKT ALLAVLCLCL RGAAGSDPEA EMNFEGIESK FSLRTPAEPD
60 70 80 90 100
EDVCYLVPGQ MDSLAQCNFN HTSKTFVVIH GWTVTGMYES WVPKLVDALY
110 120 130 140 150
KREPDSNVIV VDWLVRAQQH YPVSAAYTKL VGKDVAMFID WMEEKFNYPL
160 170 180 190 200
NNVHLLGYSL GAHAAGIAGS LTKKKVNRIT GLDPAGPTFE YADAPIRLSP
210 220 230 240 250
DDADFVDVLH TYTRGSPDRS IGIQKPVGHI DIYPNGGGFQ PGCNLGEALR
260 270 280 290 300
LIAEKGFSDV DQLVKCSHER SIHLFIDSLL YEEKPSMAYR CNTKEAFEKG
310 320 330 340 350
LCLSCRKNRC NNLGYKVNRV RTKRNTKMYL KTRAQMPYKV FHYQVKIHFF
360 370 380 390 400
GKTNVTKVDQ PFLISLYGTL DESENIPFTL PEVSSNKTFS FLIYTEVDIG
410 420 430 440 450
DLLMLKLQWE KDTFFSWSDW WTPFAFTIQR VRVKSGETQK KVVFCSRDGS
460 470 480 490
SRLGKGEEAA IFVKCLEQPV SRKRGGAKKA SKENSAHESA
Length:490
Mass (Da):55,132
Last modified:October 1, 1989 - v1
Checksum:iC014D23363E81FF3
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti377P → A in CAA43037 (PubMed:1730055).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X14670 mRNA Translation: CAA32800.1
X60547 Genomic DNA Translation: CAA43037.1
PIRiS04331
RefSeqiNP_990613.1, NM_205282.1
UniGeneiGga.1152

Genome annotation databases

EnsembliENSGALT00000037774; ENSGALP00000036979; ENSGALG00000015425
GeneIDi396219
KEGGigga:396219

Similar proteinsi

Entry informationi

Entry nameiLIPL_CHICK
AccessioniPrimary (citable) accession number: P11602
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: May 23, 2018
This is version 142 of the entry and version 1 of the sequence. See 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

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