Skip Header

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

Lipoprotein lipase

Gene

LPL

Organism
Gallus gallus (Chicken)
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.

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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Keywords - Ligandi

Heparin-binding

Protein family/group databases

ESTHERichick-lipli. Lipoprotein_Lipase.

Names & Taxonomyi

Protein namesi
Recommended name:
Lipoprotein lipase (EC:3.1.1.34)
Short name:
LPL
Gene namesi
Name:LPL
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
ProteomesiUP000000539 Componenti: Chromosome Z

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

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi306 – 3061R → Q: Some loss of heparin-binding ability; when associated with Q-307 and Q-309. 1 Publication
Mutagenesisi307 – 3071K → Q: Some loss of heparin-binding ability; when associated with Q-306 and Q-309. 1 Publication
Mutagenesisi309 – 3091R → Q: Some loss of heparin-binding ability; when associated with Q-306 and Q-307. 1 Publication
Mutagenesisi346 – 3461K → N: Reduced heparin-binding ability and some decrease in specific enzymatic activity. 1 Publication
Mutagenesisi430 – 4301R → 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 Publication
Mutagenesisi432 – 4321R → 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 Publication
Mutagenesisi434 – 4341K → 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 Publication
Mutagenesisi440 – 4401K → 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 Publication
Mutagenesisi441 – 4411K → 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 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2525Add
BLAST
Chaini26 – 490465Lipoprotein lipase1 PublicationPRO_0000017782Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi54 ↔ 67PROSITE-ProRule annotation
Glycosylationi70 – 701N-linked (GlcNAc...) (complex)1 Publication
Modified residuei121 – 1211Nitrated tyrosineBy similarity
Modified residuei191 – 1911Nitrated tyrosineBy similarity
Disulfide bondi243 ↔ 266PROSITE-ProRule annotation
Disulfide bondi291 ↔ 310PROSITE-ProRule annotation
Disulfide bondi302 ↔ 305PROSITE-ProRule annotation
Modified residuei343 – 3431Nitrated tyrosineBy similarity
Glycosylationi354 – 3541N-linked (GlcNAc...)1 Publication
Glycosylationi386 – 3861N-linked (GlcNAc...)1 Publication
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.
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.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi9031.ENSGALP00000036979.

Structurei

3D structure databases

ProteinModelPortaliP11602.
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-bindingAdd
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.
InParanoidiP11602.
KOiK01059.
OMAiESVANCH.
PhylomeDBiP11602.

Family and domain databases

Gene3Di2.60.60.20. 1 hit.
3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR016272. Lipase_LIPH.
IPR008976. Lipase_LipOase.
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.

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti377 – 3771P → A in CAA43037 (PubMed:1730055).Curated

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.

Cross-referencesi

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.

3D structure databases

ProteinModelPortaliP11602.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9031.ENSGALP00000036979.

Protein family/group databases

ESTHERichick-lipli. Lipoprotein_Lipase.

Proteomic databases

PaxDbiP11602.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSGALT00000037774; ENSGALP00000036979; ENSGALG00000015425.
GeneIDi396219.
KEGGigga:396219.

Organism-specific databases

CTDi4023.

Phylogenomic databases

eggNOGiNOG40923.
GeneTreeiENSGT00760000119069.
HOGENOMiHOG000038553.
HOVERGENiHBG002259.
InParanoidiP11602.
KOiK01059.
OMAiESVANCH.
PhylomeDBiP11602.

Miscellaneous databases

NextBioi20816271.
PROiP11602.

Family and domain databases

Gene3Di2.60.60.20. 1 hit.
3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR016272. Lipase_LIPH.
IPR008976. Lipase_LipOase.
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...

Publicationsi

  1. "Avian adipose lipoprotein lipase: cDNA sequence and reciprocal regulation of mRNA levels in adipose and heart."
    Cooper D.A., Stein J.C., Strieleman P.J., Bensadoun A.
    Biochim. Biophys. Acta 1008:92-101(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: White leghorn.
    Tissue: Adipose tissue.
  2. "The structure and complete nucleotide sequence of the avian lipoprotein lipase gene."
    Cooper D.A., Lu S.C., Viswanath R., Freiman R.N., Bensadoun A.
    Biochim. Biophys. Acta 1129:166-171(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: White leghorn.
  3. "Occurrence of sulfate in an asparagine-linked complex oligosaccharide of chicken adipose lipoprotein lipase."
    Hoogewerf A.J., Bensadoun A.
    J. Biol. Chem. 266:1048-1057(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT ASN-70; ASN-354 AND ASN-386, STRUCTURE OF CARBOHYDRATES.
  4. "Identification of a heparin-binding domain in the distal carboxyl-terminal region of lipoprotein lipase by site-directed mutagenesis."
    Sendak R.A., Bensadoun A.
    J. Lipid Res. 39:1310-1315(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: HEPARIN-BINDING DOMAIN, MUTAGENESIS OF ARG-306; LYS-307; ARG-309; LYS-346; ARG-430; ARG-432; LYS-434; LYS-440 AND LYS-441.

Entry informationi

Entry nameiLIPL_CHICK
AccessioniPrimary (citable) accession number: P11602
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: July 22, 2015
This is version 125 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

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 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.