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P11602 (LIPL_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Lipoprotein lipase

Short name=LPL
EC=3.1.1.34
Gene names
Name:LPL
OrganismGallus gallus (Chicken) [Reference proteome]
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus

Protein attributes

Sequence length490 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

Triacylglycerol + H2O = diacylglycerol + a carboxylate.

Subunit structure

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

Subcellular location

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.

Post-translational modification

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.

Sequence similarities

Belongs to the AB hydrolase superfamily. Lipase family.

Contains 1 PLAT domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525
Chain26 – 490465Lipoprotein lipase Ref.1
PRO_0000017782

Regions

Domain341 – 464124PLAT
Region346 – 44196Heparin-binding

Sites

Active site1591Nucleophile By similarity
Active site1831Charge relay system By similarity
Active site2681Charge relay system By similarity

Amino acid modifications

Modified residue1211Nitrated tyrosine By similarity
Modified residue1911Nitrated tyrosine By similarity
Modified residue3431Nitrated tyrosine By similarity
Glycosylation701N-linked (GlcNAc...) (complex) Ref.3
Glycosylation3541N-linked (GlcNAc...) Ref.3
Glycosylation3861N-linked (GlcNAc...) Ref.3
Disulfide bond54 ↔ 67 By similarity
Disulfide bond243 ↔ 266 By similarity
Disulfide bond291 ↔ 310 By similarity
Disulfide bond302 ↔ 305 By similarity
Disulfide bond445 ↔ 465 By similarity

Experimental info

Mutagenesis3061R → Q: Some loss of heparin-binding ability; when associated with Q-307 and Q-309. Ref.4
Mutagenesis3071K → Q: Some loss of heparin-binding ability; when associated with Q-306 and Q-309. Ref.4
Mutagenesis3091R → Q: Some loss of heparin-binding ability; when associated with Q-306 and Q-307. Ref.4
Mutagenesis3461K → N: Reduced heparin-binding ability and some decrease in specific enzymatic activity. Ref.4
Mutagenesis4301R → 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. Ref.4
Mutagenesis4321R → 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. Ref.4
Mutagenesis4341K → 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. Ref.4
Mutagenesis4401K → 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. Ref.4
Mutagenesis4411K → 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. Ref.4
Sequence conflict3771P → A in CAA43037. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P11602 [UniParc].

Last modified October 1, 1989. Version 1.
Checksum: C014D23363E81FF3

FASTA49055,132
        10         20         30         40         50         60 
MERGRGMGKT ALLAVLCLCL RGAAGSDPEA EMNFEGIESK FSLRTPAEPD EDVCYLVPGQ 

        70         80         90        100        110        120 
MDSLAQCNFN HTSKTFVVIH GWTVTGMYES WVPKLVDALY KREPDSNVIV VDWLVRAQQH 

       130        140        150        160        170        180 
YPVSAAYTKL VGKDVAMFID WMEEKFNYPL NNVHLLGYSL GAHAAGIAGS LTKKKVNRIT 

       190        200        210        220        230        240 
GLDPAGPTFE YADAPIRLSP DDADFVDVLH TYTRGSPDRS IGIQKPVGHI DIYPNGGGFQ 

       250        260        270        280        290        300 
PGCNLGEALR LIAEKGFSDV DQLVKCSHER SIHLFIDSLL YEEKPSMAYR CNTKEAFEKG 

       310        320        330        340        350        360 
LCLSCRKNRC NNLGYKVNRV RTKRNTKMYL KTRAQMPYKV FHYQVKIHFF GKTNVTKVDQ 

       370        380        390        400        410        420 
PFLISLYGTL DESENIPFTL PEVSSNKTFS FLIYTEVDIG DLLMLKLQWE KDTFFSWSDW 

       430        440        450        460        470        480 
WTPFAFTIQR VRVKSGETQK KVVFCSRDGS SRLGKGEEAA IFVKCLEQPV SRKRGGAKKA 

       490 
SKENSAHESA 

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References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X14670 mRNA. Translation: CAA32800.1.
X60547 Genomic DNA. Translation: CAA43037.1.
PIRS04331.
RefSeqNP_990613.1. NM_205282.1.
UniGeneGga.1152.

3D structure databases

ProteinModelPortalP11602.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9031.ENSGALP00000036979.

Proteomic databases

PaxDbP11602.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSGALT00000037774; ENSGALP00000036979; ENSGALG00000015425.
GeneID396219.
KEGGgga:396219.

Organism-specific databases

CTD4023.

Phylogenomic databases

eggNOGNOG40923.
GeneTreeENSGT00750000117234.
HOGENOMHOG000038553.
HOVERGENHBG002259.
InParanoidP11602.
KOK01059.
PhylomeDBP11602.

Family and domain databases

Gene3D2.60.60.20. 1 hit.
3.40.50.1820. 1 hit.
InterProIPR029058. AB_hydrolase.
IPR000734. Lipase.
IPR008976. Lipase_LipOase.
IPR013818. Lipase_N.
IPR002330. Lipo_Lipase.
IPR016272. Lipoprotein_lipase_LIPH.
IPR001024. PLAT/LH2_dom.
[Graphical view]
PANTHERPTHR11610. PTHR11610. 1 hit.
PTHR11610:SF3. PTHR11610:SF3. 1 hit.
PfamPF00151. Lipase. 1 hit.
PF01477. PLAT. 1 hit.
[Graphical view]
PIRSFPIRSF000865. Lipoprotein_lipase_LIPH. 1 hit.
PRINTSPR00822. LIPOLIPASE.
PR00821. TAGLIPASE.
SMARTSM00308. LH2. 1 hit.
[Graphical view]
SUPFAMSSF49723. SSF49723. 1 hit.
SSF53474. SSF53474. 1 hit.
TIGRFAMsTIGR03230. lipo_lipase. 1 hit.
PROSITEPS00120. LIPASE_SER. 1 hit.
PS50095. PLAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20816271.
PROP11602.

Entry information

Entry nameLIPL_CHICK
AccessionPrimary (citable) accession number: P11602
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: June 11, 2014
This is version 116 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families