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P11602

- LIPL_CHICK

UniProt

P11602 - LIPL_CHICK

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Protein

Lipoprotein lipase

Gene
LPL
Organism
Gallus gallus (Chicken)
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.

Catalytic activityi

Triacylglycerol + H2O = diacylglycerol + a carboxylate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei159 – 1591Nucleophile By similarity
Active sitei183 – 1831Charge relay system By similarity
Active sitei268 – 2681Charge relay system By similarity

GO - Molecular functioni

  1. heparin binding Source: UniProtKB-KW
  2. lipoprotein lipase activity Source: UniProtKB-EC

GO - Biological processi

  1. positive regulation of cholesterol storage Source: Ensembl
  2. positive regulation of macrophage derived foam cell differentiation Source: Ensembl
  3. positive regulation of sequestering of triglyceride Source: Ensembl
  4. triglyceride catabolic process Source: Ensembl
  5. triglyceride homeostasis Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Keywords - Ligandi

Heparin-binding

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus
ProteomesiUP000000539: 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.

GO - Cellular componenti

  1. anchored component of membrane Source: UniProtKB-KW
  2. cell surface Source: Ensembl
  3. chylomicron Source: UniProtKB-KW
  4. plasma membrane Source: UniProtKB-SubCell
  5. very-low-density lipoprotein particle Source: UniProtKB-KW
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 ↔ 67 By similarity
Glycosylationi70 – 701N-linked (GlcNAc...) (complex)1 Publication
Modified residuei121 – 1211Nitrated tyrosine By similarity
Modified residuei191 – 1911Nitrated tyrosine By similarity
Disulfide bondi243 ↔ 266 By similarity
Disulfide bondi291 ↔ 310 By similarity
Disulfide bondi302 ↔ 305 By similarity
Modified residuei343 – 3431Nitrated tyrosine By similarity
Glycosylationi354 – 3541N-linked (GlcNAc...)1 Publication
Glycosylationi386 – 3861N-linked (GlcNAc...)1 Publication
Disulfide bondi445 ↔ 465 By similarity

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 By similarity. 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.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini341 – 464124PLATAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni346 – 44196Heparin-bindingAdd
BLAST

Sequence similaritiesi

Contains 1 PLAT domain.

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG40923.
GeneTreeiENSGT00750000117234.
HOGENOMiHOG000038553.
HOVERGENiHBG002259.
InParanoidiP11602.
KOiK01059.
PhylomeDBiP11602.

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.

P11602-1 [UniParc]FASTAAdd to Basket

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MERGRGMGKT ALLAVLCLCL RGAAGSDPEA EMNFEGIESK FSLRTPAEPD    50
EDVCYLVPGQ MDSLAQCNFN HTSKTFVVIH GWTVTGMYES WVPKLVDALY 100
KREPDSNVIV VDWLVRAQQH YPVSAAYTKL VGKDVAMFID WMEEKFNYPL 150
NNVHLLGYSL GAHAAGIAGS LTKKKVNRIT GLDPAGPTFE YADAPIRLSP 200
DDADFVDVLH TYTRGSPDRS IGIQKPVGHI DIYPNGGGFQ PGCNLGEALR 250
LIAEKGFSDV DQLVKCSHER SIHLFIDSLL YEEKPSMAYR CNTKEAFEKG 300
LCLSCRKNRC NNLGYKVNRV RTKRNTKMYL KTRAQMPYKV FHYQVKIHFF 350
GKTNVTKVDQ PFLISLYGTL DESENIPFTL PEVSSNKTFS FLIYTEVDIG 400
DLLMLKLQWE KDTFFSWSDW WTPFAFTIQR VRVKSGETQK KVVFCSRDGS 450
SRLGKGEEAA IFVKCLEQPV SRKRGGAKKA SKENSAHESA 490
Length:490
Mass (Da):55,132
Last modified:October 1, 1989 - v1
Checksum:iC014D23363E81FF3
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti377 – 3771P → A in CAA43037. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
X14670 mRNA. Translation: CAA32800.1 .
X60547 Genomic DNA. Translation: CAA43037.1 .
PIRi S04331.
RefSeqi NP_990613.1. NM_205282.1.
UniGenei Gga.1152.

3D structure databases

ProteinModelPortali P11602.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9031.ENSGALP00000036979.

Proteomic databases

PaxDbi P11602.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSGALT00000037774 ; ENSGALP00000036979 ; ENSGALG00000015425 .
GeneIDi 396219.
KEGGi gga:396219.

Organism-specific databases

CTDi 4023.

Phylogenomic databases

eggNOGi NOG40923.
GeneTreei ENSGT00750000117234.
HOGENOMi HOG000038553.
HOVERGENi HBG002259.
InParanoidi P11602.
KOi K01059.
PhylomeDBi P11602.

Miscellaneous databases

NextBioi 20816271.
PROi P11602.

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

  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: June 11, 2014
This is version 116 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

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