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Protein

Lipoprotein lipase

Gene

LPL

Organism
Felis catus (Cat) (Felis silvestris catus)
Status
Reviewed-Annotation score: Annotation score: 4 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 sitei162 – 1621NucleophileBy similarity
Active sitei186 – 1861Charge relay systemPROSITE-ProRule annotation
Active sitei271 – 2711Charge relay systemPROSITE-ProRule annotation

GO - Molecular functioni

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

GO - Biological processi

  1. lipid catabolic process Source: UniProtKB-KW
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
OrganismiFelis catus (Cat) (Felis silvestris catus)
Taxonomic identifieri9685 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraFeliformiaFelidaeFelinaeFelis
ProteomesiUP000011712: Unplaced

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

  1. anchored component of membrane Source: UniProtKB-KW
  2. chylomicron Source: UniProtKB-KW
  3. plasma membrane Source: UniProtKB-SubCell
  4. very-low-density lipoprotein particle Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Chylomicron, Membrane, Secreted, VLDL

Pathology & Biotechi

Involvement in diseasei

Defects in LPL are a cause of chylomicronemia syndrome, also known as type I hyperlipoproteinemia. Animals exhibit reduced body mass, growth rates, and increased stillbirth rates.

Keywords - Diseasei

Disease mutation, Hyperlipidemia

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Sequence AnalysisAdd
BLAST
Chaini24 – 478455Lipoprotein lipasePRO_0000017774Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi57 ↔ 70PROSITE-ProRule annotation
Glycosylationi73 – 731N-linked (GlcNAc...)Sequence Analysis
Modified residuei124 – 1241Nitrated tyrosineBy similarity
Modified residuei194 – 1941Nitrated tyrosineBy similarity
Disulfide bondi246 ↔ 269PROSITE-ProRule annotation
Disulfide bondi294 ↔ 313PROSITE-ProRule annotation
Disulfide bondi305 ↔ 308PROSITE-ProRule annotation
Modified residuei346 – 3461Nitrated tyrosineBy similarity
Glycosylationi389 – 3891N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi448 ↔ 468PROSITE-ProRule annotation

Post-translational modificationi

Tyrosine nitration after lipopolysaccharide (LPS) challenge down-regulates the lipase activity.By similarity

Keywords - PTMi

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

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi9685.ENSFCAP00000011284.

Structurei

3D structure databases

ProteinModelPortaliP55031.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini344 – 467124PLATPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni349 – 44496Heparin-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

eggNOGiNOG40923.
HOVERGENiHBG002259.
InParanoidiP55031.
KOiK01059.

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.

P55031-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MESKTLFLMA LGIWLQSLTT TRGWVAADDR ITGGRDFIDI ESKFALRTPE
60 70 80 90 100
DIAEDTCHLI PGVTESVANC HFNHTSKTFV VIHGWTVTGM YESWVPKLVA
110 120 130 140 150
APYKREPDSN VIVVDWLSRA QQHYPVSAGY TKLVGKDVAK FINWMAEEFH
160 170 180 190 200
YPLDNVHLLG YSLGAHAAGI AGSLTNKKVN RITGLDPAGP NFEYAEAPSR
210 220 230 240 250
LSPDDADFVD VLHTFTRGSP GRSIGIQKPV GHVDIYPNGG TFQPGCNIGE
260 270 280 290 300
AIRVIAERGL GDVDQLVKCS HERSIHLFID SLLNEENPSK AYRCNSKEAF
310 320 330 340 350
EKGLCLSCRK NRCNNLGYEI NKVRAKRSSK MYLKTRSQMP YKVFHYQVKI
360 370 380 390 400
HFSGTESDTQ TNQVFEISLY GTVAESENIP FTLPEISANK TYSFLIYTEV
410 420 430 440 450
DIGELLMLKL KWKSDSYFSW SDWWSSPGFT IEKIRVKAGE TQKKVIFCSR
460 470
EKVSHLQKGK ASVVFVKCHD KSLNKKSG
Length:478
Mass (Da):53,668
Last modified:October 1, 1996 - v1
Checksum:iF57014446127E8C9
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti435 – 4351R → G in chylomicronemia syndrome. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U42725 mRNA. Translation: AAB03848.1.
RefSeqiNP_001036032.1. NM_001042567.1.

Genome annotation databases

GeneIDi727696.
KEGGifca:727696.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U42725 mRNA. Translation: AAB03848.1.
RefSeqiNP_001036032.1. NM_001042567.1.

3D structure databases

ProteinModelPortaliP55031.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9685.ENSFCAP00000011284.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi727696.
KEGGifca:727696.

Organism-specific databases

CTDi4023.

Phylogenomic databases

eggNOGiNOG40923.
HOVERGENiHBG002259.
InParanoidiP55031.
KOiK01059.

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. "A mutation in the lipoprotein lipase gene is the molecular basis of chylomicronemia in a colony of domestic cats."
    Ginzinger D.G., Lewis M.E.S., Ma Y., Jones B.R., Liu G., Jones S.D.
    J. Clin. Invest. 97:1257-1266(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT CHYLOMICRONEMIA SYNDROME GLY-435.

Entry informationi

Entry nameiLIPL_FELCA
AccessioniPrimary (citable) accession number: P55031
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: January 7, 2015
This is version 98 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.