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Protein

Lipoprotein lipase

Gene

LPL

Organism
Neovison vison (American mink) (Mustela vison)
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.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

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Keywords - Ligandi

Heparin-binding

Protein family/group databases

ESTHERimusvi-lipli. Lipoprotein_Lipase.

Names & Taxonomyi

Protein namesi
Recommended name:
Lipoprotein lipase (EC:3.1.1.34)
Short name:
LPL
Gene namesi
Name:LPL
OrganismiNeovison vison (American mink) (Mustela vison)
Taxonomic identifieri452646 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaMustelidaeMustelinaeNeovison

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

Involvement in diseasei

Defects in LPL are a cause of chylomicronemia syndrome, also known as type I hyperlipoproteinemia.

Keywords - Diseasei

Disease mutation, Hyperlipidemia

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 27By similarityAdd BLAST27
ChainiPRO_000001777728 – 475Lipoprotein lipaseAdd BLAST448

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi54 ↔ 67PROSITE-ProRule annotation
Glycosylationi70N-linked (GlcNAc...)Sequence analysis1
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
Glycosylationi386N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi445 ↔ 465PROSITE-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 (By similarity). Interacts with GPIHBP1. Interacts with LMF1 and SEL1L (By similarity).By similarity

Structurei

3D structure databases

ProteinModelPortaliO46647.
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-bindingBy similarityAdd BLAST96

Sequence similaritiesi

Belongs to the AB hydrolase superfamily. Lipase family.Curated
Contains 1 PLAT domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

HOVERGENiHBG002259.

Family and domain databases

CDDicd00707. Pancreat_lipase_like. 1 hit.
Gene3Di2.60.60.20. 1 hit.
3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR013818. Lipase/vitellogenin.
IPR016272. Lipase_LIPH.
IPR033906. 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.

O46647-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MESKALLLVA LGMWFQSLTA TRGGVAAADR GGDFIDIESK FALRTPEDTA
60 70 80 90 100
EDTCHLIPGV TESVANCHFN HSSKTFVVIH GWTVTGMYES WVPKLVAALY
110 120 130 140 150
KREPDSNVIV VDWLSRAQQH YPVSAGYTKL VGKDVAKFIN WMAEEFHYPL
160 170 180 190 200
DNVHLLGYSL GAHAAGIAGS LTNKKVNRIT GLDPAGPNFE YAEAPSRLSP
210 220 230 240 250
DDADFVDVLH TFTRGSPGRS IGIQKPVGHV DIYPNGGTFQ PGCNIGEAIR
260 270 280 290 300
VIAERGLGDV DQLVKCSHER SIHLFIDSLL NEENPSKAYR CNSKEAFEKG
310 320 330 340 350
LCLSCRKNRC NNLGYEINKV RAKRSSKMYL KTRSQMPYKV FHYQVKIHFS
360 370 380 390 400
GTESDTQTNQ AFEISLYGTV AESENIPFTL PEVSANKTYS FLIYTEVDIG
410 420 430 440 450
ELLMLKLKWK SDSYFSWSDW WSSPGFAIEK IRVKAGETQK KVIFCSREKV
460 470
SHLQKGKASV VFVKCHDKSL NKKSG
Length:475
Mass (Da):52,968
Last modified:June 1, 1998 - v1
Checksum:i2F2DBF0090F0FB7C
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti241P → L in chylomicronemia syndrome; no lipase activity. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ223493 Genomic DNA. Translation: CAA11411.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ223493 Genomic DNA. Translation: CAA11411.1.

3D structure databases

ProteinModelPortaliO46647.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

ESTHERimusvi-lipli. Lipoprotein_Lipase.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG002259.

Family and domain databases

CDDicd00707. Pancreat_lipase_like. 1 hit.
Gene3Di2.60.60.20. 1 hit.
3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR013818. Lipase/vitellogenin.
IPR016272. Lipase_LIPH.
IPR033906. 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...

Entry informationi

Entry nameiLIPL_NEOVI
AccessioniPrimary (citable) accession number: O46647
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: June 1, 1998
Last modified: November 30, 2016
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

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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 one 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.