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Protein

Lipoprotein lipase

Gene

LPL

Organism
Homo sapiens (Human)
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 similarity1 Publication

Catalytic activityi

Triacylglycerol + H2O = diacylglycerol + a carboxylate.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei159Nucleophile1
Active sitei183Charge relay system1
Active sitei268Charge relay system1

GO - Molecular functioni

  • apolipoprotein binding Source: BHF-UCL
  • heparin binding Source: UniProtKB
  • lipoprotein lipase activity Source: UniProtKB
  • phospholipase activity Source: BHF-UCL
  • receptor binding Source: BHF-UCL
  • triglyceride binding Source: Ensembl
  • triglyceride lipase activity Source: BHF-UCL

GO - Biological processi

  • cholesterol homeostasis Source: BHF-UCL
  • chylomicron remodeling Source: BHF-UCL
  • fatty acid biosynthetic process Source: BHF-UCL
  • lipoprotein metabolic process Source: Reactome
  • phospholipid metabolic process Source: BHF-UCL
  • positive regulation of chemokine secretion Source: BHF-UCL
  • positive regulation of cholesterol storage Source: BHF-UCL
  • positive regulation of inflammatory response Source: BHF-UCL
  • positive regulation of macrophage derived foam cell differentiation Source: BHF-UCL
  • positive regulation of sequestering of triglyceride Source: BHF-UCL
  • response to cold Source: Ensembl
  • response to drug Source: Ensembl
  • response to glucose Source: AgBase
  • retinoid metabolic process Source: Reactome
  • triglyceride biosynthetic process Source: Ensembl
  • triglyceride catabolic process Source: UniProtKB
  • triglyceride homeostasis Source: BHF-UCL
  • triglyceride metabolic process Source: BHF-UCL
  • very-low-density lipoprotein particle remodeling Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Keywords - Ligandi

Heparin-binding

Enzyme and pathway databases

BioCyciZFISH:HS10931-MONOMER.
BRENDAi3.1.1.34. 2681.
ReactomeiR-HSA-174800. Chylomicron-mediated lipid transport.
R-HSA-381340. Transcriptional regulation of white adipocyte differentiation.
R-HSA-975634. Retinoid metabolism and transport.

Protein family/group databases

ESTHERihuman-LPL. Lipoprotein_Lipase.

Chemistry databases

SwissLipidsiSLP:000000568.

Names & Taxonomyi

Protein namesi
Recommended name:
Lipoprotein lipase (EC:3.1.1.341 Publication)
Short name:
LPL
Gene namesi
Name:LPL
Synonyms:LIPD
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 8

Organism-specific databases

HGNCiHGNC:6677. LPL.

Subcellular locationi

  • Cell membrane By similarity; Lipid-anchorGPI-anchor By similarity
  • Secreted 1 Publication

  • 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

Lipoprotein lipase deficiency (LPL deficiency)54 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionRecessive disorder usually manifesting in childhood. On a normal diet, patients often present with abdominal pain, hepatosplenomegaly, lipemia retinalis, eruptive xanthomata, and massive hypertriglyceridemia, sometimes complicated with acute pancreatitis.
See also OMIM:238600
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01194836D → N in LPL deficiency; has approximately 80% of the specific activity of wild-type enzyme. 4 PublicationsCorresponds to variant rs1801177dbSNPEnsembl.1
Natural variantiVAR_05791470N → S in LPL deficiency; produces an inactive protein which is not secreted into the media. 2 Publications1
Natural variantiVAR_05791596V → L in LPL deficiency; gives rise to a 80% decrease in specific catalytic activity. 1 PublicationCorresponds to variant rs373088068dbSNPEnsembl.1
Natural variantiVAR_05791698A → T in LPL deficiency; decreases the specific activity of the enzyme; reduces the secretion of the mutant protein significantly; the total LPL mass is reduced compared to that of the wild-type construct. 1 PublicationCorresponds to variant rs145657341dbSNPEnsembl.1
Natural variantiVAR_004211102R → S in LPL deficiency. 1 PublicationCorresponds to variant rs118204073dbSNPEnsembl.1
Natural variantiVAR_004212113W → G in LPL deficiency. 1
Natural variantiVAR_004213113W → R in LPL deficiency. 2 PublicationsCorresponds to variant rs118204069dbSNPEnsembl.1
Natural variantiVAR_057917128T → A in LPL deficiency. 2 Publications1
Natural variantiVAR_057918132G → R in LPL deficiency; synthesized as a catalytically inactive form. 2 Publications1
Natural variantiVAR_004214163H → R in LPL deficiency. 1 Publication1
Natural variantiVAR_004215169G → E in LPL deficiency; loss of activity. 1 PublicationCorresponds to variant rs118204063dbSNPEnsembl.1
Natural variantiVAR_004216181G → S in LPL deficiency. 1 Publication1
Natural variantiVAR_057919181G → V in LPL deficiency; synthesized as a catalytically inactive form. 2 Publications1
Natural variantiVAR_004217183D → G in LPL deficiency; lacks both triolein and tributyrin esterase activities. 3 PublicationsCorresponds to variant rs118204064dbSNPEnsembl.1
Natural variantiVAR_057920183D → H in LPL deficiency. 1 PublicationCorresponds to variant rs781614031dbSNPEnsembl.1
Natural variantiVAR_004218183D → N in LPL deficiency; lacks both triolein and tributyrin esterase activities. 2 Publications1
Natural variantiVAR_004219184P → R in LPL deficiency; Nijmegen; loss of activity. 1 Publication1
Natural variantiVAR_004220185A → T in LPL deficiency; 3.2% of activity. Corresponds to variant rs748349562dbSNPEnsembl.1
Natural variantiVAR_057921186G → E in LPL deficiency. 1 Publication1
Natural variantiVAR_057922190E → G in LPL deficiency. 1 Publication1
Natural variantiVAR_004221199S → C in LPL deficiency; mild hypertriglyceridemia; partial activity. 2 PublicationsCorresponds to variant rs118204072dbSNPEnsembl.1
Natural variantiVAR_057923201D → V in LPL deficiency. 1 Publication1
Natural variantiVAR_004222203A → T in LPL deficiency; Bethesda; loss of activity and abnormal heparin binding. 1 PublicationCorresponds to variant rs118204056dbSNPEnsembl.1
Natural variantiVAR_004223207D → E in LPL deficiency. 1 PublicationCorresponds to variant rs118204076dbSNPEnsembl.1
Natural variantiVAR_057924208V → I in LPL deficiency; decreases the specific activity of the enzyme; has a mild effect on the secretion of the mutant enzyme; the total LPL mass is reduced compared to that of the wild-type construct. 1 PublicationCorresponds to variant rs568397156dbSNPEnsembl.1
Natural variantiVAR_057925210H → D in LPL deficiency; complete loss of enzyme activity. 1 Publication1
Natural variantiVAR_004224210H → Q in LPL deficiency; loss of activity. 1
Natural variantiVAR_004225215G → E in LPL deficiency; loss of activity. 12 PublicationsCorresponds to variant rs118204057dbSNPEnsembl.1
Natural variantiVAR_057926215G → R in LPL deficiency. 2 Publications1
Natural variantiVAR_004226220S → R in LPL deficiency; 2.0% of activity. Corresponds to variant rs757546424dbSNPEnsembl.1
Natural variantiVAR_004227221I → T in LPL deficiency; loss of activity. 5 PublicationsCorresponds to variant rs118204061dbSNPEnsembl.1
Natural variantiVAR_004228222G → E in LPL deficiency. 1 PublicationCorresponds to variant rs118204075dbSNPEnsembl.1
Natural variantiVAR_057927225K → R in LPL deficiency. 1 Publication1
Natural variantiVAR_057928227V → A in LPL deficiency. 1 PublicationCorresponds to variant rs528243561dbSNPEnsembl.1
Natural variantiVAR_004229231D → E in LPL deficiency; loss of activity. 3 PublicationsCorresponds to variant rs118204067dbSNPEnsembl.1
Natural variantiVAR_004230232I → S in LPL deficiency. 1 PublicationCorresponds to variant rs770601263dbSNPEnsembl.1
Natural variantiVAR_004231234P → L in LPL deficiency; loss of activity. 2 PublicationsCorresponds to variant rs118204060dbSNPEnsembl.1
Natural variantiVAR_004232243C → S in LPL deficiency; loss of activity. 1 Publication1
Natural variantiVAR_057929252I → T in LPL deficiency. 1 PublicationCorresponds to variant rs118204080dbSNPEnsembl.1
Natural variantiVAR_057930266C → W in LPL deficiency. 1 PublicationCorresponds to variant rs118204082dbSNPEnsembl.1
Natural variantiVAR_057931270R → C in LPL deficiency. 4 PublicationsCorresponds to variant rs118204077dbSNPEnsembl.1
Natural variantiVAR_004233270R → H in LPL deficiency; loss of activity. 6 PublicationsCorresponds to variant rs118204062dbSNPEnsembl.1
Natural variantiVAR_004234271S → T in LPL deficiency. 1 PublicationCorresponds to variant rs28934893dbSNPEnsembl.1
Natural variantiVAR_004235277D → N in LPL deficiency; 5% of full activity. 5 PublicationsCorresponds to variant rs118204068dbSNPEnsembl.1
Natural variantiVAR_004236278S → C in LPL deficiency. 1
Natural variantiVAR_057932279L → R in LPL deficiency; decreases the specific activity of the enzyme; the total LPL mass is reduced compared to that of the wild-type construct. 2 PublicationsCorresponds to variant rs35414700dbSNPEnsembl.1
Natural variantiVAR_057933279L → V in LPL deficiency; decreases the specific activity of the enzyme; the total LPL mass is reduced compared to that of the wild-type construct. 1 PublicationCorresponds to variant rs371282890dbSNPEnsembl.1
Natural variantiVAR_004237286S → G in LPL deficiency. 1 Publication1
Natural variantiVAR_004238286S → R in LPL deficiency. 1 Publication1
Natural variantiVAR_011949288A → T in LPL deficiency; the LPL mass level is approximately 67% of the normal; the activity is 32% of the nornal. 3 PublicationsCorresponds to variant rs1800011dbSNPEnsembl.1
Natural variantiVAR_057934289Y → H in LPL deficiency; no enzyme activity. 1 Publication1
Natural variantiVAR_057935297F → L in LPL deficiency and hyperlipidemia; synthesized as a catalytically inactive form; total amount is almost equal to that of the normal enzyme; non-releasable by heparin due to the abnormal structure of the mutant protein. 2 Publications1
Natural variantiVAR_057936303L → F in LPL deficiency; approximately 6% of normal LPL activity and 40% of LPL mass are detected in the patient's postheparin plasma; results in the production of a functionally inactive enzyme. 1 Publication1
Natural variantiVAR_057937305C → R in LPL deficiency. 1 PublicationCorresponds to variant rs773235712dbSNPEnsembl.1
Natural variantiVAR_057938310C → Y in LPL deficiency; decreases the specific activity of the enzyme; reduces the secretion of the mutant protein significantly; the total LPL mass is reduced compared to that of the wild-type construct. 1 Publication1
Natural variantiVAR_057939313L → P in LPL deficiency. 1 Publication1
Natural variantiVAR_004239318N → S in LPL deficiency; loss of activity; frequent mutation. 8 PublicationsCorresponds to variant rs268dbSNPEnsembl.1
Natural variantiVAR_057940325S → R in LPL deficiency; has no effect on the specific activity of the enzyme; has a mild effect on the secretion of the mutant enzyme; the total LPL mass is reduced compared to that of the wild-type construct. 1 PublicationCorresponds to variant rs761265900dbSNPEnsembl.1
Natural variantiVAR_057941328M → R in LPL deficiency. 1 Publication1
Natural variantiVAR_004240328M → T in LPL deficiency. 1
Natural variantiVAR_057942330L → F in LPL deficiency. 1 Publication1
Natural variantiVAR_004241330L → P in LPL deficiency. 1
Natural variantiVAR_004242361A → T in LPL deficiency. 2 PublicationsCorresponds to variant rs118204071dbSNPEnsembl.1
Natural variantiVAR_057943365S → F in LPL deficiency; increases the specific activity of the enzyme; has a mild effect on the secretion of the mutant enzyme; the total LPL mass is reduced compared to that of the wild-type construct. 1 PublicationCorresponds to variant rs546542623dbSNPEnsembl.1
Natural variantiVAR_004243392L → V in LPL deficiency; loss of activity. 1 PublicationCorresponds to variant rs118204078dbSNPEnsembl.1
Natural variantiVAR_004244423 – 424Missing in LPL deficiency; affects the protein folding. 2
Natural variantiVAR_004245437E → K in LPL deficiency. 1 Publication1
Natural variantiVAR_004246437E → V in LPL deficiency. 1 Publication1
Natural variantiVAR_057944445C → Y in LPL deficiency; has 48% of normal activity in vitro; decreased levels of activity account for by the lower protein mass levels of the mutants rather than by decreased enzymatic activities. 1 PublicationCorresponds to variant rs118204079dbSNPEnsembl.1
Natural variantiVAR_057945448E → K in LPL deficiency; results in a moderate reduction in catalytic activity. 1 PublicationCorresponds to variant rs149089920dbSNPEnsembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi159S → G: Lacks both triolein and tributyrin esterase activities. 1 Publication1
Mutagenesisi159S → T: Lacks both triolein and tributyrin esterase activities. 1 Publication1
Mutagenesisi268H → G: Lacks both triolein and tributyrin esterase activities. 1 Publication1
Mutagenesisi268H → Q: Lacks both triolein and tributyrin esterase activities. 1 Publication1

Keywords - Diseasei

Disease mutation, Hyperlipidemia

Organism-specific databases

DisGeNETi4023.
MalaCardsiLPL.
MIMi238600. phenotype.
OpenTargetsiENSG00000175445.
Orphaneti309015. Familial lipoprotein lipase deficiency.
70470. Hyperlipoproteinemia type 5.
PharmGKBiPA232.

Chemistry databases

ChEMBLiCHEMBL2060.
DrugBankiDB05269. AST-120.
DB06439. Tyloxapol.

Polymorphism and mutation databases

BioMutaiLPL.
DMDMi126314.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 271 PublicationAdd BLAST27
ChainiPRO_000001777528 – 475Lipoprotein lipaseAdd BLAST448

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi54 ↔ 67PROSITE-ProRule annotation
Glycosylationi70N-linked (GlcNAc...)1 Publication1
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

Proteomic databases

EPDiP06858.
MaxQBiP06858.
PaxDbiP06858.
PeptideAtlasiP06858.
PRIDEiP06858.

PTM databases

iPTMnetiP06858.
PhosphoSitePlusiP06858.

Expressioni

Gene expression databases

BgeeiENSG00000175445.
CleanExiHS_LPL.
ExpressionAtlasiP06858. baseline and differential.
GenevisibleiP06858. HS.

Organism-specific databases

HPAiHPA048749.

Interactioni

Subunit structurei

Homodimer (By similarity). Interacts with APOC2; the interaction activates LPL activity in the presence of lipids (By similarity). Interacts with GPIHBP1 (PubMed:17997385). Interacts with SEL1L and LMF1 (PubMed:25066055).By similarity2 Publications

GO - Molecular functioni

  • apolipoprotein binding Source: BHF-UCL
  • receptor binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi110205. 18 interactors.
IntActiP06858. 14 interactors.
MINTiMINT-1369348.
STRINGi9606.ENSP00000309757.

Chemistry databases

BindingDBiP06858.

Structurei

3D structure databases

ProteinModelPortaliP06858.
SMRiP06858.
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

eggNOGiENOG410IJUA. Eukaryota.
ENOG4111GMM. LUCA.
GeneTreeiENSGT00760000119069.
HOGENOMiHOG000038553.
HOVERGENiHBG002259.
InParanoidiP06858.
KOiK01059.
OMAiESVANCH.
OrthoDBiEOG091G052B.
PhylomeDBiP06858.
TreeFamiTF324997.

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.

P06858-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MESKALLVLT LAVWLQSLTA SRGGVAAADQ RRDFIDIESK FALRTPEDTA
60 70 80 90 100
EDTCHLIPGV AESVATCHFN HSSKTFMVIH GWTVTGMYES WVPKLVAALY
110 120 130 140 150
KREPDSNVIV VDWLSRAQEH YPVSAGYTKL VGQDVARFIN WMEEEFNYPL
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 CSSKEAFEKG
310 320 330 340 350
LCLSCRKNRC NNLGYEINKV RAKRSSKMYL KTRSQMPYKV FHYQVKIHFS
360 370 380 390 400
GTESETHTNQ AFEISLYGTV AESENIPFTL PEVSTNKTYS FLIYTEVDIG
410 420 430 440 450
ELLMLKLKWK SDSYFSWSDW WSSPGFAIQK IRVKAGETQK KVIFCSREKV
460 470
SHLQKGKAPA VFVKCHDKSL NKKSG
Length:475
Mass (Da):53,162
Last modified:January 1, 1988 - v1
Checksum:iFBD00FCD334FB8AA
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01194836D → N in LPL deficiency; has approximately 80% of the specific activity of wild-type enzyme. 4 PublicationsCorresponds to variant rs1801177dbSNPEnsembl.1
Natural variantiVAR_05791470N → S in LPL deficiency; produces an inactive protein which is not secreted into the media. 2 Publications1
Natural variantiVAR_04981971H → Q.Corresponds to variant rs11542065dbSNPEnsembl.1
Natural variantiVAR_05791596V → L in LPL deficiency; gives rise to a 80% decrease in specific catalytic activity. 1 PublicationCorresponds to variant rs373088068dbSNPEnsembl.1
Natural variantiVAR_05791698A → T in LPL deficiency; decreases the specific activity of the enzyme; reduces the secretion of the mutant protein significantly; the total LPL mass is reduced compared to that of the wild-type construct. 1 PublicationCorresponds to variant rs145657341dbSNPEnsembl.1
Natural variantiVAR_004211102R → S in LPL deficiency. 1 PublicationCorresponds to variant rs118204073dbSNPEnsembl.1
Natural variantiVAR_004212113W → G in LPL deficiency. 1
Natural variantiVAR_004213113W → R in LPL deficiency. 2 PublicationsCorresponds to variant rs118204069dbSNPEnsembl.1
Natural variantiVAR_057917128T → A in LPL deficiency. 2 Publications1
Natural variantiVAR_057918132G → R in LPL deficiency; synthesized as a catalytically inactive form. 2 Publications1
Natural variantiVAR_004214163H → R in LPL deficiency. 1 Publication1
Natural variantiVAR_004215169G → E in LPL deficiency; loss of activity. 1 PublicationCorresponds to variant rs118204063dbSNPEnsembl.1
Natural variantiVAR_004216181G → S in LPL deficiency. 1 Publication1
Natural variantiVAR_057919181G → V in LPL deficiency; synthesized as a catalytically inactive form. 2 Publications1
Natural variantiVAR_004217183D → G in LPL deficiency; lacks both triolein and tributyrin esterase activities. 3 PublicationsCorresponds to variant rs118204064dbSNPEnsembl.1
Natural variantiVAR_057920183D → H in LPL deficiency. 1 PublicationCorresponds to variant rs781614031dbSNPEnsembl.1
Natural variantiVAR_004218183D → N in LPL deficiency; lacks both triolein and tributyrin esterase activities. 2 Publications1
Natural variantiVAR_004219184P → R in LPL deficiency; Nijmegen; loss of activity. 1 Publication1
Natural variantiVAR_004220185A → T in LPL deficiency; 3.2% of activity. Corresponds to variant rs748349562dbSNPEnsembl.1
Natural variantiVAR_057921186G → E in LPL deficiency. 1 Publication1
Natural variantiVAR_057922190E → G in LPL deficiency. 1 Publication1
Natural variantiVAR_004221199S → C in LPL deficiency; mild hypertriglyceridemia; partial activity. 2 PublicationsCorresponds to variant rs118204072dbSNPEnsembl.1
Natural variantiVAR_057923201D → V in LPL deficiency. 1 Publication1
Natural variantiVAR_004222203A → T in LPL deficiency; Bethesda; loss of activity and abnormal heparin binding. 1 PublicationCorresponds to variant rs118204056dbSNPEnsembl.1
Natural variantiVAR_004223207D → E in LPL deficiency. 1 PublicationCorresponds to variant rs118204076dbSNPEnsembl.1
Natural variantiVAR_057924208V → I in LPL deficiency; decreases the specific activity of the enzyme; has a mild effect on the secretion of the mutant enzyme; the total LPL mass is reduced compared to that of the wild-type construct. 1 PublicationCorresponds to variant rs568397156dbSNPEnsembl.1
Natural variantiVAR_057925210H → D in LPL deficiency; complete loss of enzyme activity. 1 Publication1
Natural variantiVAR_004224210H → Q in LPL deficiency; loss of activity. 1
Natural variantiVAR_004225215G → E in LPL deficiency; loss of activity. 12 PublicationsCorresponds to variant rs118204057dbSNPEnsembl.1
Natural variantiVAR_057926215G → R in LPL deficiency. 2 Publications1
Natural variantiVAR_004226220S → R in LPL deficiency; 2.0% of activity. Corresponds to variant rs757546424dbSNPEnsembl.1
Natural variantiVAR_004227221I → T in LPL deficiency; loss of activity. 5 PublicationsCorresponds to variant rs118204061dbSNPEnsembl.1
Natural variantiVAR_004228222G → E in LPL deficiency. 1 PublicationCorresponds to variant rs118204075dbSNPEnsembl.1
Natural variantiVAR_057927225K → R in LPL deficiency. 1 Publication1
Natural variantiVAR_057928227V → A in LPL deficiency. 1 PublicationCorresponds to variant rs528243561dbSNPEnsembl.1
Natural variantiVAR_004229231D → E in LPL deficiency; loss of activity. 3 PublicationsCorresponds to variant rs118204067dbSNPEnsembl.1
Natural variantiVAR_004230232I → S in LPL deficiency. 1 PublicationCorresponds to variant rs770601263dbSNPEnsembl.1
Natural variantiVAR_004231234P → L in LPL deficiency; loss of activity. 2 PublicationsCorresponds to variant rs118204060dbSNPEnsembl.1
Natural variantiVAR_004232243C → S in LPL deficiency; loss of activity. 1 Publication1
Natural variantiVAR_057929252I → T in LPL deficiency. 1 PublicationCorresponds to variant rs118204080dbSNPEnsembl.1
Natural variantiVAR_057930266C → W in LPL deficiency. 1 PublicationCorresponds to variant rs118204082dbSNPEnsembl.1
Natural variantiVAR_057931270R → C in LPL deficiency. 4 PublicationsCorresponds to variant rs118204077dbSNPEnsembl.1
Natural variantiVAR_004233270R → H in LPL deficiency; loss of activity. 6 PublicationsCorresponds to variant rs118204062dbSNPEnsembl.1
Natural variantiVAR_004234271S → T in LPL deficiency. 1 PublicationCorresponds to variant rs28934893dbSNPEnsembl.1
Natural variantiVAR_004235277D → N in LPL deficiency; 5% of full activity. 5 PublicationsCorresponds to variant rs118204068dbSNPEnsembl.1
Natural variantiVAR_004236278S → C in LPL deficiency. 1
Natural variantiVAR_057932279L → R in LPL deficiency; decreases the specific activity of the enzyme; the total LPL mass is reduced compared to that of the wild-type construct. 2 PublicationsCorresponds to variant rs35414700dbSNPEnsembl.1
Natural variantiVAR_057933279L → V in LPL deficiency; decreases the specific activity of the enzyme; the total LPL mass is reduced compared to that of the wild-type construct. 1 PublicationCorresponds to variant rs371282890dbSNPEnsembl.1
Natural variantiVAR_004237286S → G in LPL deficiency. 1 Publication1
Natural variantiVAR_004238286S → R in LPL deficiency. 1 Publication1
Natural variantiVAR_011949288A → T in LPL deficiency; the LPL mass level is approximately 67% of the normal; the activity is 32% of the nornal. 3 PublicationsCorresponds to variant rs1800011dbSNPEnsembl.1
Natural variantiVAR_057934289Y → H in LPL deficiency; no enzyme activity. 1 Publication1
Natural variantiVAR_057935297F → L in LPL deficiency and hyperlipidemia; synthesized as a catalytically inactive form; total amount is almost equal to that of the normal enzyme; non-releasable by heparin due to the abnormal structure of the mutant protein. 2 Publications1
Natural variantiVAR_057936303L → F in LPL deficiency; approximately 6% of normal LPL activity and 40% of LPL mass are detected in the patient's postheparin plasma; results in the production of a functionally inactive enzyme. 1 Publication1
Natural variantiVAR_057937305C → R in LPL deficiency. 1 PublicationCorresponds to variant rs773235712dbSNPEnsembl.1
Natural variantiVAR_057938310C → Y in LPL deficiency; decreases the specific activity of the enzyme; reduces the secretion of the mutant protein significantly; the total LPL mass is reduced compared to that of the wild-type construct. 1 Publication1
Natural variantiVAR_057939313L → P in LPL deficiency. 1 Publication1
Natural variantiVAR_004239318N → S in LPL deficiency; loss of activity; frequent mutation. 8 PublicationsCorresponds to variant rs268dbSNPEnsembl.1
Natural variantiVAR_057940325S → R in LPL deficiency; has no effect on the specific activity of the enzyme; has a mild effect on the secretion of the mutant enzyme; the total LPL mass is reduced compared to that of the wild-type construct. 1 PublicationCorresponds to variant rs761265900dbSNPEnsembl.1
Natural variantiVAR_057941328M → R in LPL deficiency. 1 Publication1
Natural variantiVAR_004240328M → T in LPL deficiency. 1
Natural variantiVAR_057942330L → F in LPL deficiency. 1 Publication1
Natural variantiVAR_004241330L → P in LPL deficiency. 1
Natural variantiVAR_004242361A → T in LPL deficiency. 2 PublicationsCorresponds to variant rs118204071dbSNPEnsembl.1
Natural variantiVAR_057943365S → F in LPL deficiency; increases the specific activity of the enzyme; has a mild effect on the secretion of the mutant enzyme; the total LPL mass is reduced compared to that of the wild-type construct. 1 PublicationCorresponds to variant rs546542623dbSNPEnsembl.1
Natural variantiVAR_011950370V → M.1 PublicationCorresponds to variant rs298dbSNPEnsembl.1
Natural variantiVAR_011951379T → A.1 PublicationCorresponds to variant rs300dbSNPEnsembl.1
Natural variantiVAR_004243392L → V in LPL deficiency; loss of activity. 1 PublicationCorresponds to variant rs118204078dbSNPEnsembl.1
Natural variantiVAR_004244423 – 424Missing in LPL deficiency; affects the protein folding. 2
Natural variantiVAR_011952427A → T.1 PublicationCorresponds to variant rs5934dbSNPEnsembl.1
Natural variantiVAR_004245437E → K in LPL deficiency. 1 Publication1
Natural variantiVAR_004246437E → V in LPL deficiency. 1 Publication1
Natural variantiVAR_057944445C → Y in LPL deficiency; has 48% of normal activity in vitro; decreased levels of activity account for by the lower protein mass levels of the mutants rather than by decreased enzymatic activities. 1 PublicationCorresponds to variant rs118204079dbSNPEnsembl.1
Natural variantiVAR_057945448E → K in LPL deficiency; results in a moderate reduction in catalytic activity. 1 PublicationCorresponds to variant rs149089920dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M15856 mRNA. Translation: AAB59536.1.
X14390 mRNA. Translation: CAA32564.1.
X54516 mRNA. Translation: CAA38372.1.
M76722 Genomic DNA. Translation: AAA59528.1.
S76076 Genomic DNA. Translation: AAB21000.1.
S76077 Genomic DNA. Translation: AAB20999.1.
BT006726 mRNA. Translation: AAP35372.1.
AK312311 mRNA. Translation: BAG35236.1.
CH471080 Genomic DNA. Translation: EAW63764.1.
BC011353 mRNA. Translation: AAH11353.1.
X68111 Genomic DNA. Translation: CAA48230.1.
CCDSiCCDS6012.1.
PIRiA26082. LIHUL.
RefSeqiNP_000228.1. NM_000237.2.
UniGeneiHs.180878.

Genome annotation databases

EnsembliENST00000311322; ENSP00000309757; ENSG00000175445.
GeneIDi4023.
KEGGihsa:4023.
UCSCiuc003wzk.5. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

SHMPD

The Singapore human mutation and polymorphism database

Wikipedia

Lipoprotein lipase entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M15856 mRNA. Translation: AAB59536.1.
X14390 mRNA. Translation: CAA32564.1.
X54516 mRNA. Translation: CAA38372.1.
M76722 Genomic DNA. Translation: AAA59528.1.
S76076 Genomic DNA. Translation: AAB21000.1.
S76077 Genomic DNA. Translation: AAB20999.1.
BT006726 mRNA. Translation: AAP35372.1.
AK312311 mRNA. Translation: BAG35236.1.
CH471080 Genomic DNA. Translation: EAW63764.1.
BC011353 mRNA. Translation: AAH11353.1.
X68111 Genomic DNA. Translation: CAA48230.1.
CCDSiCCDS6012.1.
PIRiA26082. LIHUL.
RefSeqiNP_000228.1. NM_000237.2.
UniGeneiHs.180878.

3D structure databases

ProteinModelPortaliP06858.
SMRiP06858.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110205. 18 interactors.
IntActiP06858. 14 interactors.
MINTiMINT-1369348.
STRINGi9606.ENSP00000309757.

Chemistry databases

BindingDBiP06858.
ChEMBLiCHEMBL2060.
DrugBankiDB05269. AST-120.
DB06439. Tyloxapol.
SwissLipidsiSLP:000000568.

Protein family/group databases

ESTHERihuman-LPL. Lipoprotein_Lipase.

PTM databases

iPTMnetiP06858.
PhosphoSitePlusiP06858.

Polymorphism and mutation databases

BioMutaiLPL.
DMDMi126314.

Proteomic databases

EPDiP06858.
MaxQBiP06858.
PaxDbiP06858.
PeptideAtlasiP06858.
PRIDEiP06858.

Protocols and materials databases

DNASUi4023.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000311322; ENSP00000309757; ENSG00000175445.
GeneIDi4023.
KEGGihsa:4023.
UCSCiuc003wzk.5. human.

Organism-specific databases

CTDi4023.
DisGeNETi4023.
GeneCardsiLPL.
GeneReviewsiLPL.
HGNCiHGNC:6677. LPL.
HPAiHPA048749.
MalaCardsiLPL.
MIMi238600. phenotype.
609708. gene.
neXtProtiNX_P06858.
OpenTargetsiENSG00000175445.
Orphaneti309015. Familial lipoprotein lipase deficiency.
70470. Hyperlipoproteinemia type 5.
PharmGKBiPA232.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IJUA. Eukaryota.
ENOG4111GMM. LUCA.
GeneTreeiENSGT00760000119069.
HOGENOMiHOG000038553.
HOVERGENiHBG002259.
InParanoidiP06858.
KOiK01059.
OMAiESVANCH.
OrthoDBiEOG091G052B.
PhylomeDBiP06858.
TreeFamiTF324997.

Enzyme and pathway databases

BioCyciZFISH:HS10931-MONOMER.
BRENDAi3.1.1.34. 2681.
ReactomeiR-HSA-174800. Chylomicron-mediated lipid transport.
R-HSA-381340. Transcriptional regulation of white adipocyte differentiation.
R-HSA-975634. Retinoid metabolism and transport.

Miscellaneous databases

GeneWikiiLipoprotein_lipase.
GenomeRNAii4023.
PROiP06858.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000175445.
CleanExiHS_LPL.
ExpressionAtlasiP06858. baseline and differential.
GenevisibleiP06858. HS.

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_HUMAN
AccessioniPrimary (citable) accession number: P06858
Secondary accession number(s): B2R5T9
, Q16282, Q16283, Q96FC4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 1, 1988
Last modified: November 30, 2016
This is version 205 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. 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.