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UniProtKB - P06858 (LIPL_HUMAN)

Protein

Lipoprotein lipase

Gene

LPL

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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) (PubMed:27578112). 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 similarity2 Publications

Catalytic activityi

Triacylglycerol + H2O = diacylglycerol + a carboxylate.2 Publications

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
  • signaling receptor binding Source: BHF-UCL
  • triglyceride binding Source: Ensembl
  • triglyceride lipase activity Source: BHF-UCL
View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

Keywordsi

Molecular functionHeparin-binding, Hydrolase
Biological processLipid degradation, Lipid metabolism

Enzyme and pathway databases

BRENDAi3.1.1.34 2681
ReactomeiR-HSA-381340 Transcriptional regulation of white adipocyte differentiation
R-HSA-8963889 Assembly of active LPL and LIPC lipase complexes
R-HSA-8963901 Chylomicron remodeling
R-HSA-975634 Retinoid metabolism and transport
SIGNORiP06858

Protein family/group databases

ESTHERihuman-LPL Lipoprotein_Lipase

Chemistry databases

SwissLipidsiSLP:000000568

Names & Taxonomyi

Protein namesi
Recommended name:
Lipoprotein lipase (EC:3.1.1.342 Publications)
Short name:
LPL
Gene namesi
Name:LPL
Synonyms:LIPD
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
Proteomesi
  • UP000005640 Componenti: Chromosome 8

Organism-specific databases

EuPathDBiHostDB:ENSG00000175445.14
HGNCiHGNC:6677 LPL
MIMi609708 gene
neXtProtiNX_P06858

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Chylomicron, Membrane, Secreted, VLDL

Pathology & Biotechi

Involvement in diseasei

Lipoprotein lipase deficiency (LPL deficiency)55 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 dbSNP:rs1801177EnsemblClinVar.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 dbSNP:rs373088068Ensembl.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 dbSNP:rs145657341Ensembl.1
Natural variantiVAR_004211102R → S in LPL deficiency. 1 PublicationCorresponds to variant dbSNP:rs118204073EnsemblClinVar.1
Natural variantiVAR_004212113W → G in LPL deficiency. 1
Natural variantiVAR_004213113W → R in LPL deficiency. 2 PublicationsCorresponds to variant dbSNP:rs118204069EnsemblClinVar.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 dbSNP:rs118204063EnsemblClinVar.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 dbSNP:rs118204064EnsemblClinVar.1
Natural variantiVAR_057920183D → H in LPL deficiency. 1 PublicationCorresponds to variant dbSNP:rs781614031Ensembl.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 dbSNP:rs748349562Ensembl.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 dbSNP:rs118204072EnsemblClinVar.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 dbSNP:rs118204056EnsemblClinVar.1
Natural variantiVAR_004223207D → E in LPL deficiency. 1 PublicationCorresponds to variant dbSNP:rs118204076EnsemblClinVar.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 dbSNP:rs568397156Ensembl.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 dbSNP:rs118204057EnsemblClinVar.1
Natural variantiVAR_057926215G → R in LPL deficiency. 2 Publications1
Natural variantiVAR_004226220S → R in LPL deficiency; 2.0% of activity. Corresponds to variant dbSNP:rs757546424Ensembl.1
Natural variantiVAR_004227221I → T in LPL deficiency; loss of activity. 5 PublicationsCorresponds to variant dbSNP:rs118204061EnsemblClinVar.1
Natural variantiVAR_004228222G → E in LPL deficiency. 1 PublicationCorresponds to variant dbSNP:rs118204075EnsemblClinVar.1
Natural variantiVAR_057927225K → R in LPL deficiency. 1 Publication1
Natural variantiVAR_057928227V → A in LPL deficiency. 1 PublicationCorresponds to variant dbSNP:rs528243561Ensembl.1
Natural variantiVAR_004229231D → E in LPL deficiency; loss of activity. 3 PublicationsCorresponds to variant dbSNP:rs118204067EnsemblClinVar.1
Natural variantiVAR_004230232I → S in LPL deficiency. 1 PublicationCorresponds to variant dbSNP:rs770601263Ensembl.1
Natural variantiVAR_004231234P → L in LPL deficiency; loss of activity. 2 PublicationsCorresponds to variant dbSNP:rs118204060EnsemblClinVar.1
Natural variantiVAR_004232243C → S in LPL deficiency; loss of activity. 1 Publication1
Natural variantiVAR_057929252I → T in LPL deficiency. 1 PublicationCorresponds to variant dbSNP:rs118204080EnsemblClinVar.1
Natural variantiVAR_057930266C → W in LPL deficiency. 1 PublicationCorresponds to variant dbSNP:rs118204082EnsemblClinVar.1
Natural variantiVAR_057931270R → C in LPL deficiency. 4 PublicationsCorresponds to variant dbSNP:rs118204077EnsemblClinVar.1
Natural variantiVAR_004233270R → H in LPL deficiency; loss of activity. 6 PublicationsCorresponds to variant dbSNP:rs118204062EnsemblClinVar.1
Natural variantiVAR_004234271S → T in LPL deficiency. 1 PublicationCorresponds to variant dbSNP:rs118204059EnsemblClinVar.1
Natural variantiVAR_004235277D → N in LPL deficiency; 5% of full activity. 5 PublicationsCorresponds to variant dbSNP:rs118204068EnsemblClinVar.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 dbSNP:rs35414700Ensembl.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 dbSNP:rs371282890Ensembl.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 dbSNP:rs1800011Ensembl.1
Natural variantiVAR_057934289Y → H in LPL deficiency; no enzyme activity. 1 Publication1
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 dbSNP:rs773235712Ensembl.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 PublicationCorresponds to variant dbSNP:rs1409123950Ensembl.1
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 dbSNP:rs268EnsemblClinVar.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 dbSNP:rs761265900Ensembl.1
Natural variantiVAR_057941328M → R in LPL deficiency. 1 Publication1
Natural variantiVAR_004240328M → T in LPL deficiency. Corresponds to variant dbSNP:rs1181582051Ensembl.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 dbSNP:rs118204071EnsemblClinVar.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 dbSNP:rs546542623Ensembl.1
Natural variantiVAR_004243392L → V in LPL deficiency; loss of activity. 1 PublicationCorresponds to variant dbSNP:rs118204078EnsemblClinVar.1
Natural variantiVAR_077541404M → R in LPL deficiency; decreased protein secretion; loss of lipoprotein lipase activity. 1 Publication1
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 dbSNP:rs118204079EnsemblClinVar.1
Natural variantiVAR_057945448E → K in LPL deficiency; results in a moderate reduction in catalytic activity. 1 PublicationCorresponds to variant dbSNP:rs149089920Ensembl.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
GeneReviewsiLPL
MalaCardsiLPL
MIMi238600 phenotype
OpenTargetsiENSG00000175445
Orphaneti309015 Familial lipoprotein lipase deficiency
70470 Hyperlipoproteinemia type 5
PharmGKBiPA232

Chemistry databases

ChEMBLiCHEMBL2060
DrugBankiDB09278 Activated charcoal
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...) asparagine1 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...) asparagineSequence 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
ProteomicsDBi51936

PTM databases

iPTMnetiP06858
PhosphoSitePlusiP06858

Expressioni

Gene expression databases

BgeeiENSG00000175445 Expressed in 223 organ(s), highest expression level in adipose tissue
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

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridi110205, 19 interactors
IntActiP06858, 15 interactors
MINTiP06858
STRINGi9606.ENSP00000309757

Chemistry databases

BindingDBiP06858

Structurei

3D structure databases

ProteinModelPortaliP06858
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

Keywords - Domaini

Signal

Phylogenomic databases

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

Family and domain databases

CDDicd00707 Pancreat_lipase_like, 1 hit
Gene3Di3.40.50.1820, 1 hit
InterProiView protein in InterPro
IPR029058 AB_hydrolase
IPR013818 Lipase/vitellogenin
IPR016272 Lipase_LIPH
IPR033906 Lipase_N
IPR002330 Lipo_Lipase
IPR001024 PLAT/LH2_dom
IPR036392 PLAT/LH2_dom_sf
IPR000734 TAG_lipase
PANTHERiPTHR11610 PTHR11610, 1 hit
PTHR11610:SF3 PTHR11610:SF3, 1 hit
PfamiView protein in Pfam
PF00151 Lipase, 1 hit
PF01477 PLAT, 1 hit
PIRSFiPIRSF000865 Lipoprotein_lipase_LIPH, 1 hit
PRINTSiPR00822 LIPOLIPASE
PR00821 TAGLIPASE
SMARTiView protein in SMART
SM00308 LH2, 1 hit
SUPFAMiSSF49723 SSF49723, 1 hit
SSF53474 SSF53474, 1 hit
TIGRFAMsiTIGR03230 lipo_lipase, 1 hit
PROSITEiView protein in PROSITE
PS00120 LIPASE_SER, 1 hit
PS50095 PLAT, 1 hit

Sequence (1+)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 4 potential isoforms that are computationally mapped.Show allAlign All

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

Computationally mapped potential isoform sequencesi

There are 4 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
E5RJI0E5RJI0_HUMAN
Lipoprotein lipase
LPL
129Annotation score:
E5RHN7E5RHN7_HUMAN
Lipoprotein lipase
LPL
105Annotation score:
E7EW14E7EW14_HUMAN
Lipoprotein lipase
LPL
115Annotation score:
E5RJZ4E5RJZ4_HUMAN
Lipoprotein lipase
LPL
39Annotation score:

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 dbSNP:rs1801177EnsemblClinVar.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 dbSNP:rs11542065EnsemblClinVar.1
Natural variantiVAR_05791596V → L in LPL deficiency; gives rise to a 80% decrease in specific catalytic activity. 1 PublicationCorresponds to variant dbSNP:rs373088068Ensembl.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 dbSNP:rs145657341Ensembl.1
Natural variantiVAR_004211102R → S in LPL deficiency. 1 PublicationCorresponds to variant dbSNP:rs118204073EnsemblClinVar.1
Natural variantiVAR_004212113W → G in LPL deficiency. 1
Natural variantiVAR_004213113W → R in LPL deficiency. 2 PublicationsCorresponds to variant dbSNP:rs118204069EnsemblClinVar.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 dbSNP:rs118204063EnsemblClinVar.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 dbSNP:rs118204064EnsemblClinVar.1
Natural variantiVAR_057920183D → H in LPL deficiency. 1 PublicationCorresponds to variant dbSNP:rs781614031Ensembl.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 dbSNP:rs748349562Ensembl.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 dbSNP:rs118204072EnsemblClinVar.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 dbSNP:rs118204056EnsemblClinVar.1
Natural variantiVAR_004223207D → E in LPL deficiency. 1 PublicationCorresponds to variant dbSNP:rs118204076EnsemblClinVar.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 dbSNP:rs568397156Ensembl.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 dbSNP:rs118204057EnsemblClinVar.1
Natural variantiVAR_057926215G → R in LPL deficiency. 2 Publications1
Natural variantiVAR_004226220S → R in LPL deficiency; 2.0% of activity. Corresponds to variant dbSNP:rs757546424Ensembl.1
Natural variantiVAR_004227221I → T in LPL deficiency; loss of activity. 5 PublicationsCorresponds to variant dbSNP:rs118204061EnsemblClinVar.1
Natural variantiVAR_004228222G → E in LPL deficiency. 1 PublicationCorresponds to variant dbSNP:rs118204075EnsemblClinVar.1
Natural variantiVAR_057927225K → R in LPL deficiency. 1 Publication1
Natural variantiVAR_057928227V → A in LPL deficiency. 1 PublicationCorresponds to variant dbSNP:rs528243561Ensembl.1
Natural variantiVAR_004229231D → E in LPL deficiency; loss of activity. 3 PublicationsCorresponds to variant dbSNP:rs118204067EnsemblClinVar.1
Natural variantiVAR_004230232I → S in LPL deficiency. 1 PublicationCorresponds to variant dbSNP:rs770601263Ensembl.1
Natural variantiVAR_004231234P → L in LPL deficiency; loss of activity. 2 PublicationsCorresponds to variant dbSNP:rs118204060EnsemblClinVar.1
Natural variantiVAR_004232243C → S in LPL deficiency; loss of activity. 1 Publication1
Natural variantiVAR_057929252I → T in LPL deficiency. 1 PublicationCorresponds to variant dbSNP:rs118204080EnsemblClinVar.1
Natural variantiVAR_057930266C → W in LPL deficiency. 1 PublicationCorresponds to variant dbSNP:rs118204082EnsemblClinVar.1
Natural variantiVAR_057931270R → C in LPL deficiency. 4 PublicationsCorresponds to variant dbSNP:rs118204077EnsemblClinVar.1
Natural variantiVAR_004233270R → H in LPL deficiency; loss of activity. 6 PublicationsCorresponds to variant dbSNP:rs118204062EnsemblClinVar.1
Natural variantiVAR_004234271S → T in LPL deficiency. 1 PublicationCorresponds to variant dbSNP:rs118204059EnsemblClinVar.1
Natural variantiVAR_004235277D → N in LPL deficiency; 5% of full activity. 5 PublicationsCorresponds to variant dbSNP:rs118204068EnsemblClinVar.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 dbSNP:rs35414700Ensembl.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 dbSNP:rs371282890Ensembl.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 dbSNP:rs1800011Ensembl.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 dbSNP:rs773235712Ensembl.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 PublicationCorresponds to variant dbSNP:rs1409123950Ensembl.1
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 dbSNP:rs268EnsemblClinVar.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 dbSNP:rs761265900Ensembl.1
Natural variantiVAR_057941328M → R in LPL deficiency. 1 Publication1
Natural variantiVAR_004240328M → T in LPL deficiency. Corresponds to variant dbSNP:rs1181582051Ensembl.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 dbSNP:rs118204071EnsemblClinVar.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 dbSNP:rs546542623Ensembl.1
Natural variantiVAR_011950370V → M1 PublicationCorresponds to variant dbSNP:rs298Ensembl.1
Natural variantiVAR_011951379T → A1 PublicationCorresponds to variant dbSNP:rs300EnsemblClinVar.1
Natural variantiVAR_004243392L → V in LPL deficiency; loss of activity. 1 PublicationCorresponds to variant dbSNP:rs118204078EnsemblClinVar.1
Natural variantiVAR_077541404M → R in LPL deficiency; decreased protein secretion; loss of lipoprotein lipase activity. 1 Publication1
Natural variantiVAR_004244423 – 424Missing in LPL deficiency; affects the protein folding. 2
Natural variantiVAR_011952427A → T1 PublicationCorresponds to variant dbSNP:rs5934EnsemblClinVar.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 dbSNP:rs118204079EnsemblClinVar.1
Natural variantiVAR_057945448E → K in LPL deficiency; results in a moderate reduction in catalytic activity. 1 PublicationCorresponds to variant dbSNP:rs149089920Ensembl.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

Similar proteinsi

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
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110205, 19 interactors
IntActiP06858, 15 interactors
MINTiP06858
STRINGi9606.ENSP00000309757

Chemistry databases

BindingDBiP06858
ChEMBLiCHEMBL2060
DrugBankiDB09278 Activated charcoal
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
ProteomicsDBi51936

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
EuPathDBiHostDB:ENSG00000175445.14
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
OMAiFAIEKIR
OrthoDBiEOG091G052B
PhylomeDBiP06858
TreeFamiTF324997

Enzyme and pathway databases

BRENDAi3.1.1.34 2681
ReactomeiR-HSA-381340 Transcriptional regulation of white adipocyte differentiation
R-HSA-8963889 Assembly of active LPL and LIPC lipase complexes
R-HSA-8963901 Chylomicron remodeling
R-HSA-975634 Retinoid metabolism and transport
SIGNORiP06858

Miscellaneous databases

GeneWikiiLipoprotein_lipase
GenomeRNAii4023
PROiPR:P06858
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000175445 Expressed in 223 organ(s), highest expression level in adipose tissue
CleanExiHS_LPL
ExpressionAtlasiP06858 baseline and differential
GenevisibleiP06858 HS

Family and domain databases

CDDicd00707 Pancreat_lipase_like, 1 hit
Gene3Di3.40.50.1820, 1 hit
InterProiView protein in InterPro
IPR029058 AB_hydrolase
IPR013818 Lipase/vitellogenin
IPR016272 Lipase_LIPH
IPR033906 Lipase_N
IPR002330 Lipo_Lipase
IPR001024 PLAT/LH2_dom
IPR036392 PLAT/LH2_dom_sf
IPR000734 TAG_lipase
PANTHERiPTHR11610 PTHR11610, 1 hit
PTHR11610:SF3 PTHR11610:SF3, 1 hit
PfamiView protein in Pfam
PF00151 Lipase, 1 hit
PF01477 PLAT, 1 hit
PIRSFiPIRSF000865 Lipoprotein_lipase_LIPH, 1 hit
PRINTSiPR00822 LIPOLIPASE
PR00821 TAGLIPASE
SMARTiView protein in SMART
SM00308 LH2, 1 hit
SUPFAMiSSF49723 SSF49723, 1 hit
SSF53474 SSF53474, 1 hit
TIGRFAMsiTIGR03230 lipo_lipase, 1 hit
PROSITEiView protein in PROSITE
PS00120 LIPASE_SER, 1 hit
PS50095 PLAT, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiLIPL_HUMAN
AccessioniPrimary (citable) accession number: P06858
Secondary accession number(s): B2R5T9
, Q16282, Q16283, Q96FC4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 1, 1988
Last modified: November 7, 2018
This is version 225 of the entry and version 1 of the sequence. See 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. SIMILARITY comments
    Index of protein domains and families
  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. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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