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Entry version 235 (16 Oct 2019)
Sequence version 1 (01 Jan 1988)
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Protein

Lipoprotein lipase

Gene

LPL

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Key enzyme in triglyceride metabolism. Catalyzes the hydrolysis of triglycerides from circulating chylomicrons and very low density lipoproteins (VLDL), and thereby plays an important role in lipid clearance from the blood stream, lipid utilization and storage (PubMed:8675619, PubMed:11342582, PubMed:27578112). Mediates margination of triglyceride-rich lipoprotein particles in capillaries (PubMed:24726386). Recruited to its site of action on the luminal surface of vascular endothelium by binding to GPIHBP1 and cell surface heparan sulfate proteoglycans (PubMed:11342582, PubMed:27811232).5 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

The apolipoprotein APOC2 acts as a coactivator of LPL activity (By similarity). Ca2+ binding promotes protein stability and formation of the active homodimer (PubMed:16179346). Interaction with GPIHBP1 protects LPL against inactivation by ANGPTL4 (PubMed:27929370, PubMed:29899144).By similarity3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei159Nucleophile2 Publications1
Active sitei183Charge relay system1 Publication1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi194Calcium; via carbonyl oxygen1 Publication1
Metal bindingi197Calcium; via carbonyl oxygen1 Publication1
Metal bindingi199Calcium; via carbonyl oxygen1 Publication1
Metal bindingi202Calcium1 Publication1
Active sitei268Charge relay system1 Publication1 Publication1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

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

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

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BRENDAi
3.1.1.34 2681

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-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

SIGNOR Signaling Network Open Resource

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SIGNORi
P06858

Protein family/group databases

ESTHER database of the Alpha/Beta-hydrolase fold superfamily of proteins

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ESTHERi
human-LPL Lipoprotein_Lipase

Chemistry databases

SwissLipids knowledge resource for lipid biology

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SwissLipidsi
SLP:000000568

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Lipoprotein lipase (EC:3.1.1.345 Publications)
Short name:
LPL
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:LPL
Synonyms:LIPD
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 8

Organism-specific databases

Human Gene Nomenclature Database

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HGNCi
HGNC:6677 LPL

Online Mendelian Inheritance in Man (OMIM)

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MIMi
609708 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_P06858

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>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 & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Chylomicron, Extracellular matrix, Membrane, Secreted, VLDL

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Hyperlipoproteinemia 1 (HLPP1)55 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal recessive metabolic disorder characterized by defective breakdown of dietary fats, impaired clearance of chylomicrons from plasma causing the plasma to have a milky appearance, and severe hypertriglyceridemia. On a normal diet, patients often present with abdominal pain, hepatosplenomegaly, lipemia retinalis, eruptive xanthomata, and massive hypertriglyceridemia, sometimes complicated with acute pancreatitis.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_05791470N → S in HLPP1; produces an inactive protein which is not secreted into the media. 2 Publications1
Natural variantiVAR_05791596V → L in HLPP1; gives rise to a 80% decrease in specific catalytic activity. 1 PublicationCorresponds to variant dbSNP:rs373088068Ensembl.1
Natural variantiVAR_05791698A → T in HLPP1; 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 HLPP1. 1 PublicationCorresponds to variant dbSNP:rs118204073EnsemblClinVar.1
Natural variantiVAR_004212113W → G in HLPP1. 1
Natural variantiVAR_004213113W → R in HLPP1. 2 PublicationsCorresponds to variant dbSNP:rs118204069EnsemblClinVar.1
Natural variantiVAR_057917128T → A in HLPP1. 2 Publications1
Natural variantiVAR_057918132G → R in HLPP1; synthesized as a catalytically inactive form. 2 Publications1
Natural variantiVAR_004214163H → R in HLPP1. 1 Publication1
Natural variantiVAR_004215169G → E in HLPP1; loss of activity. 1 PublicationCorresponds to variant dbSNP:rs118204063EnsemblClinVar.1
Natural variantiVAR_004216181G → S in HLPP1. 1 Publication1
Natural variantiVAR_057919181G → V in HLPP1; synthesized as a catalytically inactive form. 2 Publications1
Natural variantiVAR_004217183D → G in HLPP1; lacks both triolein and tributyrin esterase activities. 3 PublicationsCorresponds to variant dbSNP:rs118204064EnsemblClinVar.1
Natural variantiVAR_057920183D → H in HLPP1. 1 PublicationCorresponds to variant dbSNP:rs781614031Ensembl.1
Natural variantiVAR_004218183D → N in HLPP1; lacks both triolein and tributyrin esterase activities. 2 PublicationsCorresponds to variant dbSNP:rs781614031Ensembl.1
Natural variantiVAR_004219184P → R in HLPP1; Nijmegen; loss of activity. 1 Publication1
Natural variantiVAR_004220185A → T in HLPP1; 3.2% of activity. Corresponds to variant dbSNP:rs748349562Ensembl.1
Natural variantiVAR_057921186G → E in HLPP1. 1 Publication1
Natural variantiVAR_057922190E → G in HLPP1. 1 Publication1
Natural variantiVAR_004221199S → C in HLPP1; mild hypertriglyceridemia; partial activity. 2 PublicationsCorresponds to variant dbSNP:rs118204072EnsemblClinVar.1
Natural variantiVAR_057923201D → V in HLPP1; almost complete loss of enzyme activity. 2 Publications1
Natural variantiVAR_004222203A → T in HLPP1; Bethesda; loss of activity and abnormal heparin binding. 2 PublicationsCorresponds to variant dbSNP:rs118204056EnsemblClinVar.1
Natural variantiVAR_004223207D → E in HLPP1. 1 PublicationCorresponds to variant dbSNP:rs118204076EnsemblClinVar.1
Natural variantiVAR_057924208V → I in HLPP1; 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 HLPP1; complete loss of enzyme activity. 1 Publication1
Natural variantiVAR_004224210H → Q in HLPP1; loss of activity. 1
Natural variantiVAR_004225215G → E in HLPP1; loss of activity. 13 PublicationsCorresponds to variant dbSNP:rs118204057EnsemblClinVar.1
Natural variantiVAR_057926215G → R in HLPP1. 2 Publications1
Natural variantiVAR_004226220S → R in HLPP1; 2.0% of activity. Corresponds to variant dbSNP:rs757546424Ensembl.1
Natural variantiVAR_004227221I → T in HLPP1; loss of activity. 6 PublicationsCorresponds to variant dbSNP:rs118204061EnsemblClinVar.1
Natural variantiVAR_004228222G → E in HLPP1. 1 PublicationCorresponds to variant dbSNP:rs118204075EnsemblClinVar.1
Natural variantiVAR_057927225K → R in HLPP1. 1 Publication1
Natural variantiVAR_057928227V → A in HLPP1. 1 PublicationCorresponds to variant dbSNP:rs528243561Ensembl.1
Natural variantiVAR_004229231D → E in HLPP1; loss of activity. 3 PublicationsCorresponds to variant dbSNP:rs118204067EnsemblClinVar.1
Natural variantiVAR_004230232I → S in HLPP1; loss of activity. 2 PublicationsCorresponds to variant dbSNP:rs770601263Ensembl.1
Natural variantiVAR_004231234P → L in HLPP1; loss of activity. 3 PublicationsCorresponds to variant dbSNP:rs118204060EnsemblClinVar.1
Natural variantiVAR_004232243C → S in HLPP1; loss of activity. 1 Publication1
Natural variantiVAR_057929252I → T in HLPP1. 1 PublicationCorresponds to variant dbSNP:rs118204080EnsemblClinVar.1
Natural variantiVAR_057930266C → W in HLPP1. 1 PublicationCorresponds to variant dbSNP:rs118204082EnsemblClinVar.1
Natural variantiVAR_057931270R → C in HLPP1. 4 PublicationsCorresponds to variant dbSNP:rs118204077EnsemblClinVar.1
Natural variantiVAR_004233270R → H in HLPP1; loss of activity. 6 PublicationsCorresponds to variant dbSNP:rs118204062EnsemblClinVar.1
Natural variantiVAR_004234271S → T in HLPP1. 1 PublicationCorresponds to variant dbSNP:rs118204059EnsemblClinVar.1
Natural variantiVAR_004235277D → N in HLPP1; 5% of full activity. 5 PublicationsCorresponds to variant dbSNP:rs118204068EnsemblClinVar.1
Natural variantiVAR_004236278S → C in HLPP1. 1
Natural variantiVAR_057932279L → R in HLPP1; 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 HLPP1; 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 HLPP1. 1 Publication1
Natural variantiVAR_004238286S → R in HLPP1. 1 Publication1
Natural variantiVAR_011949288A → T in HLPP1; 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 HLPP1; no enzyme activity. 1 PublicationCorresponds to variant dbSNP:rs1161884343Ensembl.1
Natural variantiVAR_057935297F → L in HLPP1 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 HLPP1; 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 HLPP1. 1 PublicationCorresponds to variant dbSNP:rs773235712Ensembl.1
Natural variantiVAR_057938310C → Y in HLPP1; 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 HLPP1. 1 Publication1
Natural variantiVAR_057940325S → R in HLPP1; 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 HLPP1. 1 Publication1
Natural variantiVAR_004240328M → T in HLPP1. Corresponds to variant dbSNP:rs1181582051Ensembl.1
Natural variantiVAR_057942330L → F in HLPP1. 1 Publication1
Natural variantiVAR_004241330L → P in HLPP1. 1
Natural variantiVAR_004242361A → T in HLPP1. 2 PublicationsCorresponds to variant dbSNP:rs118204071EnsemblClinVar.1
Natural variantiVAR_057943365S → F in HLPP1; 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 HLPP1; loss of activity. 1 PublicationCorresponds to variant dbSNP:rs118204078EnsemblClinVar.1
Natural variantiVAR_077541404M → R in HLPP1; decreased protein secretion; loss of interaction with GPIHBP1; decreased lipoprotein lipase activity. 2 Publications1
Natural variantiVAR_004244423 – 424Missing in HLPP1; affects the protein folding. 2
Natural variantiVAR_004245437E → K in HLPP1. 1 Publication1
Natural variantiVAR_004246437E → V in HLPP1. 1 Publication1
Natural variantiVAR_057944445C → Y in HLPP1; 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; loss of interaction with GPIHBP1. 3 PublicationsCorresponds to variant dbSNP:rs118204079EnsemblClinVar.1
Natural variantiVAR_057945448E → K in HLPP1; results in a moderate reduction in catalytic activity. 1 PublicationCorresponds to variant dbSNP:rs149089920Ensembl.1
Hyperlipidemia, familial combined, 3 (FCHL3)6 Publications
Disease susceptibility is associated with variations affecting the gene represented in this entry.
Disease descriptionA disorder characterized by a variable pattern of elevated levels of serum total cholesterol, triglycerides or both. It is observed in a percentage of individuals with premature coronary heart disease. FCHL3 inheritance is autosomal dominant.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01194836D → N in FCHL3; associated with disease susceptibility; has approximately 80% of the specific activity of wild-type enzyme. 4 PublicationsCorresponds to variant dbSNP:rs1801177EnsemblClinVar.1
Natural variantiVAR_004239318N → S in FCHL3; associated with disease susceptibility; loss of activity; frequent mutation. 7 PublicationsCorresponds to variant dbSNP:rs268EnsemblClinVar.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi159S → G: Loss of enzyme activity with triolein and tributyrin. 2 Publications1
Mutagenesisi159S → T: Loss of enzyme activity with triolein and tributyrin. 1 Publication1
Mutagenesisi183D → G or N: Loss of enzyme activity with triolein and tributyrin. 1 Publication1
Mutagenesisi199S → G: Loss of enzyme activity. 1 Publication1
Mutagenesisi201D → E: No effect on enzyme activity. 1 Publication1
Mutagenesisi202D → E: Loss of enzyme activity. 1 Publication1
Mutagenesisi268H → G: Loss of enzyme activity with triolein and tributyrin. 1 Publication1
Mutagenesisi268H → Q: Loss of enzyme activity with triolein and tributyrin. 1 Publication1
Mutagenesisi417W → A: Loss of interaction with lipoprotein particles, but no effect on interaction with GPIHBP1; when associated with 420-A-A-421. 1 Publication1
Mutagenesisi420 – 421WW → AA: Loss of interaction with lipoprotein particles, but no effect on interaction with GPIHBP1; when associated with A-417. 1 Publication2
Mutagenesisi430K → N: Impaired heparin-binding; when associated with N-432 and N-437. 1 Publication1
Mutagenesisi432R → N: Impaired heparin-binding; when associated with N-430 and N-437. 1 Publication1
Mutagenesisi434K → N: Impaired heparin-binding; when associated with N-430 and N-432. 1 Publication1

Keywords - Diseasei

Disease mutation, Hyperlipidemia

Organism-specific databases

DisGeNET

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DisGeNETi
4023

GeneReviews a resource of expert-authored, peer-reviewed disease descriptions.

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GeneReviewsi
LPL

MalaCards human disease database

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MalaCardsi
LPL
MIMi144250 phenotype
238600 phenotype

Open Targets

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OpenTargetsi
ENSG00000175445

Orphanet; a database dedicated to information on rare diseases and orphan drugs

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Orphaneti
309015 Familial lipoprotein lipase deficiency

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA232

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

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Pharosi
P06858

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL2060

Drug and drug target database

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DrugBanki
DB13751 Glycyrrhizic acid
DB09568 Omega-3-carboxylic acids
DB13928 Semaglutide
DB06439 Tyloxapol

DrugCentral

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DrugCentrali
P06858

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
LPL

Domain mapping of disease mutations (DMDM)

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DMDMi
126314

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 271 PublicationAdd BLAST27
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000001777528 – 475Lipoprotein lipaseAdd BLAST448

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi54 ↔ 67PROSITE-ProRule annotationCombined sources1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi70N-linked (GlcNAc...) asparagineCombined sources2 Publications1
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei121Nitrated tyrosineBy similarity1
Modified residuei191Nitrated tyrosineBy similarity1
Disulfide bondi243 ↔ 266PROSITE-ProRule annotationCombined sources1 Publication
Disulfide bondi291 ↔ 310PROSITE-ProRule annotationCombined sources1 Publication
Disulfide bondi302 ↔ 305PROSITE-ProRule annotationCombined sources1 Publication
Modified residuei343Nitrated tyrosineBy similarity1
Glycosylationi386N-linked (GlcNAc...) asparagineCombined sources1 Publication1
Disulfide bondi445 ↔ 465PROSITE-ProRule annotationCombined sources1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

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

Keywords - PTMi

Disulfide bond, Glycoprotein, Nitration

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P06858

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P06858

MassIVE - Mass Spectrometry Interactive Virtual Environment

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MassIVEi
P06858

MaxQB - The MaxQuant DataBase

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MaxQBi
P06858

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
P06858

PeptideAtlas

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PeptideAtlasi
P06858

PRoteomics IDEntifications database

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PRIDEi
P06858

ProteomicsDB: a multi-organism proteome resource

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ProteomicsDBi
51936

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P06858

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
P06858

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Detected in blood plasma (PubMed:2340307, PubMed:11893776, PubMed:12641539). Detected in milk (at protein level) (PubMed:2340307).3 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000175445 Expressed in 223 organ(s), highest expression level in adipose tissue

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P06858 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P06858 HS

Organism-specific databases

Human Protein Atlas

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HPAi
HPA048749

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer (PubMed:16179346, PubMed:26725083, PubMed:11893776) (Probable).

Interacts with GPIHBP1 with 1:1 stoichiometry (PubMed:17997385, PubMed:27929370, PubMed:26725083, PubMed:27811232, PubMed:29899144, PubMed:30559189).

Interacts with APOC2; the interaction activates LPL activity in the presence of lipids (By similarity). Interaction with heparan sulfate proteoglycans is required to protect LPL against loss of activity (PubMed:11342582). Associates with lipoprotein particles in blood plasma (PubMed:11342582, PubMed:11893776).

Interacts with LMF1 and SEL1L; interaction with SEL1L is required to prevent aggregation of newly synthesized LPL in the endoplasmic reticulum (ER), and for normal export of LPL from the ER to the extracellular space (PubMed:25066055).

Interacts with SORL1; SORL1 acts as a sorting receptor, promoting LPL localization to endosomes and later to lysosomes, leading to degradation of newly synthesized LPL (PubMed:21385844).

By similarity1 Publication11 Publications

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
110205, 19 interactors

Protein interaction database and analysis system

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IntActi
P06858, 17 interactors

Molecular INTeraction database

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MINTi
P06858

STRING: functional protein association networks

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STRINGi
9606.ENSP00000309757

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P06858

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1475
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P06858

Database of comparative protein structure models

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ModBasei
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Protein Data Bank in Europe - Knowledge Base

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PDBe-KBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini341 – 464PLATPROSITE-ProRule annotationAdd BLAST124

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni32 – 53Interaction with GPIHBP11 PublicationAdd BLAST22
Regioni417 – 421Important for interaction with lipoprotein particles1 Publication5
Regioni430 – 434Important for heparin binding1 Publication5
Regioni443 – 467Interaction with GPIHBP12 PublicationsAdd BLAST25

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the AB hydrolase superfamily. Lipase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
ENOG410IJUA Eukaryota
ENOG4111GMM LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000157178

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000038553

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P06858

KEGG Orthology (KO)

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KOi
K01059

Identification of Orthologs from Complete Genome Data

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OMAi
TRDMMPY

Database of Orthologous Groups

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OrthoDBi
534956at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P06858

TreeFam database of animal gene trees

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TreeFami
TF324997

Family and domain databases

Conserved Domains Database

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CDDi
cd00707 Pancreat_lipase_like, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
3.40.50.1820, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View 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

The PANTHER Classification System

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PANTHERi
PTHR11610 PTHR11610, 1 hit
PTHR11610:SF3 PTHR11610:SF3, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF00151 Lipase, 1 hit
PF01477 PLAT, 1 hit

PIRSF; a whole-protein classification database

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PIRSFi
PIRSF000865 Lipoprotein_lipase_LIPH, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00822 LIPOLIPASE
PR00821 TAGLIPASE

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00308 LH2, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF49723 SSF49723, 1 hit
SSF53474 SSF53474, 1 hit

TIGRFAMs; a protein family database

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TIGRFAMsi
TIGR03230 lipo_lipase, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS00120 LIPASE_SER, 1 hit
PS50095 PLAT, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 5 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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iFBD00FCD334FB8AA
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 5 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
E5RHN7E5RHN7_HUMAN
Lipoprotein lipase
LPL
105Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E5RJI0E5RJI0_HUMAN
Lipoprotein lipase
LPL
129Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E7EW14E7EW14_HUMAN
Lipoprotein lipase
LPL
115Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E5RJZ4E5RJZ4_HUMAN
Lipoprotein lipase
LPL
39Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A3B3IT60A0A3B3IT60_HUMAN
Lipoprotein lipase
LPL
38Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01194836D → N in FCHL3; associated with disease susceptibility; has approximately 80% of the specific activity of wild-type enzyme. 4 PublicationsCorresponds to variant dbSNP:rs1801177EnsemblClinVar.1
Natural variantiVAR_05791470N → S in HLPP1; 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 HLPP1; gives rise to a 80% decrease in specific catalytic activity. 1 PublicationCorresponds to variant dbSNP:rs373088068Ensembl.1
Natural variantiVAR_05791698A → T in HLPP1; 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 HLPP1. 1 PublicationCorresponds to variant dbSNP:rs118204073EnsemblClinVar.1
Natural variantiVAR_004212113W → G in HLPP1. 1
Natural variantiVAR_004213113W → R in HLPP1. 2 PublicationsCorresponds to variant dbSNP:rs118204069EnsemblClinVar.1
Natural variantiVAR_057917128T → A in HLPP1. 2 Publications1
Natural variantiVAR_057918132G → R in HLPP1; synthesized as a catalytically inactive form. 2 Publications1
Natural variantiVAR_004214163H → R in HLPP1. 1 Publication1
Natural variantiVAR_004215169G → E in HLPP1; loss of activity. 1 PublicationCorresponds to variant dbSNP:rs118204063EnsemblClinVar.1
Natural variantiVAR_004216181G → S in HLPP1. 1 Publication1
Natural variantiVAR_057919181G → V in HLPP1; synthesized as a catalytically inactive form. 2 Publications1
Natural variantiVAR_004217183D → G in HLPP1; lacks both triolein and tributyrin esterase activities. 3 PublicationsCorresponds to variant dbSNP:rs118204064EnsemblClinVar.1
Natural variantiVAR_057920183D → H in HLPP1. 1 Publication