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Entry version 186 (08 May 2019)
Sequence version 3 (27 Jul 2011)
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Protein

Lipoprotein lipase

Gene

Lpl

Organism
Mus musculus (Mouse)
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). Mediates margination of triglyceride-rich lipoprotein particles in capillaries (PubMed:24726386). Recruited to its site of action on vascular endothelium by binding to GPIHBP1 and cell surface heparan sulfate proteoglycans (PubMed:20620994, PubMed:24726386, PubMed:27811232).4 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 ‘Function’ 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. Interaction with GPIHBP1 protects LPL against inactivation by ANGPTL4 (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 sitei159NucleophileBy similarity1
Active sitei183Charge relay systemPROSITE-ProRule annotation1
<p>This subsection of the ‘Function’ 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 oxygenBy similarity1
Metal bindingi197Calcium; via carbonyl oxygenBy similarity1
Metal bindingi199Calcium; via carbonyl oxygenBy similarity1
Metal bindingi202CalciumBy similarity1
Active sitei268Charge relay systemPROSITE-ProRule annotation1

<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

More...
BRENDAi
3.1.1.34 3474

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-MMU-8963889 Assembly of active LPL and LIPC lipase complexes
R-MMU-8963901 Chylomicron remodeling

Protein family/group databases

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

More...
ESTHERi
mouse-lipli Lipoprotein_Lipase

<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:3.1.1.341 Publication)
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
<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>OrganismiMus musculus (Mouse)
<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 identifieri10090 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<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
  • UP000000589 <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

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...
MGIi
MGI:96820 Lpl

<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 describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Mice are born at the expected Mendelian rate. At birth, mutant pups have threefold higher plasma triglyceride levels and sevenfold higher VLDL cholesterol levels relative to wild-type. After suckling they become progressively pale, then cyanotic, and die at about 18 hours after birth. At 18 hours after birth, their plasma triglyceride levels reach 15'090 mg/dl, compared to 188 mg/dl for wild-type. At the same time point, VLDL cholesterol levels reach 280 mg/dl in mutant pups, compared to 6 mg/dl in wild-type. Mutant pups show severly reduced adipose tissue, and their livers are deficient in intracellular lipid droplets. Likewise, the numbers of intracellular lipid droplets in skeletal muscle are severely reduced. Lungs display lipid-filled alveoli and dilated capillaries that are engorged with lipoprotein particles. These particles are marginated and seem to block the access of red blood cells to the vascular endothelium.1 Publication

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL3309051

<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 – 27Sequence analysisAdd 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_000001777628 – 474Lipoprotein lipaseAdd BLAST447

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 annotation
<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...) asparagineSequence analysis1
<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 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

<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
N-glycosylated.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Nitration

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P11152

MaxQB - The MaxQuant DataBase

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MaxQBi
P11152

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

More...
PaxDbi
P11152

PeptideAtlas

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PeptideAtlasi
P11152

PRoteomics IDEntifications database

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PRIDEi
P11152

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P11152

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

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PhosphoSitePlusi
P11152

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
P11152

<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 white and brown adipose tissue and heart muscle, especially at the lumenal surface of capillaries (PubMed:25066055, PubMed:27811232, PubMed:20620994). Detected on capillary endothelium in the lactating mammary gland (PubMed:27811232). Detected in blood plasma (at protein level) (PubMed:17403372, PubMed:25066055). Expressed in liver, epididymal fat, heart, psoas muscle, lactating mammary gland, adrenal, lung, and ovary. Highest levels in heart and adrenal gland.5 Publications

<p>This subsection of the ‘Expression’ section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified ‘at the protein level’.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

Maximum expression in adipose tissue during early development. In heart, low levels 6 days before birth increasing 278-fold as animals reach adulthood.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSMUSG00000015568 Expressed in 319 organ(s), highest expression level in brown adipose tissue

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P11152 MM

<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:25066055). Interacts with GPIHBP1 with 1:1 stoichiometry (PubMed:17403372, PubMed:20620994, PubMed:24726386). 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. Associates with lipoprotein particles in blood plasma (By similarity). 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).By similarity4 Publications

GO - Molecular functioni

Protein-protein interaction databases

Protein interaction database and analysis system

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IntActi
P11152, 4 interactors

STRING: functional protein association networks

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STRINGi
10090.ENSMUSP00000015712

<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

3D structure databases

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

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SMRi
P11152

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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 GPIHBP1By similarityAdd BLAST22
Regioni417 – 421Important for interaction with lipoprotein particlesBy similarity5
Regioni430 – 434Important for heparin bindingBy similarity5
Regioni443 – 467Interaction with GPIHBP1By similarityAdd 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
P11152

KEGG Orthology (KO)

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KOi
K01059

Identification of Orthologs from Complete Genome Data

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OMAi
KWNSDSY

Database of Orthologous Groups

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OrthoDBi
534956at2759

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>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<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.

P11152-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MESKALLLVV LGVWLQSLTA FRGGVAAADA GRDFSDIESK FALRTPEDTA
60 70 80 90 100
EDTCHLIPGL ADSVSNCHFN HSSKTFVVIH GWTVTGMYES WVPKLVAALY
110 120 130 140 150
KREPDSNVIV VDWLYRAQQH YPVSAGYTKL VGNDVARFIN WMEEEFNYPL
160 170 180 190 200
DNVHLLGYSL GAHAAGVAGS LTNKKVNRIT GLDPAGPNFE YAEAPSRLSP
210 220 230 240 250
DDADFVDVLH TFTRGSPGRS IGIQKPVGHV DIYPNGGTFQ PGCNIGEAIR
260 270 280 290 300
VIAERGLGDV DQLVKCSHER SIHLFIDSLL NEENPSKAYR CNSKEAFEKG
310 320 330 340 350
LCLSCRKNRC NNLGYEINKV RAKRSSKMYL KTRSQMPYKV FHYQVKIHFS
360 370 380 390 400
GTEDGKQHNQ AFEISLYGTV AESENIPFTL PEVSTNKTYS FLIYTEVDIG
410 420 430 440 450
ELLMMKLKWI SDSYFSWPDW WSSPSFVIER IRVKAGETQK KVIFCAREKV
460 470
SHLQKGKDSA VFVKCHDKSL KKSG
Length:474
Mass (Da):53,109
Last modified:July 27, 2011 - v3
<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:iE5895C98B7AE16CD
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti129K → Y no nucleotide entry (PubMed:2723548).Curated1
Sequence conflicti147N → K in AAA39441 (PubMed:1765386).Curated1
Sequence conflicti354D → N no nucleotide entry (PubMed:2723548).Curated1
Sequence conflicti410I → M no nucleotide entry (PubMed:2723548).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
M60847
, M60838, M60839, M60840, M60842, M60843, M60844, M60845, M60846 Genomic DNA Translation: AAA39441.1
AK002645 mRNA Translation: BAB22256.1
AK017272 mRNA No translation available.
AK045064 mRNA Translation: BAC32204.1
AK086023 mRNA Translation: BAC39594.1
AK150355 mRNA Translation: BAE29491.1
AK150375 mRNA Translation: BAE29507.1
AK150457 mRNA Translation: BAE29577.1
AK150488 mRNA Translation: BAE29604.1
AK150505 mRNA Translation: BAE29618.1
AK150593 mRNA Translation: BAE29686.1
AK150672 mRNA Translation: BAE29754.1
AK151006 mRNA Translation: BAE30029.1
AK151093 mRNA Translation: BAE30105.1
AK151105 mRNA Translation: BAE30115.1
AK151369 mRNA Translation: BAE30343.1
AK151434 mRNA Translation: BAE30397.1
AK151521 mRNA Translation: BAE30470.1
AK151540 mRNA Translation: BAE30486.1
AK151563 mRNA Translation: BAE30505.1
AK151630 mRNA Translation: BAE30564.1
AK151679 mRNA Translation: BAE30604.1
AK151727 mRNA Translation: BAE30645.1
AK151772 mRNA Translation: BAE30678.1
AK151801 mRNA Translation: BAE30701.1
AK151828 mRNA Translation: BAE30723.1
AK151866 mRNA Translation: BAE30754.1
AK151870 mRNA Translation: BAE30758.1
AK151872 mRNA Translation: BAE30760.1
AK151893 mRNA Translation: BAE30777.1
AK152014 mRNA Translation: BAE30876.1
AK152035 mRNA Translation: BAE30894.1
AK152049 mRNA Translation: BAE30905.1
AK152053 mRNA Translation: BAE30909.1
AK152079 mRNA Translation: BAE30930.1
AK152350 mRNA Translation: BAE31144.1
AK152657 mRNA Translation: BAE31394.1
AK153148 mRNA Translation: BAE31758.1
AK153242 mRNA Translation: BAE31834.1
AK153425 mRNA Translation: BAE31984.1
AK159268 mRNA Translation: BAE34947.1
AK170486 mRNA Translation: BAE41828.1
BC003305 mRNA Translation: AAH03305.1
M65258 mRNA Translation: AAA39442.1
J03302 mRNA Translation: AAA39440.1
M63335 Genomic DNA Translation: AAC04464.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS40357.1

Protein sequence database of the Protein Information Resource

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PIRi
A40570

NCBI Reference Sequences

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RefSeqi
NP_032535.2, NM_008509.2

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENSMUST00000015712; ENSMUSP00000015712; ENSMUSG00000015568
ENSMUST00000168401; ENSMUSP00000132259; ENSMUSG00000015568

Database of genes from NCBI RefSeq genomes

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GeneIDi
16956

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
mmu:16956

UCSC genome browser

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UCSCi
uc009lwq.1 mouse

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M60847
, M60838, M60839, M60840, M60842, M60843, M60844, M60845, M60846 Genomic DNA Translation: AAA39441.1
AK002645 mRNA Translation: BAB22256.1
AK017272 mRNA No translation available.
AK045064 mRNA Translation: BAC32204.1
AK086023 mRNA Translation: BAC39594.1
AK150355 mRNA Translation: BAE29491.1
AK150375 mRNA Translation: BAE29507.1
AK150457 mRNA Translation: BAE29577.1
AK150488 mRNA Translation: BAE29604.1
AK150505 mRNA Translation: BAE29618.1
AK150593 mRNA Translation: BAE29686.1
AK150672 mRNA Translation: BAE29754.1
AK151006 mRNA Translation: BAE30029.1
AK151093 mRNA Translation: BAE30105.1
AK151105 mRNA Translation: BAE30115.1
AK151369 mRNA Translation: BAE30343.1
AK151434 mRNA Translation: BAE30397.1
AK151521 mRNA Translation: BAE30470.1
AK151540 mRNA Translation: BAE30486.1
AK151563 mRNA Translation: BAE30505.1
AK151630 mRNA Translation: BAE30564.1
AK151679 mRNA Translation: BAE30604.1
AK151727 mRNA Translation: BAE30645.1
AK151772 mRNA Translation: BAE30678.1
AK151801 mRNA Translation: BAE30701.1
AK151828 mRNA Translation: BAE30723.1
AK151866 mRNA Translation: BAE30754.1
AK151870 mRNA Translation: BAE30758.1
AK151872 mRNA Translation: BAE30760.1
AK151893 mRNA Translation: BAE30777.1
AK152014 mRNA Translation: BAE30876.1
AK152035 mRNA Translation: BAE30894.1
AK152049 mRNA Translation: BAE30905.1
AK152053 mRNA Translation: BAE30909.1
AK152079 mRNA Translation: BAE30930.1
AK152350 mRNA Translation: BAE31144.1
AK152657 mRNA Translation: BAE31394.1
AK153148 mRNA Translation: BAE31758.1
AK153242 mRNA Translation: BAE31834.1
AK153425 mRNA Translation: BAE31984.1
AK159268 mRNA Translation: BAE34947.1
AK170486 mRNA Translation: BAE41828.1
BC003305 mRNA Translation: AAH03305.1
M65258 mRNA Translation: AAA39442.1
J03302 mRNA Translation: AAA39440.1
M63335 Genomic DNA Translation: AAC04464.1
CCDSiCCDS40357.1
PIRiA40570
RefSeqiNP_032535.2, NM_008509.2

3D structure databases

SMRiP11152
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP11152, 4 interactors
STRINGi10090.ENSMUSP00000015712

Chemistry databases

ChEMBLiCHEMBL3309051

Protein family/group databases

ESTHERimouse-lipli Lipoprotein_Lipase

PTM databases

iPTMnetiP11152
PhosphoSitePlusiP11152
SwissPalmiP11152

Proteomic databases

jPOSTiP11152
MaxQBiP11152
PaxDbiP11152
PeptideAtlasiP11152
PRIDEiP11152

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000015712; ENSMUSP00000015712; ENSMUSG00000015568
ENSMUST00000168401; ENSMUSP00000132259; ENSMUSG00000015568
GeneIDi16956
KEGGimmu:16956
UCSCiuc009lwq.1 mouse

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
4023
MGIiMGI:96820 Lpl

Phylogenomic databases

eggNOGiENOG410IJUA Eukaryota
ENOG4111GMM LUCA
GeneTreeiENSGT00940000157178
HOGENOMiHOG000038553
InParanoidiP11152
KOiK01059
OMAiKWNSDSY
OrthoDBi534956at2759
TreeFamiTF324997

Enzyme and pathway databases

BRENDAi3.1.1.34 3474
ReactomeiR-MMU-8963889 Assembly of active LPL and LIPC lipase complexes
R-MMU-8963901 Chylomicron remodeling

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

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ChiTaRSi
Lpl mouse

Protein Ontology

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PROi
PR:P11152

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000015568 Expressed in 319 organ(s), highest expression level in brown adipose tissue
GenevisibleiP11152 MM

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

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiLIPL_MOUSE
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P11152
Secondary accession number(s): Q05956
, Q542L4, Q9D3M9, Q9DCM8
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 27, 2011
Last modified: May 8, 2019
This is version 186 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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