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Entry version 156 (12 Aug 2020)
Sequence version 1 (01 Oct 1989)
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Protein

Lipoprotein lipase

Gene

LPL

Organism
Gallus gallus (Chicken)
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 (By similarity). 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 (By similarity). Although it has both phospholipase and triglyceride lipase activities it is primarily a triglyceride lipase with low but detectable phospholipase activity (By similarity). Mediates margination of triglyceride-rich lipoprotein particles in capillaries (By similarity). Recruited to its site of action on the luminal surface of vascular endothelium by binding to GPIHBP1 and cell surface heparan sulfate proteoglycans (By similarity).By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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%5Fsection">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

Ca2+ binding promotes protein stability and formation of the active homodimer.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 sitei159NucleophileBy similarity1
Active sitei183Charge relay systemPROSITE-ProRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 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

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-GGA-8963889, Assembly of active LPL and LIPC lipase complexes

Protein family/group databases

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

More...
ESTHERi
chick-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%5Fand%5Ftaxonomy%5Fsection">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:3.1.1.34By similarity)
Short name:
LPL
Alternative name(s):
Phospholipase A1 (EC:3.1.1.32By similarity)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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>OrganismiGallus gallus (Chicken)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 identifieri9031 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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
  • UP000000539 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">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 Z

<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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi306R → Q: Some loss of heparin-binding ability; when associated with Q-307 and Q-309. 1 Publication1
Mutagenesisi307K → Q: Some loss of heparin-binding ability; when associated with Q-306 and Q-309. 1 Publication1
Mutagenesisi309R → Q: Some loss of heparin-binding ability; when associated with Q-306 and Q-307. 1 Publication1
Mutagenesisi346K → N: Reduced heparin-binding ability and some decrease in specific enzymatic activity. 1 Publication1
Mutagenesisi430R → N: Reduced heparin-binding ability and some reduction in specific enzymatic activity. Almost complete loss of heparin binding and greatly reduced specific enzymatic activity; when associated with N-432 and N-434. 1 Publication1
Mutagenesisi432R → N: Reduced heparin-binding ability. Almost complete loss of heparin binding and greatly reduced specific enzymatic activity; when associated with N-430 and N-434. 1 Publication1
Mutagenesisi434K → N: Reduced heparin-binding ability. Almost complete loss of heparin binding and greatly reduced specific enzymatic activity; when associated with N-430 and N-432. 1 Publication1
Mutagenesisi440K → N: No change in heparin-binding activity nor in specific enzymatic activity. Reduced heparin-binding activity and decreased specific enzymatic activity; when associated with N-441. 1 Publication1
Mutagenesisi441K → N: Reduced heparin-binding activity and decreased specific enzymatic activity. No further reduction of heparin-binding nor of specific enzymatic activity; when associated with N-440. 1 Publication1

<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 – 25Add BLAST25
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000001778226 – 490Lipoprotein lipase1 PublicationAdd BLAST465

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%5Fprocessing%5Fsection">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...) (complex) asparagine1 Publication1
<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 residuei1213'-nitrotyrosineBy similarity1
Modified residuei1913'-nitrotyrosineBy similarity1
Disulfide bondi243 ↔ 266PROSITE-ProRule annotation
Disulfide bondi291 ↔ 310PROSITE-ProRule annotation
Disulfide bondi302 ↔ 305PROSITE-ProRule annotation
Modified residuei3433'-nitrotyrosineBy similarity1
Glycosylationi354N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi386N-linked (GlcNAc...) asparagine1 Publication1
Disulfide bondi445 ↔ 465PROSITE-ProRule annotation

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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

N-glycan at Asn-70 is a triantennary complex oligosaccharide containing sialic acid, galactose, mannose, and N-acetylglucosamine, the reducing GlcNAc being sulfated at C6.1 Publication
Tyrosine nitration after lipopolysaccharide (LPS) challenge down-regulates the lipase activity.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Nitration

Proteomic databases

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

More...
PaxDbi
P11602

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P11602

<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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSGALG00000015425, Expressed in heart and 11 other tissues

<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer.

Interacts with GPIHBP1 with 1:1 stoichiometry (By similarity).

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.

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 (By similarity).

By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
9031.ENSGALP00000036979

<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

More...
SMRi
P11602

Database of comparative protein structure models

More...
ModBasei
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%5Fand%5Fdomains%5Fsection">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
Regioni243 – 266Essential for determining substrate specificityBy similarityAdd BLAST24
Regioni417 – 421Important for interaction with lipoprotein particlesBy similarity5
Regioni430 – 441Heparin-binding1 PublicationAdd BLAST12
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

More...
eggNOGi
ENOG502QQ7P, Eukaryota

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000157178

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_027171_1_0_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P11602

KEGG Orthology (KO)

More...
KOi
K01059

Identification of Orthologs from Complete Genome Data

More...
OMAi
TRDMMPY

Database of Orthologous Groups

More...
OrthoDBi
534956at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P11602

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00707, Pancreat_lipase_like, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.40.50.1820, 1 hit

Integrated resource of protein families, domains and functional sites

More...
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

More...
PANTHERi
PTHR11610, PTHR11610, 1 hit
PTHR11610:SF3, PTHR11610:SF3, 1 hit

Pfam protein domain database

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

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF000865, Lipoprotein_lipase_LIPH, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00822, LIPOLIPASE
PR00821, TAGLIPASE

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00308, LH2, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF49723, SSF49723, 1 hit
SSF53474, SSF53474, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR03230, lipo_lipase, 1 hit

PROSITE; a protein domain and family database

More...
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%5Flength">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>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

P11602-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MERGRGMGKT ALLAVLCLCL RGAAGSDPEA EMNFEGIESK FSLRTPAEPD
60 70 80 90 100
EDVCYLVPGQ MDSLAQCNFN HTSKTFVVIH GWTVTGMYES WVPKLVDALY
110 120 130 140 150
KREPDSNVIV VDWLVRAQQH YPVSAAYTKL VGKDVAMFID WMEEKFNYPL
160 170 180 190 200
NNVHLLGYSL GAHAAGIAGS LTKKKVNRIT GLDPAGPTFE YADAPIRLSP
210 220 230 240 250
DDADFVDVLH TYTRGSPDRS IGIQKPVGHI DIYPNGGGFQ PGCNLGEALR
260 270 280 290 300
LIAEKGFSDV DQLVKCSHER SIHLFIDSLL YEEKPSMAYR CNTKEAFEKG
310 320 330 340 350
LCLSCRKNRC NNLGYKVNRV RTKRNTKMYL KTRAQMPYKV FHYQVKIHFF
360 370 380 390 400
GKTNVTKVDQ PFLISLYGTL DESENIPFTL PEVSSNKTFS FLIYTEVDIG
410 420 430 440 450
DLLMLKLQWE KDTFFSWSDW WTPFAFTIQR VRVKSGETQK KVVFCSRDGS
460 470 480 490
SRLGKGEEAA IFVKCLEQPV SRKRGGAKKA SKENSAHESA
Length:490
Mass (Da):55,132
Last modified:October 1, 1989 - 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:iC014D23363E81FF3
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 conflicti377P → A in CAA43037 (PubMed:1730055).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
X14670 mRNA Translation: CAA32800.1
X60547 Genomic DNA Translation: CAA43037.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S04331

NCBI Reference Sequences

More...
RefSeqi
NP_990613.1, NM_205282.1

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSGALT00000037774; ENSGALP00000036979; ENSGALG00000015425

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
396219

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
gga:396219

<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
X14670 mRNA Translation: CAA32800.1
X60547 Genomic DNA Translation: CAA43037.1
PIRiS04331
RefSeqiNP_990613.1, NM_205282.1

3D structure databases

SMRiP11602
ModBaseiSearch...

Protein-protein interaction databases

STRINGi9031.ENSGALP00000036979

Protein family/group databases

ESTHERichick-lipli, Lipoprotein_Lipase

PTM databases

iPTMnetiP11602

Proteomic databases

PaxDbiP11602

Genome annotation databases

EnsembliENSGALT00000037774; ENSGALP00000036979; ENSGALG00000015425
GeneIDi396219
KEGGigga:396219

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
4023

Phylogenomic databases

eggNOGiENOG502QQ7P, Eukaryota
GeneTreeiENSGT00940000157178
HOGENOMiCLU_027171_1_0_1
InParanoidiP11602
KOiK01059
OMAiTRDMMPY
OrthoDBi534956at2759
PhylomeDBiP11602

Enzyme and pathway databases

ReactomeiR-GGA-8963889, Assembly of active LPL and LIPC lipase complexes

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P11602

Gene expression databases

BgeeiENSGALG00000015425, Expressed in heart and 11 other tissues

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
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<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_CHICK
<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: P11602
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: August 12, 2020
This is version 156 of the entry and version 1 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

Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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