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Entry version 107 (02 Jun 2021)
Sequence version 1 (01 Jan 1998)
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Protein

Pancreatic lipase-related protein 2

Gene

PNLIPRP2

Organism
Cavia porcellus (Guinea pig)
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

Lipase that primarily hydrolyzes triglycerides and galactosylglycerides (PubMed:8490016, PubMed:17401110, PubMed:20083229, PubMed:8939760).

In neonates, may play a major role in pancreatic digestion of dietary fats such as milk fat globules enriched in long-chain triglycerides (By similarity).

Hydrolyzes short- medium- and long-chain fatty acyls in triglycerides without apparent positional specificity (PubMed:8490016, PubMed:8939760).

Can completely deacylates triacylglycerols (By similarity).

When liver matures and bile salt synthesis increases, it likely functions mainly as a galactolipase and monoacylglycerol lipase. Hydrolyzes monogalactosyldiglycerols (MGDG) and digalactosyldiacylglycerols (DGDG) present in plant-based diet releasing long-chain polyunsaturated fatty acids (PubMed:20083229, PubMed:8939760).

Hydrolyzes medium- and long-chain fatty acyls in galactolipids. May act together with LIPF to hydrolyze partially digested triglycerides (By similarity).

Hydrolyzes long-chain monoglycerides with high efficiency. In cytotoxic T cells, contributes to perforin-dependent cell lysis, but is unlikely to mediate direct cytotoxicity (By similarity).

Has also low phospholipase activity, but its physiological relevance is not clear (By similarity).

By similarity4 Publications

<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

CLPS stimulates triacylglycerol lipase activity. Not inhibited by bile salts.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: triacylglycerol degradation

This protein is involved in the pathway triacylglycerol degradation, which is part of Glycerolipid metabolism.By similarity
View all proteins of this organism that are known to be involved in the pathway triacylglycerol degradation and in Glycerolipid metabolism.

Pathwayi: Glycolipid metabolism

This protein is involved in Glycolipid metabolism.By similarity
View all proteins of this organism that are known to be involved in Glycolipid metabolism.

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 sitei154NucleophileBy similarity1
Active sitei178Charge relay systemPROSITE-ProRule annotationBy similarity1
<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 bindingi189Calcium; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi192Calcium; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi194CalciumCombined sources1 Publication1
Metal bindingi197CalciumCombined sources1 Publication1
Active sitei247Charge relay systemPROSITE-ProRule annotationBy similarity1

<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 functionHydrolase
Biological processLipid degradation, Lipid metabolism
LigandCalcium, Metal-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.1.1.26, 1225

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P81139

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00256

Protein family/group databases

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

More...
ESTHERi
cavpo-2plrp, Pancreatic_lipase

Chemistry databases

SwissLipids knowledge resource for lipid biology

More...
SwissLipidsi
SLP:000001439

<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:
Pancreatic lipase-related protein 2By similarity
Short name:
PL-RP2By similarity
Alternative name(s):
Cytotoxic T lymphocyte lipaseBy similarity
GPL1 Publication
Galactolipase (EC:3.1.1.262 Publications)
Triacylglycerol lipase (EC:3.1.1.32 Publications)
<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:PNLIPRP2By similarity
<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>OrganismiCavia porcellus (Guinea pig)
<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 identifieri10141 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaHystricomorphaCaviidaeCavia
<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
  • UP000005447 <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: Unassembled WGS sequence

<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

Keywords - Cellular componenti

Cytoplasmic vesicle, Membrane, Secreted

<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

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL2169729

<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 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_00000903571 – 434Pancreatic lipase-related protein 2Add BLAST434

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 bondi4 ↔ 10PROSITE-ProRule annotationBy similarity
Disulfide bondi92 ↔ 103PROSITE-ProRule annotationBy similarity
Disulfide bondi239 ↔ 245PROSITE-ProRule annotationBy similarity
Disulfide bondi269 ↔ 280PROSITE-ProRule annotationBy similarity
Disulfide bondi283 ↔ 288PROSITE-ProRule annotationBy similarity
<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>Glycosylationi318N-linked (GlcNAc...) asparagineBy similarity1
Disulfide bondi418 ↔ 434PROSITE-ProRule annotationBy similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

<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

Pancreas.1 Publication

<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

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
10141.ENSCPOP00000020465

<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

1434
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

More...
SMRi
P81139

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
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%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>Domaini322 – 434PLATPROSITE-ProRule annotationAdd BLAST113

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>Regioni76 – 88Required for galactolipase activityBy similarityAdd BLAST13
Regioni240 – 244Required for galactolipase activityBy similarity5

<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.Sequence analysis

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG502QUK7, Eukaryota

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P81139

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
IPR002331, Lipase_panc
IPR001024, PLAT/LH2_dom
IPR036392, PLAT/LH2_dom_sf
IPR000734, TAG_lipase

The PANTHER Classification System

More...
PANTHERi
PTHR11610, PTHR11610, 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
PR00823, PANCLIPASE
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

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.

P81139-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
AEVCYSHLGC FSDEKPWAGT SQRPIKSLPS DPKKINTRFL LYTNENQNSY
60 70 80 90 100
QLITATDIAT IKASNFNLNR KTRFIIHGFT DSGENSWLSD MCKNMFQVEK
110 120 130 140 150
VNCICVDWKG GSKAQYSQAS QNIRVVGAEV AYLVQVLSTS LNYAPENVHI
160 170 180 190 200
IGHSLGAHTA GEAGKRLNGL VGRITGLDPA EPYFQDTPEE VRLDPSDAKF
210 220 230 240 250
VDVIHTDISP ILPSLGFGMS QKVGHMDFFP NGGKDMPGCK TGISCNHHRS
260 270 280 290 300
IEYYHSSILN PEGFLGYPCA SYDEFQESGC FPCPAKGCPK MGHFADQYPG
310 320 330 340 350
KTNAVEQTFF LNTGASDNFT RWRYKVTVTL SGEKDPSGNI NVALLGKNGN
360 370 380 390 400
SAQYQVFKGT LKPDASYTNS IDVELNVGTI QKVTFLWKRS GISVSKPKMG
410 420 430
ASRITVQSGK DGTKYNFCSS DIVQENVEQT LSPC
Length:434
Mass (Da):47,678
Last modified:January 1, 1998 - 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:iE15EED77F3DD59D2
GO

Sequence databases

Protein sequence database of the Protein Information Resource

More...
PIRi
A49488

<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

PIRiA49488

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1GPLX-ray2.01A1-434[»]
SMRiP81139
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

STRINGi10141.ENSCPOP00000020465

Chemistry databases

ChEMBLiCHEMBL2169729
SwissLipidsiSLP:000001439

Protein family/group databases

ESTHERicavpo-2plrp, Pancreatic_lipase

Phylogenomic databases

eggNOGiENOG502QUK7, Eukaryota
InParanoidiP81139

Enzyme and pathway databases

UniPathwayiUPA00256
BRENDAi3.1.1.26, 1225
SABIO-RKiP81139

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
IPR002331, Lipase_panc
IPR001024, PLAT/LH2_dom
IPR036392, PLAT/LH2_dom_sf
IPR000734, TAG_lipase
PANTHERiPTHR11610, PTHR11610, 1 hit
PfamiView protein in Pfam
PF00151, Lipase, 1 hit
PF01477, PLAT, 1 hit
PIRSFiPIRSF000865, Lipoprotein_lipase_LIPH, 1 hit
PRINTSiPR00823, PANCLIPASE
PR00821, TAGLIPASE
SMARTiView protein in SMART
SM00308, LH2, 1 hit
SUPFAMiSSF49723, SSF49723, 1 hit
SSF53474, SSF53474, 1 hit
PROSITEiView protein in PROSITE
PS00120, LIPASE_SER, 1 hit
PS50095, PLAT, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
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 nameiLIPR2_CAVPO
<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: P81139
<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: August 30, 2005
Last sequence update: January 1, 1998
Last modified: June 2, 2021
This is version 107 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

3D-structure, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
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