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Entry version 112 (02 Jun 2021)
Sequence version 1 (01 Jan 1998)
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Protein

Allene oxide synthase-lipoxygenase protein

Gene
N/A
Organism
Plexaura homomalla (Black sea rod)
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

Bifunctional enzyme which is responsible for allene oxide biosynthesis via a two-step reaction which involves conversion of arachidonic acid to a 8R-hydroperoxide intermediate followed by conversion of the hydroperoxide to allene oxide.

2 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 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Protein has several cofactor binding sites:

<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

Lipoxygenase activity is stimulated by calcium, sodium, lithium and potassium ions. Calcium binding promotes interaction with membranes and thus facilitates access to substrates.2 Publications

<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: arachidonate metabolism

This protein is involved in the pathway arachidonate metabolism, which is part of Lipid metabolism.
View all proteins of this organism that are known to be involved in the pathway arachidonate metabolism and in Lipid metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 bindingi353Iron (heme axial ligand); catalytic1
Metal bindingi387Calcium 1; via carbonyl oxygen; structural1 Publication1
Metal bindingi389Calcium 1; via carbonyl oxygen; structural1 Publication1
Metal bindingi390Calcium 2; via carbonyl oxygen; structural1 Publication1
Metal bindingi391Calcium 2; structural1 Publication1
Metal bindingi416Calcium 2; structural1 Publication1
Metal bindingi417Calcium 2; via carbonyl oxygen; structural1 Publication1
Metal bindingi419Calcium 2; structural1 Publication1
Metal bindingi452Calcium 1; via carbonyl oxygen; structural1 Publication1
Metal bindingi454Calcium 1; via carbonyl oxygen; structural1 Publication1
Metal bindingi757Iron; catalytic1
Metal bindingi762Iron; catalytic1
Metal bindingi943Iron; catalytic1
Metal bindingi947Iron; catalytic1
Metal bindingi1066Iron; via carboxylate; catalytic1

<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 functionDioxygenase, Lyase, Multifunctional enzyme, Oxidoreductase
Biological processFatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism, Oxylipin biosynthesis
LigandCalcium, Heme, Iron, Metal-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
1.13.11.40, 4917

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

More...
UniPathwayi
UPA00383

Protein family/group databases

PeroxiBase, a peroxidase database

More...
PeroxiBasei
5626, PhoKatLox01

Chemistry databases

SwissLipids knowledge resource for lipid biology

More...
SwissLipidsi
SLP:000001660

<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:
Allene oxide synthase-lipoxygenase protein
Including the following 2 domains:
Allene oxide synthase (EC:4.2.1.92)
Alternative name(s):
Hydroperoxidehydrase
Arachidonate 8-lipoxygenase (EC:1.13.11.40)
<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>OrganismiPlexaura homomalla (Black sea rod)
<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 identifieri47982 [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 lineageiEukaryotaMetazoaCnidariaAnthozoaOctocoralliaAlcyonaceaHolaxoniaPlexauridaePlexaura

<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

Cytoplasm, Membrane

<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>Mutagenesisi411D → A: Reduces stimulation of LOX-activity by calcium and membrane binding. Abolishes stimulation of LOX-activity by calcium and membrane binding; when associated with A-419. 1 Publication1
Mutagenesisi413W → A: Reduces stimulation of LOX-activity by calcium and membrane binding. 1 Publication1
Mutagenesisi419E → A: Reduces stimulation of LOX-activity by calcium and membrane binding. Abolishes stimulation of LOX-activity by calcium and membrane binding; when associated with A-411. 1 Publication1
Mutagenesisi449W → A: Reduces LOX-activity in the absence of membranes and increases activity in the presence of liposomes. May alter protein structure. 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 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_00002207241 – 1066Allene oxide synthase-lipoxygenase proteinAdd BLAST1066

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
O16025

<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

Dimer.

2 Publications

<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

11066
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
O16025

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
O16025

<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>Domaini374 – 490PLATPROSITE-ProRule annotationAdd BLAST117
Domaini491 – 1066LipoxygenasePROSITE-ProRule annotationAdd BLAST576

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>Regioni1 – 371Allene oxide synthaseAdd BLAST371
Regioni372 – 1066Arachidonate 8-lipoxygenaseAdd BLAST695

<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

In the C-terminal section; belongs to the lipoxygenase family.Curated

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.40.180.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR037060, Catalase_core_sf
IPR020835, Catalase_sf
IPR000907, LipOase
IPR013819, LipOase_C
IPR036226, LipOase_C_sf
IPR020834, LipOase_CS
IPR020833, LipOase_Fe_BS
IPR001885, LipOase_mml
IPR001024, PLAT/LH2_dom
IPR036392, PLAT/LH2_dom_sf

The PANTHER Classification System

More...
PANTHERi
PTHR11771, PTHR11771, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00305, Lipoxygenase, 1 hit
PF01477, PLAT, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00087, LIPOXYGENASE
PR00467, MAMLPOXGNASE

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
SSF48484, SSF48484, 1 hit
SSF49723, SSF49723, 1 hit
SSF56634, SSF56634, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00711, LIPOXYGENASE_1, 1 hit
PS00081, LIPOXYGENASE_2, 1 hit
PS51393, LIPOXYGENASE_3, 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.

O16025-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MTWKNFGFEI FGEKYGQEEL EKRIKDEHTP PPDSPVFGGL KLKLKKEKFK
60 70 80 90 100
TLFTLGTTLK GFRRATHTVG TGGIGEITIV NDPKFPEHEF FTAGRTFPAR
110 120 130 140 150
LRHANLKYPD DAGADARSFS IKFADSDSDG PLDIVMNTGE ANIFWNSPSL
160 170 180 190 200
EDFVPVEEGD AAEEYVYKNP YYYYNLVEAL RRAPDTFAHL YYYSQVTMPF
210 220 230 240 250
KAKDGKVRYC RYRALPGDVD IKEEDESGRL TEEEQRKIWI FSRHENEKRP
260 270 280 290 300
DDYLRKEYVE RLQKGPVNYR LQIQIHEASP DDTATIFHAG ILWDKETHPW
310 320 330 340 350
FDLAKVSIKT PLSPDVLEKT AFNIANQPAS LGLLEAKSPE DYNSIGELRV
360 370 380 390 400
AVYTWVQHLR KLKIGSLVPA GQNAIYNVEV ETGDREHAGT DATITIRITG
410 420 430 440 450
AKGRTDYLKL DKWFHNDFEA GSKEQYTVQG FDVGDIQLIE LHSDGGGYWS
460 470 480 490 500
GDPDWFVNRV IIISSTQDRV YSFPCFRWVI KDMVLFPGEA TLPFNEVPAI
510 520 530 540 550
VSEQRQKELE QRKLTYQWDY VSDDMPGNIK AKTHDDLPRD VQFTDEKSRS
560 570 580 590 600
YQESRKAALV NLGIGSLFTM FENWDSYDDY HILYRNWILG GTPNMADRWH
610 620 630 640 650
EDRWFGYQFL NGANPVILTR CDALPSNFPV TNEHVNASLD RGKNLDEEIK
660 670 680 690 700
DGHIYIVDFK VLVGAKSYGG PVLEDIGYKV PDHLKHDEAD IRYCAAPLAL
710 720 730 740 750
FYVNKLGHLM PIAIQINQEP GPENPIWTPH EENEHDWMMA KFWLGVAESN
760 770 780 790 800
FHQLNTHLLR THLTTESFAL STWRNLASAH PVFKLLQPHI YGVLAIDTIG
810 820 830 840 850
RKELIGSGGI VDQSLSLGGG GHVTFMEKCF KEVNLQDYHL PNALKKRGVD
860 870 880 890 900
DPSKLPGFYY RDDGLALWEA IETFIGEIIA IFYKNDDDVK RDNEIQSWIY
910 920 930 940 950
DVHKNGWRVN PGHQDHGVPA SFESREQLKE VLTSLVFTFS CQHAAVNFSQ
960 970 980 990 1000
KDHYGFTPNA PAVLRHPPPK KKGEATLQSI LSTLPSKSQA AKAIATVYIL
1010 1020 1030 1040 1050
TKFSEDERYL GNYSATAWED KDALDAINRF QDKLEDISKK IKQRNENLEV
1060
PYIYLLPERI PNGTAI
Length:1,066
Mass (Da):121,783
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:iDD26886BD1EE95D7
GO

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
AF003692 mRNA Translation: AAC47743.1

Protein sequence database of the Protein Information Resource

More...
PIRi
T30903

<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
AF003692 mRNA Translation: AAC47743.1
PIRiT30903

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
1U5UX-ray2.00A/B1-374[»]
2FNQX-ray3.20A/B374-1066[»]
3DY5X-ray3.51A/C1-1066[»]
3FG1X-ray1.85A/B/C/D374-1066[»]
3FG3X-ray1.90A/B/C/D374-1066[»]
3FG4X-ray2.31A/B/C/D374-1066[»]
4QWTX-ray2.00A/B/C/D374-1066[»]
SMRiO16025
ModBaseiSearch...
PDBe-KBiSearch...

Chemistry databases

SwissLipidsiSLP:000001660

Protein family/group databases

PeroxiBasei5626, PhoKatLox01

Proteomic databases

PRIDEiO16025

Enzyme and pathway databases

UniPathwayiUPA00383
BRENDAi1.13.11.40, 4917

Miscellaneous databases

EvolutionaryTraceiO16025

Family and domain databases

Gene3Di2.40.180.10, 1 hit
InterProiView protein in InterPro
IPR037060, Catalase_core_sf
IPR020835, Catalase_sf
IPR000907, LipOase
IPR013819, LipOase_C
IPR036226, LipOase_C_sf
IPR020834, LipOase_CS
IPR020833, LipOase_Fe_BS
IPR001885, LipOase_mml
IPR001024, PLAT/LH2_dom
IPR036392, PLAT/LH2_dom_sf
PANTHERiPTHR11771, PTHR11771, 1 hit
PfamiView protein in Pfam
PF00305, Lipoxygenase, 1 hit
PF01477, PLAT, 1 hit
PRINTSiPR00087, LIPOXYGENASE
PR00467, MAMLPOXGNASE
SMARTiView protein in SMART
SM00308, LH2, 1 hit
SUPFAMiSSF48484, SSF48484, 1 hit
SSF49723, SSF49723, 1 hit
SSF56634, SSF56634, 1 hit
PROSITEiView protein in PROSITE
PS00711, LIPOXYGENASE_1, 1 hit
PS00081, LIPOXYGENASE_2, 1 hit
PS51393, LIPOXYGENASE_3, 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 nameiAOSL_PLEHO
<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: O16025
<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: September 19, 2002
Last sequence update: January 1, 1998
Last modified: June 2, 2021
This is version 112 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)

<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

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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