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Entry version 98 (11 Dec 2019)
Sequence version 1 (26 Apr 2005)
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Protein

Dolichyl-phosphate-mannose--protein mannosyltransferase 2

Gene

PMT2

Organism
Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
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

Protein mannosyltransferase (PMT) involved in hyphal growth and drug sensitivity. Transfers mannose from Dol-P-mannose to Ser or Thr residues on proteins. PMT1, PMT2 and PMT4 account for most of the protein-O-glycosylation activity, while PMT5 and PMT6 may specifically modulate a much narrower spectrum of target proteins. Essential protein that plays an important role in virulence.1 Publication

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

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

This protein is involved in the pathway protein glycosylation, which is part of Protein modification.Curated
View all proteins of this organism that are known to be involved in the pathway protein glycosylation and in Protein modification.

<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 functionGlycosyltransferase, Transferase
Biological processVirulence

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.4.1.109 1096

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

More...
UniPathwayi
UPA00378

<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:
Dolichyl-phosphate-mannose--protein mannosyltransferase 2Curated (EC:2.4.1.1091 PublicationBy similarity)
Short name:
Protein mannosyltransferase 2
<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:PMT21 Publication
Ordered Locus Names:CAALFM_C306890WA
ORF Names:CaO19.14104, CaO19.6812
<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>OrganismiCandida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
<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 identifieri237561 [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 lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeCandida/Lodderomyces cladeCandida
<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
  • UP000000559 <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 3

Organism-specific databases

Candida Genome Database

More...
CGDi
CAL0000187219 PMT2

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
FungiDB:C3_06890W_A

<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 Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei59 – 79Helical; Name=1Sequence analysisAdd BLAST21
Transmembranei152 – 169Helical; Name=2Sequence analysisAdd BLAST18
Transmembranei176 – 194Helical; Name=3Sequence analysisAdd BLAST19
Transmembranei200 – 218Helical; Name=4Sequence analysisAdd BLAST19
Transmembranei252 – 272Helical; Name=5Sequence analysisAdd BLAST21
Transmembranei288 – 308Helical; Name=6Sequence analysisAdd BLAST21
Transmembranei615 – 635Helical; Name=7Sequence analysisAdd BLAST21
Transmembranei655 – 675Helical; Name=8Sequence analysisAdd BLAST21
Transmembranei679 – 699Helical; Name=9Sequence analysisAdd BLAST21
Transmembranei718 – 738Helical; Name=10Sequence analysisAdd BLAST21

Keywords - Cellular componenti

Endoplasmic reticulum, 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

<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

Disruption of both alleles leads to letality. Disruption of only one allele impairs filamentation and leads to an altered cell wall composition with reduced amounts of beta-1,6-glucan and shows reduced virulence in a mouse model of hematogenously disseminated candidiasis (HDC) and using reconstituted human epithelium (RHE).2 Publications

<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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004305771 – 769Dolichyl-phosphate-mannose--protein mannosyltransferase 2Add BLAST769

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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>Glycosylationi8N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi132N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi226N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi324N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi408N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi453N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi462N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1

Keywords - PTMi

Glycoprotein

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
Q5ADM9

<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 reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Transcribed in the yeast form, but expression is increased two to threefold during hyphal induction. Also induced during cell wall regeneration. Up-regulated more than twofold when PMT1 expression is impaired. MSB2 functions not only to secure basal levels of the PMT2 transcripts but is needed also for up-regulation of both transcripts upon PMT1 inhibition.3 Publications

<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

PMT1 and PMT2 form a functional heterodimer.

By similarity

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
5476.C4YP57

<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>Domaini342 – 397MIR 1PROSITE-ProRule annotationAdd BLAST56
Domaini412 – 468MIR 2PROSITE-ProRule annotationAdd BLAST57
Domaini474 – 534MIR 3PROSITE-ProRule annotationAdd BLAST61

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi40 – 43Poly-AspSequence analysis4

<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 glycosyltransferase 39 family.Curated

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q5ADM9

KEGG Orthology (KO)

More...
KOi
K00728

Identification of Orthologs from Complete Genome Data

More...
OMAi
FWAMGRV

Database of Orthologous Groups

More...
OrthoDBi
203029at2759

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR027005 GlyclTrfase_39-like
IPR003342 Glyco_trans_39/83
IPR036300 MIR_dom_sf
IPR016093 MIR_motif
IPR032421 PMT_4TMC

The PANTHER Classification System

More...
PANTHERi
PTHR10050 PTHR10050, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF02815 MIR, 1 hit
PF02366 PMT, 1 hit
PF16192 PMT_4TMC, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00472 MIR, 3 hits

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF82109 SSF82109, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50919 MIR, 3 hits

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

Q5ADM9-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSTSVEPNET EALLRKQNDL STTASIEEKY PHQQGEAAED DDDTLKRTQY
60 70 80 90 100
DEAKETAESL KQVESILAPI VFTALSFFVR FYRISVNDHV VWDEAHFGKF
110 120 130 140 150
GSYYLRHEFY HDVHPPLGKM LVGLSGYLAG YNGSWDFPSG EKYPDYIDYT
160 170 180 190 200
KMRLFNATFS ALCVPLAYFT GKEVGFSMFT TWLFTLMVAL ESSYVTLGKF
210 220 230 240 250
ILLDSMLLFF TVATVFCFSR FNNFNNKSQE FSRKWWKWIL LTGVSIGCTC
260 270 280 290 300
SVKMVGLFVT TLVGIYTVVD LWNKLSDKSI SWTKYIQHWF ARIVALILVP
310 320 330 340 350
IFIFMLSFKV HFDLLYKSGT GDANMSSLFQ ANLAGSDVGG GPREVSMFHS
360 370 380 390 400
VITLKNQGLS GGLLHSHVQT FPEGSKQQQV TTYGHKDSNN NWIFQRARGQ
410 420 430 440 450
PYYDTSGNTT DIEYIFDGMH VRLMHPQTGR NLHTHDIPAP VSKSEYEVAC
460 470 480 490 500
YGNLTIGDPK DNWTVEIMEQ ASDEDKMRLH PLTSSFRLKN EVMNCYLGVT
510 520 530 540 550
GTTLPQWGFR QGEVVCYKNP FKKDKRTWWN IENNRNAVLP PAPEDFKLPK
560 570 580 590 600
TKFIRDFIQL NLAMMATNNA LVPDTEKQDD LASSFWQWPT LNVGIRMCGW
610 620 630 640 650
GPENPKYYMI GSPATTWTST VGVILFAFIV LYYLIRWQRQ YVDFPSTNPH
660 670 680 690 700
KLKLFLMGGI YPMFGWGLHF LPFAIMGRVT YVHHYVPALY FAMLVFCYEV
710 720 730 740 750
ESFSSRLNKP NASPVSKLLY LAIYIGLLSL VAGTFWYFRY LSWGMEGPKE
760
DWKHLKLLES WRVSDDQYT
Length:769
Mass (Da):88,372
Last modified:April 26, 2005 - 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:i4E847200A44585C0
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
CP017625 Genomic DNA Translation: AOW28694.1

NCBI Reference Sequences

More...
RefSeqi
XP_719907.1, XM_714814.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
3638538

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
cal:CAALFM_C306890WA

<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
CP017625 Genomic DNA Translation: AOW28694.1
RefSeqiXP_719907.1, XM_714814.1

3D structure databases

Database of comparative protein structure models

More...
ModBasei
Search...

SWISS-MODEL Interactive Workspace

More...
SWISS-MODEL-Workspacei
Submit a new modelling project...

Protein-protein interaction databases

STRINGi5476.C4YP57

Proteomic databases

PRIDEiQ5ADM9

Genome annotation databases

GeneIDi3638538
KEGGical:CAALFM_C306890WA

Organism-specific databases

CGDiCAL0000187219 PMT2
EuPathDBiFungiDB:C3_06890W_A

Phylogenomic databases

InParanoidiQ5ADM9
KOiK00728
OMAiFWAMGRV
OrthoDBi203029at2759

Enzyme and pathway databases

UniPathwayiUPA00378
BRENDAi2.4.1.109 1096

Miscellaneous databases

Protein Ontology

More...
PROi
PR:Q5ADM9

Family and domain databases

InterProiView protein in InterPro
IPR027005 GlyclTrfase_39-like
IPR003342 Glyco_trans_39/83
IPR036300 MIR_dom_sf
IPR016093 MIR_motif
IPR032421 PMT_4TMC
PANTHERiPTHR10050 PTHR10050, 1 hit
PfamiView protein in Pfam
PF02815 MIR, 1 hit
PF02366 PMT, 1 hit
PF16192 PMT_4TMC, 1 hit
SMARTiView protein in SMART
SM00472 MIR, 3 hits
SUPFAMiSSF82109 SSF82109, 1 hit
PROSITEiView protein in PROSITE
PS50919 MIR, 3 hits

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

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 nameiPMT2_CANAL
<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: Q5ADM9
Secondary accession number(s): A0A1D8PKL8
<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: October 29, 2014
Last sequence update: April 26, 2005
Last modified: December 11, 2019
This is version 98 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 programFungal 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
  3. Candida albicans
    Candida albicans: entries and gene names
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