KCNK2_MOUSE
ID KCNK2_MOUSE Reviewed; 426 AA.
AC P97438; Q4VQI2;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 3.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Potassium channel subfamily K member 2;
DE AltName: Full=Outward rectifying potassium channel protein TREK-1;
DE AltName: Full=TREK-1 K(+) channel subunit {ECO:0000303|PubMed:10321245, ECO:0000303|PubMed:24496152};
DE AltName: Full=Two pore potassium channel TPKC1;
GN Name=Kcnk2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC TISSUE=Brain;
RX PubMed=9003761; DOI=10.1002/j.1460-2075.1996.tb01077.x;
RA Fink M., Duprat F., Lesage F., Reyes R., Romey G., Heurteaux C.,
RA Lazdunski M.;
RT "Cloning, functional expression and brain localization of a novel
RT unconventional outward rectifier K+ channel.";
RL EMBO J. 15:6854-6862(1996).
RN [2]
RP SEQUENCE REVISION.
RA Fink M., Duprat F., Lesage F., Reyes R., Romey G., Heurteaux C.,
RA Lazdunski M.;
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=BALB/cJ;
RX PubMed=16636285; DOI=10.1073/pnas.0600463103;
RA Honore E., Patel A.J., Chemin J., Suchyna T., Sachs F.;
RT "Desensitization of mechano-gated K2P channels.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:6859-6864(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND ACTIVITY REGULATION.
RX PubMed=10321245; DOI=10.1038/8084;
RA Patel A.J., Honore E., Lesage F., Fink M., Romey G., Lazdunski M.;
RT "Inhalational anesthetics activate two-pore-domain background K+
RT channels.";
RL Nat. Neurosci. 2:422-426(1999).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-348, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP INTERACTION WITH BVES, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=22354168; DOI=10.1172/jci59410;
RA Froese A., Breher S.S., Waldeyer C., Schindler R.F., Nikolaev V.O.,
RA Rinne S., Wischmeyer E., Schlueter J., Becher J., Simrick S., Vauti F.,
RA Kuhtz J., Meister P., Kreissl S., Torlopp A., Liebig S.K., Laakmann S.,
RA Mueller T.D., Neumann J., Stieber J., Ludwig A., Maier S.K., Decher N.,
RA Arnold H.H., Kirchhof P., Fabritz L., Brand T.;
RT "Popeye domain containing proteins are essential for stress-mediated
RT modulation of cardiac pacemaking in mice.";
RL J. Clin. Invest. 122:1119-1130(2012).
RN [8]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, INTERACTION WITH KCNK1, TISSUE
RP SPECIFICITY, DISULFIDE BOND, AND MUTAGENESIS OF CYS-108.
RX PubMed=24496152; DOI=10.1038/ncomms4227;
RA Hwang E.M., Kim E., Yarishkin O., Woo D.H., Han K.S., Park N., Bae Y.,
RA Woo J., Kim D., Park M., Lee C.J., Park J.Y.;
RT "A disulphide-linked heterodimer of TWIK-1 and TREK-1 mediates passive
RT conductance in astrocytes.";
RL Nat. Commun. 5:3227-3227(2014).
RN [9]
RP INTERACTION WITH BVES.
RX PubMed=26642364; DOI=10.1172/jci79562;
RA Schindler R.F., Scotton C., Zhang J., Passarelli C., Ortiz-Bonnin B.,
RA Simrick S., Schwerte T., Poon K.L., Fang M., Rinne S., Froese A.,
RA Nikolaev V.O., Grunert C., Mueller T., Tasca G., Sarathchandra P.,
RA Drago F., Dallapiccola B., Rapezzi C., Arbustini E., Di Raimo F.R.,
RA Neri M., Selvatici R., Gualandi F., Fattori F., Pietrangelo A., Li W.,
RA Jiang H., Xu X., Bertini E., Decher N., Wang J., Brand T., Ferlini A.;
RT "POPDC1S201F causes muscular dystrophy and arrhythmia by affecting protein
RT trafficking.";
RL J. Clin. Invest. 126:239-253(2016).
CC -!- FUNCTION: Ion channel that contributes to passive transmembrane
CC potassium transport. Reversibly converts between a voltage-insensitive
CC potassium leak channel and a voltage-dependent outward rectifying
CC potassium channel in a phosphorylation-dependent manner. In astrocytes,
CC forms mostly heterodimeric potassium channels with KCNK1, with only a
CC minor proportion of functional channels containing homodimeric KCNK2
CC (PubMed:24496152). In astrocytes, the heterodimer formed by KCNK1 and
CC KCNK2 is required for rapid glutamate release in response to activation
CC of G-protein coupled receptors, such as F2R and CNR1 (PubMed:24496152).
CC {ECO:0000269|PubMed:10321245, ECO:0000269|PubMed:16636285,
CC ECO:0000269|PubMed:24496152, ECO:0000269|PubMed:9003761}.
CC -!- ACTIVITY REGULATION: Inhibited by barium (PubMed:9003761). Activated by
CC volatile general anesthetics such as chloroform, diethyl ether,
CC halothane and isoflurane (PubMed:10321245).
CC {ECO:0000269|PubMed:10321245, ECO:0000269|PubMed:9003761}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Note=Channel activation is extremely rapid (PubMed:9003761). Single
CC channel conductance is about 14 pS (PubMed:9003761).
CC {ECO:0000269|PubMed:9003761};
CC -!- SUBUNIT: Homodimer; disulfide-linked (PubMed:24496152). Heterodimer
CC with KCNK1; disulfide-linked (PubMed:24496152). Interacts with BVES;
CC the interaction enhances KCNK2 surface expression and is inhibited by
CC cAMP (PubMed:22354168, PubMed:26642364). {ECO:0000269|PubMed:22354168,
CC ECO:0000269|PubMed:24496152, ECO:0000269|PubMed:26642364, ECO:0000305}.
CC -!- INTERACTION:
CC P97438; D3YVF0: Akap5; NbExp=4; IntAct=EBI-7091062, EBI-7091108;
CC P97438; Q6PHU5: Sort1; NbExp=4; IntAct=EBI-7091062, EBI-6985663;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane
CC {ECO:0000269|PubMed:10321245, ECO:0000269|PubMed:16636285,
CC ECO:0000269|PubMed:22354168, ECO:0000269|PubMed:24496152}; Multi-pass
CC membrane protein {ECO:0000305}. Note=Location at the cell membrane
CC requires interaction with KCNK1. Is not detected at the cell membrane
CC when KCNK1 is absent. {ECO:0000269|PubMed:24496152}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane
CC {ECO:0000269|PubMed:9003761}; Multi-pass membrane protein
CC {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=TREK-1b;
CC IsoId=P97438-1; Sequence=Displayed;
CC Name=2; Synonyms=TREK-1a;
CC IsoId=P97438-2; Sequence=VSP_053951;
CC -!- TISSUE SPECIFICITY: Detected in hippocampus astrocytes (at protein
CC level) (PubMed:24496152). High expression in brain and lung. Also
CC detected in kidney, heart and skeletal muscle. Not detected in liver.
CC In the brain, highest expression in olfactory bulb, hippocampus and
CC cerebellum. {ECO:0000269|PubMed:22354168, ECO:0000269|PubMed:24496152,
CC ECO:0000269|PubMed:9003761}.
CC -!- PTM: Phosphorylation at Ser-348 controls the reversible conversion from
CC a leak channel to a voltage-dependent channel. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the two pore domain potassium channel (TC
CC 1.A.1.8) family. {ECO:0000305}.
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DR EMBL; U73488; AAC53005.2; -; mRNA.
DR EMBL; AY736359; AAV48996.1; -; mRNA.
DR EMBL; AC121882; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC124527; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS48480.1; -. [P97438-1]
DR CCDS; CCDS48481.1; -. [P97438-2]
DR RefSeq; NP_001153322.1; NM_001159850.1. [P97438-1]
DR RefSeq; NP_034737.2; NM_010607.3. [P97438-2]
DR PDB; 6CQ6; X-ray; 3.10 A; A/B=35-337.
DR PDB; 6CQ8; X-ray; 3.00 A; A/B=35-337.
DR PDB; 6CQ9; X-ray; 2.80 A; A/B=35-339.
DR PDB; 6V36; X-ray; 3.40 A; A/B=35-338.
DR PDB; 6V37; X-ray; 2.80 A; A/B=35-338.
DR PDB; 6V3C; X-ray; 3.51 A; A/B=35-338.
DR PDB; 6V3I; X-ray; 3.40 A; A/B=35-338.
DR PDB; 6W7B; X-ray; 3.88 A; A/B=35-339.
DR PDB; 6W7C; X-ray; 3.40 A; A/B=35-339.
DR PDB; 6W7D; X-ray; 3.50 A; A/B=36-337.
DR PDB; 6W7E; X-ray; 3.29 A; A/B=35-337.
DR PDB; 6W82; X-ray; 3.60 A; A/B=36-337.
DR PDB; 6W83; X-ray; 3.90 A; A/B=36-337.
DR PDB; 6W84; X-ray; 3.70 A; A/B=36-337.
DR PDB; 6W85; X-ray; 3.80 A; A/B=36-337.
DR PDB; 6W86; X-ray; 3.30 A; A/B=36-337.
DR PDB; 6W87; X-ray; 3.20 A; A/B=36-337.
DR PDB; 6W88; X-ray; 3.20 A; A/B=36-337.
DR PDB; 6W8A; X-ray; 3.00 A; A/B=36-337.
DR PDB; 6W8C; X-ray; 2.60 A; A/B=36-337.
DR PDB; 6W8F; X-ray; 3.40 A; A/B=36-337.
DR PDBsum; 6CQ6; -.
DR PDBsum; 6CQ8; -.
DR PDBsum; 6CQ9; -.
DR PDBsum; 6V36; -.
DR PDBsum; 6V37; -.
DR PDBsum; 6V3C; -.
DR PDBsum; 6V3I; -.
DR PDBsum; 6W7B; -.
DR PDBsum; 6W7C; -.
DR PDBsum; 6W7D; -.
DR PDBsum; 6W7E; -.
DR PDBsum; 6W82; -.
DR PDBsum; 6W83; -.
DR PDBsum; 6W84; -.
DR PDBsum; 6W85; -.
DR PDBsum; 6W86; -.
DR PDBsum; 6W87; -.
DR PDBsum; 6W88; -.
DR PDBsum; 6W8A; -.
DR PDBsum; 6W8C; -.
DR PDBsum; 6W8F; -.
DR AlphaFoldDB; P97438; -.
DR SMR; P97438; -.
DR DIP; DIP-58579N; -.
DR IntAct; P97438; 3.
DR MINT; P97438; -.
DR STRING; 10090.ENSMUSP00000078416; -.
DR TCDB; 1.A.1.9.1; the voltage-gated ion channel (vic) superfamily.
DR GlyGen; P97438; 2 sites.
DR iPTMnet; P97438; -.
DR PhosphoSitePlus; P97438; -.
DR PaxDb; P97438; -.
DR PRIDE; P97438; -.
DR ProteomicsDB; 269268; -. [P97438-1]
DR ProteomicsDB; 269269; -. [P97438-2]
DR Antibodypedia; 34619; 126 antibodies from 20 providers.
DR DNASU; 16526; -.
DR Ensembl; ENSMUST00000110920; ENSMUSP00000106545; ENSMUSG00000037624. [P97438-2]
DR Ensembl; ENSMUST00000192723; ENSMUSP00000141849; ENSMUSG00000037624. [P97438-2]
DR Ensembl; ENSMUST00000193319; ENSMUSP00000141891; ENSMUSG00000037624. [P97438-1]
DR GeneID; 16526; -.
DR KEGG; mmu:16526; -.
DR UCSC; uc007eak.2; mouse. [P97438-1]
DR UCSC; uc011wyj.2; mouse. [P97438-2]
DR CTD; 3776; -.
DR MGI; MGI:109366; Kcnk2.
DR VEuPathDB; HostDB:ENSMUSG00000037624; -.
DR eggNOG; KOG1418; Eukaryota.
DR GeneTree; ENSGT00940000156560; -.
DR HOGENOM; CLU_022504_10_0_1; -.
DR InParanoid; P97438; -.
DR OMA; TSQISHW; -.
DR PhylomeDB; P97438; -.
DR TreeFam; TF313947; -.
DR Reactome; R-MMU-1299503; TWIK related potassium channel (TREK).
DR Reactome; R-MMU-5576886; Phase 4 - resting membrane potential.
DR BioGRID-ORCS; 16526; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Kcnk2; mouse.
DR PRO; PR:P97438; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; P97438; protein.
DR Bgee; ENSMUSG00000037624; Expressed in caudate-putamen and 220 other tissues.
DR ExpressionAtlas; P97438; baseline and differential.
DR Genevisible; P97438; MM.
DR GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
DR GO; GO:0097449; C:astrocyte projection; ISO:MGI.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:0043679; C:axon terminus; ISO:MGI.
DR GO; GO:0044305; C:calyx of Held; ISO:MGI.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; IDA:MGI.
DR GO; GO:0015271; F:outward rectifier potassium channel activity; ISS:UniProtKB.
DR GO; GO:0019870; F:potassium channel inhibitor activity; ISO:MGI.
DR GO; GO:0022841; F:potassium ion leak channel activity; ISS:UniProtKB.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; IDA:MGI.
DR GO; GO:0003231; P:cardiac ventricle development; IEA:Ensembl.
DR GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl.
DR GO; GO:0090102; P:cochlea development; IEA:Ensembl.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IDA:MGI.
DR GO; GO:0007613; P:memory; IEA:Ensembl.
DR GO; GO:0060044; P:negative regulation of cardiac muscle cell proliferation; ISO:MGI.
DR GO; GO:2000279; P:negative regulation of DNA biosynthetic process; ISO:MGI.
DR GO; GO:0010942; P:positive regulation of cell death; ISO:MGI.
DR GO; GO:1900039; P:positive regulation of cellular response to hypoxia; ISO:MGI.
DR GO; GO:0071805; P:potassium ion transmembrane transport; ISO:MGI.
DR GO; GO:0006813; P:potassium ion transport; IDA:MGI.
DR GO; GO:0042391; P:regulation of membrane potential; IGI:MGI.
DR GO; GO:0048678; P:response to axon injury; IEA:Ensembl.
DR GO; GO:0009612; P:response to mechanical stimulus; IEA:Ensembl.
DR GO; GO:0030322; P:stabilization of membrane potential; IBA:GO_Central.
DR InterPro; IPR003280; 2pore_dom_K_chnl.
DR InterPro; IPR003976; 2pore_dom_K_chnl_TREK.
DR InterPro; IPR013099; K_chnl_dom.
DR PANTHER; PTHR11003; PTHR11003; 1.
DR Pfam; PF07885; Ion_trans_2; 2.
DR PRINTS; PR01333; 2POREKCHANEL.
DR PRINTS; PR01499; TREKCHANNEL.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Disulfide bond;
KW Glycoprotein; Ion channel; Ion transport; Membrane; Phosphoprotein;
KW Potassium; Potassium channel; Potassium transport; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..426
FT /note="Potassium channel subfamily K member 2"
FT /id="PRO_0000101743"
FT TOPO_DOM 1..61
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 62..82
FT /note="Helical"
FT /evidence="ECO:0000255"
FT INTRAMEM 144..170
FT /note="Pore-forming; Name=Pore-forming 1"
FT /evidence="ECO:0000255"
FT TRANSMEM 172..192
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 193..222
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 223..243
FT /note="Helical"
FT /evidence="ECO:0000255"
FT INTRAMEM 253..283
FT /note="Pore-forming; Name=Pore-forming 2"
FT /evidence="ECO:0000255"
FT TRANSMEM 288..308
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 309..426
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 369..426
FT /note="Required for basal channel activity"
FT REGION 393..426
FT /note="Essential for chloroform and halothane sensitivity"
FT MOD_RES 348
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 134
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 108
FT /note="Interchain"
FT /evidence="ECO:0000269|PubMed:24496152"
FT VAR_SEQ 2..16
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9003761"
FT /id="VSP_053951"
FT MUTAGEN 108
FT /note="C->S: Abolishes formation of a disulfide-linked
FT heterodimer with KCNK1."
FT /evidence="ECO:0000269|PubMed:24496152"
FT CONFLICT 78
FT /note="T -> A (in Ref. 2; AAC53005)"
FT /evidence="ECO:0000305"
FT HELIX 51..104
FT /evidence="ECO:0007829|PDB:6W8C"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:6V36"
FT HELIX 111..125
FT /evidence="ECO:0007829|PDB:6W8C"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:6W8A"
FT HELIX 144..155
FT /evidence="ECO:0007829|PDB:6W8C"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:6W7E"
FT HELIX 168..207
FT /evidence="ECO:0007829|PDB:6W8C"
FT TURN 208..211
FT /evidence="ECO:0007829|PDB:6W8C"
FT STRAND 212..216
FT /evidence="ECO:0007829|PDB:6W8C"
FT HELIX 220..237
FT /evidence="ECO:0007829|PDB:6W8C"
FT HELIX 239..249
FT /evidence="ECO:0007829|PDB:6W8C"
FT HELIX 253..264
FT /evidence="ECO:0007829|PDB:6W8C"
FT STRAND 270..272
FT /evidence="ECO:0007829|PDB:6W8C"
FT TURN 274..276
FT /evidence="ECO:0007829|PDB:6CQ9"
FT STRAND 277..279
FT /evidence="ECO:0007829|PDB:6CQ9"
FT HELIX 285..333
FT /evidence="ECO:0007829|PDB:6W8C"
SQ SEQUENCE 426 AA; 46844 MW; 8C298C01F5BDB61A CRC64;
MLASASRERP GYTAGVAAPD LLDPKSAAQN SKPRLSFSSK PTVLASRVES DSAINVMKWK
TVSTIFLVVV LYLIIGATVF KALEQPQEIS QRTTIVIQKQ TFIAQHACVN STELDELIQQ
IVAAINAGII PLGNSSNQVS HWDLGSSFFF AGTVITTIGF GNISPRTEGG KIFCIIYALL
GIPLFGFLLA GVGDQLGTIF GKGIAKVEDT FIKWNVSQTK IRIISTIIFI LFGCVLFVAL
PAVIFKHIEG WSALDAIYFV VITLTTIGFG DYVAGGSDIE YLDFYKPVVW FWILVGLAYF
AAVLSMIGDW LRVISKKTKE EVGEFRAHAA EWTANVTAEF KETRRRLSVE IYDKFQRATS
VKRKLSAELA GNHNQELTPC RRTLSVNHLT SEREVLPPLL KAESIYLNGL TPHCAGEDIA
VIENMK
