RNC_MOUSE
ID RNC_MOUSE Reviewed; 1373 AA.
AC Q5HZJ0;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Ribonuclease 3;
DE EC=3.1.26.3 {ECO:0000250|UniProtKB:Q9NRR4};
DE AltName: Full=Protein Drosha;
DE AltName: Full=Ribonuclease III;
DE Short=RNase III;
GN Name=Drosha; Synonyms=Etohi2, Rn3, Rnasen;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryonic stem cell, and Sympathetic ganglion;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryonic brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP INTERACTION WITH SRRT.
RX PubMed=19632182; DOI=10.1016/j.cell.2009.04.046;
RA Gruber J.J., Zatechka D.S., Sabin L.R., Yong J., Lum J.J., Kong M.,
RA Zong W.-X., Zhang Z., Lau C.-K., Rawlings J., Cherry S., Ihle J.N.,
RA Dreyfuss G., Thompson C.B.;
RT "Ars2 links the nuclear cap-binding complex to RNA interference and cell
RT proliferation.";
RL Cell 138:328-339(2009).
RN [4]
RP FUNCTION, AND INTERACTION WITH CPSF3; DGCR8 AND ISY1.
RX PubMed=26255770; DOI=10.1016/j.cell.2015.07.008;
RA Du P., Wang L., Sliz P., Gregory R.I.;
RT "A biogenesis step upstream of microprocessor controls miR-17~92
RT expression.";
RL Cell 162:885-899(2015).
CC -!- FUNCTION: Ribonuclease III double-stranded (ds) RNA-specific
CC endoribonuclease that is involved in the initial step of microRNA
CC (miRNA) biogenesis. Component of the microprocessor complex that is
CC required to process primary miRNA transcripts (pri-miRNAs) to release
CC precursor miRNA (pre-miRNA) in the nucleus. Within the microprocessor
CC complex, DROSHA cleaves the 3' and 5' strands of a stem-loop in pri-
CC miRNAs (processing center 11 bp from the dsRNA-ssRNA junction) to
CC release hairpin-shaped pre-miRNAs that are subsequently cut by the
CC cytoplasmic DICER to generate mature miRNAs (PubMed:26255770). Involved
CC also in pre-rRNA processing. Cleaves double-strand RNA and does not
CC cleave single-strand RNA. Involved in the formation of GW bodies.
CC {ECO:0000250|UniProtKB:Q9NRR4, ECO:0000269|PubMed:26255770}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.3;
CC Evidence={ECO:0000250|UniProtKB:Q9NRR4};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q9NRR4};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q9NRR4};
CC Note=Each RNase III domain binds at least one Mg(2+) or Mn(2+) ion.
CC {ECO:0000250|UniProtKB:Q9NRR4};
CC -!- SUBUNIT: Component of the microprocessor complex, or pri-miRNA
CC processing protein complex, which is composed of DROSHA and DGCR8 (By
CC similarity). The microprocessor complex is a heterotrimer; each of the
CC two DROSHA RNase III domains binds one DGCR8 (via C-terminal region)
CC (By similarity). Interacts with SP1 and SNIP1 (By similarity).
CC Interacts with SRRT/ARS2 (PubMed:19632182). Interacts with CPSF3 and
CC ISY1; this interaction is in an RNA dependent manner (PubMed:26255770).
CC Interacts with PUS10; interaction promotes pri-miRNAs processing (By
CC similarity). {ECO:0000250|UniProtKB:Q9NRR4,
CC ECO:0000269|PubMed:19632182, ECO:0000269|PubMed:26255770}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9NRR4}. Nucleus,
CC nucleolus {ECO:0000250|UniProtKB:Q9NRR4}. Note=A fraction is
CC translocated to the nucleolus during the S phase of the cell cycle.
CC Localized in GW bodies (GWBs), also known as P-bodies.
CC {ECO:0000250|UniProtKB:Q9NRR4}.
CC -!- DOMAIN: The 2 RNase III domains form an intramolecular dimer where the
CC domain 1 cuts the 3'strand while the domain 2 cleaves the 5'strand of
CC pri-miRNAs, independently of each other.
CC {ECO:0000250|UniProtKB:Q9NRR4}.
CC -!- SIMILARITY: Belongs to the ribonuclease III family. {ECO:0000305}.
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DR EMBL; AK144147; BAE25729.1; -; mRNA.
DR EMBL; AK148640; BAE28629.1; -; mRNA.
DR EMBL; BC088999; AAH88999.1; -; mRNA.
DR CCDS; CCDS49583.1; -.
DR RefSeq; NP_001123621.1; NM_001130149.1.
DR RefSeq; NP_081075.3; NM_026799.3.
DR AlphaFoldDB; Q5HZJ0; -.
DR BMRB; Q5HZJ0; -.
DR SMR; Q5HZJ0; -.
DR BioGRID; 199531; 13.
DR ComplexPortal; CPX-3081; Microprocessor complex.
DR CORUM; Q5HZJ0; -.
DR IntAct; Q5HZJ0; 1.
DR STRING; 10090.ENSMUSP00000129279; -.
DR iPTMnet; Q5HZJ0; -.
DR PhosphoSitePlus; Q5HZJ0; -.
DR EPD; Q5HZJ0; -.
DR MaxQB; Q5HZJ0; -.
DR PaxDb; Q5HZJ0; -.
DR PeptideAtlas; Q5HZJ0; -.
DR PRIDE; Q5HZJ0; -.
DR ProteomicsDB; 299851; -.
DR Antibodypedia; 22652; 291 antibodies from 37 providers.
DR DNASU; 14000; -.
DR Ensembl; ENSMUST00000090292; ENSMUSP00000087762; ENSMUSG00000022191.
DR Ensembl; ENSMUST00000169061; ENSMUSP00000129279; ENSMUSG00000022191.
DR GeneID; 14000; -.
DR KEGG; mmu:14000; -.
DR UCSC; uc007via.2; mouse.
DR CTD; 29102; -.
DR MGI; MGI:1261425; Drosha.
DR VEuPathDB; HostDB:ENSMUSG00000022191; -.
DR eggNOG; KOG1817; Eukaryota.
DR GeneTree; ENSGT00730000111052; -.
DR InParanoid; Q5HZJ0; -.
DR OMA; CSNFCEK; -.
DR OrthoDB; 935825at2759; -.
DR PhylomeDB; Q5HZJ0; -.
DR TreeFam; TF314734; -.
DR BioGRID-ORCS; 14000; 7 hits in 75 CRISPR screens.
DR ChiTaRS; Drosha; mouse.
DR PRO; PR:Q5HZJ0; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q5HZJ0; protein.
DR Bgee; ENSMUSG00000022191; Expressed in floor plate of midbrain and 226 other tissues.
DR Genevisible; Q5HZJ0; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0070877; C:microprocessor complex; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0014069; C:postsynaptic density; IDA:MGI.
DR GO; GO:0017151; F:DEAD/H-box RNA helicase binding; ISO:MGI.
DR GO; GO:0003725; F:double-stranded RNA binding; IBA:GO_Central.
DR GO; GO:0004521; F:endoribonuclease activity; IDA:MGI.
DR GO; GO:0001530; F:lipopolysaccharide binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070878; F:primary miRNA binding; IDA:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0070412; F:R-SMAD binding; ISO:MGI.
DR GO; GO:0004525; F:ribonuclease III activity; ISO:MGI.
DR GO; GO:0046332; F:SMAD binding; ISO:MGI.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; ISO:MGI.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; ISO:MGI.
DR GO; GO:0010586; P:miRNA metabolic process; IMP:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:BHF-UCL.
DR GO; GO:0031054; P:pre-miRNA processing; IDA:MGI.
DR GO; GO:0031053; P:primary miRNA processing; ISO:MGI.
DR GO; GO:0010468; P:regulation of gene expression; IMP:MGI.
DR GO; GO:0050727; P:regulation of inflammatory response; IMP:MGI.
DR GO; GO:2000628; P:regulation of miRNA metabolic process; IMP:MGI.
DR GO; GO:0045589; P:regulation of regulatory T cell differentiation; IMP:MGI.
DR GO; GO:0006396; P:RNA processing; IBA:GO_Central.
DR GO; GO:0006364; P:rRNA processing; IEA:InterPro.
DR CDD; cd19877; DSRM_RNAse_III_meta_like; 1.
DR CDD; cd00593; RIBOc; 2.
DR Gene3D; 1.10.1520.10; -; 2.
DR HAMAP; MF_00104; RNase_III; 1.
DR InterPro; IPR014720; dsRBD_dom.
DR InterPro; IPR011907; RNase_III.
DR InterPro; IPR000999; RNase_III_dom.
DR InterPro; IPR044442; RNAse_III_DSRM__animal.
DR InterPro; IPR036389; RNase_III_sf.
DR PANTHER; PTHR11207; PTHR11207; 1.
DR Pfam; PF00035; dsrm; 1.
DR Pfam; PF14622; Ribonucleas_3_3; 1.
DR Pfam; PF00636; Ribonuclease_3; 1.
DR SMART; SM00358; DSRM; 1.
DR SMART; SM00535; RIBOc; 2.
DR SUPFAM; SSF69065; SSF69065; 2.
DR PROSITE; PS50137; DS_RBD; 1.
DR PROSITE; PS00517; RNASE_3_1; 2.
DR PROSITE; PS50142; RNASE_3_2; 2.
PE 1: Evidence at protein level;
KW Endonuclease; Hydrolase; Magnesium; Manganese; Metal-binding; Nuclease;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Ribosome biogenesis;
KW RNA-binding; Zinc.
FT CHAIN 1..1373
FT /note="Ribonuclease 3"
FT /id="PRO_0000384374"
FT DOMAIN 875..1055
FT /note="RNase III 1"
FT DOMAIN 1106..1232
FT /note="RNase III 2"
FT DOMAIN 1259..1333
FT /note="DRBM"
FT REGION 1..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 119..406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 389..1364
FT /note="Necessary for interaction with DGCR8 and pri-miRNA
FT processing activity"
FT /evidence="ECO:0000250|UniProtKB:Q9NRR4"
FT REGION 447..496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..70
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..99
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..163
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..203
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..314
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..394
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 447..477
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 478..492
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 535
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9NRR4"
FT BINDING 537
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9NRR4"
FT BINDING 548
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9NRR4"
FT BINDING 560
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9NRR4"
FT BINDING 608
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9NRR4"
FT BINDING 675
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9NRR4"
FT BINDING 679
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9NRR4"
FT BINDING 968
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O67082"
FT BINDING 1025
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9NRR4"
FT BINDING 1041
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O67082"
FT BINDING 1044
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O67082"
FT BINDING 1146
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O67082"
FT BINDING 1218
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O67082"
FT BINDING 1221
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O67082"
FT SITE 1214
FT /note="Important for activity"
FT /evidence="ECO:0000250"
FT MOD_RES 354
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NRR4"
FT MOD_RES 372
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NRR4"
SQ SEQUENCE 1373 AA; 158828 MW; ED1DBEE2FFD89A6B CRC64;
MQGNTCHRMS YHPGRGCPRG RGGHGARPSA PAFRPQNLRL LHPQQPPAQY QYEPPSAPSS
SYSNSQAPSF MPPRPDFVPY PPPAAPSAQG PLPPCPVRPP YPNHQMRHPF PVPPCFPPMP
PPMPCPNNPP ASGAPPGQGT FPFMVPPPSM PHPPPPPVMP QQVNYQYPPG YSHSFPPPGF
NSYQNNSSSF PPSANSSSTP HFRHLPPYSL PKAQNERRSP ERLKHYDDHR HRDHSHGRGE
RHRSLERRER GRSPERRRPE SRYRSDYDRG RTPPPRHRSY ERSRERDRER HRHREARRSP
SLERSYKKEY KRSGRSYALP VAPEPAGCTP ELPGEMIKTT ESWAPPPENV NHRSPSREKK
RARWEEEKDR WSDSQGSGKE KNYTSIKEKE AEEVPPEKTE EEEEELLKPV WIRCTHSESY
YSSDPMDQVG DSTVVGTSRL RDLYDKFEEE LGNRQEKAKA ARPPWEPPKT KLDEDLESSS
ESECETDDDS TCSSSSDSEV FDVIAEIKRK KAHPDRLHDE LWYNDPGQMN DGPLCKCSAK
ARRTGIRHSI YPGEEAIKPC RPMTNNAGRL FHYRITVSPP TNFLTDRPTV IEYDDHEYIF
EGFSMFAHAP LTNIPLCKVI RFNIDYTIHF IEEMMPENFC VKGLELFSLF LFRDILELYD
WNLKGPLFED SPPCCPRFHF MPRFVRFLPD GGKEVLSMHQ ILLYLLRCSK ALVPEEEIAN
MLQWEELEWQ KYAEECKGMI VTNPGTKPSS VRIDQLDREQ FNPEVITFPI IVHFGIRPAQ
LSYAGDPQYQ KLWKSYVKLR HLLANSPKVK QTDKQKLAQR EEALQKIRQK NTMRREVTVE
LSSQGFWKTG IRSDVCQHAM MLPVLTHHIR YHQCLMHLDK LIGYTFQDRC LLQLAMTHPS
HHLNFGMNPD HARNSLSNCG IRQPKYGDRK VHHMHMRKKG INTLINIMSR LGQDDPTPSR
INHNERLEFL GDAVVEFLTS VHLYYLFPSL EEGGLATYRT AIVQNQHLAM LAKKLELDRF
MLYAHGPDLC RESDLRHAMA NCFEALIGAV YLEGSLEEAK QLFGRLLFND PDLREVWLNY
PLHPLQLQEP NTDRQLIETS PVLQKLTEFE EAIGVIFTHV RLLARAFTLR TVGFNHLTLG
HNQRMEFLGD SIMQLVATEY LFIHFPDHHE GHLTLLRSSL VNNRTQAKVA EELGMQEYAI
TNDKTKRPVA LRTKTLADLL ESFIAALYID KDLEYVHTFM NVCFFPRLKE FILNQDWNDP
KSQLQQCCLT LRTEGKEPDI PLYKTLQTVG PSHARTYTVA VYFKGERIGC GKGPSIQQAE
MGAAMDALEK YNFPQMAHQK RFIERKYRQE LKEMRWEREH QEREPEEAED IKK
