TDRD6_HUMAN
ID TDRD6_HUMAN Reviewed; 2096 AA.
AC O60522; B3KWU2; F5H5M3; Q5HYB1; Q5VTS4; Q6ZMX5;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 2.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Tudor domain-containing protein 6;
DE AltName: Full=Antigen NY-CO-45;
DE AltName: Full=Cancer/testis antigen 41.2;
DE Short=CT41.2;
GN Name=TDRD6 {ECO:0000312|HGNC:HGNC:21339};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1161 (ISOFORM 1), NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 887-2066 (ISOFORM 2), AND VARIANT GLU-1014.
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1073-2096 (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1271-2096 (ISOFORM 1).
RC TISSUE=Colon tumor;
RX PubMed=9610721;
RX DOI=10.1002/(sici)1097-0215(19980529)76:5<652::aid-ijc7>3.0.co;2-p;
RA Scanlan M.J., Chen Y.-T., Williamson B., Gure A.O., Stockert E.,
RA Gordan J.D., Tuereci O., Sahin U., Pfreundschuh M., Old L.J.;
RT "Characterization of human colon cancer antigens recognized by autologous
RT antibodies.";
RL Int. J. Cancer 76:652-658(1998).
CC -!- FUNCTION: Tudor domain-containing protein involved in germ cell
CC development, more specifically the formation of chromatoid body (during
CC spermiogenesis), Balbiani body (during oogenesis), germ plasm (upon
CC fertilization), and for proper miRNA expression and spliceosome
CC maturation (By similarity). Essential for RNA-dependent helicase UPF1
CC localization to chromatoid body, for UPF1-UPF2 and UPF1-DDX4
CC interactions which are required for mRNA degradation, using the
CC extended 3' UTR-triggered nonsense-mediated mRNA decay (NMD) pathway.
CC Involved in spliceosome maturation and mRNA splicing in prophase I
CC spermatocytes through interaction with arginine N-methyltransferase
CC PRMT5 and symmetrically arginine dimethylated SNRPB (small nuclear
CC ribonucleoprotein-associated protein) (By similarity).
CC {ECO:0000250|UniProtKB:F1R237, ECO:0000250|UniProtKB:P61407}.
CC -!- SUBUNIT: Found in a mRNP complex (i.e. messenger ribonucleoproteins
CC which correspond to mRNA with bound proteins), at least composed of
CC TDRD1, TDRD6, TDRD7 and DDX4. Found in a complex, at least composed of
CC PIWIL1, PIWIL2, DDX4 and TDRD6. Interacts with Tex19.1 and probably
CC Tex19.2. Interacts with PRMT5. Interacts with SNRPB (when methylated);
CC to trigger spliceosome formation. {ECO:0000250|UniProtKB:P61407}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P61407}.
CC Note=Present in chromatoid body (CB) of spermatids, also named
CC processing bodies (P-bodies) in somatic cells. Detected in the
CC multilobular cytoplasmic CBs (also called intermitochondrial cementin)
CC in pachytene spermatocytes and as a single perinuclear CB in haploid
CC round spermatids. Colocalizes in CB with DDX4, PIWIL1, PIWIL2, TDRD1
CC and TDRD7. {ECO:0000250|UniProtKB:P61407}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O60522-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O60522-2; Sequence=VSP_044801;
CC -!- DOMAIN: The tudor domains recognize and bind to proteins with
CC dimethylated arginine residues. {ECO:0000250|UniProtKB:P61407}.
CC -!- PTM: Undergoes proteolytic cleavage near the C-terminal by an unknown
CC protease during the transition from meiosis I to meiosis II in primary
CC spermatocytes. {ECO:0000250|UniProtKB:P61407}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC18034.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAI45997.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL591242; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK125838; BAG54254.1; -; mRNA.
DR EMBL; AK131455; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BX648686; CAI45997.1; ALT_INIT; mRNA.
DR EMBL; AF039442; AAC18034.1; ALT_FRAME; mRNA.
DR CCDS; CCDS34470.1; -. [O60522-1]
DR CCDS; CCDS55017.1; -. [O60522-2]
DR RefSeq; NP_001010870.1; NM_001010870.2. [O60522-1]
DR RefSeq; NP_001161831.1; NM_001168359.1. [O60522-2]
DR AlphaFoldDB; O60522; -.
DR SMR; O60522; -.
DR BioGRID; 128720; 4.
DR IntAct; O60522; 2.
DR STRING; 9606.ENSP00000346065; -.
DR iPTMnet; O60522; -.
DR PhosphoSitePlus; O60522; -.
DR SwissPalm; O60522; -.
DR BioMuta; TDRD6; -.
DR EPD; O60522; -.
DR jPOST; O60522; -.
DR MassIVE; O60522; -.
DR MaxQB; O60522; -.
DR PaxDb; O60522; -.
DR PeptideAtlas; O60522; -.
DR PRIDE; O60522; -.
DR ProteomicsDB; 26920; -.
DR ProteomicsDB; 49457; -. [O60522-1]
DR Antibodypedia; 48657; 7 antibodies from 6 providers.
DR DNASU; 221400; -.
DR Ensembl; ENST00000316081.11; ENSP00000346065.5; ENSG00000180113.16. [O60522-1]
DR Ensembl; ENST00000544460.5; ENSP00000443299.1; ENSG00000180113.16. [O60522-2]
DR GeneID; 221400; -.
DR KEGG; hsa:221400; -.
DR MANE-Select; ENST00000316081.11; ENSP00000346065.5; NM_001010870.3; NP_001010870.1.
DR UCSC; uc003oyj.4; human. [O60522-1]
DR CTD; 221400; -.
DR DisGeNET; 221400; -.
DR GeneCards; TDRD6; -.
DR HGNC; HGNC:21339; TDRD6.
DR HPA; ENSG00000180113; Tissue enhanced (testis).
DR MIM; 611200; gene.
DR neXtProt; NX_O60522; -.
DR OpenTargets; ENSG00000180113; -.
DR PharmGKB; PA134945900; -.
DR VEuPathDB; HostDB:ENSG00000180113; -.
DR eggNOG; KOG2039; Eukaryota.
DR GeneTree; ENSGT00940000159049; -.
DR HOGENOM; CLU_001126_1_0_1; -.
DR InParanoid; O60522; -.
DR OMA; VDYGQTK; -.
DR OrthoDB; 496838at2759; -.
DR PhylomeDB; O60522; -.
DR PathwayCommons; O60522; -.
DR Reactome; R-HSA-5601884; PIWI-interacting RNA (piRNA) biogenesis.
DR SignaLink; O60522; -.
DR BioGRID-ORCS; 221400; 9 hits in 1065 CRISPR screens.
DR ChiTaRS; TDRD6; human.
DR GenomeRNAi; 221400; -.
DR Pharos; O60522; Tdark.
DR PRO; PR:O60522; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; O60522; protein.
DR Bgee; ENSG00000180113; Expressed in secondary oocyte and 131 other tissues.
DR ExpressionAtlas; O60522; baseline and differential.
DR Genevisible; O60522; HS.
DR GO; GO:0033391; C:chromatoid body; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0043186; C:P granule; IBA:GO_Central.
DR GO; GO:0030719; P:P granule organization; IBA:GO_Central.
DR GO; GO:0034587; P:piRNA metabolic process; IBA:GO_Central.
DR GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB.
DR CDD; cd04508; TUDOR; 6.
DR Gene3D; 2.40.50.90; -; 7.
DR InterPro; IPR035437; SNase_OB-fold_sf.
DR InterPro; IPR002999; Tudor.
DR Pfam; PF00567; TUDOR; 7.
DR SMART; SM00333; TUDOR; 8.
DR PROSITE; PS50304; TUDOR; 6.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cytoplasm; Developmental protein; Differentiation;
KW Phosphoprotein; Reference proteome; Repeat; Spermatogenesis.
FT CHAIN 1..2096
FT /note="Tudor domain-containing protein 6"
FT /id="PRO_0000183167"
FT DOMAIN 65..120
FT /note="Tudor 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00211"
FT DOMAIN 310..369
FT /note="Tudor 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00211"
FT DOMAIN 536..593
FT /note="Tudor 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00211"
FT DOMAIN 816..875
FT /note="Tudor 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00211"
FT DOMAIN 1033..1088
FT /note="Tudor 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00211"
FT DOMAIN 1352..1411
FT /note="Tudor 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00211"
FT DOMAIN 1567..1626
FT /note="Tudor 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00211"
FT DOMAIN 2026..2084
FT /note="Tudor 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00211"
FT REGION 287..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 293
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P61407"
FT MOD_RES 1722
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P61407"
FT MOD_RES 2062
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P61407"
FT VAR_SEQ 2058..2087
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044801"
FT VARIANT 192
FT /note="R -> Q (in dbSNP:rs7750596)"
FT /id="VAR_029050"
FT VARIANT 398
FT /note="T -> A (in dbSNP:rs3799277)"
FT /id="VAR_029051"
FT VARIANT 795
FT /note="I -> M (in dbSNP:rs9463234)"
FT /id="VAR_052423"
FT VARIANT 1014
FT /note="Q -> E (in dbSNP:rs9381472)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_029052"
FT CONFLICT 1273
FT /note="E -> K (in Ref. 4; AAC18034)"
FT /evidence="ECO:0000305"
FT CONFLICT 1455
FT /note="Q -> R (in Ref. 3; CAI45997)"
FT /evidence="ECO:0000305"
FT CONFLICT 1955
FT /note="M -> V (in Ref. 3; CAI45997)"
FT /evidence="ECO:0000305"
FT CONFLICT 2016
FT /note="A -> D (in Ref. 4; AAC18034)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2096 AA; 236517 MW; 19FED65D6FE68E44 CRC64;
MCSTPGMPAP GASLALRVSF VDVHPDVIPV QLWGLVGERR GEYLRLSREI QEAAATRGQW
ALGSASASPG ELCLVQVGLL WHRCRVVSRQ AQESRVFLLD EGRTITAGAG SLAPGRREFF
NLPSEVLGCV LAGLVPAGCG AGSGEPPQHW PADAVDFLSN LQGKEVHGCV LDVLLLHRLV
LLEVPDVFQQ MRELGLARRV PDSLFRSLLE RYLTAATASV GSGVPVLSRV PLKQKQPGLD
YFYPQLQLGV TEAVVITQVC HPHRIHCQLR SVSQEIHRLS ESMAQVYRGS TGTGDENSTS
ATWEEREESP DKPGSPCASC GLDGHWYRAL LLETFRPQRC AQVLHVDYGR KELVSCSSLR
YLLPEYFRMP VVTYPCALYG LWDGGRGWSR SQVGDLKTLI LGKAVNAKIE FYCSFEHVYY
VSLYGEDGIN LNRVFGVQSC CLADRVLQSQ ATEEEEPETS QSQSPAEEVD EEISLPALRS
IRLKMNAFYD AQVEFVKNPS EFWIRLRKHN VTFSKLMRRM CGFYSSASKL DGVVLKPEPD
DLCCVKWKEN GYYRAIVTKL DDKSVDVFLV DRGNSENVDW YDVRMLLPQF RQLPILAVKC
TLADIWPLGK TWSQEAVSFF KKTVLHKELV IHILDKQDHQ YVIEILDESR TGEENISKVI
AQAGYAKYQE FETKENILVN AHSPGHVSNH FTTESNKIPF AKTGEGEQKA KRENKTTSVS
KALSDTTVVT NGSTELVVQE KVKRASVYFP LMQNCLEIKP GSSSKGELEV GSTVEVRVSY
VENPGYFWCQ LTRNIQGLKT LMSDIQYYCK NTAAPHQRNT LACLAKRTVN RQWSRALISG
IQSVEHVNVT FVDYGDREMV SVKNIYSISE EFLKVKAQAF RCSLYNLIQP VGQNPFVWDV
KAIQAFNEFI DNAWQKNLEL KCTIFALASI NEELFNIVDL LTPFQSACHF LVEKRLARPV
KLQKPLESSV QLHSYFYSTH DMKIGSEELV YITHIDDPWT FYCQLARNAN ILEQLSCSIT
QLSKVLLNLK TSPLNPGTLC LAKYTDGNWY RGIVIEKEPK KVFFVDFGNI YVVTSDDLLP
IPSDAYDVLL LPMQAVRCSL SDIPDHIPEE VVVWFQETIL DKSLKALVVA KDPDGTLIIE
LYGDNIQISA SINKKLGLLS YKDRIRKKES EVLCSTTETL EEKNENMKLP CTEYLSKSVG
YKLPNKEILE ESYKPQINSS YKELKLLQSL TKTNLVTQYQ DSVGNKNSQV FPLTTEKKEE
ISAETPLKTA RVEATLSERK IGDSCDKDLP LKFCEFPQKT IMPGFKTTVY VSHINDLSDF
YVQLIEDEAE ISHLSERLNS VKTRPEYYVG PPLQRGDMIC AVFPEDNLWY RAVIKEQQPN
DLLSVQFIDY GNVSVVHTNK IGRLDLVNAI LPGLCIHCSL QGFEVPDNKN SKKMMHYFSQ
RTSEAAIRCE FVKFQDRWEV ILADEHGIIA DDMISRYALS EKSQVELSTQ VIKSASSKSV
NKSDIDTSVF LNWYNPEKKM IRAYATVIDG PEYFWCQFAD TEKLQCLEVE VQTAGEQVAD
RRNCIPCPYI GDPCIVRYRE DGHYYRALIT NICEDYLVSV RLVDFGNIED CVDPKALWAI
PSELLSVPMQ AFPCCLSGFN ISEGLCSQEG NDYFYEIITE DVLEITILEI RRDVCDIPLA
IVDLKSKGKS INEKMEKYSK TGIKSALPYE NIDSEIKQTL GSYNLDVGLK KLSNKAVQNK
IYMEQQTDEL AEITEKDVNI IGTKPSNFRD PKTDNICEGF ENPCKDKIDT EELEGELECH
LVDKAEFDDK YLITGFNTLL PHANETKEIL ELNSLEVPLS PDDESKEFLE LESIELQNSL
VVDEEKGELS PVPPNVPLSQ ECVTKGAMEL FTLQLPLSCE AEKQPELELP TAQLPLDDKM
DPLSLGVSQK AQESMCTEDM RKSSCVESFD DQRRMSLHLH GADCDPKTQN EMNICEEEFV
EYKNRDAISA LMPLFSEEES SDGSKHNNGL PDHISAQLQN TYTLKAFTVG SKCVVWSSLR
NTWSKCEILE TAEEGTRVLN LSNGMEEIVN PENVWNGIPK LDKSPPEKRG LEVMEI
