CNTLN_MOUSE
ID CNTLN_MOUSE Reviewed; 1397 AA.
AC A2AM05; A0PJC6; Q3TNP8; Q5EBN8; Q8C748; Q8C9U3; Q8CD25; Q8CE32; Q8R2F0;
AC Q8R2P3;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Centlein;
DE AltName: Full=Centrosomal protein;
GN Name=Cntln {ECO:0000250|UniProtKB:Q9NXG0};
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] {ECO:0000305, ECO:0000312|EMBL:BAC35037.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-701 AND 774-1397 (ISOFORM 1).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC35037.2};
RC TISSUE=Embryonic stomach {ECO:0000312|EMBL:BAC35037.2},
RC Embryonic testis {ECO:0000312|EMBL:BAC27472.1},
RC Neonatal skin {ECO:0000312|EMBL:BAC26307.1},
RC Ovary {ECO:0000312|EMBL:BAE38040.1}, and
RC Thymus {ECO:0000312|EMBL:BAC30624.1};
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 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 [3] {ECO:0000305, ECO:0000312|EMBL:AAH89374.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 273-705 (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 715-1397 (ISOFORM 4).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH89374.1}, and
RC FVB/N {ECO:0000312|EMBL:AAH24869.1};
RC TISSUE=Brain {ECO:0000312|EMBL:AAI25625.1},
RC Eye {ECO:0000312|EMBL:AAH89374.1}, and
RC Mammary tumor {ECO:0000312|EMBL:AAH24869.1};
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 [4] {ECO:0000305, ECO:0000312|EMBL:CAM15709.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 996-1376 (ISOFORM 1).
RA Beale E.G., Boston W.L., Ott K., Yasmin R., Desvergne B., Wahli W.;
RT "A partial cDNA encoding the mouse ortholog of hypothetical human protein
RT FLJ20276.";
RL Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-5 AND SER-9, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE
RP ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5; SER-9; SER-1219 AND
RP THR-1334, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Lung, Spleen, and Testis;
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).
CC -!- FUNCTION: Required for centrosome cohesion and recruitment of CEP68 to
CC centrosomes. {ECO:0000250|UniProtKB:Q9NXG0}.
CC -!- SUBUNIT: Interacts with CEP250 and CEP68. Interacts with NEK2; the
CC interaction leads to phosphorylation of CNTLN.
CC {ECO:0000250|UniProtKB:Q9NXG0}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome, centriole {ECO:0000250|UniProtKB:A9ZSY0}.
CC Note=Colocalizes with gamma-tubulin during interphase and mitosis.
CC Appears to associate with the mother centriole during G1 phase and with
CC daughter centrioles towards G1/S phase. Localizes to the proximal ends
CC of the centrioles. Levels are high at interphase centrosomes but are
CC reduced on mitotic spindle poles. {ECO:0000250|UniProtKB:A9ZSY0,
CC ECO:0000250|UniProtKB:Q9NXG0}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1 {ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:16141072,
CC ECO:0000269|Ref.4};
CC IsoId=A2AM05-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:16141072};
CC IsoId=A2AM05-2; Sequence=VSP_052786, VSP_052787;
CC Name=3 {ECO:0000269|PubMed:15489334};
CC IsoId=A2AM05-3; Sequence=VSP_052785;
CC Name=4;
CC IsoId=A2AM05-4; Sequence=VSP_032866;
CC -!- PTM: Phosphorylated directly or indirectly by NEK2.
CC {ECO:0000250|UniProtKB:Q9NXG0}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH24869.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=BAC26307.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK029118; BAC26307.1; ALT_INIT; mRNA.
DR EMBL; AK031604; BAC27472.1; -; mRNA.
DR EMBL; AK040554; BAC30624.1; -; mRNA.
DR EMBL; AK052558; BAC35037.2; -; mRNA.
DR EMBL; AK165111; BAE38040.1; -; mRNA.
DR EMBL; AL805906; CAM13729.1; -; Genomic_DNA.
DR EMBL; AL806524; CAM13729.1; JOINED; Genomic_DNA.
DR EMBL; BX470174; CAM13729.1; JOINED; Genomic_DNA.
DR EMBL; AL805906; CAM13730.1; -; Genomic_DNA.
DR EMBL; BX470174; CAM13730.1; JOINED; Genomic_DNA.
DR EMBL; AL806524; CAM15708.1; -; Genomic_DNA.
DR EMBL; AL806524; CAM15709.1; -; Genomic_DNA.
DR EMBL; AL805906; CAM15709.1; JOINED; Genomic_DNA.
DR EMBL; BX470174; CAM15709.1; JOINED; Genomic_DNA.
DR EMBL; BX470174; CAM21915.1; -; Genomic_DNA.
DR EMBL; AL805906; CAM21915.1; JOINED; Genomic_DNA.
DR EMBL; AL806524; CAM21915.1; JOINED; Genomic_DNA.
DR EMBL; BX470174; CAM21916.1; -; Genomic_DNA.
DR EMBL; AL805906; CAM21916.1; JOINED; Genomic_DNA.
DR EMBL; BC024869; AAH24869.1; ALT_SEQ; mRNA.
DR EMBL; BC027370; AAH27370.1; -; mRNA.
DR EMBL; BC089374; AAH89374.1; -; mRNA.
DR EMBL; BC125622; AAI25623.1; -; mRNA.
DR EMBL; BC125624; AAI25625.1; -; mRNA.
DR EMBL; AF483477; AAL89759.1; -; mRNA.
DR CCDS; CCDS18302.1; -. [A2AM05-2]
DR CCDS; CCDS51216.1; -. [A2AM05-4]
DR RefSeq; NP_780484.2; NM_175275.4. [A2AM05-4]
DR RefSeq; NP_796359.1; NM_177385.4. [A2AM05-2]
DR RefSeq; XP_006538089.1; XM_006538026.3. [A2AM05-1]
DR AlphaFoldDB; A2AM05; -.
DR SMR; A2AM05; -.
DR STRING; 10090.ENSMUSP00000099883; -.
DR iPTMnet; A2AM05; -.
DR PhosphoSitePlus; A2AM05; -.
DR EPD; A2AM05; -.
DR jPOST; A2AM05; -.
DR MaxQB; A2AM05; -.
DR PaxDb; A2AM05; -.
DR PRIDE; A2AM05; -.
DR Antibodypedia; 24606; 87 antibodies from 16 providers.
DR Ensembl; ENSMUST00000047023; ENSMUSP00000044138; ENSMUSG00000038070. [A2AM05-1]
DR Ensembl; ENSMUST00000102819; ENSMUSP00000099883; ENSMUSG00000038070. [A2AM05-2]
DR Ensembl; ENSMUST00000107190; ENSMUSP00000102808; ENSMUSG00000038070. [A2AM05-3]
DR Ensembl; ENSMUST00000169371; ENSMUSP00000130491; ENSMUSG00000038070. [A2AM05-4]
DR GeneID; 338349; -.
DR KEGG; mmu:338349; -.
DR UCSC; uc008tlk.2; mouse. [A2AM05-2]
DR UCSC; uc008tll.2; mouse. [A2AM05-4]
DR UCSC; uc008tln.2; mouse. [A2AM05-3]
DR CTD; 54875; -.
DR MGI; MGI:2443104; Cntln.
DR VEuPathDB; HostDB:ENSMUSG00000038070; -.
DR eggNOG; ENOG502QRVC; Eukaryota.
DR GeneTree; ENSGT00440000034932; -.
DR HOGENOM; CLU_006488_1_0_1; -.
DR InParanoid; A2AM05; -.
DR OMA; MSNMFEN; -.
DR OrthoDB; 846281at2759; -.
DR PhylomeDB; A2AM05; -.
DR BioGRID-ORCS; 338349; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Cntln; mouse.
DR PRO; PR:A2AM05; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; A2AM05; protein.
DR Bgee; ENSMUSG00000038070; Expressed in saccule of membranous labyrinth and 209 other tissues.
DR Genevisible; A2AM05; MM.
DR GO; GO:0005814; C:centriole; ISO:MGI.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; ISO:MGI.
DR GO; GO:0010457; P:centriole-centriole cohesion; ISO:MGI.
DR GO; GO:0033365; P:protein localization to organelle; ISO:MGI.
DR InterPro; IPR038810; CNTLN.
DR PANTHER; PTHR18957; PTHR18957; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton;
KW Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19131326"
FT CHAIN 2..1397
FT /note="Centlein"
FT /id="PRO_0000328976"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 56..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 422..449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 485..521
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 95..126
FT /evidence="ECO:0000255"
FT COILED 405..481
FT /evidence="ECO:0000255"
FT COILED 674..778
FT /evidence="ECO:0000255"
FT COILED 973..1114
FT /evidence="ECO:0000255"
FT COILED 1152..1299
FT /evidence="ECO:0000255"
FT COMPBIAS 1..17
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 430..449
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 485..506
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19131326"
FT MOD_RES 5
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 22
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NXG0"
FT MOD_RES 1219
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1334
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..1135
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_052785"
FT VAR_SEQ 285..318
FT /note="LEENLIEAKKEIESAQTKYNVVSQQLNNKQAELL -> QGGPVSMSCPGPSF
FT LQQPNIRFSLNNKLSIQIHQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_052786"
FT VAR_SEQ 319..1397
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_052787"
FT VAR_SEQ 865
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_032866"
FT CONFLICT 484
FT /note="S -> F (in Ref. 1; BAC35037)"
FT /evidence="ECO:0000305"
FT CONFLICT 701
FT /note="S -> P (in Ref. 1; BAC35037)"
FT /evidence="ECO:0000305"
FT CONFLICT 1021
FT /note="F -> L (in Ref. 4; AAL89759)"
FT /evidence="ECO:0000305"
FT CONFLICT 1056
FT /note="M -> T (in Ref. 4; AAL89759)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1397 AA; 160747 MW; 644CC6C2843C3F27 CRC64;
MAARSPSSSP PPPPVRRSSR RSLRVGRGAE VHAVRSEASG LAGAAREVVA DKSDLLWRGE
EGSGGRRGSG RAGAAVAPVA SAPAGSWWPE GLSSEEAKAT RSQLLEEELS SLKEELALCQ
ADKEFVWSLW RRLQATNPDL TQTVSLVVER EKQKSEAKDR KVLEILQVKD SKIQELEQTE
SVLKQELHDL VKLKTLVDEE NAFLRKELCD LQKKFKDKSQ EVKDAKECVQ SKEEQNRLVI
KNLEEENERL RTRCTDLLND LEKLRNQEAH WRKEKHSVDT RVKVLEENLI EAKKEIESAQ
TKYNVVSQQL NNKQAELLQK DMDITLIRKE LQELQNVYKQ NSAHTAQQAD LIQQLQALNM
DTQKVLRNQE DVHTAESMSY QKLYNELHMC FETTKSNEVM LRQSVVNLQG QLFQKEQENV
KLKEKLEESQ GTAPSLSPHD SDSSHSGKAP LSTLETLMIS QKSEIEYLQK KLKVANEKLM
ANRSCDQDFS EKGTEGKHKE PPVKRSRSLS PKSSFMGSEE LRKLKKAERK IENLEKTLQL
KSQENDELRD AHEKRKERLQ MLHTNYRAVK EQLKQWEEDS GMAESRQMKR AEPHQLRQED
SDAVWNELAY FKRENQELMV QKMTLQDELD ELKMHMSIDK TTIQELNRCM AEKREEQLFR
QHEDAEVKKS TPEKNEKAIS EETLQKVIEL ENRLKSFEKN SRKLKEESKR LKKENDFLKS
HLKHYQEDSE AREKELEQLL RVSKDVEHDK SELQTKITAL ETEVTTLRRQ VTEAKALRGK
DEEVVCPEER AHRPTDKAKS EMATTDVRAR RCDCKTATTK VKFKAAKRKC SVGRHHTVLN
HSIKVMSHVE NLSKDGWEDV SEGSSDSETQ TFQNLGTIIV ETSQNISPIE DGRNQKEIDQ
TEGSCAQQRA MQTYSCEDIK APQSISHNKN TKKMTFQKKS GSLQKSLHSA LPARVNREKC
KNLPAQKSSS STISLRERIV SLQQQNSLLQ NARRAAEASA KEYKEANEKL LHQQQVSDHR
FQTSRQTIKK LTLDLAELRK EKEDLLKKVE SSSDIMSLAE EVSRIMAPQI KVTTLGPSRS
MDLEMKQLQC KLKNATNELT KQSSNVKSLR MELLAKDDHI KEMHERTSRM ERDITMKRHL
IEDLKFRQKV NSESNESFNE MLETLEKKVK SLTEECSNKK VSVDSLKQRL NVAVKEKSQY
EQMYQKTKEE LEKKDLKMSV LISKLNDTET AMAQIETAAS EQLQGLALQS EQVLEGAQKK
LLSANEKIEE FTVFVKALVN ELQSDVHGTR HQIRELKKMQ KSRHACKTST HKAQTLAASI
LNISRSDLEE ILDTEDELEI EKTKIDIEND KEWMLYIQKL LEGQLPFASY LLEAVLEKIK
ENKKLTEGYF TVMKDTK
