KN14A_ARATH
ID KN14A_ARATH Reviewed; 1273 AA.
AC Q9LX99; B3H459; O23652; Q0WVP0;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Kinesin-like protein KIN-14A {ECO:0000305};
DE AltName: Full=Geminivirus Rep-interacting motor protein {ECO:0000303|PubMed:12172024};
DE AltName: Full=Geminivirus replication protein-interacting protein {ECO:0000312|EMBL:AAM49809.1};
DE AltName: Full=Kinesin CDKA-1-associated protein 1 {ECO:0000303|PubMed:15247388};
DE AltName: Full=Kinesin-like protein KCA1 {ECO:0000303|PubMed:15247388};
DE AltName: Full=Kinesin-like protein for actin-based chloroplast movement 1 {ECO:0000303|PubMed:20418504};
GN Name=KIN14A {ECO:0000305};
GN Synonyms=GRIMP {ECO:0000312|EMBL:AAM49809.1},
GN KAC1 {ECO:0000303|PubMed:20418504}, KCA1 {ECO:0000303|PubMed:15247388},
GN KSN1 {ECO:0000303|PubMed:12571277}, TH65 {ECO:0000303|Ref.5};
GN OrderedLocusNames=At5g10470 {ECO:0000312|Araport:AT5G10470};
GN ORFNames=F12B17.180 {ECO:0000312|EMBL:CAB89396.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH GEMINIVIRUS AL1, DEVELOPMENTAL
RP STAGE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND PHOSPHORYLATION.
RC STRAIN=cv. Columbia;
RX PubMed=12172024; DOI=10.1105/tpc.003681;
RA Kong L.-J., Hanley-Bowdoin L.;
RT "A geminivirus replication protein interacts with a protein kinase and a
RT motor protein that display different expression patterns during plant
RT development and infection.";
RL Plant Cell 14:1817-1832(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 473-866, AND INTERACTION WITH CDKA-1.
RX DOI=10.1093/jxb/48.12.2113;
RA de Veylder L., Segers G., Glab N., van Montagu M., Inze D.;
RT "Identification of proteins interacting with the Arabidopsis Cdc2aAt
RT protein.";
RL J. Exp. Bot. 48:2111-2112(1997).
RN [6]
RP GENE FAMILY.
RX PubMed=11472632; DOI=10.1186/1471-2164-2-2;
RA Reddy A.S., Day I.S.;
RT "Kinesins in the Arabidopsis genome: a comparative analysis among
RT eukaryotes.";
RL BMC Genomics 2:2-2(2001).
RN [7]
RP INTERACTION WITH LUE1/KSS.
RX PubMed=12571277; DOI=10.1242/jcs.00274;
RA Bouquin T., Mattsson O., Naested H., Foster R., Mundy J.;
RT "The Arabidopsis lue1 mutant defines a katanin p60 ortholog involved in
RT hormonal control of microtubule orientation during cell growth.";
RL J. Cell Sci. 116:791-801(2003).
RN [8]
RP FUNCTION, SUBUNIT, INTERACTION WITH CDKA-1, AND SUBCELLULAR LOCATION.
RX PubMed=15247388; DOI=10.1104/pp.104.044818;
RA Vanstraelen M., Torres Acosta J.A., De Veylder L., Inze D., Geelen D.;
RT "A plant-specific subclass of C-terminal kinesins contains a conserved a-
RT type cyclin-dependent kinase site implicated in folding and dimerization.";
RL Plant Physiol. 135:1417-1429(2004).
RN [9]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=16448571; DOI=10.1186/1471-2164-7-18;
RA Richardson D.N., Simmons M.P., Reddy A.S.;
RT "Comprehensive comparative analysis of kinesins in photosynthetic
RT eukaryotes.";
RL BMC Genomics 7:18-18(2006).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF SER-841 AND SER-845.
RX PubMed=16461285; DOI=10.1016/j.cub.2005.12.035;
RA Vanstraelen M., Van Damme D., De Rycke R., Mylle E., Inze D., Geelen D.;
RT "Cell cycle-dependent targeting of a kinesin at the plasma membrane
RT demarcates the division site in plant cells.";
RL Curr. Biol. 16:308-314(2006).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [12]
RP FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP ASN-134 AND LYS-426.
RX PubMed=20418504; DOI=10.1073/pnas.0912773107;
RA Suetsugu N., Yamada N., Kagawa T., Yonekura H., Uyeda T.Q., Kadota A.,
RA Wada M.;
RT "Two kinesin-like proteins mediate actin-based chloroplast movement in
RT Arabidopsis thaliana.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:8860-8865(2010).
RN [13]
RP REVIEW.
RX PubMed=22038119; DOI=10.1007/s00709-011-0343-9;
RA Zhu C., Dixit R.;
RT "Functions of the Arabidopsis kinesin superfamily of microtubule-based
RT motor proteins.";
RL Protoplasma 249:887-899(2012).
RN [14]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=27310016; DOI=10.1371/journal.pone.0157429;
RA Suetsugu N., Higa T., Gotoh E., Wada M.;
RT "Light-induced movements of chloroplasts and nuclei are regulated in both
RT cp-actin-filament-dependent and -independent manners in Arabidopsis
RT thaliana.";
RL PLoS ONE 11:E0157429-E0157429(2016).
CC -!- FUNCTION: Kinesin-like protein required for chloroplast movements and
CC anchor to the plasma membrane. Mediates chloroplast movement via
CC chloroplast actin (cp-actin) filaments. Required for the chloroplast
CC avoidance response under high intensity blue light (PubMed:20418504,
CC PubMed:27310016). Mediates redundantly with CHUP1 the nuclear avoidance
CC response under high intensity blue light (PubMed:27310016). May act as
CC a mitotic kinesin (PubMed:15247388). Probably involved in division
CC plane determination (PubMed:16461285). {ECO:0000269|PubMed:15247388,
CC ECO:0000269|PubMed:16461285, ECO:0000269|PubMed:20418504,
CC ECO:0000269|PubMed:27310016}.
CC -!- SUBUNIT: Homodimer and heterodimer with KCA2 (PubMed:15247388).
CC Interacts with CDKA-1 (Ref.5, PubMed:15247388). Interacts with AL1, a
CC geminivirus (TGMV) protein essential for viral replication
CC (PubMed:12172024). Interacts with LUE1/KSS (PubMed:12571277).
CC {ECO:0000269|PubMed:12172024, ECO:0000269|PubMed:12571277,
CC ECO:0000269|PubMed:15247388, ECO:0000269|Ref.5}.
CC -!- INTERACTION:
CC Q9LX99; Q9SEX2: AAA1; NbExp=3; IntAct=EBI-2025621, EBI-2025583;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytoskeleton, spindle.
CC Chromosome. Cell membrane. Cytoplasm, cytoskeleton, phragmoplast.
CC Note=Localizes to the spindle apparatus and condensed chromosomes in
CC mitotic cells. Localizes in the forming cell plate and the cortical
CC division zone (CDZ) during cytokinesis.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9LX99-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9LX99-2; Sequence=VSP_041595;
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:12172024}.
CC -!- DEVELOPMENTAL STAGE: Not developmentally regulated.
CC {ECO:0000269|PubMed:12172024}.
CC -!- PTM: Part of the phosphorylation is not CDK-dependent.
CC {ECO:0000269|PubMed:12172024}.
CC -!- DISRUPTION PHENOTYPE: Impaired chloroplast accumulation and slow
CC avoidance movement under strong blue light (PubMed:20418504). Double
CC mutant kac1kac2 exhibits an increase in leaf transmittance and a
CC partial defect in nuclear avoidance response under strong blue light
CC exposure (PubMed:27310016). {ECO:0000269|PubMed:20418504,
CC ECO:0000269|PubMed:27310016}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. KIN-14 subfamily.
CC {ECO:0000303|PubMed:16448571}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE98808.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence.; Evidence={ECO:0000305};
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DR EMBL; AY100691; AAM49809.1; -; mRNA.
DR EMBL; AL353995; CAB89396.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91546.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91547.1; -; Genomic_DNA.
DR EMBL; AK226701; BAE98808.1; ALT_SEQ; mRNA.
DR EMBL; AJ001729; CAA04956.1; -; mRNA.
DR PIR; T49992; T49992.
DR RefSeq; NP_001078565.1; NM_001085096.1. [Q9LX99-2]
DR RefSeq; NP_196609.1; NM_121085.3. [Q9LX99-1]
DR AlphaFoldDB; Q9LX99; -.
DR SMR; Q9LX99; -.
DR BioGRID; 16189; 2.
DR DIP; DIP-46998N; -.
DR IntAct; Q9LX99; 2.
DR STRING; 3702.AT5G10470.2; -.
DR iPTMnet; Q9LX99; -.
DR PaxDb; Q9LX99; -.
DR PRIDE; Q9LX99; -.
DR ProteomicsDB; 238402; -. [Q9LX99-1]
DR EnsemblPlants; AT5G10470.1; AT5G10470.1; AT5G10470. [Q9LX99-1]
DR EnsemblPlants; AT5G10470.2; AT5G10470.2; AT5G10470. [Q9LX99-2]
DR GeneID; 830911; -.
DR Gramene; AT5G10470.1; AT5G10470.1; AT5G10470. [Q9LX99-1]
DR Gramene; AT5G10470.2; AT5G10470.2; AT5G10470. [Q9LX99-2]
DR KEGG; ath:AT5G10470; -.
DR Araport; AT5G10470; -.
DR TAIR; locus:2142444; AT5G10470.
DR eggNOG; KOG0239; Eukaryota.
DR HOGENOM; CLU_008815_0_0_1; -.
DR InParanoid; Q9LX99; -.
DR OMA; IVTIHIH; -.
DR OrthoDB; 364605at2759; -.
DR PhylomeDB; Q9LX99; -.
DR PRO; PR:Q9LX99; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LX99; baseline and differential.
DR Genevisible; Q9LX99; AT.
DR GO; GO:0009504; C:cell plate; IDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0009524; C:phragmoplast; IDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008017; F:microtubule binding; IDA:TAIR.
DR GO; GO:0003777; F:microtubule motor activity; IEA:InterPro.
DR GO; GO:0009904; P:chloroplast accumulation movement; IGI:UniProtKB.
DR GO; GO:0009903; P:chloroplast avoidance movement; IGI:UniProtKB.
DR GO; GO:0000911; P:cytokinesis by cell plate formation; TAS:TAIR.
DR GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR GO; GO:0007017; P:microtubule-based process; IBA:GO_Central.
DR GO; GO:0031022; P:nuclear migration along microfilament; IGI:UniProtKB.
DR GO; GO:0000913; P:preprophase band assembly; TAS:TAIR.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR030109; KIN-14.
DR InterPro; IPR019821; Kinesin_motor_CS.
DR InterPro; IPR001752; Kinesin_motor_dom.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR47972:SF22; PTHR47972:SF22; 1.
DR Pfam; PF00225; Kinesin; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00129; KISc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cell membrane; Chromosome; Coiled coil;
KW Cytoplasm; Cytoskeleton; Host-virus interaction; Membrane; Microtubule;
KW Motor protein; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..1273
FT /note="Kinesin-like protein KIN-14A"
FT /id="PRO_0000311998"
FT DOMAIN 142..456
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 827..847
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1136..1157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 59..89
FT /evidence="ECO:0000255"
FT COILED 466..511
FT /evidence="ECO:0000255"
FT COILED 559..595
FT /evidence="ECO:0000255"
FT COILED 627..657
FT /evidence="ECO:0000255"
FT COMPBIAS 829..847
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1140..1154
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 223..230
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT VAR_SEQ 683
FT /note="N -> NS (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_041595"
FT MUTAGEN 134
FT /note="N->K: Decreases protein stability."
FT /evidence="ECO:0000269|PubMed:20418504"
FT MUTAGEN 426
FT /note="K->N: Decreases protein stability."
FT /evidence="ECO:0000269|PubMed:20418504"
FT MUTAGEN 841
FT /note="S->A: No effect on cellular localization; when
FT associated with A-845."
FT /evidence="ECO:0000269|PubMed:16461285"
FT MUTAGEN 841
FT /note="S->E: Loss of cell plate and plasma membrane
FT targeting; when associated with E-845."
FT /evidence="ECO:0000269|PubMed:16461285"
FT MUTAGEN 845
FT /note="S->A: No effect on cellular localization; when
FT associated with A-841."
FT /evidence="ECO:0000269|PubMed:16461285"
FT MUTAGEN 845
FT /note="S->E: Loss of cell plate and plasma membrane
FT targeting; when associated with E-841."
FT /evidence="ECO:0000269|PubMed:16461285"
SQ SEQUENCE 1273 AA; 141036 MW; C0B2B83752CEB9F9 CRC64;
MADQRSKTNR WNWEVSGFEP RKSSSNASFA ESTGHRTTGP LLRRNSISTP SLPPKQAIAS
KVNGLKEKVK LAKEDYLELR QEATDLQEYS NAKLDRVTRY LGVLAEKSRK LDQFVLETEA
RISPLINEKK RLFNDLLTAK GNIKVFCRAR PLFEDEGPSV IEFPGDCTIC VNTSDDTLSN
PKKDFEFDRV YGPHVGQAAL FSDVQPFVQS ALDGSNVSIL SYGQTNAGKT YTMEGSNHDR
GLYARCFEEL FDLANSDSTS TSRFSFSLSV FEIYNEQIRD LLSETQSNLP NINMDLHESV
IELGQEKVDN PLEFLGVLKS AFLNRGNYKS KFNVTHLIVS IHIYYSNTIT GENIYSKLSL
VDLAGSEGLI MENDSGDHVT DLLHVMNSIS ALGDVLSSLT SGKDSIPYDN SILTRVLADS
LGGSSKTLMI VNICPSVQTL SETISCLNYA ARARNTVPSL GNRDTIKKWR DVASDARKEL
LEKERENQNL KQEVVGLKKA LKDANDQCVL LYSEVQRAWK VSFTLQSDLK SENIMLVDKH
RLEKEQNSQL RNQIAQFLQL DQEQKLQMQQ QDSAIQNLQA KITDLESQVS EAVRSDTTRT
GDALQSQDIF SPIPKAVEGT TDSSSVTKKL EEELKKRDAL IERLHEENEK LFDRLTERSM
AVSTQVLSPS LRASPNIQPA NVNRGEGYSA EAVALPSTPN KNNGAITLVK SGTDLVKTTP
AGEYLTAALN DFDPEEYEGL AAIADGANKL LMLVLAAVIK AGASREHEIL AEIRDSVFSF
IRKMEPRRVM DTMLVSRVRI LYIRSLLARS PELQTIRVSP VECFLEKPNT GRSKSTSRGS
SPGRSPVRYL DTQIHGFKVN IKAERRNKLA SVVSRMRGLE QDAGRQQVTG VKLREMQDEA
KSFAIGNKAL AALFVHTPAG ELQRQIRLWL AENFEFLSVT SDDVSGGNGG QLELLSTAIM
DGWMAGLGAA VPPHTDALGQ LLSEYAKRVY TSQMQHMKDI AGTLAAEEAE DAGQVSKLRS
ALESVDHKRR KILQQMKSDA ALLNLEEGSS PIPNPSTAAE DSRLASLISL DGILKQVKEI
TRQASVHVLS KSKKKALLES LDELTERMPS LLDIDHPCAQ REIATAHQLV ETIPEQEDTN
ILEQSHDRRP SLESISSGET DVSQWNVLQF NTGSSAPFII KCGGNNNSEL VIKADARVQE
PKGGEIVRVV PRPSVLVNMS LEEMKQMFVQ LPEALSLLAL ARTADGTRAR YSRLYKTLAM
KVPSLKDLVS ELE
