DSLE_ARATH
ID DSLE_ARATH Reviewed; 696 AA.
AC Q9M2N5; Q5IH79;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Zinc finger BED domain-containing protein DAYSLEEPER;
DE AltName: Full=Transposase-like protein DAYSLEEPER;
GN Name=HAT; OrderedLocusNames=At3g42170; ORFNames=T27B3.40;
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], FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS
RP OF VAL-70; HIS-73; CYS-88; CYS-91; LEU-109; HIS-112 AND CYS-118.
RC STRAIN=cv. Columbia;
RX PubMed=16015335; DOI=10.1038/nature03667;
RA Bundock P., Hooykaas P.;
RT "An Arabidopsis hAT-like transposase is essential for plant development.";
RL Nature 436:282-284(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
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 [6]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=23067104; DOI=10.1186/1471-2229-12-192;
RA Knip M., de Pater S., Hooykaas P.J.;
RT "The SLEEPER genes: a transposase-derived angiosperm-specific gene
RT family.";
RL BMC Plant Biol. 12:192-192(2012).
CC -!- FUNCTION: Transposase-like protein that is essential for plant growth
CC and development. Binds the promoter region of the DNA helicase KU70 and
CC genes involved in chromatin remodeling. May regulate global gene
CC expression by recruiting other cellular factors.
CC {ECO:0000269|PubMed:16015335, ECO:0000269|PubMed:23067104}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:23067104}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23067104}.
CC -!- DISRUPTION PHENOTYPE: Very slow growth and absence of expansion of
CC cotyledons or development of normal leaves or floral organs. Short root
CC with an excess of abnormal root hairs. Extremely rare production of
CC some photosynthetic tissue. {ECO:0000269|PubMed:16015335,
CC ECO:0000269|PubMed:23067104}.
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DR EMBL; AY728267; AAW28145.1; -; mRNA.
DR EMBL; AL137079; CAB68118.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77728.1; -; Genomic_DNA.
DR EMBL; BT003157; AAO24589.1; -; mRNA.
DR EMBL; AK227645; BAE99632.1; -; mRNA.
DR PIR; T46111; T46111.
DR RefSeq; NP_189803.1; NM_114084.3.
DR AlphaFoldDB; Q9M2N5; -.
DR SMR; Q9M2N5; -.
DR BioGRID; 529778; 7.
DR STRING; 3702.AT3G42170.1; -.
DR iPTMnet; Q9M2N5; -.
DR PaxDb; Q9M2N5; -.
DR PRIDE; Q9M2N5; -.
DR ProteomicsDB; 224294; -.
DR EnsemblPlants; AT3G42170.1; AT3G42170.1; AT3G42170.
DR GeneID; 3769417; -.
DR Gramene; AT3G42170.1; AT3G42170.1; AT3G42170.
DR KEGG; ath:AT3G42170; -.
DR Araport; AT3G42170; -.
DR TAIR; locus:2100809; AT3G42170.
DR eggNOG; KOG1121; Eukaryota.
DR HOGENOM; CLU_009123_1_2_1; -.
DR InParanoid; Q9M2N5; -.
DR OrthoDB; 223749at2759; -.
DR PhylomeDB; Q9M2N5; -.
DR PRO; PR:Q9M2N5; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M2N5; baseline and differential.
DR Genevisible; Q9M2N5; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IPI:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0009791; P:post-embryonic development; IMP:TAIR.
DR InterPro; IPR045259; DAYSLEEPER-like.
DR InterPro; IPR025525; hAT-like_transposase_RNase-H.
DR InterPro; IPR008906; HATC_C_dom.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR003656; Znf_BED.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR PANTHER; PTHR23272; PTHR23272; 1.
DR Pfam; PF05699; Dimer_Tnp_hAT; 1.
DR Pfam; PF14372; DUF4413; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR SUPFAM; SSF57667; SSF57667; 1.
DR PROSITE; PS50808; ZF_BED; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Metal-binding; Nucleus; Reference proteome; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..696
FT /note="Zinc finger BED domain-containing protein
FT DAYSLEEPER"
FT /id="PRO_0000429561"
FT ZN_FING 65..132
FT /note="BED-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00027"
FT REGION 129..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 592..674
FT /note="HATC (Hobo-Ac-Tam3) domain"
FT BINDING 88
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00027"
FT BINDING 91
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00027"
FT BINDING 112
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00027"
FT BINDING 125
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00027"
FT MUTAGEN 70
FT /note="V->A: Loss of DNA-binding capacity."
FT /evidence="ECO:0000269|PubMed:16015335"
FT MUTAGEN 73
FT /note="H->A: Loss of DNA-binding capacity."
FT /evidence="ECO:0000269|PubMed:16015335"
FT MUTAGEN 88
FT /note="C->A: Loss of DNA-binding capacity."
FT /evidence="ECO:0000269|PubMed:16015335"
FT MUTAGEN 91
FT /note="C->A: Loss of DNA-binding capacity."
FT /evidence="ECO:0000269|PubMed:16015335"
FT MUTAGEN 109
FT /note="L->A: Loss of DNA-binding capacity."
FT /evidence="ECO:0000269|PubMed:16015335"
FT MUTAGEN 112
FT /note="H->A: Loss of DNA-binding capacity."
FT /evidence="ECO:0000269|PubMed:16015335"
FT MUTAGEN 118
FT /note="C->A: Loss of DNA-binding capacity."
FT /evidence="ECO:0000269|PubMed:16015335"
FT CONFLICT 338
FT /note="A -> G (in Ref. 1; AAW28145)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 696 AA; 78814 MW; 284852E0A1ABAABB CRC64;
MEVYNDDTEM RSPETQPIKE TALEVYNDTA EIRSPETQPI EETALEVYND TEMVSPETQP
IKRRKKKSMV WEHFTIEAVE PNCRRAFCKG CNQSFAYSNG NKVAGTSHLK RHIFKGTCPA
LIHTHDNDNN PLMSTPYTPK TDTPRRRYRS QNNASPYVAF NQDKCRQEIA KMIIMHDYPL
HMVQHPGFVS FVQSIQPHFD AVSFNNVQGD CVATYLAEKQ NVMKSLEGIP GRFCLTLDFW
TSKLTLGYVF ITAHYIDSDW KIQKKLLNVL MESYPEADEA LSLAVANCVS EWGLEGKLFN
VTFNHPASNS AVENIRPQLC IKNPGILDGQ LVIGNCVART FGSLAKDVLE KGKDVIKNIR
DSVKHVKTSE SHEERFTELK EQLQVPSEKV LSLDDQTQWN TTYMMLVAAS ELKEVFSCLD
TADPDYKKPP SAEDWRHVEA LCTFLKPLFE AVSTLQSTGN PSAVTFFHEV WKTQSDLSRA
IAGEDPFVTG IAKTMQEKVD KYWRDCSLVL AMAVVMDPRF KMKLVEFSFS KIFGEDAGKN
IKTVDDGIHE LFTEYMALPS PQNTTSEGGK ADGLSDFDTY IMETTGQNLK SELDQYLDET
LLPRVQEFDV LDWWKQNKLK YPTLSKMARD ILSIPVSAAA FDYVFDMEPR EMDEYKTSLR
PETVEALICA REWLLESNAS SSAAAQNASA TIKSEA
