RLT2_ARATH
ID RLT2_ARATH Reviewed; 1694 AA.
AC Q9FFH1; Q94B27;
DT 09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 153.
DE RecName: Full=Homeobox-DDT domain protein RLT2 {ECO:0000305};
DE AltName: Full=Protein RINGLET 2 {ECO:0000303|PubMed:22694359};
GN Name=RLT2 {ECO:0000303|PubMed:22694359};
GN OrderedLocusNames=At5g44180 {ECO:0000312|Araport:AT5G44180,
GN ECO:0000312|EMBL:AED95070.1};
GN ORFNames=MLN1.10 {ECO:0000312|EMBL:BAB10985.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9330910; DOI=10.1093/dnares/4.3.215;
RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT features of the 1.6 Mb regions covered by twenty physically assigned P1
RT clones.";
RL DNA Res. 4:215-230(1997).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1392-1694 AND 1440-1694.
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-806 AND SER-808, AND
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 [5]
RP FUNCTION, INTERACTION WITH CHR11, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=22694359; DOI=10.1111/j.1365-313x.2012.05074.x;
RA Li G., Zhang J., Li J., Yang Z., Huang H., Xu L.;
RT "Imitation Switch chromatin remodeling factors and their interacting
RT RINGLET proteins act together in controlling the plant vegetative phase in
RT Arabidopsis.";
RL Plant J. 72:261-270(2012).
RN [6]
RP INTERACTION WITH CHR11.
RX PubMed=23691993; DOI=10.1111/jipb.12069;
RA Dong J., Gao Z., Liu S., Li G., Yang Z., Huang H., Xu L.;
RT "SLIDE, the protein interacting domain of Imitation Switch remodelers,
RT binds DDT-domain proteins of different subfamilies in chromatin remodeling
RT complexes.";
RL J. Integr. Plant Biol. 55:928-937(2013).
RN [7]
RP FUNCTION.
RX PubMed=23872538; DOI=10.1105/tpc.113.112714;
RA Sundaram S., Kertbundit S., Shakirov E.V., Iyer L.M., Juricek M.,
RA Hall T.C.;
RT "Gene networks and chromatin and transcriptional regulation of the
RT phaseolin promoter in Arabidopsis.";
RL Plant Cell 25:2601-2617(2013).
CC -!- FUNCTION: Transcriptional regulator required for the maintenance of the
CC plant vegetative phase. In association with CHR11 or CHR17 may prevent
CC the early activation of the vegetative-to-reproductive transition by
CC regulating key genes that contribute to flower timing, such as FT,
CC SEP1, SEP3, AGL8/FUL, SOC1 and FLC (PubMed:22694359). Involved in the
CC transcriptional regulation of seed-specific gene expression
CC (PubMed:23872538). {ECO:0000269|PubMed:22694359,
CC ECO:0000269|PubMed:23872538}.
CC -!- SUBUNIT: Interacts with CHR11 (PubMed:22694359). Interacts (via the DDT
CC domain) with CHR11 (via C-terminus) (PubMed:23691993).
CC {ECO:0000269|PubMed:22694359, ECO:0000269|PubMed:23691993}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22694359}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences. {ECO:0000305};
CC Name=1;
CC IsoId=Q9FFH1-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Highly expressed in growing tissues such as
CC inflorescence and flower meristems, young leaves and floral organs.
CC Expressed in roots, rosette and cauline leaves, stems, flowers,
CC inflorescences and siliques. {ECO:0000269|PubMed:22694359}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but the double mutant plants rlt-1 and rlt2-1 are small and
CC display early flowering. {ECO:0000269|PubMed:22694359}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK68833.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB005239; BAB10985.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95070.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM68709.1; -; Genomic_DNA.
DR EMBL; AY042893; AAK68833.1; ALT_INIT; mRNA.
DR EMBL; AY072465; AAL66880.1; -; mRNA.
DR RefSeq; NP_001318738.1; NM_001344536.1. [Q9FFH1-1]
DR RefSeq; NP_199231.1; NM_123785.1. [Q9FFH1-1]
DR AlphaFoldDB; Q9FFH1; -.
DR SMR; Q9FFH1; -.
DR STRING; 3702.AT5G44180.1; -.
DR iPTMnet; Q9FFH1; -.
DR PaxDb; Q9FFH1; -.
DR PRIDE; Q9FFH1; -.
DR ProteomicsDB; 228161; -. [Q9FFH1-1]
DR EnsemblPlants; AT5G44180.1; AT5G44180.1; AT5G44180. [Q9FFH1-1]
DR EnsemblPlants; AT5G44180.3; AT5G44180.3; AT5G44180. [Q9FFH1-1]
DR GeneID; 834441; -.
DR Gramene; AT5G44180.1; AT5G44180.1; AT5G44180. [Q9FFH1-1]
DR Gramene; AT5G44180.3; AT5G44180.3; AT5G44180. [Q9FFH1-1]
DR KEGG; ath:AT5G44180; -.
DR Araport; AT5G44180; -.
DR TAIR; locus:2167628; AT5G44180.
DR eggNOG; ENOG502QQYM; Eukaryota.
DR InParanoid; Q9FFH1; -.
DR OMA; MWDNMLH; -.
DR OrthoDB; 70733at2759; -.
DR PhylomeDB; Q9FFH1; -.
DR PRO; PR:Q9FFH1; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FFH1; baseline and differential.
DR GO; GO:0031010; C:ISWI-type complex; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IPI:TAIR.
DR GO; GO:0009908; P:flower development; IEA:UniProtKB-KW.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:InterPro.
DR GO; GO:0010228; P:vegetative to reproductive phase transition of meristem; IGI:TAIR.
DR CDD; cd00086; homeodomain; 1.
DR InterPro; IPR007759; Asxl_HARE-HTH.
DR InterPro; IPR018501; DDT_dom.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR001356; Homeobox_dom.
DR InterPro; IPR044977; RLT1/2/3.
DR InterPro; IPR028942; WHIM1_dom.
DR InterPro; IPR028941; WHIM2_dom.
DR PANTHER; PTHR36968; PTHR36968; 1.
DR Pfam; PF02791; DDT; 1.
DR Pfam; PF05066; HARE-HTH; 1.
DR Pfam; PF00046; Homeodomain; 1.
DR Pfam; PF15612; WHIM1; 1.
DR Pfam; PF15613; WSD; 1.
DR SMART; SM00571; DDT; 1.
DR SMART; SM00389; HOX; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR PROSITE; PS50827; DDT; 1.
DR PROSITE; PS50071; HOMEOBOX_2; 1.
DR PROSITE; PS51913; HTH_HARE; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; DNA-binding; Flowering; Homeobox; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..1694
FT /note="Homeobox-DDT domain protein RLT2"
FT /id="PRO_0000435114"
FT DOMAIN 514..573
FT /note="DDT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00063"
FT DOMAIN 696..765
FT /note="HTH HARE-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01261"
FT DNA_BIND 17..76
FT /note="Homeobox"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 795..822
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1450..1541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1555..1639
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1655..1674
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 796..813
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1514..1528
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1623..1637
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 806
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT MOD_RES 808
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT CONFLICT 1673
FT /note="T -> A (in Ref. 3; AAK68833/AAL66880)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1694 AA; 190386 MW; A701F3E8E56B4BFB CRC64;
MEGGSEKTTP EGCGGESKSK RKMKTAAQLE VLENTYSAEP YPSEAIRADL SVKLNLSDRQ
LQMWFCHRRL KERKSTTPSK RQRKELVTPT AMESWEPPVN AGDLVAGNEL DSRRAARGSG
GSGVTVVRRF NEPSSAEVRA IGYVEAQLGE RLRDNGPVLG MEFDPLPPGA FGMPIEMPSH
RKATRQAFET NIYVRSDVKP IKDHVRPIRE YQFIPELPSS RTDHSERVSP SHHFGVPLDG
SVMRVSAVSA GHRDDYKISP QIPNLNLATH QGKPGHVYSP NLVEYDSPYQ KSYMDTAAQV
HDDPFVKSER EVGNEDEDDD ALQLERHRKN EEARIAREVE AHEKRIRREL EKQDMLRRKR
EEQIRKEMER QDRERRKEEE RLLREKQREE ERYLKEQMRE LQRREKFLKK ETIRAEKMRQ
KEEMRKEKEV ARLKAANERA IARKIAKESM ELIEDERLEL MEVAALTKGL PSMLALDFET
LQNLDEYRDK QAIFPPTSVK LKKPFAVKPW NGSDENVANL LMVWRFLITF ADVLGLWPFT
LDEFAQAFHD YDPRLMGEIH IVLLKTIIKD IEGVVRTLST GVGANQNVAA NPGGGHPHVV
EGAYAWGFDI RSWRKNLNVF TWPEILRQLA LSAGLGPQLK KMNIRTVSVH DDNEANNSEN
VIFNLRKGVA AENAFAKMQE RGLSNPRRSR HRLTPGTVKF AAFHVLSLEG EKGLNILEVA
EKIQKSGLRD LTTSRTPEAS VAAALSRDTK LFERVAPSTY CVRASYRKDA GDAETIFAEA
RERIRAFKSG ITDVEDVDDA ERDEDSESDV GEDPEVDVNL KKEDPNPLKV ENLIGVEPLL
ENGKLDTVPM KTELGLPLTP SLPEEMKDEK RDDTLADQSL EDAVANGEDS ACFDESKLGE
QWVQGLVEGD YSNLSSEERL NALVALIGIA TEGNTIRIAL EERLEVASAL KKQMWGEVQL
DKRWKEESLI RANYLSYPTA KPGLNIATPA SGNQESSSAD VTPISSQDPV SLPQIDVNNV
IAGPSLQLQE NVPGVENLQY QQQQGYTADR ERLRAQLKAY VGYKAEELYV YRSLPLGQDR
RRNRYWRFSA SASRNDPGCG RIFVELQDGR WRLIDSEEAF DYLVKSLDVR GVRESHLHFM
LLKIEASFKE ALRRNVAANP GVCSISSSLD SDTAEISTTF KIELGDSNAV ERCSVLQRFH
SFEKWMWDNM LHPSALSAFK YGAKQSSPLF RICRICAELH FVGDICCPSC GQMHAGPDVG
ELCFAEQVAQ LGDNLRRGDT GFILRSSILS PLRIRLLKVQ LALVEASLPP EGLEAFWTEN
LRKSWGMKLL SSSSHEDLYQ VLTTLEAALK RDFLSSNFET TSELLGLQEG ALASDLTCGV
NVLPWIPKTA GGVALRLFDF DSSIVYTPDQ NNDPLKDKES EDFVGLETNI LRNLHEKDVM
ETPVQVAAYK QEENWTDPGL GGVSSSGRGG RPPRGRGRPR ARGNGKKPAV SVKPPRGAAN
SNGETMLRPR AQPRGGRKNG RRSGTKGRKR PTQGTLGICN EVGGGRRVKE VAVTAKTSLP
DNDDDWIETP ELQDDDGEAS SSGRSFQYED YDDDDVMAPI DDFDGGGESS KLVGRGEFSL
HSDDEYEEEE EEEEDMNMKM DVNVVDDEDE DYINEDSYGR KQHGISISND AATRKRFNKF
EDPDLTSSSS SDFQ
