RLT1_ARATH
ID RLT1_ARATH Reviewed; 1705 AA.
AC F4HY56; Q9SGP0;
DT 09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 25-MAY-2022, entry version 73.
DE RecName: Full=Homeobox-DDT domain protein RLT1 {ECO:0000305};
DE AltName: Full=Protein HOMEOBOX-1 {ECO:0000305};
DE AltName: Full=Protein RINGLET 1 {ECO:0000303|PubMed:22694359};
GN Name=RLT1 {ECO:0000303|PubMed:22694359}; Synonyms=HB-1 {ECO:0000305};
GN OrderedLocusNames=At1g28420 {ECO:0000312|Araport:AT1G28420,
GN ECO:0000312|EMBL:AEE30975.1};
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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 FUNCTION, INTERACTION WITH CHR11 AND CHR17, TISSUE SPECIFICITY, AND
RP 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 [4]
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).
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. {ECO:0000269|PubMed:22694359}.
CC -!- SUBUNIT: Interacts with CHR11 and CHR17 (PubMed:22694359). Interacts
CC (via the DDT domain) with CHR11 (via C-terminus) (PubMed:23691993).
CC {ECO:0000269|PubMed:22694359, ECO:0000269|PubMed:23691993}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00063}.
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=AAF16763.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC010155; AAF16763.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE30975.1; -; Genomic_DNA.
DR PIR; E86410; E86410.
DR RefSeq; NP_174164.2; NM_102610.4.
DR AlphaFoldDB; F4HY56; -.
DR SMR; F4HY56; -.
DR STRING; 3702.AT1G28420.1; -.
DR iPTMnet; F4HY56; -.
DR PaxDb; F4HY56; -.
DR PRIDE; F4HY56; -.
DR ProteomicsDB; 227991; -.
DR EnsemblPlants; AT1G28420.1; AT1G28420.1; AT1G28420.
DR GeneID; 839740; -.
DR Gramene; AT1G28420.1; AT1G28420.1; AT1G28420.
DR KEGG; ath:AT1G28420; -.
DR Araport; AT1G28420; -.
DR TAIR; locus:2032505; AT1G28420.
DR eggNOG; ENOG502QQYM; Eukaryota.
DR HOGENOM; CLU_001241_0_1_1; -.
DR InParanoid; F4HY56; -.
DR OMA; LTEGEYC; -.
DR OrthoDB; 70733at2759; -.
DR PRO; PR:F4HY56; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; F4HY56; baseline and differential.
DR GO; GO:0031010; C:ISWI-type complex; IDA:TAIR.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS: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:0048510; P:regulation of timing of transition from vegetative to reproductive phase; 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 DNA-binding; Flowering; Homeobox; Nucleus; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..1705
FT /note="Homeobox-DDT domain protein RLT1"
FT /id="PRO_0000435113"
FT DOMAIN 549..608
FT /note="DDT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00063"
FT DOMAIN 731..800
FT /note="HTH HARE-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01261"
FT DNA_BIND 39..98
FT /note="Homeobox"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 118..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 237..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 296..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 352..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1028..1053
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1198..1229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1441..1502
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1561..1635
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1652..1705
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..45
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..162
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..267
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..322
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 354..414
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1029..1053
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1457..1477
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1579..1599
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1682..1705
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1705 AA; 191990 MW; 6B5CEB6EAD979F69 CRC64;
MEMGSDGEDQ KIRSVVGDAN LNNKKKKIDN NSSSKDGRVK PKRQMKTPFQ LETLEKVYSE
EKYPSEATRA ELSEKLDLSD RQLQMWFCHR RLKDKKDGQS NKPVKSSVAA VQSASVNELP
AAAGSVPEQD SRSDSGSESG CSPYSNSRRN FASGSSSSRA ELDEYETMGK PSYESRLSTM
VHRAIVCIEA QLGEPLRDDG PILGMEFDPL PPGAFGTPIA MQKHLLHPYE SDLYERHDPR
PRRSHAAARS FHEQQSLDDP SSFTPNMYER YSENHARGMD YEVARSRISS FMHANGPVPR
SYVTPGHASR NCSTSQQDMP SPIESAHHGD RFLLEKDSSV LGTEDPYLLP DGVRKSSDVH
RKGKINDGRL GRGSETRENH GPKDLEKLEI QRKKNEERMR KEMERNERER RKEEERLMRE
RIKEEERLQR EQRREVERRE KFLQRENERA EKKKQKDEIR REKDAIRRKL AIEKATARRI
AKESMDLIED EQLELMELAA ISKGLPSVLQ LDHDTLQNLE VYRDSLSTFP PKSLQLKMPF
AISPWKDSDE TVGNLLMVWR FLISFSDVLD LWPFTLDEFI QAFHDYDSRL LGEIHVTLLR
SIIRDVEDVA RTPFSGIGNN QYTTANPEGG HPQIVEGAYA WGFDIRSWKK HLNPLTWPEI
LRQLALSAGF GPKLKKKHSR LTNTGDKDEA KGCEDVISTI RNGTAAESAF ASMREKGLLA
PRKSRHRLTP GTVKFAAFHV LSLEGSKGLT VLELADKIQK SGLRDLTTSK TPEASISVAL
TRDVKLFERI APSTYCVRAP YVKDPKDGEA ILADARKKIR AFENGFTGPE DVNDLERDED
FEIDIDEDPE VDDLATLASA SKSAVLGEAN VLSGKGVDTM FCDVKADVKS ELEKEFSSPP
PSTMKSIVPQ HSERHKNTVV GGVDAVIDES NQGQSWIQGL TEGDYCHLSV EERLNALVAL
VGIANEGNSI RTGLEDRMEA ANALKKQMWA EAQLDNSCMR DVLKLDLQNL ASSKTESTIG
LPIIQSSTRE RDSFDRDPSQ LLDETKPLED LSNDLHKSSA ERALINQDAN ISQENYASKR
SRSQLKSYIG HKAEEVYPYR SLPLGQDRRH NRYWHFAVSV SKSDPCSRLL FVELHDGKWL
LIDSEEAFDI LVASLDMRGI RESHLRIMLQ KIEGSFKENA CKDIKLARNP FLTEKSVVNH
SPTDSVSPSS SAISGSNSDS METSTSIRVD LGRNDTENKN LSKRFHDFQR WMWTETYSSL
PSCARKYGKK RSELLATCDA CVASYLSEYT FCSSCHQRLD VVDSSEILDS GLAVSPLPFG
VRLLKPLLVF LEASVPDEAL ESFWTEDQRK KWGFRLNTSS SPGELLQVLT SLESAIKKES
LSSNFMSAKE LLGAANAEAD DQGSVDVLPW IPKTVSAVAL RLSELDASII YVKPEKPEVI
PEDENEQISL FPRDSPFKGK GPREQEDQDE VAPNPGNRNK KRARVSLGSG SNRKVKRKKA
QSGLNKFVVG RRNVAVNSNL MAVELNHQVP GKGKRTVRKR PERIDEDNSH LVNRMANIVR
PKSEEVEEDE EEEEQTFRDI NEDWAAGETP REMEEDWANE TPNRMMTPMQ VDDESDNSVG
VESEDEDGGG QFVDYSQRNK WGLDWNSNLN VAIEEDEEEE VVGVGRVEGE DDAEMSESSE
DDDVPANNAA NNYDRESEGY SSSDS
