RSL4_ARATH
ID RSL4_ARATH Reviewed; 258 AA.
AC Q8LEG1; A0A178WM21; C0SUX8; Q9SFY5;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Transcription factor RSL3 {ECO:0000305};
DE AltName: Full=Basic helix-loop-helix protein 54 {ECO:0000303|PubMed:12679534};
DE Short=AtbHLH54 {ECO:0000303|PubMed:12679534};
DE Short=bHLH 54 {ECO:0000303|PubMed:12679534};
DE AltName: Full=ROOT HAIR DEFECTIVE 6-LIKE 4 {ECO:0000303|PubMed:20139979};
DE Short=Protein RHD SIX-LIKE 4 {ECO:0000303|PubMed:20139979};
DE AltName: Full=Transcription factor EN 114 {ECO:0000305};
DE AltName: Full=Transcription factor bHLH54 {ECO:0000305};
DE AltName: Full=bHLH transcription factor bHLH054 {ECO:0000303|PubMed:12679534};
GN Name=RSL4 {ECO:0000303|PubMed:20139979};
GN Synonyms=BHLH54 {ECO:0000303|PubMed:12679534}, EN114 {ECO:0000305};
GN OrderedLocusNames=At1g27740 {ECO:0000312|Araport:AT1G27740};
GN ORFNames=T22C5.19 {ECO:0000312|EMBL:AAF24948.1};
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].
RA Fujita M.;
RT "ORF cloning and analysis of Arabidopsis transcription factor genes.";
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [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].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP TISSUE SPECIFICITY, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=12679534; DOI=10.1093/molbev/msg088;
RA Heim M.A., Jakoby M., Werber M., Martin C., Weisshaar B., Bailey P.C.;
RT "The basic helix-loop-helix transcription factor family in plants: a
RT genome-wide study of protein structure and functional diversity.";
RL Mol. Biol. Evol. 20:735-747(2003).
RN [6]
RP GENE FAMILY.
RX PubMed=12897250; DOI=10.1105/tpc.013839;
RA Toledo-Ortiz G., Huq E., Quail P.H.;
RT "The Arabidopsis basic/helix-loop-helix transcription factor family.";
RL Plant Cell 15:1749-1770(2003).
RN [7]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=14600211; DOI=10.1105/tpc.151140;
RA Bailey P.C., Martin C., Toledo-Ortiz G., Quail P.H., Huq E., Heim M.A.,
RA Jakoby M., Werber M., Weisshaar B.;
RT "Update on the basic helix-loop-helix transcription factor gene family in
RT Arabidopsis thaliana.";
RL Plant Cell 15:2497-2502(2003).
RN [8]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=20139979; DOI=10.1038/ng.529;
RA Yi K., Menand B., Bell E., Dolan L.;
RT "A basic helix-loop-helix transcription factor controls cell growth and
RT size in root hairs.";
RL Nat. Genet. 42:264-267(2010).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, INDUCTION BY LOW PHOSPHATE, D-BOX MOTIF,
RP UBIQUITINATION, AND MUTAGENESIS OF ARG-98 AND LEU-101.
RX PubMed=27251390; DOI=10.1038/nplants.2015.138;
RA Datta S., Prescott H., Dolan L.;
RT "Intensity of a pulse of RSL4 transcription factor synthesis determines
RT Arabidopsis root hair cell size.";
RL Nat. Plants 1:15138-15138(2015).
RN [10]
RP FUNCTION.
RX PubMed=27452638; DOI=10.1111/nph.14095;
RA Vijayakumar P., Datta S., Dolan L.;
RT "ROOT HAIR DEFECTIVE SIX-LIKE4 (RSL4) promotes root hair elongation by
RT transcriptionally regulating the expression of genes required for cell
RT growth.";
RL New Phytol. 212:944-953(2016).
RN [11]
RP FUNCTION, AND INDUCTION BY LOW PHOSPHATE.
RX PubMed=29651114; DOI=10.1038/s41467-018-03851-3;
RA Bhosale R., Giri J., Pandey B.K., Giehl R.F.H., Hartmann A., Traini R.,
RA Truskina J., Leftley N., Hanlon M., Swarup K., Rashed A., Voss U.,
RA Alonso J., Stepanova A., Yun J., Ljung K., Brown K.M., Lynch J.P.,
RA Dolan L., Vernoux T., Bishopp A., Wells D., von Wiren N., Bennett M.J.,
RA Swarup R.;
RT "A mechanistic framework for auxin dependent Arabidopsis root hair
RT elongation to low external phosphate.";
RL Nat. Commun. 9:1409-1409(2018).
RN [12]
RP INDUCTION BY JASMONATE.
RX PubMed=31988260; DOI=10.1105/tpc.19.00617;
RA Han X., Zhang M., Yang M., Hu Y.;
RT "Arabidopsis JAZ proteins interact with and suppress RHD6 transcription
RT factor to regulate jasmonate-stimulated root hair development.";
RL Plant Cell 32:1049-1062(2020).
CC -!- FUNCTION: Transcription factor involved in the regulation of root hair
CC elongation (PubMed:20139979, PubMed:27251390, PubMed:27452638). Is
CC sufficient to promote postmitotic cell growth in root-hair cells and is
CC a direct transcriptional target of RHD6 and RSL1 (PubMed:20139979).
CC Involved in the regulation of root hair elongation in response to low
CC phosphate (PubMed:27251390, PubMed:29651114). Controls root hair cell
CC growth by regulating the expression of genes encoding proteins involved
CC in cell signaling, cell wall modification and secretion
CC (PubMed:27452638). {ECO:0000269|PubMed:20139979,
CC ECO:0000269|PubMed:27251390, ECO:0000269|PubMed:27452638,
CC ECO:0000269|PubMed:29651114}.
CC -!- SUBUNIT: Homodimer. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981,
CC ECO:0000269|PubMed:20139979, ECO:0000269|PubMed:27251390}.
CC -!- TISSUE SPECIFICITY: Expressed constitutively in roots, leaves, and
CC flowers (PubMed:12679534). Expressed in root epidermal hair cells
CC (PubMed:20139979). {ECO:0000269|PubMed:12679534,
CC ECO:0000269|PubMed:20139979}.
CC -!- INDUCTION: Induced by jasmonate (JA) treatment (PubMed:31988260).
CC Induced by low phosphate conditions (PubMed:27251390, PubMed:29651114).
CC {ECO:0000269|PubMed:27251390, ECO:0000269|PubMed:29651114,
CC ECO:0000269|PubMed:31988260}.
CC -!- DOMAIN: D-box [RxxLxxxN] motif functions as a recognition motif for the
CC ubiquitination machinery. {ECO:0000269|PubMed:27251390}.
CC -!- PTM: Ubiquitinated (Probable). Ubiquitination leads to its subsequent
CC degradation by the 26S proteasome (PubMed:27251390).
CC {ECO:0000269|PubMed:27251390, ECO:0000305|PubMed:27251390}.
CC -!- DISRUPTION PHENOTYPE: Strong reduction in root hair number, density and
CC length in seedlings. {ECO:0000269|PubMed:20139979}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF24948.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB493481; BAH30319.1; -; mRNA.
DR EMBL; AC012375; AAF24948.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE30871.1; -; Genomic_DNA.
DR EMBL; AY085436; AAM62663.1; -; mRNA.
DR PIR; B86402; B86402.
DR RefSeq; NP_564293.1; NM_102539.3.
DR AlphaFoldDB; Q8LEG1; -.
DR SMR; Q8LEG1; -.
DR BioGRID; 24902; 3.
DR STRING; 3702.AT1G27740.1; -.
DR PaxDb; Q8LEG1; -.
DR PRIDE; Q8LEG1; -.
DR EnsemblPlants; AT1G27740.1; AT1G27740.1; AT1G27740.
DR GeneID; 839667; -.
DR Gramene; AT1G27740.1; AT1G27740.1; AT1G27740.
DR KEGG; ath:AT1G27740; -.
DR Araport; AT1G27740; -.
DR TAIR; locus:2199221; AT1G27740.
DR eggNOG; ENOG502QWSN; Eukaryota.
DR HOGENOM; CLU_1241620_0_0_1; -.
DR InParanoid; Q8LEG1; -.
DR OMA; PAMLDSW; -.
DR OrthoDB; 987931at2759; -.
DR PhylomeDB; Q8LEG1; -.
DR PRO; PR:Q8LEG1; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8LEG1; baseline and differential.
DR Genevisible; Q8LEG1; AT.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:TAIR.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:TAIR.
DR GO; GO:0009733; P:response to auxin; IEP:TAIR.
DR GO; GO:0048766; P:root hair initiation; IMP:TAIR.
DR Gene3D; 4.10.280.10; -; 1.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
DR Pfam; PF00010; HLH; 1.
DR SMART; SM00353; HLH; 1.
DR SUPFAM; SSF47459; SSF47459; 1.
DR PROSITE; PS50888; BHLH; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Nucleus; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..258
FT /note="Transcription factor RSL3"
FT /id="PRO_0000358751"
FT DOMAIN 173..222
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 119..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 173..186
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 187..222
FT /note="Helix-loop-helix motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT MOTIF 98..105
FT /note="D-box"
FT /evidence="ECO:0000269|PubMed:27251390"
FT COMPBIAS 133..177
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 98
FT /note="R->G: Decreases degradation by the 26S proteasome
FT and increases the lifetime of RSL4 protein; when associated
FT with V-101."
FT /evidence="ECO:0000269|PubMed:27251390"
FT MUTAGEN 101
FT /note="L->V: Decreases degradation by the 26S proteasome
FT and increases the lifetime of RSL4 protein; when associated
FT with G-98."
FT /evidence="ECO:0000269|PubMed:27251390"
SQ SEQUENCE 258 AA; 29160 MW; DF2E9CF8DD6F4240 CRC64;
MDVFVDGELE SLLGMFNFDQ CSSSKEERPR DELLGLSSLY NGHLHQHQHH NNVLSSDHHA
FLLPDMFPFG AMPGGNLPAM LDSWDQSHHL QETSSLKRKL LDVENLCKTN SNCDVTRQEL
AKSKKKQRVS SESNTVDESN TNWVDGQSLS NSSDDEKASV TSVKGKTRAT KGTATDPQSL
YARKRREKIN ERLKTLQNLV PNGTKVDIST MLEEAVHYVK FLQLQIKLLS SDDLWMYAPL
AYNGLDMGFH HNLLSRLM
