RSL2_ARATH
ID RSL2_ARATH Reviewed; 352 AA.
AC Q84WK0; O81756; Q8S3D3;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Transcription factor RSL2 {ECO:0000305};
DE AltName: Full=Basic helix-loop-helix protein 85 {ECO:0000303|PubMed:12679534};
DE Short=AtbHLH85 {ECO:0000303|PubMed:12679534};
DE Short=bHLH 85 {ECO:0000303|PubMed:12679534};
DE AltName: Full=Protein ROOT HAIR DEFECTIVE 6-LIKE 2 {ECO:0000303|PubMed:20139979};
DE Short=Protein RHD SIX-LIKE 2 {ECO:0000303|PubMed:20139979};
DE AltName: Full=Transcription factor EN 115 {ECO:0000305};
DE AltName: Full=Transcription factor bHLH85 {ECO:0000305};
DE AltName: Full=bHLH transcription factor bHLH085 {ECO:0000303|PubMed:12679534};
GN Name=RSL2 {ECO:0000303|PubMed:20139979};
GN Synonyms=BHLH85 {ECO:0000303|PubMed:12679534}, EN115 {ECO:0000305};
GN OrderedLocusNames=At4g33880 {ECO:0000312|Araport:AT4G33880};
GN ORFNames=F17I5.70 {ECO:0000312|EMBL:CAA19870.1};
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], TISSUE SPECIFICITY, INDUCTION, GENE FAMILY, AND
RP NOMENCLATURE.
RC STRAIN=cv. Columbia; TISSUE=Root;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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 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, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP 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.
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 [10]
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 [11]
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:27452638). Does not seem to be a
CC 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:29651114). {ECO:0000269|PubMed:20139979,
CC ECO:0000269|PubMed:27452638, ECO:0000269|PubMed:29651114}.
CC -!- SUBUNIT: Homodimer. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981,
CC ECO:0000269|PubMed:20139979}.
CC -!- TISSUE SPECIFICITY: Expressed in roots (PubMed:12679534). Expressed in
CC root epidermal hair cells (PubMed:20139979).
CC {ECO:0000269|PubMed:12679534, ECO:0000269|PubMed:20139979}.
CC -!- INDUCTION: Induced by jasmonate (JA) treatment (PubMed:12679534,
CC PubMed:31988260). Induced by low phosphate conditions
CC (PubMed:29651114). {ECO:0000269|PubMed:12679534,
CC ECO:0000269|PubMed:29651114, ECO:0000269|PubMed:31988260}.
CC -!- DISRUPTION PHENOTYPE: Reduced length of root hairs.
CC {ECO:0000269|PubMed:20139979}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA19870.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB80105.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF488616; AAM10959.1; -; mRNA.
DR EMBL; AL031032; CAA19870.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161584; CAB80105.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE86287.1; -; Genomic_DNA.
DR EMBL; BT003137; AAO24569.1; -; mRNA.
DR EMBL; AK228110; BAF00068.1; -; mRNA.
DR PIR; T05216; T05216.
DR RefSeq; NP_195114.2; NM_119546.3.
DR AlphaFoldDB; Q84WK0; -.
DR SMR; Q84WK0; -.
DR BioGRID; 14813; 13.
DR IntAct; Q84WK0; 10.
DR STRING; 3702.AT4G33880.1; -.
DR PaxDb; Q84WK0; -.
DR PRIDE; Q84WK0; -.
DR EnsemblPlants; AT4G33880.1; AT4G33880.1; AT4G33880.
DR GeneID; 829531; -.
DR Gramene; AT4G33880.1; AT4G33880.1; AT4G33880.
DR KEGG; ath:AT4G33880; -.
DR Araport; AT4G33880; -.
DR TAIR; locus:2118934; AT4G33880.
DR eggNOG; ENOG502R684; Eukaryota.
DR HOGENOM; CLU_066110_1_0_1; -.
DR InParanoid; Q84WK0; -.
DR OMA; YWNLGSH; -.
DR OrthoDB; 987931at2759; -.
DR PhylomeDB; Q84WK0; -.
DR PRO; PR:Q84WK0; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q84WK0; baseline and differential.
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: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 2: Evidence at transcript level;
KW DNA-binding; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..352
FT /note="Transcription factor RSL2"
FT /id="PRO_0000358777"
FT DOMAIN 272..321
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 160..277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 272..285
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 286..321
FT /note="Helix-loop-helix motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT COMPBIAS 174..193
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..237
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 246..260
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 44
FT /note="A -> T (in Ref. 1; AAM10959)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 352 AA; 38770 MW; AFEF4240622565BB CRC64;
MEAMGEWSNN LGGMYTYATE EADFMNQLLA SYDHPGTGSS SGAAASGDHQ GLYWNLGSHH
NHLSLVSEAG SFCFSQESSS YSAGNSGYYT VVPPTVEENQ NETMDFGMED VTINTNSYLV
GEETSECDVE KYSSGKTLMP LETVVENHDD EESLLQSEIS VTTTKSLTGS KKRSRATSTD
KNKRARVNKR AQKNVEMSGD NNEGEEEEGE TKLKKRKNGA MMSRQNSSTT FCTEEESNCA
DQDGGGEDSS SKEDDPSKAL NLNGKTRASR GAATDPQSLY ARKRRERINE RLRILQNLVP
NGTKVDISTM LEEAVHYVKF LQLQIKLLSS DDLWMYAPIA FNGMDIGLSS PR
