RHL1_ARATH
ID RHL1_ARATH Reviewed; 355 AA.
AC O81242; B3H502; Q9SBG7;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=DNA-binding protein RHL1;
DE AltName: Full=Protein ELONGATED HYPOCOTYL 7;
DE AltName: Full=Protein ROOT HAIRLESS 1;
GN Name=RHL1; Synonyms=HYP7; OrderedLocusNames=At1g48380; ORFNames=F11A17.7;
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 [GENOMIC DNA / MRNA] (ISOFORM 1), TISSUE SPECIFICITY,
RP DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX PubMed=9649505; DOI=10.1101/gad.12.13.2013;
RA Schneider K., Mathur J., Boudonck K., Wells B., Dolan L., Roberts K.;
RT "The ROOT HAIRLESS 1 gene encodes a nuclear protein required for root hair
RT initiation in Arabidopsis.";
RL Genes Dev. 12:2013-2021(1998).
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] (ISOFORM 1).
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 FUNCTION, MUTAGENESIS OF GLY-79, AND INTERACTION WITH TOP6A AND TOP6B.
RX PubMed=16339310; DOI=10.1073/pnas.0505883102;
RA Sugimoto-Shirasu K., Roberts G.R., Stacey N.J., McCann M.C., Maxwell A.,
RA Roberts K.;
RT "RHL1 is an essential component of the plant DNA topoisomerase VI complex
RT and is required for ploidy-dependent cell growth.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:18736-18741(2005).
RN [6]
RP INTERACTION WITH BIN4.
RX PubMed=17951446; DOI=10.1105/tpc.107.054361;
RA Kirik V., Schrader A., Uhrig J.F., Hulskamp M.;
RT "MIDGET unravels functions of the Arabidopsis topoisomerase VI complex in
RT DNA endoreduplication, chromatin condensation, and transcriptional
RT silencing.";
RL Plant Cell 19:3100-3110(2007).
RN [7]
RP INTERACTION WITH BIN4.
RX PubMed=18055605; DOI=10.1105/tpc.107.054833;
RA Breuer C., Stacey N.J., West C.E., Zhao Y., Chory J., Tsukaya H., Azumi Y.,
RA Maxwell A., Roberts K., Sugimoto-Shirasu K.;
RT "BIN4, a novel component of the plant DNA topoisomerase VI complex, is
RT required for endoreduplication in Arabidopsis.";
RL Plant Cell 19:3655-3668(2007).
CC -!- FUNCTION: Component of the DNA topoisomerase VI complex involved in
CC chromatin organization and progression of endoreduplication cycles.
CC Binds to DNA. Required for endoreduplication beyond 8C.
CC {ECO:0000269|PubMed:16339310}.
CC -!- SUBUNIT: Interacts with BIN4 and TOP6A, but not with TOP6B.
CC {ECO:0000269|PubMed:16339310, ECO:0000269|PubMed:17951446,
CC ECO:0000269|PubMed:18055605}.
CC -!- INTERACTION:
CC O81242; Q9LZ03: TOP6A; NbExp=2; IntAct=EBI-1772159, EBI-1772104;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9649505}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O81242-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O81242-2; Sequence=VSP_034979;
CC -!- TISSUE SPECIFICITY: Expressed inproliferating and endoreduplicating
CC cells. {ECO:0000269|PubMed:9649505}.
CC -!- DISRUPTION PHENOTYPE: Plants have no hairs on primary roots and have an
CC extreme dwarf and seedling lethal phenotype.
CC {ECO:0000269|PubMed:9649505}.
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DR EMBL; AF062371; AAC23500.1; -; mRNA.
DR EMBL; AF062372; AAC69460.1; -; Genomic_DNA.
DR EMBL; AC007932; AAD49759.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32282.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32283.1; -; Genomic_DNA.
DR EMBL; AY057707; AAL15337.1; -; mRNA.
DR EMBL; AY133623; AAM91453.1; -; mRNA.
DR PIR; T52177; T52177.
DR RefSeq; NP_001117449.1; NM_001123977.1. [O81242-2]
DR RefSeq; NP_564526.1; NM_103734.3. [O81242-1]
DR AlphaFoldDB; O81242; -.
DR IntAct; O81242; 2.
DR STRING; 3702.AT1G48380.2; -.
DR iPTMnet; O81242; -.
DR PRIDE; O81242; -.
DR ProteomicsDB; 236916; -. [O81242-1]
DR EnsemblPlants; AT1G48380.1; AT1G48380.1; AT1G48380. [O81242-1]
DR EnsemblPlants; AT1G48380.2; AT1G48380.2; AT1G48380. [O81242-2]
DR GeneID; 841258; -.
DR Gramene; AT1G48380.1; AT1G48380.1; AT1G48380. [O81242-1]
DR Gramene; AT1G48380.2; AT1G48380.2; AT1G48380. [O81242-2]
DR KEGG; ath:AT1G48380; -.
DR Araport; AT1G48380; -.
DR TAIR; locus:2007720; AT1G48380.
DR eggNOG; ENOG502QVIA; Eukaryota.
DR HOGENOM; CLU_040605_0_0_1; -.
DR InParanoid; O81242; -.
DR OMA; RVREEPQ; -.
DR OrthoDB; 737479at2759; -.
DR PhylomeDB; O81242; -.
DR PRO; PR:O81242; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O81242; baseline and differential.
DR Genevisible; O81242; AT.
DR GO; GO:0005730; C:nucleolus; IDA:TAIR.
DR GO; GO:0003677; F:DNA binding; IDA:TAIR.
DR GO; GO:0042023; P:DNA endoreduplication; IMP:TAIR.
DR GO; GO:0048766; P:root hair initiation; IMP:TAIR.
DR InterPro; IPR038859; RHL1.
DR PANTHER; PTHR35698; PTHR35698; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; DNA-binding; Nucleus; Reference proteome.
FT CHAIN 1..355
FT /note="DNA-binding protein RHL1"
FT /id="PRO_0000346108"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 181..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 229..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..26
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..271
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..294
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 311..325
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 173
FT /note="A -> AQVDTFHLFLHFLFKTMVATEMFNMIRRILWF (in isoform
FT 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_034979"
FT MUTAGEN 79
FT /note="G->D: In hyp7/rhl1-2; dwarf and reduced ploidy
FT phenotype, but DNA binding only slightly reduced."
FT /evidence="ECO:0000269|PubMed:16339310"
FT CONFLICT 52
FT /note="S -> T (in Ref. 1; AAC69460)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 355 AA; 38904 MW; D0B2EA050D5095BA CRC64;
MVRASSSKKG GSKGGDKDDA ESKQRKRLKT LALDNQLLSD SPAKSHSSLK PSKQVLKHHG
TDIIRKSQRK NRFLFSFPGL LAPISAATIG DLDRLSTKNP VLYLNFPQGR MKLFGTILYP
KNRYLTLQFS RGGKNVLCDD YFDNMIVFSE SWWIGTKEEN PEEARLDFPK ELAQAENTEF
DFQGGAGGAA SVKKLASPEI GSQPTETDSP EVDNEDVLSE DGEFLDDKIQ VTPPVQLTPP
VQVTPVRQSQ RNSGKKFNFA ETSSEASSGE SEGNTSDEDE KPLLEPESST RSREESQDGN
GITASASKLP EELPAKREKL KSKDSKLVQA TLSNLFKKAE EKTAGTSKAK SSSKA
