TPL_ARATH
ID TPL_ARATH Reviewed; 1131 AA.
AC Q94AI7; Q9LMQ9;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Protein TOPLESS;
DE AltName: Full=WUS-interacting protein 1;
GN Name=TPL; Synonyms=WSIP1; OrderedLocusNames=At1g15750; ORFNames=F7H2.9;
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 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 [4]
RP INTERACTION WITH WUS, AND TISSUE SPECIFICITY.
RX PubMed=16461579; DOI=10.1105/tpc.105.039107;
RA Kieffer M., Stern Y., Cook H., Clerici E., Maulbetsch C., Laux T.,
RA Davies B.;
RT "Analysis of the transcription factor WUSCHEL and its functional homologue
RT in Antirrhinum reveals a potential mechanism for their roles in meristem
RT maintenance.";
RL Plant Cell 18:560-573(2006).
RN [5]
RP FUNCTION, MUTAGENESIS OF LYS-92 AND ASN-176, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, GENE
RP FAMILY, AND NOMENCLATURE.
RX PubMed=16763149; DOI=10.1126/science.1123841;
RA Long J.A., Ohno C., Smith Z.R., Meyerowitz E.M.;
RT "TOPLESS regulates apical embryonic fate in Arabidopsis.";
RL Science 312:1520-1523(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-214, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Root;
RX PubMed=18433157; DOI=10.1021/pr8000173;
RA de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,
RA Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J.,
RA Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H.;
RT "Site-specific phosphorylation profiling of Arabidopsis proteins by mass
RT spectrometry and peptide chip analysis.";
RL J. Proteome Res. 7:2458-2470(2008).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND INTERACTION WITH IAA1; IAA2;
RP IAA3; IAA4; IAA6; IAA8; IAA9; IAA11; IAA12; IAA13; IAA14; IAA17; IAA18;
RP IAA26; IAA27 AND IAA28.
RX PubMed=18258861; DOI=10.1126/science.1151461;
RA Szemenyei H., Hannon M., Long J.A.;
RT "TOPLESS mediates auxin-dependent transcriptional repression during
RT Arabidopsis embryogenesis.";
RL Science 319:1384-1386(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-214, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-214, AND IDENTIFICATION BY
RP 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 [10]
RP FUNCTION.
RX PubMed=20190735; DOI=10.1038/nature08843;
RA Smith Z.R., Long J.A.;
RT "Control of Arabidopsis apical-basal embryo polarity by antagonistic
RT transcription factors.";
RL Nature 464:423-426(2010).
RN [11]
RP FUNCTION, AND INTERACTION WITH AFPH2.
RX PubMed=20360743; DOI=10.1038/nature08854;
RA Pauwels L., Barbero G.F., Geerinck J., Tilleman S., Grunewald W.,
RA Perez A.C., Chico J.M., Bossche R.V., Sewell J., Gil E., Garcia-Casado G.,
RA Witters E., Inze D., Long J.A., De Jaeger G., Solano R., Goossens A.;
RT "NINJA connects the co-repressor TOPLESS to jasmonate signalling.";
RL Nature 464:788-791(2010).
RN [12]
RP FUNCTION, INTERACTION WITH AP2 AND HAD19, AND MUTAGENESIS OF ASN-176.
RX PubMed=23034631; DOI=10.1242/dev.085407;
RA Krogan N.T., Hogan K., Long J.A.;
RT "APETALA2 negatively regulates multiple floral organ identity genes in
RT Arabidopsis by recruiting the co-repressor TOPLESS and the histone
RT deacetylase HDA19.";
RL Development 139:4180-4190(2012).
RN [13]
RP INTERACTION WITH TIFY5A/JAZ8.
RX PubMed=22327740; DOI=10.1105/tpc.111.093005;
RA Shyu C., Figueroa P., Depew C.L., Cooke T.F., Sheard L.B., Moreno J.E.,
RA Katsir L., Zheng N., Browse J., Howe G.A.;
RT "JAZ8 lacks a canonical degron and has an EAR motif that mediates
RT transcriptional repression of jasmonate responses in Arabidopsis.";
RL Plant Cell 24:536-550(2012).
RN [14]
RP INTERACTION WITH SPEAR3/TIE1, AND TISSUE SPECIFICITY.
RX PubMed=23444332; DOI=10.1105/tpc.113.109223;
RA Tao Q., Guo D., Wei B., Zhang F., Pang C., Jiang H., Zhang J., Wei T.,
RA Gu H., Qu L.J., Qin G.;
RT "The TIE1 transcriptional repressor links TCP transcription factors with
RT TOPLESS/TOPLESS-RELATED corepressors and modulates leaf development in
RT Arabidopsis.";
RL Plant Cell 25:421-437(2013).
RN [15]
RP INTERACTION WITH SPL.
RX PubMed=25527103; DOI=10.1016/j.jgg.2014.08.009;
RA Chen G.H., Sun J.Y., Liu M., Liu J., Yang W.C.;
RT "SPOROCYTELESS is a novel embryophyte-specific transcription repressor that
RT interacts with TPL and TCP proteins in Arabidopsis.";
RL J. Genet. Genomics 41:617-625(2014).
RN [16]
RP INTERACTION WITH ZAT2 AND ZAT3.
RX PubMed=24876252; DOI=10.1105/tpc.114.124743;
RA Borg M., Rutley N., Kagale S., Hamamura Y., Gherghinoiu M., Kumar S.,
RA Sari U., Esparza-Franco M.A., Sakamoto W., Rozwadowski K., Higashiyama T.,
RA Twell D.;
RT "An EAR-dependent regulatory module promotes male germ cell division and
RT sperm fertility in Arabidopsis.";
RL Plant Cell 26:2098-2113(2014).
RN [17]
RP INTERACTION WITH AFPH2.
RX PubMed=24416306; DOI=10.1371/journal.pone.0084891;
RA Cuellar Perez A., Nagels Durand A., Vanden Bossche R., De Clercq R.,
RA Persiau G., Van Wees S.C., Pieterse C.M., Gevaert K., De Jaeger G.,
RA Goossens A., Pauwels L.;
RT "The non-JAZ TIFY protein TIFY8 from Arabidopsis thaliana is a
RT transcriptional repressor.";
RL PLoS ONE 9:E84891-E84891(2014).
RN [18]
RP FUNCTION, INTERACTION WITH SPL, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=25378179; DOI=10.1038/cr.2014.145;
RA Wei B., Zhang J., Pang C., Yu H., Guo D., Jiang H., Ding M., Chen Z.,
RA Tao Q., Gu H., Qu L.J., Qin G.;
RT "The molecular mechanism of sporocyteless/nozzle in controlling Arabidopsis
RT ovule development.";
RL Cell Res. 25:121-134(2015).
RN [19]
RP INTERACTION WITH JAZ13.
RX PubMed=25846245; DOI=10.1111/tpj.12841;
RA Thireault C., Shyu C., Yoshida Y., St Aubin B., Campos M.L., Howe G.A.;
RT "Repression of jasmonate signaling by a non-TIFY JAZ protein in
RT Arabidopsis.";
RL Plant J. 82:669-679(2015).
RN [20]
RP SUBUNIT, AND DOMAIN.
RX PubMed=26601214; DOI=10.1126/sciadv.1500107;
RA Ke J., Ma H., Gu X., Thelen A., Brunzelle J.S., Li J., Xu H.E., Melcher K.;
RT "Structural basis for recognition of diverse transcriptional repressors by
RT the TOPLESS family of corepressors.";
RL Sci. Adv. 1:E1500107-E1500107(2015).
RN [21]
RP INTERACTION WITH MIP1A, AND SUBCELLULAR LOCATION.
RX PubMed=27015278; DOI=10.1371/journal.pgen.1005959;
RA Graeff M., Straub D., Eguen T., Dolde U., Rodrigues V., Brandt R.,
RA Wenkel S.;
RT "Microprotein-mediated recruitment of CONSTANS into a TOPLESS trimeric
RT complex represses flowering in Arabidopsis.";
RL PLoS Genet. 12:E1005959-E1005959(2016).
RN [22]
RP INTERACTION WITH GIR1 AND GIR2, AND SUBCELLULAR LOCATION.
RX PubMed=28526412; DOI=10.1016/j.bbrc.2017.05.085;
RA Wu R., Citovsky V.;
RT "Adaptor proteins GIR1 and GIR2. II. Interaction with the co-repressor
RT TOPLESS and promotion of histone deacetylation of target chromatin.";
RL Biochem. Biophys. Res. Commun. 488:609-613(2017).
RN [23]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 3-184, AND HOMODIMERIZATION.
RX PubMed=28698367; DOI=10.1073/pnas.1703054114;
RA Martin-Arevalillo R., Nanao M.H., Larrieu A., Vinos-Poyo T., Mast D.,
RA Galvan-Ampudia C., Brunoud G., Vernoux T., Dumas R., Parcy F.;
RT "Structure of the Arabidopsis TOPLESS corepressor provides insight into the
RT evolution of transcriptional repression.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:8107-8112(2017).
CC -!- FUNCTION: Transcriptional corepressor. May repress the expression of
CC root-promoting genes in the top half of the embryo to allow proper
CC differentiation of the shoot pole during the transition stage of
CC embryogenesis. Regulates the expression of PLT1 and PLT2. Negative
CC regulator of jasmonate responses. Negative regulator of auxin
CC responses. Negative regulator of multiple floral organ identity genes
CC (PubMed:23034631). Required for ovule development (PubMed:25378179).
CC {ECO:0000269|PubMed:16763149, ECO:0000269|PubMed:18258861,
CC ECO:0000269|PubMed:20190735, ECO:0000269|PubMed:20360743,
CC ECO:0000269|PubMed:23034631, ECO:0000269|PubMed:25378179}.
CC -!- SUBUNIT: Tetramer (PubMed:26601214). Homodimer (PubMed:28698367).
CC Interacts (via the LisH domain) with WUS (via the C-terminal domain)
CC (PubMed:16461579). Interacts with NINJA/AFPH2 (PubMed:20360743,
CC PubMed:24416306). Interacts with IAA1; IAA2; IAA3; IAA4; IAA6; IAA8;
CC IAA9; IAA11; IAA13; IAA14; IAA17; IAA18; IAA26; IAA27 AND IAA28
CC (PubMed:18258861). Interacts (via the LisH domain) with IAA12/BDL (via
CC domain I) (PubMed:18258861). Can form a complex with IAA12 and ARF5
CC (PubMed:20360743). Interacts with AP2 (via EAR motif) and HDA19
CC (PubMed:23034631). Interacts with TIFY5A/JAZ8 (via EAR motif)
CC (PubMed:22327740). Interacts with SPEAR3/TIE1 (PubMed:23444332).
CC Interacts with SPL (via EAR motif) (PubMed:25527103, PubMed:25378179).
CC Interacts with ZAT2 and ZAT3 (via the EAR motif) (PubMed:24876252).
CC Interacts with JAZ13 (via EAR motif) (PubMed:25846245, PubMed:16461579,
CC PubMed:18258861, PubMed:20360743, PubMed:22327740, PubMed:23034631,
CC PubMed:23444332, PubMed:24416306, PubMed:24876252, PubMed:25378179,
CC PubMed:25527103, PubMed:26601214). Interacts with GIR1 and GIR2
CC (PubMed:28526412). {ECO:0000269|PubMed:16461579,
CC ECO:0000269|PubMed:18258861, ECO:0000269|PubMed:20360743,
CC ECO:0000269|PubMed:22327740, ECO:0000269|PubMed:23034631,
CC ECO:0000269|PubMed:23444332, ECO:0000269|PubMed:24416306,
CC ECO:0000269|PubMed:24876252, ECO:0000269|PubMed:25378179,
CC ECO:0000269|PubMed:25527103, ECO:0000269|PubMed:25846245,
CC ECO:0000269|PubMed:26601214, ECO:0000269|PubMed:28526412,
CC ECO:0000269|PubMed:28698367}.
CC -!- INTERACTION:
CC Q94AI7; Q9SV55: AFPH2; NbExp=4; IntAct=EBI-2119299, EBI-1787005;
CC Q94AI7; F4HPA7: MED10B; NbExp=3; IntAct=EBI-2119299, EBI-1386239;
CC Q94AI7; C0LU16: MED21; NbExp=6; IntAct=EBI-2119299, EBI-21254755;
CC Q94AI7; Q8L746: NPR3; NbExp=3; IntAct=EBI-2119299, EBI-4441365;
CC Q94AI7; Q94AI7: TPL; NbExp=11; IntAct=EBI-2119299, EBI-2119299;
CC Q94AI7; Q9SB92: WUS; NbExp=3; IntAct=EBI-2119299, EBI-2119269;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16763149,
CC ECO:0000269|PubMed:18258861, ECO:0000269|PubMed:27015278,
CC ECO:0000269|PubMed:28526412}.
CC -!- TISSUE SPECIFICITY: Expressed in embryo and in extraembryonic tissues
CC (PubMed:16763149). Expressed in inflorescences, flowers, floral
CC meristems, developing anthers and ovules (PubMed:16461579). Detected in
CC the vascular tissues, shoot apical meristem, cotyledons and young
CC leaves (PubMed:23444332). Expressed ubiquitously in the pistils,
CC stamens and pollens (PubMed:25378179). {ECO:0000269|PubMed:16461579,
CC ECO:0000269|PubMed:16763149, ECO:0000269|PubMed:23444332,
CC ECO:0000269|PubMed:25378179}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the embryo proper during early
CC embryogenesis and in the developing vasculature in later stages
CC (PubMed:16763149). Expressed dinamically in the proximal region and in
CC the nucellus during ovule development and mainly observed in the
CC nucellus in mature ovules (PubMed:25378179).
CC {ECO:0000269|PubMed:16763149, ECO:0000269|PubMed:25378179}.
CC -!- DOMAIN: The N-terminal TOPLESS domain (TPD) (1-209) binds directly to a
CC 12-amino acid LxLxL EAR motif peptide. {ECO:0000269|PubMed:26601214}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype, due to the redundancy with
CC the other TPR proteins. {ECO:0000269|PubMed:16763149}.
CC -!- MISCELLANEOUS: The tpl-1 gain-of-function allele is suppressed by
CC mutations in the histone acetyltransferase HAG1 gene. The tpl-1 gain-
CC of-function allele suppresses developmental defects in IAA12/BDL
CC mutants.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF82145.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC034256; AAF82145.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE29356.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29357.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29358.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29359.1; -; Genomic_DNA.
DR EMBL; AY046013; AAK76687.1; -; mRNA.
DR EMBL; AY142619; AAN13188.1; -; mRNA.
DR PIR; G86291; G86291.
DR RefSeq; NP_001031050.1; NM_001035973.3.
DR RefSeq; NP_001031051.1; NM_001035974.4.
DR RefSeq; NP_563981.1; NM_101443.4.
DR RefSeq; NP_849672.1; NM_179341.3.
DR PDB; 5NQS; X-ray; 2.61 A; A/B=3-184.
DR PDB; 5NQV; X-ray; 1.95 A; A/B/C/D=3-184.
DR PDBsum; 5NQS; -.
DR PDBsum; 5NQV; -.
DR AlphaFoldDB; Q94AI7; -.
DR SMR; Q94AI7; -.
DR BioGRID; 23384; 167.
DR DIP; DIP-52391N; -.
DR IntAct; Q94AI7; 38.
DR STRING; 3702.AT1G15750.3; -.
DR iPTMnet; Q94AI7; -.
DR PaxDb; Q94AI7; -.
DR PRIDE; Q94AI7; -.
DR ProteomicsDB; 234622; -.
DR EnsemblPlants; AT1G15750.1; AT1G15750.1; AT1G15750.
DR EnsemblPlants; AT1G15750.2; AT1G15750.2; AT1G15750.
DR EnsemblPlants; AT1G15750.3; AT1G15750.3; AT1G15750.
DR EnsemblPlants; AT1G15750.4; AT1G15750.4; AT1G15750.
DR GeneID; 838144; -.
DR Gramene; AT1G15750.1; AT1G15750.1; AT1G15750.
DR Gramene; AT1G15750.2; AT1G15750.2; AT1G15750.
DR Gramene; AT1G15750.3; AT1G15750.3; AT1G15750.
DR Gramene; AT1G15750.4; AT1G15750.4; AT1G15750.
DR KEGG; ath:AT1G15750; -.
DR Araport; AT1G15750; -.
DR TAIR; locus:2036204; AT1G15750.
DR eggNOG; KOG0266; Eukaryota.
DR HOGENOM; CLU_003103_1_0_1; -.
DR InParanoid; Q94AI7; -.
DR OMA; NMLPMSF; -.
DR OrthoDB; 65958at2759; -.
DR PhylomeDB; Q94AI7; -.
DR PRO; PR:Q94AI7; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q94AI7; baseline and differential.
DR Genevisible; Q94AI7; AT.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:TAIR.
DR GO; GO:0009867; P:jasmonic acid mediated signaling pathway; IMP:TAIR.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:TAIR.
DR GO; GO:0010072; P:primary shoot apical meristem specification; IMP:TAIR.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0009733; P:response to auxin; IPI:TAIR.
DR GO; GO:0010051; P:xylem and phloem pattern formation; IGI:TAIR.
DR Gene3D; 2.130.10.10; -; 3.
DR InterPro; IPR006595; CTLH_C.
DR InterPro; IPR006594; LisH.
DR InterPro; IPR027728; Topless_fam.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR44083; PTHR44083; 1.
DR Pfam; PF00400; WD40; 2.
DR SMART; SM00668; CTLH; 1.
DR SMART; SM00667; LisH; 1.
DR SMART; SM00320; WD40; 11.
DR SUPFAM; SSF50978; SSF50978; 3.
DR PROSITE; PS50897; CTLH; 1.
DR PROSITE; PS50896; LISH; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 2.
DR PROSITE; PS50082; WD_REPEATS_2; 3.
DR PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Developmental protein; Jasmonic acid signaling pathway;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Repressor;
KW Transcription; Transcription regulation; WD repeat.
FT CHAIN 1..1131
FT /note="Protein TOPLESS"
FT /id="PRO_0000394731"
FT DOMAIN 4..36
FT /note="LisH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00126"
FT DOMAIN 34..92
FT /note="CTLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00058"
FT REPEAT 353..393
FT /note="WD 1"
FT REPEAT 415..454
FT /note="WD 2"
FT REPEAT 460..501
FT /note="WD 3"
FT REPEAT 504..545
FT /note="WD 4"
FT REPEAT 548..591
FT /note="WD 5"
FT REPEAT 595..634
FT /note="WD 6"
FT REPEAT 639..678
FT /note="WD 7"
FT REPEAT 710..756
FT /note="WD 8"
FT REPEAT 766..805
FT /note="WD 9"
FT REPEAT 833..871
FT /note="WD 10"
FT REPEAT 874..914
FT /note="WD 11"
FT REPEAT 917..956
FT /note="WD 12"
FT REPEAT 967..1005
FT /note="WD 13"
FT REPEAT 1010..1049
FT /note="WD 14"
FT REPEAT 1060..1102
FT /note="WD 15"
FT REGION 286..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1100..1131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1113..1131
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 214
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18433157,
FT ECO:0007744|PubMed:19245862, ECO:0007744|PubMed:19376835"
FT MUTAGEN 92
FT /note="K->M: No effect."
FT /evidence="ECO:0000269|PubMed:16763149"
FT MUTAGEN 176
FT /note="N->H: In tpl-1; temperature sensitive gain of
FT function; transforms the shoot pole into a second root
FT pole. No effect on the interaction with IAA12 od HAD19, but
FT loss of interaction with AP2."
FT /evidence="ECO:0000269|PubMed:16763149,
FT ECO:0000269|PubMed:23034631"
FT HELIX 4..18
FT /evidence="ECO:0007829|PDB:5NQV"
FT HELIX 22..32
FT /evidence="ECO:0007829|PDB:5NQV"
FT HELIX 38..46
FT /evidence="ECO:0007829|PDB:5NQV"
FT HELIX 50..58
FT /evidence="ECO:0007829|PDB:5NQV"
FT HELIX 67..86
FT /evidence="ECO:0007829|PDB:5NQV"
FT HELIX 90..99
FT /evidence="ECO:0007829|PDB:5NQV"
FT HELIX 102..106
FT /evidence="ECO:0007829|PDB:5NQV"
FT HELIX 109..117
FT /evidence="ECO:0007829|PDB:5NQV"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:5NQV"
FT STRAND 121..123
FT /evidence="ECO:0007829|PDB:5NQV"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:5NQV"
FT HELIX 128..130
FT /evidence="ECO:0007829|PDB:5NQV"
FT HELIX 136..153
FT /evidence="ECO:0007829|PDB:5NQV"
FT HELIX 155..157
FT /evidence="ECO:0007829|PDB:5NQV"
FT HELIX 170..178
FT /evidence="ECO:0007829|PDB:5NQV"
SQ SEQUENCE 1131 AA; 124298 MW; 6211EE51BC309299 CRC64;
MSSLSRELVF LILQFLDEEK FKETVHKLEQ ESGFFFNMKY FEDEVHNGNW DEVEKYLSGF
TKVDDNRYSM KIFFEIRKQK YLEALDKHDR PKAVDILVKD LKVFSTFNEE LFKEITQLLT
LENFRENEQL SKYGDTKSAR AIMLVELKKL IEANPLFRDK LQFPTLRNSR LRTLINQSLN
WQHQLCKNPR PNPDIKTLFV DHSCGPPNGA RAPSPVNNPL LGGIPKAGGF PPLGAHGPFQ
PTASPVPTPL AGWMSSPSSV PHPAVSAGAI ALGGPSIPAA LKHPRTPPTN ASLDYPSADS
EHVSKRTRPM GISDEVNLGV NMLPMSFSGQ AHGHSPAFKA PDDLPKTVAR TLSQGSSPMS
MDFHPIKQTL LLVGTNVGDI GLWEVGSRER LVQKTFKVWD LSKCSMPLQA ALVKEPVVSV
NRVIWSPDGS LFGVAYSRHI VQLYSYHGGE DMRQHLEIDA HVGGVNDISF STPNKQLCVI
TCGDDKTIKV WDAATGVKRH TFEGHEAPVY SVCPHYKENI QFIFSTALDG KIKAWLYDNM
GSRVDYDAPG RWCTTMAYSA DGTRLFSCGT SKDGESFIVE WNESEGAVKR TYQGFHKRSL
GVVQFDTTKN RYLAAGDDFS IKFWDMDAVQ LLTAIDGDGG LQASPRIRFN KEGSLLAVSG
NENVIKIMAN SDGLRLLHTF ENISSESSKP AINSIAAAAA AAATSAGHAD RSANVVSIQG
MNGDSRNMVD VKPVITEESN DKSKIWKLTE VSEPSQCRSL RLPENLRVAK ISRLIFTNSG
NAILALASNA IHLLWKWQRN ERNATGKATA SLPPQQWQPA SGILMTNDVA ETNPEEAVPC
FALSKNDSYV MSASGGKISL FNMMTFKTMA TFMPPPPAAT FLAFHPQDNN IIAIGMDDST
IQIYNVRVDE VKSKLKGHSK RITGLAFSNV LNVLVSSGAD AQLCVWNTDG WEKQRSKVLP
LPQGRPNSAP SDTRVQFHQD QAHFLVVHET QLAIYETTKL ECMKQWAVRE SLAPITHATF
SCDSQLVYAS FMDATVCVFS SANLRLRCRV NPSAYLPASL SNSNVHPLVI AAHPQEPNMF
AVGLSDGGVH IFEPLESEGK WGVAPPAENG SASGAPTAPS VGASASDQPQ R
