TPR1_ARATH
ID TPR1_ARATH Reviewed; 1120 AA.
AC Q0WV90; A8MR25; Q9M8L7;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 3.
DT 25-MAY-2022, entry version 118.
DE RecName: Full=Topless-related protein 1;
DE AltName: Full=Protein MODIFIER OF SNC1 10;
GN Name=TPR1; Synonyms=MOS10; OrderedLocusNames=At1g80490;
GN ORFNames=F7H12, T21F11.18;
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] (ISOFORM 1).
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 [4]
RP GENE 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 [5]
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 [6]
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 [7]
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 [8]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SNC1 AND HDA19, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=20647385; DOI=10.1073/pnas.1002828107;
RA Zhu Z., Xu F., Zhang Y., Cheng Y.T., Wiermer M., Li X., Zhang Y.;
RT "Arabidopsis resistance protein SNC1 activates immune responses through
RT association with a transcriptional corepressor.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:13960-13965(2010).
RN [9]
RP INTERACTION WITH SPEAR3/TIE1.
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 [10]
RP INTERACTION WITH SPL, AND TISSUE SPECIFICITY.
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 [11]
RP INTERACTION WITH GAF1/IDD2.
RC STRAIN=cv. Columbia;
RX PubMed=25035403; DOI=10.1105/tpc.114.125690;
RA Fukazawa J., Teramura H., Murakoshi S., Nasuno K., Nishida N., Ito T.,
RA Yoshida M., Kamiya Y., Yamaguchi S., Takahashi Y.;
RT "DELLAs function as coactivators of GAI-ASSOCIATED FACTOR1 in regulation of
RT gibberellin homeostasis and signaling in Arabidopsis.";
RL Plant Cell 26:2920-2938(2014).
RN [12]
RP INTERACTION WITH SPL.
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 [13]
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).
CC -!- FUNCTION: Transcriptional corepressor. Activates TIR-NB-LRR R protein-
CC mediated immune responses through repression of negative regulators
CC such as CNGC2/DND1 (PubMed:20647385). Negative regulator of jasmonate
CC responses (By similarity). {ECO:0000250, ECO:0000269|PubMed:20647385}.
CC -!- SUBUNIT: Tetramer (PubMed:26601214). Interacts with SNC1 (via TIR
CC domain) and HDA19 (PubMed:20647385). Interacts with SPL (via EAR motif)
CC (PubMed:25527103, PubMed:25378179). Interacts with SPEAR3/TIE1
CC (PubMed:23444332). Binds to and corepresses GAF1/IDD2
CC (PubMed:25035403). {ECO:0000269|PubMed:20647385,
CC ECO:0000269|PubMed:23444332, ECO:0000269|PubMed:25035403,
CC ECO:0000269|PubMed:25378179, ECO:0000269|PubMed:25527103,
CC ECO:0000269|PubMed:26601214}.
CC -!- INTERACTION:
CC Q0WV90; O23530: SNC1; NbExp=2; IntAct=EBI-15866619, EBI-15866586;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20647385}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=2;
CC IsoId=Q0WV90-2; Sequence=Displayed;
CC Name=1;
CC IsoId=Q0WV90-1; Sequence=VSP_039582;
CC -!- TISSUE SPECIFICITY: Highly expressed in stamen primordium,
CC microsporocyte, ovule primordium and megasporocyte during sporogenesis.
CC {ECO:0000269|PubMed:25527103}.
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: Partially suppresses the constitutive disease
CC resistance phenotype of the snc1 mutant. {ECO:0000269|PubMed:20647385}.
CC -!- MISCELLANEOUS: Overexpression of TPR1 leads to constitutive activation
CC of defense responses.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF27128.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC018849; AAF27128.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC034256; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002684; AEE36411.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE36412.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM60269.1; -; Genomic_DNA.
DR EMBL; AK226879; BAE98958.1; -; mRNA.
DR PIR; G96836; G96836.
DR RefSeq; NP_001319429.1; NM_001334989.1. [Q0WV90-2]
DR RefSeq; NP_178164.3; NM_106697.5. [Q0WV90-1]
DR RefSeq; NP_849913.2; NM_179582.2. [Q0WV90-2]
DR AlphaFoldDB; Q0WV90; -.
DR BioGRID; 29606; 54.
DR DIP; DIP-59361N; -.
DR IntAct; Q0WV90; 3.
DR STRING; 3702.AT1G80490.2; -.
DR iPTMnet; Q0WV90; -.
DR PaxDb; Q0WV90; -.
DR PRIDE; Q0WV90; -.
DR ProteomicsDB; 234100; -. [Q0WV90-2]
DR EnsemblPlants; AT1G80490.1; AT1G80490.1; AT1G80490. [Q0WV90-1]
DR EnsemblPlants; AT1G80490.2; AT1G80490.2; AT1G80490. [Q0WV90-2]
DR EnsemblPlants; AT1G80490.3; AT1G80490.3; AT1G80490. [Q0WV90-2]
DR GeneID; 844388; -.
DR Gramene; AT1G80490.1; AT1G80490.1; AT1G80490. [Q0WV90-1]
DR Gramene; AT1G80490.2; AT1G80490.2; AT1G80490. [Q0WV90-2]
DR Gramene; AT1G80490.3; AT1G80490.3; AT1G80490. [Q0WV90-2]
DR KEGG; ath:AT1G80490; -.
DR Araport; AT1G80490; -.
DR TAIR; locus:2198888; AT1G80490.
DR eggNOG; KOG0266; Eukaryota.
DR InParanoid; Q0WV90; -.
DR OMA; WFPRESA; -.
DR OrthoDB; 65958at2759; -.
DR PhylomeDB; Q0WV90; -.
DR PRO; PR:Q0WV90; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q0WV90; baseline and differential.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0010072; P:primary shoot apical meristem specification; IGI:TAIR.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR Gene3D; 2.130.10.10; -; 4.
DR InterPro; IPR006595; CTLH_C.
DR InterPro; IPR006594; LisH.
DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
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; 12.
DR SUPFAM; SSF50978; SSF50978; 1.
DR SUPFAM; SSF50998; SSF50998; 1.
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 Alternative splicing; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Repressor; Transcription; Transcription regulation; WD repeat.
FT CHAIN 1..1120
FT /note="Topless-related protein 1"
FT /id="PRO_0000394732"
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 699..745
FT /note="WD 8"
FT REPEAT 755..794
FT /note="WD 9"
FT REPEAT 822..860
FT /note="WD 10"
FT REPEAT 863..903
FT /note="WD 11"
FT REPEAT 906..945
FT /note="WD 12"
FT REPEAT 999..1038
FT /note="WD 13"
FT REPEAT 1052..1091
FT /note="WD 14"
FT REGION 210..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 283..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1087..1120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1100..1120
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 VAR_SEQ 279
FT /note="Missing (in isoform 1)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_039582"
FT CONFLICT 818
FT /note="V -> M (in Ref. 3; BAE98958)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1120 AA; 124089 MW; 32BF74AC4B5A4B91 CRC64;
MSSLSRELVF LILQFLDEEK FKETVHKLEQ ESGFFFNMKY FEDEVHNGNW DEVEKYLSGF
TKVDDNRYSM KIFFEIRKQK YLEALDRHDR PKAVDILVKD LKVFSTFNEE LFKEITQLLT
LENFRENEQL SKYGDTKSAR AIMLVELKKL IEANPLFRDK LQFPTLRTSR LRTLINQSLN
WQHQLCKNPR PNPDIKTLFV DHSCRLPNDA RAPSPVNNPL LGSLPKAEGF PPLGAHGPFQ
PTPSPVPTPL AGWMSSPSSV PHPAVSGGPI ALGAPSIQAA LKHPRTPPSN SAVDYPSGDS
DHVSKRTRPM GISDEVSLGV NMLPMTFPGQ AHGHNQTFKA PDDLPKTVAR TLSQGSSPMS
MDFHPIKQTL LLVGTNVGDI GLWEVGSRER LVQKTFKVWD LSKCSMPLQA ALVKEPVVSV
NRVIWSPDGS LFGVAYSRHI VQLYSYHGGE DMRQHLEIDA HVGGVNDIAF STPNKQLCVT
TCGDDKTIKV WDAATGVKRY TFEGHEAPVY SICPHYKENI QFIFSTALDG KIKAWLYDNM
GSRVDYEAPG RWCTTMAYSA DGTRLFSCGT SKDGESFIVE WNESEGAVKR TYQGFHKRSL
GVVQFDTTKN RYLAAGDDFS IKFWDMDTIQ LLTAIDADGG LQASPRIRFN KEGSLLAVSA
NDNMIKVMAN SDGLRLLHTV ENLSSESSKP AINSIPMVER PASVVSIPGM NGDSRNMVDV
KPVITEESND KSKVWKLTEV GEPSQCRSLR LPENMRVTKI SRLIFTNSGN AILALASNAI
HLLWKWQRND RNATGKATAS LPPQQWQPAS GILMTNDVAE TNPEEAVPCF ALSKNDSYVM
SASGGKISLF NMMTFKTMAT FMPPPPAATF LAFHPQDNNI IAIGMDDSTI QIYNVRVDEV
KSKLKGHSKR ITGLAFSNVL NVLVSSGADA QLCVWNTDGW EKQKSKVLQI PQGRSTSSLS
DTRVQFHQDQ VHFLVVHETQ LAIYETTKLE CMKQWPVRES AAPITHATFS CDSQLIYTSF
MDATICVFSS ANLRLRCRVN PSAYLPASLS NSNVHPLVIA AHPQESNMFA VGLSDGGVHI
FEPLESEGKW GVAPPPENGS ASAVTATPSV GASASDQPQR
