TPR1_ORYSJ
ID TPR1_ORYSJ Reviewed; 1129 AA.
AC Q5NBT9; A0A0P0V0G9;
DT 16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Protein TPR1 {ECO:0000303|PubMed:24336200};
DE AltName: Full=Aberrant spikelet and panicle1-related 2 {ECO:0000303|PubMed:22136599};
DE AltName: Full=Protein ASP1-RELATED 2 {ECO:0000303|PubMed:22136599};
DE Short=OsASPR2 {ECO:0000303|PubMed:22136599};
DE AltName: Full=Topless-related protein 1 {ECO:0000303|PubMed:24336200};
DE AltName: Full=Topless-related protein 2 {ECO:0000303|PubMed:26601214};
DE Short=OsTPR2 {ECO:0000303|PubMed:26601214};
GN Name=TPR1 {ECO:0000303|PubMed:24336200};
GN Synonyms=ASPR2 {ECO:0000303|PubMed:22136599},
GN TPR2 {ECO:0000303|PubMed:26601214};
GN OrderedLocusNames=Os01g0254100 {ECO:0000312|EMBL:BAF04530.1},
GN LOC_Os01g15020 {ECO:0000305};
GN ORFNames=OsJ_01134 {ECO:0000312|EMBL:EEE54253.1},
GN OSNPB_010254100 {ECO:0000312|EMBL:BAS71375.1},
GN P0705D01.10-1 {ECO:0000312|EMBL:BAD81067.1};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947 {ECO:0000312|Proteomes:UP000059680};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], GENE FAMILY, AND NOMENCLATURE.
RX PubMed=22136599; DOI=10.1111/j.1365-313x.2011.04872.x;
RA Yoshida A., Ohmori Y., Kitano H., Taguchi-Shiobara F., Hirano H.;
RT "Aberrant spikelet and panicle1, encoding a TOPLESS-related transcriptional
RT co-repressor, is involved in the regulation of meristem fate in rice.";
RL Plant J. 70:327-339(2012).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12447438; DOI=10.1038/nature01184;
RA Sasaki T., Matsumoto T., Yamamoto K., Sakata K., Baba T., Katayose Y.,
RA Wu J., Niimura Y., Cheng Z., Nagamura Y., Antonio B.A., Kanamori H.,
RA Hosokawa S., Masukawa M., Arikawa K., Chiden Y., Hayashi M., Okamoto M.,
RA Ando T., Aoki H., Arita K., Hamada M., Harada C., Hijishita S., Honda M.,
RA Ichikawa Y., Idonuma A., Iijima M., Ikeda M., Ikeno M., Ito S., Ito T.,
RA Ito Y., Ito Y., Iwabuchi A., Kamiya K., Karasawa W., Katagiri S.,
RA Kikuta A., Kobayashi N., Kono I., Machita K., Maehara T., Mizuno H.,
RA Mizubayashi T., Mukai Y., Nagasaki H., Nakashima M., Nakama Y.,
RA Nakamichi Y., Nakamura M., Namiki N., Negishi M., Ohta I., Ono N., Saji S.,
RA Sakai K., Shibata M., Shimokawa T., Shomura A., Song J., Takazaki Y.,
RA Terasawa K., Tsuji K., Waki K., Yamagata H., Yamane H., Yoshiki S.,
RA Yoshihara R., Yukawa K., Zhong H., Iwama H., Endo T., Ito H., Hahn J.H.,
RA Kim H.-I., Eun M.-Y., Yano M., Jiang J., Gojobori T.;
RT "The genome sequence and structure of rice chromosome 1.";
RL Nature 420:312-316(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [7]
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND GENE FAMILY.
RX PubMed=22020753; DOI=10.1007/s00425-011-1532-7;
RA Gao X., Chen Z., Zhang J., Li X., Chen G., Li X., Wu C.;
RT "OsLIS-L1 encoding a lissencephaly type-1-like protein with WD40 repeats is
RT required for plant height and male gametophyte formation in rice.";
RL Planta 235:713-727(2012).
RN [8]
RP INTERACTION WITH D53, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=24336200; DOI=10.1038/nature12870;
RA Jiang L., Liu X., Xiong G., Liu H., Chen F., Wang L., Meng X., Liu G.,
RA Yu H., Yuan Y., Yi W., Zhao L., Ma H., He Y., Wu Z., Melcher K., Qian Q.,
RA Xu H.E., Wang Y., Li J.;
RT "DWARF 53 acts as a repressor of strigolactone signalling in rice.";
RL Nature 504:401-405(2013).
RN [9]
RP INTERACTION WITH WOX1.
RX PubMed=25697101; DOI=10.1016/j.jgg.2014.12.005;
RA Lu Z., Shao G., Xiong J., Jiao Y., Wang J., Liu G., Meng X., Liang Y.,
RA Xiong G., Wang Y., Li J.;
RT "MONOCULM 3, an ortholog of WUSCHEL in rice, is required for tiller bud
RT formation.";
RL J. Genet. Genomics 42:71-78(2015).
RN [10]
RP INTERACTION WITH MOF1.
RX PubMed=32680975; DOI=10.1104/pp.20.00658;
RA Ren D., Rao Y., Yu H., Xu Q., Cui Y., Xia S., Yu X., Liu H., Hu H., Xue D.,
RA Zeng D., Hu J., Zhang G., Gao Z., Zhu L., Zhang Q., Shen L., Guo L.,
RA Qian Q.;
RT "MORE FLORET 1 encodes a MYB transcription factor that regulates spikelet
RT development in rice.";
RL Plant Physiol. 184:251-265(2020).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 1-209 OF APOPROTEIN AND IN
RP COMPLEX WITH EAR MOTIF, SUBUNIT, DOMAIN, NOMENCLATURE, AND MUTAGENESIS OF
RP ARG-67; TYR-68; LYS-71; PHE-74; PHE-104; LEU-111; LEU-118; LEU-130; LEU-150
RP AND ASN-176.
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: Probable downstream regulator of strigolactones signaling.
CC {ECO:0000250|UniProtKB:Q0J7U6}.
CC -!- SUBUNIT: Tetramer (PubMed:26601214). Interacts with D53
CC (PubMed:24336200). Interacts with WOX1 (PubMed:25697101,
CC PubMed:24336200, PubMed:26601214). Interacts with MOF1
CC (PubMed:32680975). {ECO:0000269|PubMed:24336200,
CC ECO:0000269|PubMed:25697101, ECO:0000269|PubMed:26601214,
CC ECO:0000269|PubMed:32680975}.
CC -!- TISSUE SPECIFICITY: Expressed in panicles, stems, leaves, spikelets and
CC seed endosperm. {ECO:0000269|PubMed:22020753}.
CC -!- DEVELOPMENTAL STAGE: Highest expression in endosperm at 7 days after
CC pollination and in flag leaf at 14 days after heading.
CC {ECO:0000269|PubMed:22020753}.
CC -!- DOMAIN: The N-terminal TOPLESS domain (TPD)(1-209) binds directly to a
CC 12-amino acid LxLxL EAR motif peptide, but no binding if the leucin
CC residues are replaced. {ECO:0000269|PubMed:26601214}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAS71376.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB638271; BAL44268.1; -; mRNA.
DR EMBL; AP000492; BAD81067.1; -; Genomic_DNA.
DR EMBL; AP008207; BAF04530.1; -; Genomic_DNA.
DR EMBL; AP014957; BAS71375.1; -; Genomic_DNA.
DR EMBL; AP014957; BAS71376.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CM000138; EEE54253.1; -; Genomic_DNA.
DR RefSeq; XP_015617818.1; XM_015762332.1.
DR PDB; 4ZHE; X-ray; 2.50 A; A/B/C/D=1-209.
DR PDB; 5C6Q; X-ray; 3.25 A; A=1-209.
DR PDB; 5C6V; X-ray; 3.10 A; A/B/C/D=1-209.
DR PDB; 5C7E; X-ray; 3.10 A; A/B/C/D/E/F=1-209.
DR PDB; 5C7F; X-ray; 2.70 A; A/B/C/D=1-209.
DR PDB; 5J9K; X-ray; 2.55 A; A/B=1-209.
DR PDB; 5JA5; X-ray; 2.00 A; A=1-209.
DR PDB; 5JGC; X-ray; 2.08 A; A=1-209.
DR PDB; 5JHP; X-ray; 3.15 A; A/B/C/D=1-209.
DR PDBsum; 4ZHE; -.
DR PDBsum; 5C6Q; -.
DR PDBsum; 5C6V; -.
DR PDBsum; 5C7E; -.
DR PDBsum; 5C7F; -.
DR PDBsum; 5J9K; -.
DR PDBsum; 5JA5; -.
DR PDBsum; 5JGC; -.
DR PDBsum; 5JHP; -.
DR AlphaFoldDB; Q5NBT9; -.
DR SMR; Q5NBT9; -.
DR STRING; 4530.OS01T0254100-01; -.
DR iPTMnet; Q5NBT9; -.
DR PaxDb; Q5NBT9; -.
DR PRIDE; Q5NBT9; -.
DR EnsemblPlants; Os01t0254100-01; Os01t0254100-01; Os01g0254100.
DR GeneID; 4327709; -.
DR Gramene; Os01t0254100-01; Os01t0254100-01; Os01g0254100.
DR KEGG; osa:4327709; -.
DR eggNOG; KOG0266; Eukaryota.
DR InParanoid; Q5NBT9; -.
DR OMA; MTNDIVG; -.
DR OrthoDB; 94792at2759; -.
DR PlantReactome; R-OSA-5632095; Brassinosteroid signaling.
DR PlantReactome; R-OSA-5654828; Strigolactone signaling.
DR PlantReactome; R-OSA-6787011; Jasmonic acid signaling.
DR PlantReactome; R-OSA-6788019; Salicylic acid signaling.
DR Proteomes; UP000000763; Chromosome 1.
DR Proteomes; UP000007752; Chromosome 1.
DR Proteomes; UP000059680; Chromosome 1.
DR GO; GO:0009791; P:post-embryonic development; IEA:UniProt.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0048608; P:reproductive structure development; IEA:UniProt.
DR GO; GO:0048367; P:shoot system development; IEA:UniProt.
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; 11.
DR SUPFAM; SSF50978; SSF50978; 2.
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; 4.
DR PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Reference proteome; Repeat; WD repeat.
FT CHAIN 1..1129
FT /note="Protein TPR1"
FT /id="PRO_0000435821"
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 337..377
FT /note="WD 1"
FT /evidence="ECO:0000255"
FT REPEAT 398..437
FT /note="WD 2"
FT /evidence="ECO:0000255"
FT REPEAT 443..485
FT /note="WD 3"
FT /evidence="ECO:0000255"
FT REPEAT 487..527
FT /note="WD 4"
FT /evidence="ECO:0000255"
FT REPEAT 579..618
FT /note="WD 5"
FT /evidence="ECO:0000255"
FT REPEAT 623..662
FT /note="WD 6"
FT /evidence="ECO:0000255"
FT REPEAT 762..801
FT /note="WD 7"
FT /evidence="ECO:0000255"
FT REPEAT 829..867
FT /note="WD 8"
FT /evidence="ECO:0000255"
FT REPEAT 870..910
FT /note="WD 9"
FT /evidence="ECO:0000255"
FT REPEAT 913..952
FT /note="WD 10"
FT /evidence="ECO:0000255"
FT REPEAT 1005..1044
FT /note="WD 11"
FT /evidence="ECO:0000255"
FT REGION 1092..1129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1099..1129
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 67
FT /note="R->A: Loss of interaction with EAR motif-containing
FT full-length proteins."
FT /evidence="ECO:0000269|PubMed:26601214"
FT MUTAGEN 68
FT /note="Y->A: Loss of interaction with EAR motif-containing
FT full-length proteins."
FT /evidence="ECO:0000269|PubMed:26601214"
FT MUTAGEN 71
FT /note="K->A: Loss of interaction with EAR motif-containing
FT full-length proteins."
FT /evidence="ECO:0000269|PubMed:26601214"
FT MUTAGEN 74
FT /note="F->A: Loss of interaction with EAR motif-containing
FT full-length proteins."
FT /evidence="ECO:0000269|PubMed:26601214"
FT MUTAGEN 104
FT /note="F->A: Loss of interaction with EAR motif-containing
FT full-length proteins."
FT /evidence="ECO:0000269|PubMed:26601214"
FT MUTAGEN 111
FT /note="L->A: Loss of interaction with EAR motif-containing
FT full-length proteins."
FT /evidence="ECO:0000269|PubMed:26601214"
FT MUTAGEN 118
FT /note="L->A: Loss of interaction with EAR motif-containing
FT full-length proteins."
FT /evidence="ECO:0000269|PubMed:26601214"
FT MUTAGEN 130
FT /note="L->A: Loss of interaction with EAR motif-containing
FT full-length proteins."
FT /evidence="ECO:0000269|PubMed:26601214"
FT MUTAGEN 150
FT /note="L->A: Loss of interaction with EAR motif-containing
FT full-length proteins."
FT /evidence="ECO:0000269|PubMed:26601214"
FT MUTAGEN 176
FT /note="N->H: Aggregates formation."
FT /evidence="ECO:0000269|PubMed:26601214"
FT HELIX 3..18
FT /evidence="ECO:0007829|PDB:5JA5"
FT HELIX 22..32
FT /evidence="ECO:0007829|PDB:5JA5"
FT HELIX 38..46
FT /evidence="ECO:0007829|PDB:5JA5"
FT HELIX 50..57
FT /evidence="ECO:0007829|PDB:5JA5"
FT TURN 58..60
FT /evidence="ECO:0007829|PDB:5JA5"
FT HELIX 67..86
FT /evidence="ECO:0007829|PDB:5JA5"
FT HELIX 90..99
FT /evidence="ECO:0007829|PDB:5JA5"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:5JA5"
FT TURN 105..107
FT /evidence="ECO:0007829|PDB:5JA5"
FT HELIX 109..117
FT /evidence="ECO:0007829|PDB:5JA5"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:5JA5"
FT STRAND 121..123
FT /evidence="ECO:0007829|PDB:5JGC"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:5JA5"
FT HELIX 128..130
FT /evidence="ECO:0007829|PDB:5JGC"
FT HELIX 136..153
FT /evidence="ECO:0007829|PDB:5JA5"
FT HELIX 155..157
FT /evidence="ECO:0007829|PDB:5JA5"
FT STRAND 160..162
FT /evidence="ECO:0007829|PDB:5JA5"
FT HELIX 170..184
FT /evidence="ECO:0007829|PDB:5JA5"
FT STRAND 185..188
FT /evidence="ECO:0007829|PDB:4ZHE"
FT STRAND 198..200
FT /evidence="ECO:0007829|PDB:5JA5"
SQ SEQUENCE 1129 AA; 125095 MW; 4D95D968E6DD56A3 CRC64;
MSSLSRELVF LILQFLDEEK FKETVHKLEQ ESGFFFNMKY FEEKVHAGEW DEVEKYLSGF
TKVDDNRYSM KIFFEIRKQK YLEALDRHDR AKAVDILVKD LKVFSTFNEE LYKEITQLLT
LENFRENEQL SKYGDTKSAR SIMLIELKKL IEANPLFREK LVFPTLKASR LRTLINQSLN
WQHQLCKNPR PNPDIKTLFT DHTCTPPNGA RASPVSVPLA AVPKAGGTYP PLTAHTPFQP
PPAGPSLAGW MANAAAATSS VPSAVVAASS LPVPPNQAVP IMKRPTITDY QSAESEQLMK
RLRPSGHGVD EATYPAPIPQ PLWSVEDLPR TVACTLSQGS SVTSMDFHPT RHTLLLVGST
NGEITLWEVG MRERLFSKPF KIWDIQACSP QFQSVAKESS ISINRVTWSP DGDLIGVAFA
KHLIHLHAYQ QPNETRQVLE IDAHSGAVND IAFSRPNKQL CVVTCGDDRL IKVWDMHGQK
LFSFEGHEAP VYSICPHHKE SIQFIFSTSL DGKIKAWLYD HMGSRVDYDA PGKWCTTMLY
SADGTRLFSC GTSKDGDSYL VEWNESEGSI KRTYSGFRKK SAGVGVVQFD TAQNHILAAG
EDNQIKFWDV DNTTMLSSTE ADGGLPGLPR LRFNKEGNLL AVTTVDNGFK ILANADGLRT
LRAFGNRPFE AFRSQYEASS MKVSGAPVVA GISPNIGRMD HIDRNSPAKP SPIMNGGDPA
SRSIDIKPRI SEERPDKAKP WELMEVLNAQ QCRVATMPET PDQASKVVRL LYTNSGVGLL
ALGSNAIQRL WKWARNDQNP SGKATANVVP QHWQPNSGLV MQNDTADTNP EDAVPCIALS
KNDSYVMSAC GGKVSLFNMM TFKVMTTFMP PPPASTFLAF HPQDNNIIAI GMEDSTIHIY
NVRVDEVKTR LKGHQRRITG LAFSNNLQIL VSSGADAQLC VWATDTWEKK KSVAIQMPAG
KTPSGDTWVQ FNSDWSRLLV VHETQLAIYD ASKMERIYQW IPQDALSAPI SHASYSRNSQ
LVFAAFTDGN IGIFDVENLR LRCRIAPPAY LSSAAINSNP SVYPLVVAAH PQESNQFAVG
LSDGSVKVIE PLESEGKWGT TPPTENGVPN GRTSTSSATS NPAADQIQR
