ID TON1B_ARATH Reviewed; 257 AA.
AC Q9FQ24; Q9FQ23; Q9SV48;
DT 06-FEB-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 27-MAR-2024, entry version 119.
DE RecName: Full=Protein TONNEAU 1b;
GN Name=TON1B; OrderedLocusNames=At3g55005; ORFNames=F28P10.20;
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], FUNCTION, INTERACTION WITH CEN1,
RP SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=18757558; DOI=10.1105/tpc.107.056812;
RA Azimzadeh J., Nacry P., Christodoulidou A., Drevensek S., Camilleri C.,
RA Amiour N., Parcy F., Pastuglia M., Bouchez D.;
RT "Arabidopsis TONNEAU1 proteins are essential for preprophase band formation
RT and interact with centrin.";
RL Plant Cell 20:2146-2159(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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].
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 INTERACTION WITH LNG1 AND LNG2, AND SUBCELLULAR LOCATION.
RX PubMed=22286137; DOI=10.1105/tpc.111.089748;
RA Drevensek S., Goussot M., Duroc Y., Christodoulidou A., Steyaert S.,
RA Schaefer E., Duvernois E., Grandjean O., Vantard M., Bouchez D.,
RA Pastuglia M.;
RT "The Arabidopsis TRM1-TON1 interaction reveals a recruitment network common
RT to plant cortical microtubule arrays and eukaryotic centrosomes.";
RL Plant Cell 24:178-191(2012).
CC -!- FUNCTION: Involved in the control of the dynamic organization of the
CC cortical cytoskeleton. May play a role in the organization of
CC microtubule arrays at the centrosome through interaction with centrin 1
CC (CEN1). {ECO:0000269|PubMed:18757558}.
CC -!- SUBUNIT: Interacts with CEN1, LNG1/TRM2 and LNG2/TRM1 (via C-terminus).
CC {ECO:0000269|PubMed:18757558, ECO:0000269|PubMed:22286137}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18757558,
CC ECO:0000269|PubMed:22286137}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:18757558, ECO:0000269|PubMed:22286137}.
CC Note=Localizes to cytoplasm and cortical cytoskeletal structures,
CC including the preprophase band and the interphase microtubule arrays
CC (PubMed:18757558). Recruited to cytoskeletal structures by LNG2/TRM1
CC (PubMed:22286137). {ECO:0000269|PubMed:18757558,
CC ECO:0000269|PubMed:22286137}.
CC -!- DISRUPTION PHENOTYPE: Extreme defects in morphogenesis, positioning of
CC mitotic planes and cellular organization due to dysfunction of the
CC cortical cytoskeleton and absence of the preprophase band of
CC microtubules. In the ton1 insertional mutant, the two highly similar
CC genes in tandem, TON1A and TON1B are simultaneously disrupted.
CC {ECO:0000269|PubMed:18757558}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB41084.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF280058; AAG35780.1; -; Genomic_DNA.
DR EMBL; AF280059; AAG35781.1; -; mRNA.
DR EMBL; AL049655; CAB41084.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE79326.1; -; Genomic_DNA.
DR EMBL; AY075696; AAL77702.1; -; mRNA.
DR PIR; T06720; T06720.
DR RefSeq; NP_567013.1; NM_115358.5.
DR AlphaFoldDB; Q9FQ24; -.
DR SMR; Q9FQ24; -.
DR BioGRID; 9982; 3.
DR STRING; 3702.Q9FQ24; -.
DR iPTMnet; Q9FQ24; -.
DR PaxDb; 3702-AT3G55005-1; -.
DR ProteomicsDB; 232437; -.
DR EnsemblPlants; AT3G55005.1; AT3G55005.1; AT3G55005.
DR GeneID; 824666; -.
DR Gramene; AT3G55005.1; AT3G55005.1; AT3G55005.
DR KEGG; ath:AT3G55005; -.
DR Araport; AT3G55005; -.
DR TAIR; AT3G55005; TON1B.
DR eggNOG; ENOG502QRFJ; Eukaryota.
DR HOGENOM; CLU_071412_0_0_1; -.
DR InParanoid; Q9FQ24; -.
DR OMA; WRYENEE; -.
DR OrthoDB; 2908023at2759; -.
DR PhylomeDB; Q9FQ24; -.
DR PRO; PR:Q9FQ24; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9FQ24; baseline and differential.
DR Genevisible; Q9FQ24; AT.
DR GO; GO:0030981; C:cortical microtubule cytoskeleton; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0030865; P:cortical cytoskeleton organization; IMP:UniProtKB.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IMP:UniProtKB.
DR GO; GO:0000913; P:preprophase band assembly; IMP:UniProtKB.
DR Gene3D; 1.20.960.40; -; 1.
DR InterPro; IPR006594; LisH.
DR PANTHER; PTHR15431; FGFR1 ONCOGENE PARTNER/LISH DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR15431:SF4; PROTEIN TONNEAU 1A-RELATED; 1.
DR Pfam; PF16045; LisH_2; 1.
DR PROSITE; PS50896; LISH; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Cytoskeleton; Reference proteome.
FT CHAIN 1..257
FT /note="Protein TONNEAU 1b"
FT /id="PRO_0000420917"
FT DOMAIN 73..105
FT /note="LisH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00126"
FT REGION 148..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 231..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..201
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..245
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 164
FT /note="L -> S (in Ref. 1; AEE79326)"
FT /evidence="ECO:0000305"
FT CONFLICT 190..192
FT /note="Missing (in Ref. 1; AEE79326)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 257 AA; 29185 MW; 8A80992626A20F35 CRC64;
MDDYTREMMD LKTLVTRTLE KKGVLAKIRA ELRASVFEAI EEEDRVIENN EGLPPALLGS
CNDRARQLHA SPSGRLLSAL ICEYLDWAQL NHTLKVYQPE CNSAKDSWKS EIRDFSINNG
YELNRNEDSR PLLLDVLEGF LKFENMTQVM GGSSRRESET ESSLSLDTRN PPRRSSASDS
LPHQRRSVSA SQASGAATSG YRKDESNWRY DTEDMPEEVM RASTALENLQ LDRKTRNLTS
SWRNVKDGTS EEEEGKD
//
