位置:首页 > 蛋白库 > TON1B_ARATH
TON1B_ARATH
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   25-MAY-2022, entry version 113.
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};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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; 2.
DR   STRING; 3702.AT3G55005.1; -.
DR   iPTMnet; Q9FQ24; -.
DR   PaxDb; Q9FQ24; -.
DR   PRIDE; Q9FQ24; -.
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; locus:505006399; AT3G55005.
DR   eggNOG; ENOG502QRFJ; Eukaryota.
DR   HOGENOM; CLU_071412_0_0_1; -.
DR   InParanoid; Q9FQ24; -.
DR   OMA; WRYENEE; -.
DR   OrthoDB; 1163584at2759; -.
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   InterPro; IPR006594; LisH.
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
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024