TOR_ARATH
ID TOR_ARATH Reviewed; 2481 AA.
AC Q9FR53; Q9LPM4;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Serine/threonine-protein kinase TOR {ECO:0000250|UniProtKB:Q9Y7K2};
DE EC=2.7.11.1 {ECO:0000250|UniProtKB:Q9Y7K2};
DE AltName: Full=Protein TARGET OF RAPAMYCIN {ECO:0000303|PubMed:11983923};
DE Short=AtTOR {ECO:0000303|PubMed:11983923};
GN Name=TOR {ECO:0000303|PubMed:11983923};
GN OrderedLocusNames=At1g50030 {ECO:0000312|Araport:AT1G50030};
GN ORFNames=F2J10.19 {ECO:0000305};
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 [MRNA], FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL
RP STAGE, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=11983923; DOI=10.1073/pnas.092141899;
RA Menand B., Desnos T., Nussaume L., Berger F., Bouchez D., Meyer C.,
RA Robaglia C.;
RT "Expression and disruption of the Arabidopsis TOR (target of rapamycin)
RT gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:6422-6427(2002).
RN [2]
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 [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 TISSUE SPECIFICITY.
RX PubMed=15270681; DOI=10.1042/bst0320581;
RA Robaglia C., Menand B., Lei Y., Sormani R., Nicolai M., Gery C., Teoule E.,
RA Deprost D., Meyer C.;
RT "Plant growth: the translational connection.";
RL Biochem. Soc. Trans. 32:581-584(2004).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=15607746; DOI=10.1016/j.bbrc.2004.11.117;
RA Deprost D., Truong H.N., Robaglia C., Meyer C.;
RT "An Arabidopsis homolog of RAPTOR/KOG1 is essential for early embryo
RT development.";
RL Biochem. Biophys. Res. Commun. 326:844-850(2005).
RN [6]
RP FUNCTION, AND INTERACTION WITH RAPTOR1.
RX PubMed=16377759; DOI=10.1105/tpc.105.035931;
RA Mahfouz M.M., Kim S., Delauney A.J., Verma D.P.;
RT "Arabidopsis TARGET OF RAPAMYCIN interacts with RAPTOR, which regulates the
RT activity of S6 kinase in response to osmotic stress signals.";
RL Plant Cell 18:477-490(2006).
RN [7]
RP FUNCTION, AND MISCELLANEOUS.
RX PubMed=17543119; DOI=10.1186/1471-2229-7-26;
RA Sormani R., Yao L., Menand B., Ennar N., Lecampion C., Meyer C.,
RA Robaglia C.;
RT "Saccharomyces cerevisiae FKBP12 binds Arabidopsis thaliana TOR and its
RT expression in plants leads to rapamycin susceptibility.";
RL BMC Plant Biol. 7:26-26(2007).
RN [8]
RP FUNCTION, AND MISCELLANEOUS.
RX PubMed=17721444; DOI=10.1038/sj.embor.7401043;
RA Deprost D., Yao L., Sormani R., Moreau M., Leterreux G., Nicolai M.,
RA Bedu M., Robaglia C., Meyer C.;
RT "The Arabidopsis TOR kinase links plant growth, yield, stress resistance
RT and mRNA translation.";
RL EMBO Rep. 8:864-870(2007).
RN [9]
RP FUNCTION, AND MISCELLANEOUS.
RX PubMed=20686696; DOI=10.1371/journal.pone.0011883;
RA Liu Y., Bassham D.C.;
RT "TOR is a negative regulator of autophagy in Arabidopsis thaliana.";
RL PLoS ONE 5:E11883-E11883(2010).
RN [10]
RP FUNCTION, AND MISCELLANEOUS.
RX PubMed=21428923; DOI=10.1042/bst0390477;
RA Dobrenel T., Marchive C., Sormani R., Moreau M., Mozzo M., Montane M.H.,
RA Menand B., Robaglia C., Meyer C.;
RT "Regulation of plant growth and metabolism by the TOR kinase.";
RL Biochem. Soc. Trans. 39:477-481(2011).
RN [11]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH CAULIFLOWER MOSAIC VIRUS
RP TAV, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=21343906; DOI=10.1038/emboj.2011.39;
RA Schepetilnikov M., Kobayashi K., Geldreich A., Caranta C., Robaglia C.,
RA Keller M., Ryabova L.A.;
RT "Viral factor TAV recruits TOR/S6K1 signalling to activate reinitiation
RT after long ORF translation.";
RL EMBO J. 30:1343-1356(2011).
RN [12]
RP FUNCTION.
RX PubMed=21216945; DOI=10.1105/tpc.110.074005;
RA Ahn C.S., Han J.-A., Lee H.-S., Lee S., Pai H.-S.;
RT "The PP2A regulatory subunit Tap46, a component of the TOR signaling
RT pathway, modulates growth and metabolism in plants.";
RL Plant Cell 23:185-209(2011).
RN [13]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, DOMAIN, MUTAGENESIS OF
RP 2077-ARG--LYS-2080, AND MISCELLANEOUS.
RX PubMed=21266656; DOI=10.1104/pp.110.169045;
RA Ren M., Qiu S., Venglat P., Xiang D., Feng L., Selvaraj G., Datla R.;
RT "Target of rapamycin regulates development and ribosomal RNA expression
RT through kinase domain in Arabidopsis.";
RL Plant Physiol. 155:1367-1382(2011).
RN [14]
RP INTERACTION WITH FKBP12.
RX PubMed=22134914; DOI=10.1074/jbc.m111.300749;
RA Xiong Y., Sheen J.;
RT "Rapamycin and glucose-target of rapamycin (TOR) protein signaling in
RT plants.";
RL J. Biol. Chem. 287:2836-2842(2012).
RN [15]
RP INTERACTION WITH LST8-1.
RX PubMed=22307851; DOI=10.1105/tpc.111.091306;
RA Moreau M., Azzopardi M., Clement G., Dobrenel T., Marchive C., Renne C.,
RA Martin-Magniette M.-L., Taconnat L., Renou J.-P., Robaglia C., Meyer C.;
RT "Mutations in the Arabidopsis homolog of LST8/GbetaL, a partner of the
RT target of Rapamycin kinase, impair plant growth, flowering, and metabolic
RT adaptation to long days.";
RL Plant Cell 24:463-481(2012).
RN [16]
RP FUNCTION, MISCELLANEOUS, AND TISSUE SPECIFICITY.
RX PubMed=23275579; DOI=10.1105/tpc.112.107144;
RA Ren M., Venglat P., Qiu S., Feng L., Cao Y., Wang E., Xiang D., Wang J.,
RA Alexander D., Chalivendra S., Logan D., Mattoo A., Selvaraj G., Datla R.;
RT "Target of rapamycin signaling regulates metabolism, growth, and life span
RT in Arabidopsis.";
RL Plant Cell 24:4850-4874(2012).
RN [17]
RP REVIEW ON TOR SIGNALING.
RX PubMed=23759578; DOI=10.4161/cc.25308;
RA Xiong Y., Sheen J.;
RT "Moving beyond translation: glucose-TOR signaling in the transcriptional
RT control of cell cycle.";
RL Cell Cycle 12:1989-1990(2013).
RN [18]
RP FUNCTION, DISRUPTION PHENOTYPE, INDUCTION BY AUXIN, SUBCELLULAR LOCATION,
RP PHOSPHORYLATION AT SER-2424, AND ACTIVITY REGULATION.
RX PubMed=23524850; DOI=10.1038/emboj.2013.61;
RA Schepetilnikov M., Dimitrova M., Mancera-Martinez E., Geldreich A.,
RA Keller M., Ryabova L.A.;
RT "TOR and S6K1 promote translation reinitiation of uORF-containing mRNAs via
RT phosphorylation of eIF3h.";
RL EMBO J. 32:1087-1102(2013).
RN [19]
RP REVIEW.
RX PubMed=23641244; DOI=10.3389/fpls.2013.00093;
RA Dobrenel T., Marchive C., Azzopardi M., Clement G., Moreau M., Sormani R.,
RA Robaglia C., Meyer C.;
RT "Sugar metabolism and the plant target of rapamycin kinase: a sweet
RT operaTOR?";
RL Front. Plant Sci. 4:93-93(2013).
RN [20]
RP ACTIVITY REGULATION.
RC STRAIN=cv. Columbia, and cv. Wassilewskija;
RX PubMed=23963679; DOI=10.1093/jxb/ert242;
RA Montane M.-H., Menand B.;
RT "ATP-competitive mTOR kinase inhibitors delay plant growth by triggering
RT early differentiation of meristematic cells but no developmental patterning
RT change.";
RL J. Exp. Bot. 64:4361-4374(2013).
RN [21]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=23542588; DOI=10.1038/nature12030;
RA Xiong Y., McCormack M., Li L., Hall Q., Xiang C., Sheen J.;
RT "Glucose-TOR signalling reprograms the transcriptome and activates
RT meristems.";
RL Nature 496:181-186(2013).
RN [22]
RP FUNCTION.
RX PubMed=23173928; DOI=10.1111/tpj.12080;
RA Caldana C., Li Y., Leisse A., Zhang Y., Bartholomaeus L., Fernie A.R.,
RA Willmitzer L., Giavalisco P.;
RT "Systemic analysis of inducible target of rapamycin mutants reveal a
RT general metabolic switch controlling growth in Arabidopsis thaliana.";
RL Plant J. 73:897-909(2013).
RN [23]
RP REVIEW ON KINASES.
RX PubMed=23790269; DOI=10.1016/j.tplants.2013.05.004;
RA Uhrig R.G., Labandera A.-M., Moorhead G.B.;
RT "Arabidopsis PPP family of serine/threonine protein phosphatases: many
RT targets but few engines.";
RL Trends Plant Sci. 18:505-513(2013).
RN [24]
RP REVIEW ON TOR PATHWAY.
RX PubMed=24567496; DOI=10.1093/jxb/eru049;
RA Henriques R., Boegre L., Horvath B., Magyar Z.;
RT "Balancing act: matching growth with environment by the TOR signalling
RT pathway.";
RL J. Exp. Bot. 65:2691-2701(2014).
RN [25]
RP REVIEW ON GLUCOSE SIGNALING.
RX PubMed=25530701; DOI=10.1007/s12374-014-0902-7;
RA Sheen J.;
RT "Master regulators in plant glucose signaling networks.";
RL J. Plant Biol. 57:67-79(2014).
RN [26]
RP FUNCTION, AND ACTIVITY REGULATION.
RC STRAIN=cv. Col-8;
RX PubMed=26459592; DOI=10.1016/j.bbrc.2015.10.028;
RA Kravchenko A., Citerne S., Jehanno I., Bersimbaev R.I., Veit B., Meyer C.,
RA Leprince A.S.;
RT "Mutations in the Arabidopsis Lst8 and Raptor genes encoding partners of
RT the TOR complex, or inhibition of TOR activity decrease abscisic acid (ABA)
RT synthesis.";
RL Biochem. Biophys. Res. Commun. 467:992-997(2015).
RN [27]
RP FUNCTION, DISRUPTION PHENOTYPE, AND ACTIVITY REGULATION.
RX PubMed=25979731; DOI=10.1099/vir.0.000186;
RA Ouibrahim L., Rubio A.G., Moretti A., Montane M.H., Menand B., Meyer C.,
RA Robaglia C., Caranta C.;
RT "Potyviruses differ in their requirement for TOR signalling.";
RL J. Gen. Virol. 96:2898-2903(2015).
RN [28]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=27345161; DOI=10.1016/j.cub.2016.05.005;
RA Zhang Z., Zhu J.-Y., Roh J., Marchive C., Kim S.-K., Meyer C., Sun Y.,
RA Wang W., Wang Z.-Y.;
RT "TOR signaling promotes accumulation of BZR1 to balance growth with carbon
RT availability in Arabidopsis.";
RL Curr. Biol. 26:1854-1860(2016).
RN [29]
RP FUNCTION IN AUXIN SIGNALING, AND ACTIVITY REGULATION.
RC STRAIN=cv. Columbia;
RX PubMed=27014314; DOI=10.3389/fpls.2016.00291;
RA Deng K., Yu L., Zheng X., Zhang K., Wang W., Dong P., Zhang J., Ren M.;
RT "Target of rapamycin is a key player for auxin signaling transduction in
RT Arabidopsis.";
RL Front. Plant Sci. 7:291-291(2016).
RN [30]
RP FUNCTION, AND ACTIVATION CAULIFLOWER MOSAIC VIRUS P6.
RC STRAIN=cv. Columbia;
RX PubMed=27120694; DOI=10.1111/nph.13967;
RA Zvereva A.S., Golyaev V., Turco S., Gubaeva E.G., Rajeswaran R.,
RA Schepetilnikov M.V., Srour O., Ryabova L.A., Boller T., Pooggin M.M.;
RT "Viral protein suppresses oxidative burst and salicylic acid-dependent
RT autophagy and facilitates bacterial growth on virus-infected plants.";
RL New Phytol. 211:1020-1034(2016).
RN [31]
RP FUNCTION, AND ACTIVITY REGULATION.
RC STRAIN=cv. Columbia;
RX PubMed=27479935; DOI=10.1111/nph.14118;
RA Xiong F., Zhang R., Meng Z., Deng K., Que Y., Zhuo F., Feng L., Guo S.,
RA Datla R., Ren M.;
RT "Brassinosteriod Insensitive 2 (BIN2) acts as a downstream effector of the
RT Target of Rapamycin (TOR) signaling pathway to regulate photoautotrophic
RT growth in Arabidopsis.";
RL New Phytol. 213:233-249(2017).
RN [32]
RP FUNCTION.
RC STRAIN=cv. Columbia;
RX PubMed=29084871; DOI=10.1105/tpc.17.00563;
RA Lee D.-H., Park S.J., Ahn C.S., Pai H.-S.;
RT "MRF family genes are involved in translation control, especially under
RT energy-deficient conditions, and their expression and functions are
RT modulated by the TOR signaling pathway.";
RL Plant Cell 29:2895-2920(2017).
CC -!- FUNCTION: Essential cell growth regulator that controls development
CC from early embryo to seed production. Controls plant growth in
CC environmental stress conditions. Acts through the phosphorylation of
CC downstream effectors that are recruited by the binding partner RAPTOR.
CC Acts by activating transcription, protein synthesis and ribosome
CC biogenesis, and inhibiting mRNA degradation and autophagy. Can
CC phosphorylate TAP46, a regulatory subunit of protein phosphatase 2A
CC that modulates cell growth and survival (PubMed:21216945). Involved in
CC modulating the transition from heterotrophic to photoautotrophic growth
CC by regulating the expression of chloroplast- and photosynthesis-
CC associated genes (PubMed:27479935). Essential for auxin signaling
CC transduction, probably acting in polysomes to maintain the active
CC ATPK1/S6K1 (and thus TIF3H1/eIF3h) phosphorylation status that is
CC critical for translation reinitiation (e.g. uORF-mRNAs loading)
CC (PubMed:23524850, PubMed:27014314). Promotes abscisic acid (ABA)
CC biosynthesis (PubMed:26459592). Involved in the regulation of sugar-
CC mediated (e.g. glucose and sucrose) glycolysis- and mitochondrial
CC bioenergetics-dependent root growth promotion (PubMed:23542588).
CC Required for sugar (e.g. glucose) promotion of hypocotyl elongation in
CC the dark, by activating the brassinosteroid pathway and stabilizing
CC BZR1. The regulation of BZR1 degradation is dependent on autophagy
CC (PubMed:27345161). Regulates the expression, phosphorylation and
CC ribosome association of MRFs (e.g. MRF1, MRF3 and MRF4), especially
CC under energy-deficient conditions (PubMed:29084871).
CC {ECO:0000269|PubMed:11983923, ECO:0000269|PubMed:16377759,
CC ECO:0000269|PubMed:17543119, ECO:0000269|PubMed:17721444,
CC ECO:0000269|PubMed:20686696, ECO:0000269|PubMed:21216945,
CC ECO:0000269|PubMed:21266656, ECO:0000269|PubMed:21428923,
CC ECO:0000269|PubMed:23173928, ECO:0000269|PubMed:23275579,
CC ECO:0000269|PubMed:23524850, ECO:0000269|PubMed:23542588,
CC ECO:0000269|PubMed:26459592, ECO:0000269|PubMed:27014314,
CC ECO:0000269|PubMed:27345161, ECO:0000269|PubMed:27479935,
CC ECO:0000269|PubMed:29084871}.
CC -!- FUNCTION: (Microbial infection) Binding to cauliflower mosaic virus
CC (CaMV) Tav protein is critical for both translation reinitiation and
CC viral fitness (PubMed:21343906). When activated by CaMV P6, promotes
CC CaMV translation by inhibiting cellular autophagy and suppressing both
CC silencing and innate immunity, thus confering sensitivity to P.syringae
CC (PubMed:27120694). {ECO:0000269|PubMed:21343906,
CC ECO:0000269|PubMed:27120694}.
CC -!- FUNCTION: (Microbial infection) Required during infection by some
CC potyvirus such as Watermelon mosaic virus (WMV) but not for turnip
CC mosaic virus (TuMV). {ECO:0000269|PubMed:25979731}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000250|UniProtKB:Q9Y7K2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:Q9Y7K2};
CC -!- ACTIVITY REGULATION: Almost insensitive to rapamycin (PubMed:23963679).
CC Strongly repressed by specific active site inhibitors (asTORis) such as
CC AZD-8055, TORIN2 and WYE-132, and, to a lesser extent, by KU63794, WYE-
CC 354 and TORIN1, leading to impaired photoautotrophic growth and
CC abnormally early meristematic cells differentiation (PubMed:23963679,
CC PubMed:23524850). Repression by TORIN1 leads to impaired responses to
CC auxin, including gravitropism (PubMed:23524850). Combined treatment
CC with rapamycin and active-site inhibitors (e.g. Torin1 and AZD-8055)
CC results in synergistic inhibition of activity and plant growth
CC (PubMed:27479935). Inhibition by KU63794 leads to reduced auxin content
CC in root tips (PubMed:27014314). AZD-8055 treatment reduces abscisic
CC acid (ABA) levels (PubMed:26459592). In addition, inhibition by AZD-
CC 8055 leads to a strong reduction of watermelon mosaic virus (WMV)
CC infection (PubMed:25979731). {ECO:0000269|PubMed:23524850,
CC ECO:0000269|PubMed:23963679, ECO:0000269|PubMed:25979731,
CC ECO:0000269|PubMed:26459592, ECO:0000269|PubMed:27014314,
CC ECO:0000269|PubMed:27479935}.
CC -!- SUBUNIT: Interacts with RAPTOR1 and itself. Interacts with FKBP12 in a
CC rapamycin-dependent manner. Binds to LST8-1 (PubMed:22307851).
CC Hyperactivated upon interaction with cauliflower mosaic virus (CaMV)
CC Tav protein (PubMed:21343906). {ECO:0000269|PubMed:16377759,
CC ECO:0000269|PubMed:21266656, ECO:0000269|PubMed:21343906,
CC ECO:0000269|PubMed:22134914, ECO:0000269|PubMed:22307851}.
CC -!- INTERACTION:
CC Q9FR53; O49160: TIF3C1; NbExp=3; IntAct=EBI-1382370, EBI-1635551;
CC Q9FR53; P20081: FPR1; Xeno; NbExp=3; IntAct=EBI-1382370, EBI-6961;
CC Q9FR53; P16666: ORF VI; Xeno; NbExp=6; IntAct=EBI-1382370, EBI-8597718;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21266656}. Nucleus
CC {ECO:0000255|PROSITE-ProRule:PRU00768, ECO:0000269|PubMed:21266656}.
CC Note=Associates to polysomes when activated by auxin or cauliflower
CC mosaic virus (CaMV) Tav protein. {ECO:0000269|PubMed:23524850}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9FR53-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Highly expressed in root meristems, shoot apical
CC meristem (SAM) and floral buds. {ECO:0000269|PubMed:11983923,
CC ECO:0000269|PubMed:15270681, ECO:0000269|PubMed:15607746,
CC ECO:0000269|PubMed:23275579}.
CC -!- DEVELOPMENTAL STAGE: One day after fertilization, expressed in
CC endosperm, embryo, and the chalazal proliferating tissue. At globular
CC stage, no longer expressed in endosperm, but still in embryo up to the
CC heart and torpedo stages. In mature embryo, expressed in the apical and
CC primary root meristems and dividing vascular tissues. During lateral
CC root formation, expressed in the lateral root primordia and remains
CC during the formation of the emerging secondary root meristem.
CC {ECO:0000269|PubMed:11983923}.
CC -!- INDUCTION: Activation by auxin triggers recruitment to polysomes which
CC release inactive ATPK1/S6K1. {ECO:0000269|PubMed:23524850}.
CC -!- DOMAIN: The kinase domain is required for its function.
CC {ECO:0000269|PubMed:21266656}.
CC -!- PTM: Activated by phosphorylation on Ser-2424 triggered by cauliflower
CC mosaic virus P6 and auxin. {ECO:0000269|PubMed:23524850,
CC ECO:0000269|PubMed:27120694}.
CC -!- DISRUPTION PHENOTYPE: Embryo lethality when homozygous. Premature
CC arrest of endosperm and embryo development. RNAi mutant exhibits plant
CC growth arrest and reduced expression of brassinosteroid (BR)-responsive
CC genes, as well as abolished exogenous sugar-mediated promotion of BZR1
CC accumulation (PubMed:27345161). RNAi plants are impaired in sugar-
CC mediated (e.g. glucose and sucrose) root growth promotion and
CC associated genes expression (PubMed:23542588). In response to auxin,
CC deficient plants have polysomes prebound by inactive ATPK1/S6K1, and
CC loading of uORF-mRNAs and activation TIF3H1/eIF3h are impaired
CC (PubMed:23524850). In RNAi plants, severe alteration of watermelon
CC mosaic virus (WMV) infection, but only slight delay of turnip mosaic
CC virus (TuMV) infection (PubMed:25979731). Deficient plants are
CC resistant to viral infection by cauliflower mosaic virus (CaMV), by
CC failing to support CaMV Tav protein-mediated transactivation of
CC reinitiation (PubMed:21343906). {ECO:0000269|PubMed:11983923,
CC ECO:0000269|PubMed:21343906, ECO:0000269|PubMed:23524850,
CC ECO:0000269|PubMed:23542588, ECO:0000269|PubMed:25979731,
CC ECO:0000269|PubMed:27345161}.
CC -!- MISCELLANEOUS: Inducible silencing in seedlings or adult plants leads
CC to plant growth arrest. Plants slightly silencing TOR show constitutive
CC autophagy and reduced shoot and root growth, leaf size, seed production
CC and resistance to osmotic stress. Plants overexpressing TOR show
CC increased shoot and root growth, leaf size, seed production and
CC resistance to osmotic stress. Plants expressing FKBP12 (BP12) are
CC sensitive to rapamycin. BP12 plants repressed by rapamycin exhibit
CC slower growth and development leading to poor nutrient uptake and light
CC energy utilization. {ECO:0000269|PubMed:17543119,
CC ECO:0000269|PubMed:17721444, ECO:0000269|PubMed:20686696,
CC ECO:0000269|PubMed:21266656, ECO:0000269|PubMed:21428923,
CC ECO:0000269|PubMed:23275579}.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF76442.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF178967; AAG43423.1; -; mRNA.
DR EMBL; AC015445; AAF76442.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE32509.1; -; Genomic_DNA.
DR PIR; G96536; G96536.
DR RefSeq; NP_175425.2; NM_103891.4. [Q9FR53-1]
DR AlphaFoldDB; Q9FR53; -.
DR SMR; Q9FR53; -.
DR BioGRID; 26652; 8.
DR DIP; DIP-39421N; -.
DR IntAct; Q9FR53; 10.
DR MINT; Q9FR53; -.
DR STRING; 3702.AT1G50030.1; -.
DR iPTMnet; Q9FR53; -.
DR PaxDb; Q9FR53; -.
DR PRIDE; Q9FR53; -.
DR ProteomicsDB; 228408; -. [Q9FR53-1]
DR EnsemblPlants; AT1G50030.1; AT1G50030.1; AT1G50030. [Q9FR53-1]
DR GeneID; 841427; -.
DR Gramene; AT1G50030.1; AT1G50030.1; AT1G50030. [Q9FR53-1]
DR KEGG; ath:AT1G50030; -.
DR Araport; AT1G50030; -.
DR TAIR; locus:2031090; AT1G50030.
DR eggNOG; KOG0891; Eukaryota.
DR InParanoid; Q9FR53; -.
DR OMA; DPYKHQQ; -.
DR PhylomeDB; Q9FR53; -.
DR PRO; PR:Q9FR53; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9FR53; baseline and differential.
DR Genevisible; Q9FR53; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005844; C:polysome; IDA:UniProtKB.
DR GO; GO:0031931; C:TORC1 complex; IBA:GO_Central.
DR GO; GO:0031932; C:TORC2 complex; IBA:GO_Central.
DR GO; GO:0016303; F:1-phosphatidylinositol-3-kinase activity; ISS:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR GO; GO:0004672; F:protein kinase activity; IDA:UniProtKB.
DR GO; GO:0043621; F:protein self-association; IPI:TAIR.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:InterPro.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:UniProtKB.
DR GO; GO:0009688; P:abscisic acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009734; P:auxin-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0009742; P:brassinosteroid mediated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0016311; P:dephosphorylation; IMP:TAIR.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
DR GO; GO:0009630; P:gravitropism; IMP:UniProtKB.
DR GO; GO:0010507; P:negative regulation of autophagy; IMP:UniProtKB.
DR GO; GO:0050687; P:negative regulation of defense response to virus; IMP:UniProtKB.
DR GO; GO:0016242; P:negative regulation of macroautophagy; IBA:GO_Central.
DR GO; GO:0010116; P:positive regulation of abscisic acid biosynthetic process; IMP:UniProtKB.
DR GO; GO:0010929; P:positive regulation of auxin mediated signaling pathway; IDA:UniProtKB.
DR GO; GO:1900459; P:positive regulation of brassinosteroid mediated signaling pathway; IMP:UniProtKB.
DR GO; GO:0030307; P:positive regulation of cell growth; IMP:UniProtKB.
DR GO; GO:0040019; P:positive regulation of embryonic development; IMP:UniProtKB.
DR GO; GO:1902661; P:positive regulation of glucose mediated signaling pathway; IMP:UniProtKB.
DR GO; GO:2000234; P:positive regulation of rRNA processing; IMP:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0009791; P:post-embryonic development; IMP:TAIR.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0009733; P:response to auxin; IDA:UniProtKB.
DR GO; GO:1901355; P:response to rapamycin; IDA:UniProtKB.
DR GO; GO:0009615; P:response to virus; IDA:UniProtKB.
DR GO; GO:0009303; P:rRNA transcription; IMP:TAIR.
DR GO; GO:0009745; P:sucrose mediated signaling; IMP:UniProtKB.
DR GO; GO:0031929; P:TOR signaling; IBA:GO_Central.
DR Gene3D; 1.10.1070.11; -; 1.
DR Gene3D; 1.20.120.150; -; 1.
DR Gene3D; 1.25.10.10; -; 6.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR024585; DUF3385_TOR.
DR InterPro; IPR003152; FATC_dom.
DR InterPro; IPR009076; FRB_dom.
DR InterPro; IPR036738; FRB_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000403; PI3/4_kinase_cat_dom.
DR InterPro; IPR036940; PI3/4_kinase_cat_sf.
DR InterPro; IPR018936; PI3/4_kinase_CS.
DR InterPro; IPR003151; PIK-rel_kinase_FAT.
DR InterPro; IPR014009; PIK_FAT.
DR InterPro; IPR026683; TOR.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR11139:SF112; PTHR11139:SF112; 1.
DR Pfam; PF11865; DUF3385; 1.
DR Pfam; PF02259; FAT; 1.
DR Pfam; PF02260; FATC; 1.
DR Pfam; PF08771; FRB_dom; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR SMART; SM01346; DUF3385; 1.
DR SMART; SM01343; FATC; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SUPFAM; SSF47212; SSF47212; 1.
DR SUPFAM; SSF48371; SSF48371; 2.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51189; FAT; 1.
DR PROSITE; PS51190; FATC; 1.
DR PROSITE; PS00915; PI3_4_KINASE_1; 1.
DR PROSITE; PS00916; PI3_4_KINASE_2; 1.
DR PROSITE; PS50290; PI3_4_KINASE_3; 1.
PE 1: Evidence at protein level;
KW Abscisic acid biosynthesis; Alternative splicing; ATP-binding;
KW Auxin signaling pathway; Brassinosteroid signaling pathway; Cytoplasm;
KW Developmental protein; Growth regulation; Host-virus interaction; Kinase;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Plant defense;
KW Reference proteome; Repeat; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..2481
FT /note="Serine/threonine-protein kinase TOR"
FT /id="PRO_0000409330"
FT REPEAT 205..242
FT /note="HEAT 1"
FT /evidence="ECO:0000255"
FT REPEAT 292..329
FT /note="HEAT 2"
FT /evidence="ECO:0000255"
FT REPEAT 373..410
FT /note="HEAT 3"
FT /evidence="ECO:0000255"
FT REPEAT 434..471
FT /note="HEAT 4"
FT /evidence="ECO:0000255"
FT REPEAT 569..607
FT /note="HEAT 5"
FT /evidence="ECO:0000255"
FT REPEAT 608..645
FT /note="HEAT 6"
FT /evidence="ECO:0000255"
FT REPEAT 737..775
FT /note="HEAT 7"
FT /evidence="ECO:0000255"
FT REPEAT 781..819
FT /note="HEAT 8"
FT /evidence="ECO:0000255"
FT REPEAT 866..904
FT /note="HEAT 9"
FT /evidence="ECO:0000255"
FT REPEAT 908..945
FT /note="HEAT 10"
FT /evidence="ECO:0000255"
FT REPEAT 952..992
FT /note="HEAT 11"
FT /evidence="ECO:0000255"
FT REPEAT 996..1036
FT /note="HEAT 12"
FT /evidence="ECO:0000255"
FT REPEAT 1037..1075
FT /note="HEAT 13"
FT /evidence="ECO:0000255"
FT REPEAT 1077..1114
FT /note="HEAT 14"
FT /evidence="ECO:0000255"
FT DOMAIN 1309..1887
FT /note="FAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00534"
FT DOMAIN 2065..2378
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT DOMAIN 2449..2481
FT /note="FATC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00534,
FT ECO:0000255|PROSITE-ProRule:PRU00535"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 823..847
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1179..1204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2071..2077
FT /note="G-loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 2244..2252
FT /note="Catalytic loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 2264..2289
FT /note="Activation loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 2354..2384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1505..1512
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT MOTIF 2075..2080
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000305"
FT COMPBIAS 1179..1194
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2424
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:23524850"
FT MUTAGEN 2077..2080
FT /note="Missing: Loss of nuclear localization."
FT /evidence="ECO:0000269|PubMed:21266656"
SQ SEQUENCE 2481 AA; 279190 MW; DA663EA9A9366F93 CRC64;
MSTSSQSFVA GRPASMASPS QSHRFCGPSA TASGGGSFDT LNRVIADLCS RGNPKEGAPL
AFRKHVEEAV RDLSGEASSR FMEQLYDRIA NLIESTDVAE NMGALRAIDE LTEIGFGENA
TKVSRFAGYM RTVFELKRDP EILVLASRVL GHLARAGGAM TSDEVEFQMK TAFDWLRVDR
VEYRRFAAVL ILKEMAENAS TVFNVHVPEF VDAIWVALRD PQLQVRERAV EALRACLRVI
EKRETRWRVQ WYYRMFEATQ DGLGRNAPVH SIHGSLLAVG ELLRNTGEFM MSRYREVAEI
VLRYLEHRDR LVRLSITSLL PRIAHFLRDR FVTNYLTICM NHILTVLRIP AERASGFIAL
GEMAGALDGE LIHYLPTIMS HLRDAIAPRK GRPLLEAVAC VGNIAKAMGS TVETHVRDLL
DVMFSSSLSS TLVDALDQIT ISIPSLLPTV QDRLLDCISL VLSKSHYSQA KPPVTIVRGS
TVGMAPQSSD PSCSAQVQLA LQTLARFNFK GHDLLEFARE SVVVYLDDED AATRKDAALC
CCRLIANSLS GITQFGSSRS TRAGGRRRRL VEEIVEKLLR TAVADADVTV RKSIFVALFG
NQCFDDYLAQ ADSLTAIFAS LNDEDLDVRE YAISVAGRLS EKNPAYVLPA LRRHLIQLLT
YLELSADNKC REESAKLLGC LVRNCERLIL PYVAPVQKAL VARLSEGTGV NANNNIVTGV
LVTVGDLARV GGLAMRQYIP ELMPLIVEAL MDGAAVAKRE VAVSTLGQVV QSTGYVVTPY
KEYPLLLGLL LKLLKGDLVW STRREVLKVL GIMGALDPHV HKRNQQSLSG SHGEVPRGTG
DSGQPIPSID ELPVELRPSF ATSEDYYSTV AINSLMRILR DASLLSYHKR VVRSLMIIFK
SMGLGCVPYL PKVLPELFHT VRTSDENLKD FITWGLGTLV SIVRQHIRKY LPELLSLVSE
LWSSFTLPGP IRPSRGLPVL HLLEHLCLAL NDEFRTYLPV ILPCFIQVLG DAERFNDYTY
VPDILHTLEV FGGTLDEHMH LLLPALIRLF KVDAPVAIRR DAIKTLTRVI PCVQVTGHIS
ALVHHLKLVL DGKNDELRKD AVDALCCLAH ALGEDFTIFI ESIHKLLLKH RLRHKEFEEI
HARWRRREPL IVATTATQQL SRRLPVEVIR DPVIENEIDP FEEGTDRNHQ VNDGRLRTAG
EASQRSTKED WEEWMRHFSI ELLKESPSPA LRTCAKLAQL QPFVGRELFA AGFVSCWAQL
NESSQKQLVR SLEMAFSSPN IPPEILATLL NLAEFMEHDE KPLPIDIRLL GALAEKCRVF
AKALHYKEME FEGPRSKRMD ANPVAVVEAL IHINNQLHQH EAAVGILTYA QQHLDVQLKE
SWYEKLQRWD DALKAYTLKA SQTTNPHLVL EATLGQMRCL AALARWEELN NLCKEYWSPA
EPSARLEMAP MAAQAAWNMG EWDQMAEYVS RLDDGDETKL RGLASPVSSG DGSSNGTFFR
AVLLVRRAKY DEAREYVERA RKCLATELAA LVLESYERAY SNMVRVQQLS ELEEVIEYYT
LPVGNTIAEE RRALIRNMWT QRIQGSKRNV EVWQALLAVR ALVLPPTEDV ETWLKFASLC
RKSGRISQAK STLLKLLPFD PEVSPENMQY HGPPQVMLGY LKYQWSLGEE RKRKEAFTKL
QILTRELSSV PHSQSDILAS MVSSKGANVP LLARVNLKLG TWQWALSSGL NDGSIQEIRD
AFDKSTCYAP KWAKAWHTWA LFNTAVMSHY ISRGQIASQY VVSAVTGYFY SIACAANAKG
VDDSLQDILR LLTLWFNHGA TADVQTALKT GFSHVNINTW LVVLPQIIAR IHSNNRAVRE
LIQSLLIRIG ENHPQALMYP LLVACKSISN LRRAAAQEVV DKVRQHSGAL VDQAQLVSHE
LIRVAILWHE MWHEALEEAS RLYFGEHNIE GMLKVLEPLH DMLDEGVKKD STTIQERAFI
EAYRHELKEA HECCCNYKIT GKDAELTQAW DLYYHVFKRI DKQLASLTTL DLESVSPELL
LCRDLELAVP GTYRADAPVV TISSFSRQLV VITSKQRPRK LTIHGNDGED YAFLLKGHED
LRQDERVMQL FGLVNTLLEN SRKTAEKDLS IQRYSVIPLS PNSGLIGWVP NCDTLHHLIR
EHRDARKIIL NQENKHMLSF APDYDNLPLI AKVEVFEYAL ENTEGNDLSR VLWLKSRSSE
VWLERRTNYT RSLAVMSMVG YILGLGDRHP SNLMLHRYSG KILHIDFGDC FEASMNREKF
PEKVPFRLTR MLVKAMEVSG IEGNFRSTCE NVMQVLRTNK DSVMAMMEAF VHDPLINWRL
FNFNEVPQLA LLGNNNPNAP ADVEPDEEDE DPADIDLPQP QRSTREKEIL QAVNMLGDAN
EVLNERAVVV MARMSHKLTG RDFSSSAIPS NPIADHNNLL GGDSHEVEHG LSVKVQVQKL
INQATSHENL CQNYVGWCPF W
