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Serine/threonine-protein kinase TOR (EC 2.7.11.1) (Protein TARGET OF RAPAMYCIN) (AtTOR)

 TOR_ARATH               Reviewed;        2481 AA.
Q9FR53; Q9LPM4;
31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
25-APR-2018, entry version 135.
RecName: Full=Serine/threonine-protein kinase TOR {ECO:0000250|UniProtKB:Q9Y7K2};
EC=2.7.11.1 {ECO:0000250|UniProtKB:Q9Y7K2};
AltName: Full=Protein TARGET OF RAPAMYCIN {ECO:0000303|PubMed:11983923};
Short=AtTOR {ECO:0000303|PubMed:11983923};
Name=TOR {ECO:0000303|PubMed:11983923};
OrderedLocusNames=At1g50030 {ECO:0000312|Araport:AT1G50030};
ORFNames=F2J10.19 {ECO:0000305};
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY,
DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
STRAIN=cv. Columbia;
PubMed=11983923; DOI=10.1073/pnas.092141899;
Menand B., Desnos T., Nussaume L., Berger F., Bouchez D., Meyer C.,
Robaglia C.;
"Expression and disruption of the Arabidopsis TOR (target of
rapamycin) gene.";
Proc. Natl. Acad. Sci. U.S.A. 99:6422-6427(2002).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130712; DOI=10.1038/35048500;
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S.,
White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M.,
Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
"Sequence and analysis of chromosome 1 of the plant Arabidopsis
thaliana.";
Nature 408:816-820(2000).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[4]
TISSUE SPECIFICITY.
PubMed=15270681; DOI=10.1042/BST0320581;
Robaglia C., Menand B., Lei Y., Sormani R., Nicolai M., Gery C.,
Teoule E., Deprost D., Meyer C.;
"Plant growth: the translational connection.";
Biochem. Soc. Trans. 32:581-584(2004).
[5]
TISSUE SPECIFICITY.
PubMed=15607746; DOI=10.1016/j.bbrc.2004.11.117;
Deprost D., Truong H.N., Robaglia C., Meyer C.;
"An Arabidopsis homolog of RAPTOR/KOG1 is essential for early embryo
development.";
Biochem. Biophys. Res. Commun. 326:844-850(2005).
[6]
FUNCTION, AND INTERACTION WITH RAPTOR1.
PubMed=16377759; DOI=10.1105/tpc.105.035931;
Mahfouz M.M., Kim S., Delauney A.J., Verma D.P.;
"Arabidopsis TARGET OF RAPAMYCIN interacts with RAPTOR, which
regulates the activity of S6 kinase in response to osmotic stress
signals.";
Plant Cell 18:477-490(2006).
[7]
FUNCTION, AND MISCELLANEOUS.
PubMed=17543119; DOI=10.1186/1471-2229-7-26;
Sormani R., Yao L., Menand B., Ennar N., Lecampion C., Meyer C.,
Robaglia C.;
"Saccharomyces cerevisiae FKBP12 binds Arabidopsis thaliana TOR and
its expression in plants leads to rapamycin susceptibility.";
BMC Plant Biol. 7:26-26(2007).
[8]
FUNCTION, AND MISCELLANEOUS.
PubMed=17721444; DOI=10.1038/sj.embor.7401043;
Deprost D., Yao L., Sormani R., Moreau M., Leterreux G., Nicolai M.,
Bedu M., Robaglia C., Meyer C.;
"The Arabidopsis TOR kinase links plant growth, yield, stress
resistance and mRNA translation.";
EMBO Rep. 8:864-870(2007).
[9]
FUNCTION, AND MISCELLANEOUS.
PubMed=20686696; DOI=10.1371/journal.pone.0011883;
Liu Y., Bassham D.C.;
"TOR is a negative regulator of autophagy in Arabidopsis thaliana.";
PLoS ONE 5:E11883-E11883(2010).
[10]
FUNCTION, AND MISCELLANEOUS.
PubMed=21428923; DOI=10.1042/BST0390477;
Dobrenel T., Marchive C., Sormani R., Moreau M., Mozzo M.,
Montane M.H., Menand B., Robaglia C., Meyer C.;
"Regulation of plant growth and metabolism by the TOR kinase.";
Biochem. Soc. Trans. 39:477-481(2011).
[11]
FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH CAULIFLOWER MOSAIC
VIRUS TAV, AND SUBCELLULAR LOCATION.
STRAIN=cv. Columbia;
PubMed=21343906; DOI=10.1038/emboj.2011.39;
Schepetilnikov M., Kobayashi K., Geldreich A., Caranta C.,
Robaglia C., Keller M., Ryabova L.A.;
"Viral factor TAV recruits TOR/S6K1 signalling to activate
reinitiation after long ORF translation.";
EMBO J. 30:1343-1356(2011).
[12]
FUNCTION.
PubMed=21216945; DOI=10.1105/tpc.110.074005;
Ahn C.S., Han J.-A., Lee H.-S., Lee S., Pai H.-S.;
"The PP2A regulatory subunit Tap46, a component of the TOR signaling
pathway, modulates growth and metabolism in plants.";
Plant Cell 23:185-209(2011).
[13]
FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, DOMAIN, MUTAGENESIS OF
2077-ARG--LYS-2080, AND MISCELLANEOUS.
PubMed=21266656; DOI=10.1104/pp.110.169045;
Ren M., Qiu S., Venglat P., Xiang D., Feng L., Selvaraj G., Datla R.;
"Target of rapamycin regulates development and ribosomal RNA
expression through kinase domain in Arabidopsis.";
Plant Physiol. 155:1367-1382(2011).
[14]
INTERACTION WITH FKBP12.
PubMed=22134914; DOI=10.1074/jbc.M111.300749;
Xiong Y., Sheen J.;
"Rapamycin and glucose-target of rapamycin (TOR) protein signaling in
plants.";
J. Biol. Chem. 287:2836-2842(2012).
[15]
INTERACTION WITH LST8-1.
PubMed=22307851; DOI=10.1105/tpc.111.091306;
Moreau M., Azzopardi M., Clement G., Dobrenel T., Marchive C.,
Renne C., Martin-Magniette M.-L., Taconnat L., Renou J.-P.,
Robaglia C., Meyer C.;
"Mutations in the Arabidopsis homolog of LST8/GbetaL, a partner of the
target of Rapamycin kinase, impair plant growth, flowering, and
metabolic adaptation to long days.";
Plant Cell 24:463-481(2012).
[16]
FUNCTION, MISCELLANEOUS, AND TISSUE SPECIFICITY.
PubMed=23275579; DOI=10.1105/tpc.112.107144;
Ren M., Venglat P., Qiu S., Feng L., Cao Y., Wang E., Xiang D.,
Wang J., Alexander D., Chalivendra S., Logan D., Mattoo A.,
Selvaraj G., Datla R.;
"Target of rapamycin signaling regulates metabolism, growth, and life
span in Arabidopsis.";
Plant Cell 24:4850-4874(2012).
[17]
REVIEW ON TOR SIGNALING.
PubMed=23759578; DOI=10.4161/cc.25308;
Xiong Y., Sheen J.;
"Moving beyond translation: glucose-TOR signaling in the
transcriptional control of cell cycle.";
Cell Cycle 12:1989-1990(2013).
[18]
FUNCTION, DISRUPTION PHENOTYPE, INDUCTION BY AUXIN, SUBCELLULAR
LOCATION, PHOSPHORYLATION AT SER-2424, AND ENZYME REGULATION.
PubMed=23524850; DOI=10.1038/emboj.2013.61;
Schepetilnikov M., Dimitrova M., Mancera-Martinez E., Geldreich A.,
Keller M., Ryabova L.A.;
"TOR and S6K1 promote translation reinitiation of uORF-containing
mRNAs via phosphorylation of eIF3h.";
EMBO J. 32:1087-1102(2013).
[19]
REVIEW.
PubMed=23641244; DOI=10.3389/fpls.2013.00093;
Dobrenel T., Marchive C., Azzopardi M., Clement G., Moreau M.,
Sormani R., Robaglia C., Meyer C.;
"Sugar metabolism and the plant target of rapamycin kinase: a sweet
operaTOR?";
Front. Plant Sci. 4:93-93(2013).
[20]
ENZYME REGULATION.
STRAIN=cv. Columbia, and cv. Wassilewskija;
PubMed=23963679; DOI=10.1093/jxb/ert242;
Montane M.-H., Menand B.;
"ATP-competitive mTOR kinase inhibitors delay plant growth by
triggering early differentiation of meristematic cells but no
developmental patterning change.";
J. Exp. Bot. 64:4361-4374(2013).
[21]
FUNCTION, AND DISRUPTION PHENOTYPE.
STRAIN=cv. Columbia;
PubMed=23542588; DOI=10.1038/nature12030;
Xiong Y., McCormack M., Li L., Hall Q., Xiang C., Sheen J.;
"Glucose-TOR signalling reprograms the transcriptome and activates
meristems.";
Nature 496:181-186(2013).
[22]
FUNCTION.
PubMed=23173928; DOI=10.1111/tpj.12080;
Caldana C., Li Y., Leisse A., Zhang Y., Bartholomaeus L., Fernie A.R.,
Willmitzer L., Giavalisco P.;
"Systemic analysis of inducible target of rapamycin mutants reveal a
general metabolic switch controlling growth in Arabidopsis thaliana.";
Plant J. 73:897-909(2013).
[23]
REVIEW ON KINASES.
PubMed=23790269; DOI=10.1016/j.tplants.2013.05.004;
Uhrig R.G., Labandera A.-M., Moorhead G.B.;
"Arabidopsis PPP family of serine/threonine protein phosphatases: many
targets but few engines.";
Trends Plant Sci. 18:505-513(2013).
[24]
REVIEW ON TOR PATHWAY.
PubMed=24567496; DOI=10.1093/jxb/eru049;
Henriques R., Boegre L., Horvath B., Magyar Z.;
"Balancing act: matching growth with environment by the TOR signalling
pathway.";
J. Exp. Bot. 65:2691-2701(2014).
[25]
REVIEW ON GLUCOSE SIGNALING.
PubMed=25530701; DOI=10.1007/s12374-014-0902-7;
Sheen J.;
"Master regulators in plant glucose signaling networks.";
J. Plant Biol. 57:67-79(2014).
[26]
FUNCTION, AND ENZYME REGULATION.
STRAIN=cv. Col-8;
PubMed=26459592; DOI=10.1016/j.bbrc.2015.10.028;
Kravchenko A., Citerne S., Jehanno I., Bersimbaev R.I., Veit B.,
Meyer C., Leprince A.S.;
"Mutations in the Arabidopsis Lst8 and Raptor genes encoding partners
of the TOR complex, or inhibition of TOR activity decrease abscisic
acid (ABA) synthesis.";
Biochem. Biophys. Res. Commun. 467:992-997(2015).
[27]
FUNCTION, DISRUPTION PHENOTYPE, AND ENZYME REGULATION.
PubMed=25979731; DOI=10.1099/vir.0.000186;
Ouibrahim L., Rubio A.G., Moretti A., Montane M.H., Menand B.,
Meyer C., Robaglia C., Caranta C.;
"Potyviruses differ in their requirement for TOR signalling.";
J. Gen. Virol. 96:2898-2903(2015).
[28]
FUNCTION, AND DISRUPTION PHENOTYPE.
STRAIN=cv. Columbia;
PubMed=27345161; DOI=10.1016/j.cub.2016.05.005;
Zhang Z., Zhu J.-Y., Roh J., Marchive C., Kim S.-K., Meyer C., Sun Y.,
Wang W., Wang Z.-Y.;
"TOR signaling promotes accumulation of BZR1 to balance growth with
carbon availability in Arabidopsis.";
Curr. Biol. 26:1854-1860(2016).
[29]
FUNCTION IN AUXIN SIGNALING, AND ENZYME REGULATION.
STRAIN=cv. Columbia;
PubMed=27014314; DOI=10.3389/fpls.2016.00291;
Deng K., Yu L., Zheng X., Zhang K., Wang W., Dong P., Zhang J.,
Ren M.;
"Target of rapamycin is a key player for auxin signaling transduction
in Arabidopsis.";
Front. Plant Sci. 7:291-291(2016).
[30]
FUNCTION, AND ACTIVATION CAULIFLOWER MOSAIC VIRUS P6.
STRAIN=cv. Columbia;
PubMed=27120694; DOI=10.1111/nph.13967;
Zvereva A.S., Golyaev V., Turco S., Gubaeva E.G., Rajeswaran R.,
Schepetilnikov M.V., Srour O., Ryabova L.A., Boller T., Pooggin M.M.;
"Viral protein suppresses oxidative burst and salicylic acid-dependent
autophagy and facilitates bacterial growth on virus-infected plants.";
New Phytol. 211:1020-1034(2016).
[31]
FUNCTION, AND ENZYME REGULATION.
STRAIN=cv. Columbia;
PubMed=27479935; DOI=10.1111/nph.14118;
Xiong F., Zhang R., Meng Z., Deng K., Que Y., Zhuo F., Feng L.,
Guo S., Datla R., Ren M.;
"Brassinosteriod Insensitive 2 (BIN2) acts as a downstream effector of
the Target of Rapamycin (TOR) signaling pathway to regulate
photoautotrophic growth in Arabidopsis.";
New Phytol. 213:233-249(2017).
-!- FUNCTION: Essential cell growth regulator that controls
development from early embryo to seed production. Controls plant
growth in environmental stress conditions. Acts through the
phosphorylation of downstream effectors that are recruited by the
binding partner RAPTOR. Acts by activating transcription, protein
synthesis and ribosome biogenesis, and inhibiting mRNA degradation
and autophagy. Can phosphorylate TAP46, a regulatory subunit of
protein phosphatase 2A that modulates cell growth and survival
(PubMed:21216945). Involved in modulating the transition from
heterotrophic to photoautotrophic growth by regulating the
expression of chloroplast- and photosynthesis-associated genes
(PubMed:27479935). Essential for auxin signaling transduction,
probably acting in polysomes to maintain the active ATPK1/S6K1
(and thus TIF3H1/eIF3h) phosphorylation status that is critical
for translation reinitiation (e.g. uORF-mRNAs loading)
(PubMed:23524850, PubMed:27014314). Promotes abscisic acid (ABA)
biosynthesis (PubMed:26459592). Involved in the regulation of
sugar-mediated (e.g. glucose and sucrose) glycolysis- and
mitochondrial bioenergetics-dependent root growth promotion
(PubMed:23542588). Required for sugar (e.g. glucose) promotion of
hypocotyl elongation in the dark, by activating the
brassinosteroid pathway and stabilizing BZR1. The regulation of
BZR1 degradation is dependent on autophagy (PubMed:27345161).
{ECO:0000269|PubMed:11983923, ECO:0000269|PubMed:16377759,
ECO:0000269|PubMed:17543119, ECO:0000269|PubMed:17721444,
ECO:0000269|PubMed:20686696, ECO:0000269|PubMed:21216945,
ECO:0000269|PubMed:21266656, ECO:0000269|PubMed:21428923,
ECO:0000269|PubMed:23173928, ECO:0000269|PubMed:23275579,
ECO:0000269|PubMed:23524850, ECO:0000269|PubMed:23542588,
ECO:0000269|PubMed:26459592, ECO:0000269|PubMed:27014314,
ECO:0000269|PubMed:27345161, ECO:0000269|PubMed:27479935}.
-!- FUNCTION: (Microbial infection) Binding to cauliflower mosaic
virus (CaMV) Tav protein is critical for both translation
reinitiation and viral fitness (PubMed:21343906). When activated
by CaMV P6, promotes CaMV translation by inhibiting cellular
autophagy and suppressing both silencing and innate immunity, thus
confering sensitivity to P.syringae (PubMed:27120694).
{ECO:0000269|PubMed:21343906, ECO:0000269|PubMed:27120694}.
-!- FUNCTION: (Microbial infection) Required during infection by some
potyvirus such as Watermelon mosaic virus (WMV) but not for turnip
mosaic virus (TuMV). {ECO:0000269|PubMed:25979731}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
{ECO:0000250|UniProtKB:Q9Y7K2}.
-!- ENZYME REGULATION: Almost insensitive to rapamycin
(PubMed:23963679). Strongly repressed by specific active site
inhibitors (asTORis) such as AZD-8055, TORIN2 and WYE-132, and, to
a lesser extent, by KU63794, WYE-354 and TORIN1, leading to
impaired photoautotrophic growth and abnormally early meristematic
cells differentiation (PubMed:23963679, PubMed:23524850).
Repression by TORIN1 leads to impaired responses to auxin,
including gravitropism (PubMed:23524850). Combined treatment with
rapamycin and active-site inhibitors (e.g. Torin1 and AZD-8055)
results in synergistic inhibition of activity and plant growth
(PubMed:27479935). Inhibition by KU63794 leads to reduced auxin
content in root tips (PubMed:27014314). AZD-8055 treatment reduces
abscisic acid (ABA) levels (PubMed:26459592). In addition,
inhibition by AZD-8055 leads to a strong reduction of watermelon
mosaic virus (WMV) infection (PubMed:25979731).
{ECO:0000269|PubMed:23524850, ECO:0000269|PubMed:23963679,
ECO:0000269|PubMed:25979731, ECO:0000269|PubMed:26459592,
ECO:0000269|PubMed:27014314, ECO:0000269|PubMed:27479935}.
-!- SUBUNIT: Interacts with RAPTOR1 and itself. Interacts with FKBP12
in a rapamycin-dependent manner. Binds to LST8-1
(PubMed:22307851). Hyperactivated upon interaction with
cauliflower mosaic virus (CaMV) Tav protein (PubMed:21343906).
{ECO:0000269|PubMed:16377759, ECO:0000269|PubMed:21266656,
ECO:0000269|PubMed:21343906, ECO:0000269|PubMed:22134914,
ECO:0000269|PubMed:22307851}.
-!- INTERACTION:
P20081:FPR1 (xeno); NbExp=3; IntAct=EBI-1382370, EBI-6961;
P16666:ORF VI (xeno); NbExp=6; IntAct=EBI-1382370, EBI-8597718;
O49160:TIF3C1; NbExp=3; IntAct=EBI-1382370, EBI-1635551;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21266656}.
Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768,
ECO:0000269|PubMed:21266656}. Note=Associates to polysomes when
activated by auxin or cauliflower mosaic virus (CaMV) Tav protein.
{ECO:0000269|PubMed:23524850}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=1;
Comment=A number of isoforms are produced. According to EST
sequences.;
Name=1;
IsoId=Q9FR53-1; Sequence=Displayed;
-!- TISSUE SPECIFICITY: Highly expressed in root meristems, shoot
apical meristem (SAM) and floral buds.
{ECO:0000269|PubMed:11983923, ECO:0000269|PubMed:15270681,
ECO:0000269|PubMed:15607746, ECO:0000269|PubMed:23275579}.
-!- DEVELOPMENTAL STAGE: One day after fertilization, expressed in
endosperm, embryo, and the chalazal proliferating tissue. At
globular stage, no longer expressed in endosperm, but still in
embryo up to the heart and torpedo stages. In mature embryo,
expressed in the apical and primary root meristems and dividing
vascular tissues. During lateral root formation, expressed in the
lateral root primordia and remains during the formation of the
emerging secondary root meristem. {ECO:0000269|PubMed:11983923}.
-!- INDUCTION: Activation by auxin triggers recruitment to polysomes
which release inactive ATPK1/S6K1. {ECO:0000269|PubMed:23524850}.
-!- DOMAIN: The kinase domain is required for its function.
{ECO:0000269|PubMed:21266656}.
-!- PTM: Activated by phosphorylation on Ser-2424 triggered by
cauliflower mosaic virus P6 and auxin.
{ECO:0000269|PubMed:23524850, ECO:0000269|PubMed:27120694}.
-!- DISRUPTION PHENOTYPE: Embryo lethality when homozygous. Premature
arrest of endosperm and embryo development. RNAi mutant exhibits
plant growth arrest and reduced expression of brassinosteroid
(BR)-responsive genes, as well as abolished exogenous sugar-
mediated promotion of BZR1 accumulation (PubMed:27345161). RNAi
plants are impaired in sugar-mediated (e.g. glucose and sucrose)
root growth promotion and associated genes expression
(PubMed:23542588). In response to auxin, deficient plants have
polysomes prebound by inactive ATPK1/S6K1, and loading of uORF-
mRNAs and activation TIF3H1/eIF3h are impaired (PubMed:23524850).
In RNAi plants, severe alteration of watermelon mosaic virus (WMV)
infection, but only slight delay of turnip mosaic virus (TuMV)
infection (PubMed:25979731). Deficient plants are resistant to
viral infection by cauliflower mosaic virus (CaMV), by failing to
support CaMV Tav protein-mediated transactivation of reinitiation
(PubMed:21343906). {ECO:0000269|PubMed:11983923,
ECO:0000269|PubMed:21343906, ECO:0000269|PubMed:23524850,
ECO:0000269|PubMed:23542588, ECO:0000269|PubMed:25979731,
ECO:0000269|PubMed:27345161}.
-!- MISCELLANEOUS: Inducible silencing in seedlings or adult plants
leads to plant growth arrest. Plants slightly silencing TOR show
constitutive autophagy and reduced shoot and root growth, leaf
size, seed production and resistance to osmotic stress. Plants
overexpressing TOR show increased shoot and root growth, leaf
size, seed production and resistance to osmotic stress. Plants
expressing FKBP12 (BP12) are sensitive to rapamycin. BP12 plants
repressed by rapamycin exhibit slower growth and development
leading to poor nutrient uptake and light energy utilization.
{ECO:0000269|PubMed:17543119, ECO:0000269|PubMed:17721444,
ECO:0000269|PubMed:20686696, ECO:0000269|PubMed:21266656,
ECO:0000269|PubMed:21428923, ECO:0000269|PubMed:23275579}.
-!- SIMILARITY: Belongs to the PI3/PI4-kinase family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAF76442.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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EMBL; AF178967; AAG43423.1; -; mRNA.
EMBL; AC015445; AAF76442.1; ALT_SEQ; Genomic_DNA.
EMBL; CP002684; AEE32509.1; -; Genomic_DNA.
PIR; G96536; G96536.
RefSeq; NP_175425.2; NM_103891.4. [Q9FR53-1]
UniGene; At.16944; -.
ProteinModelPortal; Q9FR53; -.
SMR; Q9FR53; -.
BioGrid; 26652; 2.
DIP; DIP-39421N; -.
IntAct; Q9FR53; 7.
MINT; Q9FR53; -.
STRING; 3702.AT1G50030.1; -.
iPTMnet; Q9FR53; -.
PaxDb; Q9FR53; -.
PRIDE; Q9FR53; -.
EnsemblPlants; AT1G50030.1; AT1G50030.1; AT1G50030. [Q9FR53-1]
GeneID; 841427; -.
Gramene; AT1G50030.1; AT1G50030.1; AT1G50030. [Q9FR53-1]
KEGG; ath:AT1G50030; -.
Araport; AT1G50030; -.
TAIR; locus:2031090; AT1G50030.
eggNOG; KOG0891; Eukaryota.
eggNOG; COG5032; LUCA.
HOGENOM; HOG000163215; -.
InParanoid; Q9FR53; -.
KO; K07203; -.
OMA; SSHQGLM; -.
OrthoDB; EOG0936000W; -.
PhylomeDB; Q9FR53; -.
Reactome; R-ATH-3371571; HSF1-dependent transactivation.
PRO; PR:Q9FR53; -.
Proteomes; UP000006548; Chromosome 1.
ExpressionAtlas; Q9FR53; baseline and differential.
Genevisible; Q9FR53; AT.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005844; C:polysome; IDA:UniProtKB.
GO; GO:0016303; F:1-phosphatidylinositol-3-kinase activity; ISS:TAIR.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
GO; GO:0004672; F:protein kinase activity; IDA:UniProtKB.
GO; GO:0043621; F:protein self-association; IPI:TAIR.
GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
GO; GO:0044877; F:protein-containing complex binding; IEA:InterPro.
GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:UniProtKB.
GO; GO:0009688; P:abscisic acid biosynthetic process; IEA:UniProtKB-KW.
GO; GO:0009734; P:auxin-activated signaling pathway; IEA:UniProtKB-KW.
GO; GO:0009742; P:brassinosteroid mediated signaling pathway; IEA:UniProtKB-KW.
GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
GO; GO:0006281; P:DNA repair; IBA:GO_Central.
GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
GO; GO:0009630; P:gravitropism; IMP:UniProtKB.
GO; GO:0010507; P:negative regulation of autophagy; IMP:UniProtKB.
GO; GO:0050687; P:negative regulation of defense response to virus; IMP:UniProtKB.
GO; GO:0010116; P:positive regulation of abscisic acid biosynthetic process; IMP:UniProtKB.
GO; GO:0010929; P:positive regulation of auxin mediated signaling pathway; IDA:UniProtKB.
GO; GO:1900459; P:positive regulation of brassinosteroid mediated signaling pathway; IMP:UniProtKB.
GO; GO:0030307; P:positive regulation of cell growth; IMP:UniProtKB.
GO; GO:0040019; P:positive regulation of embryonic development; IMP:UniProtKB.
GO; GO:1902661; P:positive regulation of glucose mediated signaling pathway; IMP:UniProtKB.
GO; GO:2000234; P:positive regulation of rRNA processing; IMP:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:UniProtKB.
GO; GO:0009791; P:post-embryonic development; IMP:TAIR.
GO; GO:0009733; P:response to auxin; IDA:UniProtKB.
GO; GO:1901355; P:response to rapamycin; IDA:UniProtKB.
GO; GO:0009615; P:response to virus; IDA:UniProtKB.
GO; GO:0009303; P:rRNA transcription; IMP:TAIR.
GO; GO:0009745; P:sucrose mediated signaling; IMP:UniProtKB.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
Gene3D; 1.10.1070.11; -; 1.
Gene3D; 1.20.120.150; -; 1.
Gene3D; 1.25.10.10; -; 3.
InterPro; IPR011989; ARM-like.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR024585; DUF3385_TOR.
InterPro; IPR003152; FATC_dom.
InterPro; IPR009076; FRB_dom.
InterPro; IPR036738; FRB_sf.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000403; PI3/4_kinase_cat_dom.
InterPro; IPR036940; PI3/4_kinase_cat_sf.
InterPro; IPR018936; PI3/4_kinase_CS.
InterPro; IPR003151; PIK-rel_kinase_FAT.
InterPro; IPR014009; PIK_FAT.
InterPro; IPR026683; TOR.
PANTHER; PTHR11139:SF9; PTHR11139:SF9; 1.
Pfam; PF11865; DUF3385; 1.
Pfam; PF02259; FAT; 1.
Pfam; PF02260; FATC; 1.
Pfam; PF08771; FRB_dom; 1.
Pfam; PF00454; PI3_PI4_kinase; 1.
SMART; SM01346; DUF3385; 1.
SMART; SM01343; FATC; 1.
SMART; SM00146; PI3Kc; 1.
SUPFAM; SSF47212; SSF47212; 1.
SUPFAM; SSF48371; SSF48371; 4.
SUPFAM; SSF56112; SSF56112; 2.
PROSITE; PS51189; FAT; 1.
PROSITE; PS51190; FATC; 1.
PROSITE; PS00915; PI3_4_KINASE_1; 1.
PROSITE; PS00916; PI3_4_KINASE_2; 1.
PROSITE; PS50290; PI3_4_KINASE_3; 1.
1: Evidence at protein level;
Abscisic acid biosynthesis; Alternative splicing; ATP-binding;
Auxin signaling pathway; Brassinosteroid signaling pathway;
Complete proteome; Cytoplasm; Developmental protein;
Growth regulation; Host-virus interaction; Kinase; Nucleotide-binding;
Nucleus; Phosphoprotein; Plant defense; Reference proteome; Repeat;
Serine/threonine-protein kinase; Transferase.
CHAIN 1 2481 Serine/threonine-protein kinase TOR.
/FTId=PRO_0000409330.
REPEAT 205 242 HEAT 1. {ECO:0000255}.
REPEAT 292 329 HEAT 2. {ECO:0000255}.
REPEAT 373 410 HEAT 3. {ECO:0000255}.
REPEAT 434 471 HEAT 4. {ECO:0000255}.
REPEAT 569 607 HEAT 5. {ECO:0000255}.
REPEAT 608 645 HEAT 6. {ECO:0000255}.
REPEAT 737 775 HEAT 7. {ECO:0000255}.
REPEAT 781 819 HEAT 8. {ECO:0000255}.
REPEAT 866 904 HEAT 9. {ECO:0000255}.
REPEAT 908 945 HEAT 10. {ECO:0000255}.
REPEAT 952 992 HEAT 11. {ECO:0000255}.
REPEAT 996 1036 HEAT 12. {ECO:0000255}.
REPEAT 1037 1075 HEAT 13. {ECO:0000255}.
REPEAT 1077 1114 HEAT 14. {ECO:0000255}.
DOMAIN 1309 1887 FAT. {ECO:0000255|PROSITE-
ProRule:PRU00534}.
DOMAIN 2091 2481 PI3K/PI4K. {ECO:0000255|PROSITE-
ProRule:PRU00269}.
DOMAIN 2449 2481 FATC. {ECO:0000255|PROSITE-
ProRule:PRU00534, ECO:0000255|PROSITE-
ProRule:PRU00535}.
MOTIF 1505 1512 Nuclear localization signal.
{ECO:0000255|PROSITE-ProRule:PRU00768}.
MOTIF 2075 2080 Nuclear localization signal.
{ECO:0000305}.
MOD_RES 2424 2424 Phosphoserine.
{ECO:0000269|PubMed:23524850}.
MUTAGEN 2077 2080 Missing: Loss of nuclear localization.
{ECO:0000269|PubMed:21266656}.
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


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