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Serine/threonine-protein kinase mTOR (EC 2.7.11.1) (FK506-binding protein 12-rapamycin complex-associated protein 1) (FKBP12-rapamycin complex-associated protein) (Mammalian target of rapamycin) (mTOR) (Mechanistic target of rapamycin) (Rapamycin target protein 1) (RAPT1)

 MTOR_RAT                Reviewed;        2549 AA.
P42346;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
01-NOV-1995, sequence version 1.
22-NOV-2017, entry version 163.
RecName: Full=Serine/threonine-protein kinase mTOR;
EC=2.7.11.1;
AltName: Full=FK506-binding protein 12-rapamycin complex-associated protein 1;
AltName: Full=FKBP12-rapamycin complex-associated protein;
AltName: Full=Mammalian target of rapamycin;
Short=mTOR;
AltName: Full=Mechanistic target of rapamycin;
AltName: Full=Rapamycin target protein 1;
Short=RAPT1;
Name=Mtor; Synonyms=Frap1, Raft1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=7822316; DOI=10.1074/jbc.270.2.815;
Sabers C.J., Martin M.M., Brunn G.J., Williams J.M., Dumont F.J.,
Wiederrecht G., Abraham R.T.;
"Isolation of a protein target of the FKBP12-rapamycin complex in
mammalian cells.";
J. Biol. Chem. 270:815-822(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
PubMed=7518356; DOI=10.1016/0092-8674(94)90570-3;
Sabatini D.M., Erdjument-Bromage H., Lui M., Tempst P., Snyder S.H.;
"RAFT1: a mammalian protein that binds to FKBP12 in a rapamycin-
dependent fashion and is homologous to yeast TORs.";
Cell 78:35-43(1994).
[3]
PROTEIN SEQUENCE OF 215-226 AND 533-541, AND IDENTIFICATION BY MASS
SPECTROMETRY.
STRAIN=Sprague-Dawley; TISSUE=Brain;
Lubec G., Kang S.U., Lubec S.;
Submitted (SEP-2007) to UniProtKB.
[4]
FUNCTION IN PHOSPHORYLATION OF RPS6KB1 AND EIF4EBP1.
PubMed=9465032; DOI=10.1073/pnas.95.4.1432;
Burnett P.E., Barrow R.K., Cohen N.A., Snyder S.H., Sabatini D.M.;
"RAFT1 phosphorylation of the translational regulators p70 S6 kinase
and 4E-BP1.";
Proc. Natl. Acad. Sci. U.S.A. 95:1432-1437(1998).
[5]
PHOSPHORYLATION AT THR-2164.
PubMed=21576368; DOI=10.1128/MCB.05437-11;
Ekim B., Magnuson B., Acosta-Jaquez H.A., Keller J.A., Feener E.P.,
Fingar D.C.;
"mTOR kinase domain phosphorylation promotes mTORC1 signaling, cell
growth, and cell cycle progression.";
Mol. Cell. Biol. 31:2787-2801(2011).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: Serine/threonine protein kinase which is a central
regulator of cellular metabolism, growth and survival in response
to hormones, growth factors, nutrients, energy and stress signals.
MTOR directly or indirectly regulates the phosphorylation of at
least 800 proteins. Functions as part of 2 structurally and
functionally distinct signaling complexes mTORC1 and mTORC2 (mTOR
complex 1 and 2). Activated mTORC1 up-regulates protein synthesis
by phosphorylating key regulators of mRNA translation and ribosome
synthesis. This includes phosphorylation of EIF4EBP1 and release
of its inhibition toward the elongation initiation factor 4E
(eiF4E). Moreover, phosphorylates and activates RPS6KB1 and
RPS6KB2 that promote protein synthesis by modulating the activity
of their downstream targets including ribosomal protein S6,
eukaryotic translation initiation factor EIF4B, and the inhibitor
of translation initiation PDCD4. Stimulates the pyrimidine
biosynthesis pathway, both by acute regulation through RPS6KB1-
mediated phosphorylation of the biosynthetic enzyme CAD, and
delayed regulation, through transcriptional enhancement of the
pentose phosphate pathway which produces 5-phosphoribosyl-1-
pyrophosphate (PRPP), an allosteric activator of CAD at a later
step in synthesis, this function is dependent on the mTORC1
complex. Regulates ribosome synthesis by activating RNA polymerase
III-dependent transcription through phosphorylation and inhibition
of MAF1 an RNA polymerase III-repressor. In parallel to protein
synthesis, also regulates lipid synthesis through SREBF1/SREBP1
and LPIN1. To maintain energy homeostasis mTORC1 may also regulate
mitochondrial biogenesis through regulation of PPARGC1A. mTORC1
also negatively regulates autophagy through phosphorylation of
ULK1. Under nutrient sufficiency, phosphorylates ULK1 at 'Ser-
758', disrupting the interaction with AMPK and preventing
activation of ULK1. Also prevents autophagy through
phosphorylation of the autophagy inhibitor DAP. mTORC1 exerts a
feedback control on upstream growth factor signaling that includes
phosphorylation and activation of GRB10 a INSR-dependent signaling
suppressor. Among other potential targets mTORC1 may phosphorylate
CLIP1 and regulate microtubules. As part of the mTORC2 complex
MTOR may regulate other cellular processes including survival and
organization of the cytoskeleton. Plays a critical role in the
phosphorylation at 'Ser-473' of AKT1, a pro-survival effector of
phosphoinositide 3-kinase, facilitating its activation by PDK1.
mTORC2 may regulate the actin cytoskeleton, through
phosphorylation of PRKCA, PXN and activation of the Rho-type
guanine nucleotide exchange factors RHOA and RAC1A or RAC1B.
mTORC2 also regulates the phosphorylation of SGK1 at 'Ser-421'.
Regulates osteoclastogenesis by adjusting the expression of CEBPB
isoforms (By similarity). {ECO:0000250|UniProtKB:P42345,
ECO:0000250|UniProtKB:Q9JLN9, ECO:0000269|PubMed:9465032}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- ENZYME REGULATION: Activation of mTORC1 by growth factors such as
insulin involves AKT1-mediated phosphorylation of TSC1-TSC2, which
leads to the activation of the RHEB GTPase a potent activator of
the protein kinase activity of mTORC1. Insulin-stimulated and
amino acid-dependent phosphorylation at Ser-1261 promotes
autophosphorylation and the activation of mTORC1. Activation by
amino acids requires relocalization of the mTORC1 complex to
lysosomes that is mediated by the Ragulator complex, SLC38A9, and
the Rag GTPases RRAGA, RRAGB, RRAGC and RRAGD. On the other hand,
low cellular energy levels can inhibit mTORC1 through activation
of PRKAA1 while hypoxia inhibits mTORC1 through a REDD1-dependent
mechanism which may also require PRKAA1. The kinase activity of
MTOR within the mTORC1 complex is positively regulated by MLST8
and negatively regulated by DEPTOR and AKT1S1. MTOR phosphorylates
RPTOR which in turn inhibits mTORC1. MTOR is the target of the
immunosuppressive and anti-cancer drug rapamycin which acts in
complex with FKBP1A/FKBP12, and specifically inhibits its kinase
activity. mTORC2 is also activated by growth factors, but seems to
be nutrient-insensitive. It may be regulated by RHEB but in an
indirect manner through the PI3K signaling pathway.
{ECO:0000250|UniProtKB:P42345, ECO:0000250|UniProtKB:Q9JLN9}.
-!- SUBUNIT: Part of the mammalian target of rapamycin complex 1
(mTORC1) which contains MTOR, MLST8, RPTOR, AKT1S1/PRAS40 and
DEPTOR. The mTORC1 complex is a 1 Md obligate dimer of two
stoichiometric heterotetramers with overall dimensions of 290 A x
210 A x 135 A. It has a rhomboid shape and a central cavity, the
dimeric interfaces are formed by interlocking interactions between
the two MTOR and the two RPTOR subunits. The MLST8 subunit forms
distal foot-like protuberances, and contacts only one MTOR within
the complex, while the small PRAS40 localizes to the midsection of
the central core, in close proximity to RPTOR. Part of the
mammalian target of rapamycin complex 2 (mTORC2) which contains
MTOR, MLST8, PRR5, RICTOR, MAPKAP1 and DEPTOR. Interacts with PRR5
and RICTOR; the interaction is direct within the mTORC2 complex.
Interacts with WAC; WAC positively regulates MTOR activity by
promoting the assembly of the TTT complex composed of TELO2, TTI1
and TTI2 and the RUVBL complex composed of RUVBL1 and RUVBL2 into
the TTT-RUVBL complex which leads to the dimerization of the
mTORC1 complex and its subsequent activation. Interacts with PLPP7
and PML. Interacts with UBQLN1. Interacts with TTI1 and TELO2.
Interacts with CLIP1; phosphorylates and regulates CLIP1.
Interacts with NBN. Interacts with BRAT1.
{ECO:0000250|UniProtKB:P42345}.
-!- INTERACTION:
Q8TB45:DEPTOR (xeno); NbExp=2; IntAct=EBI-1571489, EBI-2359040;
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000250|UniProtKB:P42345}; Peripheral membrane protein
{ECO:0000250|UniProtKB:P42345}; Cytoplasmic side
{ECO:0000250|UniProtKB:P42345}. Golgi apparatus membrane
{ECO:0000250|UniProtKB:P42345}; Peripheral membrane protein
{ECO:0000250|UniProtKB:P42345}; Cytoplasmic side
{ECO:0000250|UniProtKB:P42345}. Mitochondrion outer membrane
{ECO:0000250|UniProtKB:Q9JLN9}; Peripheral membrane protein
{ECO:0000250|UniProtKB:Q9JLN9}; Cytoplasmic side
{ECO:0000250|UniProtKB:Q9JLN9}. Lysosome
{ECO:0000250|UniProtKB:P42345}. Cytoplasm
{ECO:0000250|UniProtKB:Q9JLN9}. Nucleus, PML body
{ECO:0000250|UniProtKB:Q9JLN9}. Note=Shuttles between cytoplasm
and nucleus. Accumulates in the nucleus in response to hypoxia (By
similarity). Targeting to lysosomes depends on amino acid
availability and RRAGA and RRAGB (By similarity).
{ECO:0000250|UniProtKB:P42345, ECO:0000250|UniProtKB:Q9JLN9}.
-!- DOMAIN: The kinase domain (PI3K/PI4K) is intrinsically active but
has a highly restricted catalytic center. {ECO:0000250}.
-!- DOMAIN: The FAT domain forms three discontinuous subdomains of
alpha-helical TPR repeats plus a single subdomain of HEAT repeats.
The four domains pack sequentially to form a C-shaped a-solenoid
that clamps onto the kinase domain (By similarity). {ECO:0000250}.
-!- PTM: Autophosphorylates when part of mTORC1 or mTORC2.
Phosphorylation at Ser-1261, Ser-2159 and Thr-2164 promotes
autophosphorylation. Phosphorylation in the kinase domain
modulates the interactions of MTOR with RPTOR and PRAS40 and leads
to increased intrinsic mTORC1 kinase activity. Phosphorylation at
Thr-2173 in the ATP-binding region by AKT1 strongly reduces kinase
activity (By similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the PI3/PI4-kinase family. {ECO:0000305}.
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EMBL; L37085; AAA65929.1; -; mRNA.
EMBL; U11681; AAA20091.1; -; mRNA.
PIR; A54837; A54837.
RefSeq; NP_063971.1; NM_019906.1.
UniGene; Rn.11008; -.
ProteinModelPortal; P42346; -.
BioGrid; 248568; 4.
DIP; DIP-261N; -.
IntAct; P42346; 4.
MINT; MINT-87926; -.
STRING; 10116.ENSRNOP00000014167; -.
BindingDB; P42346; -.
ChEMBL; CHEMBL1075134; -.
iPTMnet; P42346; -.
PhosphoSitePlus; P42346; -.
PaxDb; P42346; -.
PRIDE; P42346; -.
Ensembl; ENSRNOT00000014167; ENSRNOP00000014167; ENSRNOG00000009615.
GeneID; 56718; -.
KEGG; rno:56718; -.
UCSC; RGD:68371; rat.
CTD; 2475; -.
RGD; 68371; Mtor.
eggNOG; KOG0891; Eukaryota.
eggNOG; COG5032; LUCA.
GeneTree; ENSGT00890000139466; -.
HOVERGEN; HBG005744; -.
InParanoid; P42346; -.
KO; K07203; -.
OMA; DPYKHKM; -.
OrthoDB; EOG091G0046; -.
PhylomeDB; P42346; -.
TreeFam; TF105134; -.
Reactome; R-RNO-1257604; PIP3 activates AKT signaling.
Reactome; R-RNO-1632852; Macroautophagy.
Reactome; R-RNO-165159; mTOR signalling.
Reactome; R-RNO-166208; mTORC1-mediated signalling.
Reactome; R-RNO-3371571; HSF1-dependent transactivation.
Reactome; R-RNO-380972; Energy dependent regulation of mTOR by LKB1-AMPK.
Reactome; R-RNO-389357; CD28 dependent PI3K/Akt signaling.
Reactome; R-RNO-5218920; VEGFR2 mediated vascular permeability.
Reactome; R-RNO-5628897; TP53 Regulates Metabolic Genes.
Reactome; R-RNO-6804757; Regulation of TP53 Degradation.
Reactome; R-RNO-8943724; Regulation of PTEN gene transcription.
PRO; PR:P42346; -.
Proteomes; UP000002494; Chromosome 5.
Bgee; ENSRNOG00000009615; -.
ExpressionAtlas; P42346; baseline and differential.
Genevisible; P42346; RN.
GO; GO:0005737; C:cytoplasm; ISO:RGD.
GO; GO:0005829; C:cytosol; IDA:RGD.
GO; GO:0030425; C:dendrite; ISO:RGD.
GO; GO:0012505; C:endomembrane system; ISO:RGD.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0005765; C:lysosomal membrane; ISO:RGD.
GO; GO:0005764; C:lysosome; ISS:UniProtKB.
GO; GO:0032991; C:macromolecular complex; IDA:RGD.
GO; GO:0016020; C:membrane; ISO:RGD.
GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
GO; GO:0031931; C:TORC1 complex; IDA:RGD.
GO; GO:0031932; C:TORC2 complex; ISO:RGD.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
GO; GO:0016301; F:kinase activity; ISO:RGD.
GO; GO:0051219; F:phosphoprotein binding; ISO:RGD.
GO; GO:0019904; F:protein domain specific binding; IPI:RGD.
GO; GO:0004672; F:protein kinase activity; ISO:RGD.
GO; GO:0019901; F:protein kinase binding; IPI:RGD.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:RGD.
GO; GO:0043022; F:ribosome binding; ISO:RGD.
GO; GO:0001030; F:RNA polymerase III type 1 promoter DNA binding; ISO:RGD.
GO; GO:0001031; F:RNA polymerase III type 2 promoter DNA binding; ISO:RGD.
GO; GO:0001032; F:RNA polymerase III type 3 promoter DNA binding; ISO:RGD.
GO; GO:0001156; F:TFIIIC-class transcription factor binding; ISO:RGD.
GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; ISO:RGD.
GO; GO:0007420; P:brain development; IEP:RGD.
GO; GO:0055006; P:cardiac cell development; ISO:RGD.
GO; GO:0055013; P:cardiac muscle cell development; ISO:RGD.
GO; GO:0060048; P:cardiac muscle contraction; ISO:RGD.
GO; GO:0048738; P:cardiac muscle tissue development; ISO:RGD.
GO; GO:0007569; P:cell aging; IEP:RGD.
GO; GO:0016049; P:cell growth; ISO:RGD.
GO; GO:0030030; P:cell projection organization; IGI:MGI.
GO; GO:0034198; P:cellular response to amino acid starvation; ISO:RGD.
GO; GO:0071230; P:cellular response to amino acid stimulus; ISO:RGD.
GO; GO:0071456; P:cellular response to hypoxia; ISS:UniProtKB.
GO; GO:0071233; P:cellular response to leucine; ISO:RGD.
GO; GO:1990253; P:cellular response to leucine starvation; ISO:RGD.
GO; GO:0031669; P:cellular response to nutrient levels; ISS:UniProtKB.
GO; GO:0009267; P:cellular response to starvation; ISO:RGD.
GO; GO:0006281; P:DNA repair; IBA:GO_Central.
GO; GO:0006112; P:energy reserve metabolic process; ISO:RGD.
GO; GO:0007281; P:germ cell development; ISO:RGD.
GO; GO:0003007; P:heart morphogenesis; ISO:RGD.
GO; GO:0003179; P:heart valve morphogenesis; ISO:RGD.
GO; GO:0007616; P:long-term memory; IMP:RGD.
GO; GO:0060135; P:maternal process involved in female pregnancy; IDA:RGD.
GO; GO:0048255; P:mRNA stabilization; IMP:RGD.
GO; GO:0035264; P:multicellular organism growth; ISO:RGD.
GO; GO:0010507; P:negative regulation of autophagy; IMP:RGD.
GO; GO:0045792; P:negative regulation of cell size; IMP:MGI.
GO; GO:1904193; P:negative regulation of cholangiocyte apoptotic process; IMP:RGD.
GO; GO:1904213; P:negative regulation of iodide transmembrane transport; IMP:RGD.
GO; GO:0016242; P:negative regulation of macroautophagy; ISO:RGD.
GO; GO:0014736; P:negative regulation of muscle atrophy; IMP:RGD.
GO; GO:0051534; P:negative regulation of NFAT protein import into nucleus; ISO:RGD.
GO; GO:0001933; P:negative regulation of protein phosphorylation; IMP:RGD.
GO; GO:0031397; P:negative regulation of protein ubiquitination; IMP:RGD.
GO; GO:0018105; P:peptidyl-serine phosphorylation; ISO:RGD.
GO; GO:0018107; P:peptidyl-threonine phosphorylation; ISO:RGD.
GO; GO:0016310; P:phosphorylation; ISO:RGD.
GO; GO:0030838; P:positive regulation of actin filament polymerization; ISO:RGD.
GO; GO:0010942; P:positive regulation of cell death; IMP:RGD.
GO; GO:0061051; P:positive regulation of cell growth involved in cardiac muscle cell development; IMP:RGD.
GO; GO:1904056; P:positive regulation of cholangiocyte proliferation; IMP:RGD.
GO; GO:0060999; P:positive regulation of dendritic spine development; IMP:RGD.
GO; GO:1904000; P:positive regulation of eating behavior; IMP:RGD.
GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IMP:RGD.
GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; ISO:RGD.
GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
GO; GO:0060252; P:positive regulation of glial cell proliferation; IMP:RGD.
GO; GO:1904197; P:positive regulation of granulosa cell proliferation; IMP:RGD.
GO; GO:0051549; P:positive regulation of keratinocyte migration; ISO:RGD.
GO; GO:0010592; P:positive regulation of lamellipodium assembly; ISO:RGD.
GO; GO:0046889; P:positive regulation of lipid biosynthetic process; ISS:UniProtKB.
GO; GO:0010831; P:positive regulation of myotube differentiation; ISO:RGD.
GO; GO:0050769; P:positive regulation of neurogenesis; IMP:RGD.
GO; GO:1901216; P:positive regulation of neuron death; IMP:RGD.
GO; GO:0014042; P:positive regulation of neuron maturation; IMP:RGD.
GO; GO:0010976; P:positive regulation of neuron projection development; IMP:RGD.
GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; IMP:RGD.
GO; GO:0048714; P:positive regulation of oligodendrocyte differentiation; IMP:RGD.
GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; ISO:RGD.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; IMP:RGD.
GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:RGD.
GO; GO:1904058; P:positive regulation of sensory perception of pain; IMP:RGD.
GO; GO:1904206; P:positive regulation of skeletal muscle hypertrophy; IMP:RGD.
GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IMP:RGD.
GO; GO:0051496; P:positive regulation of stress fiber assembly; ISO:RGD.
GO; GO:0045945; P:positive regulation of transcription from RNA polymerase III promoter; ISO:RGD.
GO; GO:1901838; P:positive regulation of transcription of nuclear large rRNA transcript from RNA polymerase I promoter; ISO:RGD.
GO; GO:0045727; P:positive regulation of translation; IMP:RGD.
GO; GO:1903691; P:positive regulation of wound healing, spreading of epidermal cells; ISO:RGD.
GO; GO:0009791; P:post-embryonic development; ISO:RGD.
GO; GO:0046777; P:protein autophosphorylation; IMP:RGD.
GO; GO:0006468; P:protein phosphorylation; IDA:RGD.
GO; GO:0032956; P:regulation of actin cytoskeleton organization; ISO:RGD.
GO; GO:0090335; P:regulation of brown fat cell differentiation; IMP:RGD.
GO; GO:0006109; P:regulation of carbohydrate metabolic process; IDA:RGD.
GO; GO:0043610; P:regulation of carbohydrate utilization; IDA:RGD.
GO; GO:0008361; P:regulation of cell size; ISO:RGD.
GO; GO:0031998; P:regulation of fatty acid beta-oxidation; IDA:RGD.
GO; GO:0005979; P:regulation of glycogen biosynthetic process; IDA:RGD.
GO; GO:0043087; P:regulation of GTPase activity; ISO:RGD.
GO; GO:0090559; P:regulation of membrane permeability; ISO:RGD.
GO; GO:0031641; P:regulation of myelination; ISO:RGD.
GO; GO:0045670; P:regulation of osteoclast differentiation; ISS:UniProtKB.
GO; GO:0045859; P:regulation of protein kinase activity; ISO:RGD.
GO; GO:0051896; P:regulation of protein kinase B signaling; ISO:RGD.
GO; GO:0001932; P:regulation of protein phosphorylation; ISO:RGD.
GO; GO:0032095; P:regulation of response to food; IDA:RGD.
GO; GO:0043200; P:response to amino acid; ISO:RGD.
GO; GO:0042220; P:response to cocaine; IMP:RGD.
GO; GO:0032868; P:response to insulin; ISO:RGD.
GO; GO:0043278; P:response to morphine; IMP:RGD.
GO; GO:0031529; P:ruffle organization; ISO:RGD.
GO; GO:0035176; P:social behavior; IMP:RGD.
GO; GO:0021510; P:spinal cord development; IDA:RGD.
GO; GO:0002296; P:T-helper 1 cell lineage commitment; ISO:RGD.
GO; GO:0031929; P:TOR signaling; ISO:RGD.
GO; GO:0038202; P:TORC1 signaling; ISO:RGD.
GO; GO:0008542; P:visual learning; IMP:RGD.
GO; GO:0050882; P:voluntary musculoskeletal movement; ISO:RGD.
GO; GO:0042060; P:wound healing; IEP:RGD.
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; 5.
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;
Acetylation; ATP-binding; Complete proteome; Cytoplasm;
Direct protein sequencing; Endoplasmic reticulum; Golgi apparatus;
Kinase; Lysosome; Membrane; Mitochondrion;
Mitochondrion outer membrane; Nucleotide-binding; Nucleus;
Phosphoprotein; Reference proteome; Repeat;
Serine/threonine-protein kinase; TPR repeat; Transferase.
CHAIN 1 2549 Serine/threonine-protein kinase mTOR.
/FTId=PRO_0000088810.
REPEAT 16 53 HEAT 1.
REPEAT 55 99 HEAT 2.
REPEAT 100 137 HEAT 3.
REPEAT 138 179 HEAT 4.
REPEAT 180 220 HEAT 5.
REPEAT 222 276 HEAT 6.
REPEAT 277 313 HEAT 7.
REPEAT 314 364 HEAT 8.
REPEAT 365 409 HEAT 9.
REPEAT 410 445 HEAT 10.
REPEAT 446 494 HEAT 11.
REPEAT 495 529 HEAT 12.
REPEAT 530 563 HEAT 13.
REPEAT 564 596 HEAT 14.
REPEAT 597 636 HEAT 15.
REPEAT 637 683 HEAT 16.
REPEAT 686 724 HEAT 17.
REPEAT 727 766 HEAT 18.
REPEAT 769 811 HEAT 19.
REPEAT 814 853 HEAT 20.
REPEAT 857 893 HEAT 21.
REPEAT 894 942 HEAT 22.
REPEAT 943 988 HEAT 23.
REPEAT 989 1027 HEAT 24.
REPEAT 1029 1068 HEAT 25.
REPEAT 1069 1105 HEAT 26.
REPEAT 1106 1144 HEAT 27.
REPEAT 1145 1188 HEAT 28.
REPEAT 1189 1225 HEAT 29.
REPEAT 1226 1273 HEAT 30.
REPEAT 1274 1311 HEAT 31.
REPEAT 1312 1345 HEAT 32.
REPEAT 1346 1382 TPR 1.
DOMAIN 1382 1982 FAT. {ECO:0000255|PROSITE-
ProRule:PRU00534}.
REPEAT 1383 1408 TPR 2.
REPEAT 1409 1442 TPR 3.
REPEAT 1443 1473 TPR 4.
REPEAT 1474 1507 TPR 5.
REPEAT 1508 1541 TPR 6.
REPEAT 1542 1574 TPR 7.
REPEAT 1575 1614 TPR 8.
REPEAT 1615 1649 TPR 9.
REPEAT 1650 1693 TPR 10.
REPEAT 1694 1731 TPR 11.
REPEAT 1732 1786 TPR 12.
REPEAT 1787 1846 TPR 13.
REPEAT 1898 1930 TPR 14.
REPEAT 1931 1970 TPR 15.
REPEAT 1971 2005 TPR 16.
DOMAIN 2182 2516 PI3K/PI4K. {ECO:0000255|PROSITE-
ProRule:PRU00269}.
DOMAIN 2517 2549 FATC. {ECO:0000255|PROSITE-
ProRule:PRU00534, ECO:0000255|PROSITE-
ProRule:PRU00535}.
REGION 1 651 Interaction with NBN. {ECO:0000250}.
REGION 2012 2144 Sufficient for interaction with the
FKBP1A/rapamycin complex. {ECO:0000250}.
REGION 2258 2296 Interaction with MLST8. {ECO:0000250}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:P42345}.
MOD_RES 567 567 Phosphoserine.
{ECO:0000250|UniProtKB:P42345}.
MOD_RES 1162 1162 Phosphothreonine.
{ECO:0000250|UniProtKB:P42345}.
MOD_RES 1218 1218 N6-acetyllysine.
{ECO:0000250|UniProtKB:P42345}.
MOD_RES 1261 1261 Phosphoserine.
{ECO:0000250|UniProtKB:P42345}.
MOD_RES 2159 2159 Phosphoserine.
{ECO:0000250|UniProtKB:P42345}.
MOD_RES 2164 2164 Phosphothreonine.
{ECO:0000269|PubMed:21576368}.
MOD_RES 2173 2173 Phosphothreonine; by PKB/AKT1.
{ECO:0000250|UniProtKB:P42345}.
MOD_RES 2446 2446 Phosphothreonine; by RPS6KB1.
{ECO:0000250|UniProtKB:P42345}.
MOD_RES 2448 2448 Phosphoserine; by RPS6KB1.
{ECO:0000250|UniProtKB:P42345}.
MOD_RES 2478 2478 Phosphoserine.
{ECO:0000250|UniProtKB:P42345}.
MOD_RES 2481 2481 Phosphoserine; by autocatalysis.
{ECO:0000250|UniProtKB:P42345}.
SEQUENCE 2549 AA; 288794 MW; BE841EA7B9086F99 CRC64;
MLGTGPATAT AGAATSSNVS VLQQFASGLK SRNEETRAKA AKELQHYVTM ELREMSQEES
TRFYDQLNHH IFELVSSSDA NERKGGILAI ASLIGVEGGN STRIGRFANY LRNLLPSSDP
VVMEMASKAI GRLAMAGDTF TAEYVEFEVK RALEWLGADR NEGRRHAAVL VLRELAISVP
TFFFQQVQPF FDNIFVAVWD PKQAIREGAV AALRACLILT TQREPKEMQK PQWYRHTFEE
AEKGFDETLA KEKGMNRDDR IHGALLILNE LVRISSMEGE RLREEMEEIT QQQLVHDKYC
KDLMGFGTKP RHITPFTSFQ AVQPQQSNAL VGLLGYSSHQ GLMGFGASPS PTKSTLVESR
CCRDLMEEKF DQVCQWVLKC RSSKNSLIQM TILNLLPRLA AFRPSAFTDT QYLQDTMNHV
LSCVKKEKER TAAFQALGLL SVAVRSEFKV YLPRVLDIIR AALPPKDFAH KRQKTVQVDA
TVFTCISMLA RAMGPGIQQD IKELLEPMLA VGLSPALTAV LYDLSRQIPQ LKKDIQDGLL
KMLSLVLMHK PLRHPGMPKG LAHQLASPGL TTLPEASDVA SITLALRTLG SFEFEGHSLT
QFVRHCADHF LNSEHKEIRM EAARTCSRLL TPSIHLISGH AHVVSQTAVQ VVADVLSKLL
VVGITDPDPD IRYCVLASLD ERFDAHLAQA ENLQALFVAL NDQVFEIREL AICTVGRLSS
MNPAFVMPFL RKMLIQILTE LEHSGIGRIK EQSARMLGHL VSNAPRLIRP YMEPILKALI
LKLKDPDPDP NPGVINNVLA TIGELAQVSG LEMRKWVDEL FVIIMDMLQD SSLLAKRQVA
LWTLGQLVAS TGYVVEPYRK YPTLLEVLLN FLKTEQNQGT RREAIRVLGL LGALDPYKHK
VNIGMIDQSR DASAVSLSES KSSQDSSDYS TSEMLVNMGN LPLDEFYPAV SMVALMRIFR
DQSLSHHHTM VVQAITFIFK SLGLKCVQFL PQVMPTFLNV IRVCDGAIRE FLFQQLGMLV
SFVKSHIRPY MDEIVTLMRE FWVMNTSIQS TIILLIEQIV VALGGEFKLY LPQLIPHMLR
VFMHDNSQGR IVSIKLLAAI QLFGANLDDY LHLLLPPIVK LFDAPEVPLP SRKAALETVD
RLTESLDFTD YASRIIHPIV RTLDQSPELR STAMDTLSSL VFQLGKKYQI FIPMVNKVLV
RHRINHQRYD VLICRIVKGY TLADEEEDPL IYQHRMLRSS QGDALASGPV ETGPMKKLHV
STINLQKAWG AARRVSKDDW LEWLRRLSLE LLKDSSSPSL RSCWALAQAY NPMARDLFNA
AFVSCWSELN EDQQDELIRS IELALTSQDI AEVTQTLLNL AEFMEHSDKG PLPLRDDNGI
VLLGERAAKC RAYAKALHYK ELEFQKGPTP AILESLISIN NKLQQPEAAS GVLEYAMKHF
GELEIQATWY EKLHEWEDAL VAYDKKMDTN KDDPELMLGR MRCLEALGEW GQLHQQCCEK
WTLVNDETQA KMARMAAAAA WGLGQWDSME EYTCMIPRDT HDGAFYRAVL ALHQDLFSLA
QQCIDKARDL LDAELTAMAG ESYSRAYGAM VSCHMLSELE EVIQYKLVPE RREIIRQIWW
ERLQGCQRIV EDWQKILMVR SLVVSPHEDM RTWLKYASLC GKSGRLALAH KTLVLLLGVD
PSRQLDHPLP TVHPQVTYAY MKNMWKSARK IDAFQHMQHF VQTMQQQAQH AIATEDQQHK
QELHKLMARC FLKLGEWQLN LQGINESTIP KVLQYYSAAT EHDRSWYKAW HAWAVMNFEA
VLHYKHQNQA RDEKKKLRHA SGANITNATT TATTAASAAA ATSTEGSNSE SEAESNESSP
TPSPLQKKVT EDLSKTLLLY TVPAVQGFFR SISLSRGNNL QDTLRVLTLW FDYGHWPDVN
EALVEGVKAI QIDTWLQVIP QLIARIDTPR PLVGRLIHQL LTDIGRYHPQ ALIYPLTVAS
KSTTTARHNA ANKILKNMCE HSNTLVQQAM MVSEELIRVA ILWHEMWHEG LEEASRLYFG
ERNVKGMFEV LEPLHAMMER GPQTLKETSF NQAYGRDLME AQEWCRKYMK SGNVKDLTQA
WDLYYHVFRR ISKQLPQLTS LELQYVSPKL LMCRDLELAV PGTYDPNQPI IRIQSIAPSL
QVITSKQRPR KLTLMGSNGH EFVFLLKGHE DLRQDERVMQ LFGLVNTLLA NDPTSLRKNL
SIQRYAVIPL STNSGLIGWV PHCDTLHALI RDYREKKKIL LNIEHRIMLR MAPDYDHLTL
MQKVEVFEHA VNNTAGDDLA KLLWLKSPSS EVWFDRRTNY TRSLAVMSMV GYILGLGDRH
PSNLMLDRLS GKILHIDFGD CFEVAMTREK FPEKIPFRLT RMLTNAMEVT GLDGNYRTTC
HTVMEVLREH KDSVMAVLEA FVYDPLLNWR LMDTNAKGNK RSRTRTDSYS AGQSVEILDG
VELGEPAHKK TGTTVPESIH SFIGDGLVKP EALNKKAIQI INRVRDKLTG RDFSHDDTLD
VPTQVELLIK QATSHENLCQ CYIGWCPFW


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