TOR1_YEAST
ID TOR1_YEAST Reviewed; 2470 AA.
AC P35169; D6VWN7;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 3.
DT 03-AUG-2022, entry version 210.
DE RecName: Full=Serine/threonine-protein kinase TOR1;
DE EC=2.7.11.1 {ECO:0000269|PubMed:10436010, ECO:0000305|PubMed:34535752};
DE AltName: Full=Dominant rapamycin resistance protein 1;
DE AltName: Full=Phosphatidylinositol kinase homolog TOR1;
DE AltName: Full=Target of rapamycin kinase 1;
GN Name=TOR1; Synonyms=DRR1; OrderedLocusNames=YJR066W; ORFNames=J1803;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS OF SER-1972.
RC STRAIN=RC11-8D;
RX PubMed=8413204; DOI=10.1128/mcb.13.10.6012-6023.1993;
RA Cafferkey R., Young P.R., McLaughlin M.M., Bergsma D.J., Koltin Y.,
RA Sathe G.M., Faucette L., Eng W.-K., Johnson R.K., Livi G.P.;
RT "Dominant missense mutations in a novel yeast protein related to mammalian
RT phosphatidylinositol 3-kinase and VPS34 abrogate rapamycin cytotoxicity.";
RL Mol. Cell. Biol. 13:6012-6023(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=JK9-3D;
RX PubMed=8186460; DOI=10.1091/mbc.5.1.105;
RA Helliwell S.B., Wagner P., Kunz J., Deuter-Reinhard M., Henriquez R.,
RA Hall M.N.;
RT "TOR1 and TOR2 are structurally and functionally similar but not identical
RT phosphatidylinositol kinase homologues in yeast.";
RL Mol. Biol. Cell 5:105-118(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8840504;
RX DOI=10.1002/(sici)1097-0061(199607)12:9<869::aid-yea964>3.0.co;2-1;
RA Huang M.-E., Manus V., Chuat J.-C., Galibert F.;
RT "Analysis of a 62 kb DNA sequence of chromosome X reveals 36 open reading
RT frames and a gene cluster with a counterpart on chromosome XI.";
RL Yeast 12:869-875(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [6]
RP FUNCTION, MUTAGENESIS OF SER-1972; ARG-2276 AND ASP-2294, AND INTERACTION
RP WITH FPR1.
RX PubMed=7606777; DOI=10.1016/0092-8674(95)90058-6;
RA Zheng X.-F., Florentino D., Chen J., Crabtree G.R., Schreiber S.L.;
RT "TOR kinase domains are required for two distinct functions, only one of
RT which is inhibited by rapamycin.";
RL Cell 82:121-130(1995).
RN [7]
RP FUNCTION.
RX PubMed=8741837; DOI=10.1091/mbc.7.1.25;
RA Barbet N.C., Schneider U., Helliwell S.B., Stansfield I., Tuite M.F.,
RA Hall M.N.;
RT "TOR controls translation initiation and early G1 progression in yeast.";
RL Mol. Biol. Cell 7:25-42(1996).
RN [8]
RP FUNCTION.
RX PubMed=9843498; DOI=10.1093/emboj/17.23.6924;
RA Schmidt A., Beck T., Koller A., Kunz J., Hall M.N.;
RT "The TOR nutrient signalling pathway phosphorylates NPR1 and inhibits
RT turnover of the tryptophan permease.";
RL EMBO J. 17:6924-6931(1998).
RN [9]
RP FUNCTION.
RX PubMed=9539725; DOI=10.1073/pnas.95.8.4264;
RA Berset C., Trachsel H., Altmann M.;
RT "The TOR (target of rapamycin) signal transduction pathway regulates the
RT stability of translation initiation factor eIF4G in the yeast Saccharomyces
RT cerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:4264-4269(1998).
RN [10]
RP FUNCTION.
RX PubMed=10329624; DOI=10.1093/emboj/18.10.2782;
RA Jiang Y., Broach J.R.;
RT "Tor proteins and protein phosphatase 2A reciprocally regulate Tap42 in
RT controlling cell growth in yeast.";
RL EMBO J. 18:2782-2792(1999).
RN [11]
RP FUNCTION.
RX PubMed=10198052; DOI=10.1091/mbc.10.4.987;
RA Powers T., Walter P.;
RT "Regulation of ribosome biogenesis by the rapamycin-sensitive TOR-signaling
RT pathway in Saccharomyces cerevisiae.";
RL Mol. Biol. Cell 10:987-1000(1999).
RN [12]
RP CATALYTIC ACTIVITY, AND MUTAGENESIS OF ASP-2275.
RX PubMed=10436010; DOI=10.1091/mbc.10.8.2531;
RA Alarcon C.M., Heitman J., Cardenas M.E.;
RT "Protein kinase activity and identification of a toxic effector domain of
RT the target of rapamycin TOR proteins in yeast.";
RL Mol. Biol. Cell 10:2531-2546(1999).
RN [13]
RP FUNCTION.
RX PubMed=10604478; DOI=10.1038/45287;
RA Beck T., Hall M.N.;
RT "The TOR signalling pathway controls nuclear localization of nutrient-
RT regulated transcription factors.";
RL Nature 402:689-692(1999).
RN [14]
RP SUBCELLULAR LOCATION.
RX PubMed=10973982; DOI=10.1074/jbc.m007296200;
RA Kunz J., Schneider U., Howald I., Schmidt A., Hall M.N.;
RT "HEAT repeats mediate plasma membrane localization of Tor2p in yeast.";
RL J. Biol. Chem. 275:37011-37020(2000).
RN [15]
RP FUNCTION IN AUTOPHAGY.
RX PubMed=10995454; DOI=10.1083/jcb.150.6.1507;
RA Kamada Y., Funakoshi T., Shintani T., Nagano K., Ohsumi M., Ohsumi Y.;
RT "Tor-mediated induction of autophagy via an Apg1 protein kinase complex.";
RL J. Cell Biol. 150:1507-1513(2000).
RN [16]
RP FUNCTION.
RX PubMed=11741537; DOI=10.1016/s1097-2765(01)00386-0;
RA Jacinto E., Guo B., Arndt K.T., Schmelzle T., Hall M.N.;
RT "TIP41 interacts with TAP42 and negatively regulates the TOR signaling
RT pathway.";
RL Mol. Cell 8:1017-1026(2001).
RN [17]
RP SUBUNIT.
RX PubMed=12408816; DOI=10.1016/s1097-2765(02)00636-6;
RA Loewith R., Jacinto E., Wullschleger S., Lorberg A., Crespo J.L.,
RA Bonenfant D., Oppliger W., Jenoe P., Hall M.N.;
RT "Two TOR complexes, only one of which is rapamycin sensitive, have distinct
RT roles in cell growth control.";
RL Mol. Cell 10:457-468(2002).
RN [18]
RP SUBCELLULAR LOCATION, SUBUNIT, AND INTERACTION WITH KOG1 AND LST8.
RX PubMed=12631735; DOI=10.1091/mbc.e02-09-0609;
RA Wedaman K.P., Reinke A., Anderson S., Yates J.R. III, McCaffery J.M.,
RA Powers T.;
RT "Tor kinases are in distinct membrane-associated protein complexes in
RT Saccharomyces cerevisiae.";
RL Mol. Biol. Cell 14:1204-1220(2003).
RN [19]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [20]
RP FUNCTION.
RX PubMed=15620355; DOI=10.1016/j.cell.2004.11.047;
RA Martin D.E., Soulard A., Hall M.N.;
RT "TOR regulates ribosomal protein gene expression via PKA and the forkhead
RT transcription factor FHL1.";
RL Cell 119:969-979(2004).
RN [21]
RP FUNCTION.
RX PubMed=17560372; DOI=10.1016/j.molcel.2007.04.020;
RA Urban J., Soulard A., Huber A., Lippman S., Mukhopadhyay D., Deloche O.,
RA Wanke V., Anrather D., Ammerer G., Riezman H., Broach J.R., De Virgilio C.,
RA Hall M.N., Loewith R.;
RT "Sch9 is a major target of TORC1 in Saccharomyces cerevisiae.";
RL Mol. Cell 26:663-674(2007).
RN [22]
RP FUNCTION.
RX PubMed=25767889; DOI=10.1371/journal.pone.0120250;
RA Gonzalez A., Shimobayashi M., Eisenberg T., Merle D.A., Pendl T.,
RA Hall M.N., Moustafa T.;
RT "TORC1 promotes phosphorylation of ribosomal protein S6 via the AGC kinase
RT Ypk3 in Saccharomyces cerevisiae.";
RL PLoS ONE 10:E0120250-E0120250(2015).
RN [23]
RP ACTIVITY REGULATION, INTERACTION WITH PIB2, AND SUBCELLULAR LOCATION.
RX PubMed=28483912; DOI=10.1128/mcb.00075-17;
RA Tanigawa M., Maeda T.;
RT "An In Vitro TORC1 Kinase Assay That Recapitulates the Gtr-Independent
RT Glutamine-Responsive TORC1 Activation Mechanism on Yeast Vacuoles.";
RL Mol. Cell. Biol. 37:e00075-e00075(2017).
RN [24]
RP ACTIVITY REGULATION, INTERACTION WITH PIB2, SUBCELLULAR LOCATION, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=29698392; DOI=10.1371/journal.pgen.1007334;
RA Ukai H., Araki Y., Kira S., Oikawa Y., May A.I., Noda T.;
RT "Gtr/Ego-independent TORC1 activation is achieved through a glutamine-
RT sensitive interaction with Pib2 on the vacuolar membrane.";
RL PLoS Genet. 14:e1007334-e1007334(2018).
RN [25]
RP SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF TRP-2176.
RX PubMed=32801125; DOI=10.1242/jcs.245555;
RA Uemura S., Mochizuki T., Amemiya K., Kurosaka G., Yazawa M., Nakamoto K.,
RA Ishikawa Y., Izawa S., Abe F.;
RT "Amino acid homeostatic control by TORC1 in Saccharomyces cerevisiae under
RT high hydrostatic pressure.";
RL J. Cell Sci. 133:jcs245555-jcs245555(2020).
RN [26]
RP ACTIVITY REGULATION, CATALYTIC ACTIVITY, AND INTERACTION WITH PIB2.
RX PubMed=34535752; DOI=10.1038/s42003-021-02625-w;
RA Tanigawa M., Yamamoto K., Nagatoishi S., Nagata K., Noshiro D., Noda N.N.,
RA Tsumoto K., Maeda T.;
RT "A glutamine sensor that directly activates TORC1.";
RL Commun. Biol. 4:1093-1093(2021).
RN [27]
RP STRUCTURE BY NMR OF 2438-2470.
RX PubMed=15772072; DOI=10.1074/jbc.m501116200;
RA Dames S.A., Mulet J.M., Rathgeb-Szabo K., Hall M.N., Grzesiek S.;
RT "The solution structure of the FATC domain of the protein kinase target of
RT rapamycin suggests a role for redox-dependent structural and cellular
RT stability.";
RL J. Biol. Chem. 280:20558-20564(2005).
CC -!- FUNCTION: Phosphatidylinositol 3-kinase homolog, component of TORC1,
CC which regulates multiple cellular processes to control cell growth in
CC response to environmental signals. Nutrient limitation and
CC environmental stress signals cause inactivation of TORC1. Active TORC1
CC positively controls ribosome biogenesis via control of rRNA, ribosomal
CC protein and tRNA gene expression, and rRNA processing. TORC1 positively
CC controls protein biosynthesis by regulation of mRNA stability,
CC translation initiation factor activity, and high-affinity amino acid
CC permeases that serve to provide amino acids for use by the translation
CC machinery. TORC1 also promotes growth by sequestering a number of
CC nutrient and general stress-responsive transcription factors in the
CC cytoplasm. TORC1 negatively controls macroautophagy, a process to
CC recycle surplus cytoplasmic mass under nutrient starvation conditions.
CC TORC1 controls many of these processes via TIP41-TAP42-mediated
CC inhibition of the type 2A-related phosphatases PP2A and SIT4
CC (PubMed:10198052, PubMed:10329624, PubMed:10604478, PubMed:10995454,
CC PubMed:11741537, PubMed:15620355, PubMed:7606777, PubMed:8741837,
CC PubMed:9539725, PubMed:9843498). In nutrient-rich conditions,
CC responsible for the phosphorylation of AGC S6 kinase (S6K) YPK3,
CC activating YPK3 kinase activity and promoting phosphorylation of
CC ribosomal protein S6 (PubMed:25767889). Phosphorylates kinase SCH9 at 6
CC amino acids in the C-terminus, activating SCH9 kinase activity to
CC properly regulate ribosome biogenesis, translation initiation, and
CC entry into stationary phase (PubMed:17560372).
CC {ECO:0000269|PubMed:10198052, ECO:0000269|PubMed:10329624,
CC ECO:0000269|PubMed:10604478, ECO:0000269|PubMed:10995454,
CC ECO:0000269|PubMed:11741537, ECO:0000269|PubMed:15620355,
CC ECO:0000269|PubMed:17560372, ECO:0000269|PubMed:25767889,
CC ECO:0000269|PubMed:7606777, ECO:0000269|PubMed:8741837,
CC ECO:0000269|PubMed:9539725, ECO:0000269|PubMed:9843498}.
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:0000269|PubMed:10436010};
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:0000269|PubMed:10436010,
CC ECO:0000305|PubMed:34535752};
CC -!- ACTIVITY REGULATION: Activated by the glutamine sensor PIB2 in
CC nutrient-rich conditions. {ECO:0000269|PubMed:28483912,
CC ECO:0000269|PubMed:29698392, ECO:0000269|PubMed:34535752}.
CC -!- SUBUNIT: The target of rapamycin complex 1 (TORC1) is composed of at
CC least KOG1, LST8, TCO89 and either TOR1 (TORC1-A) or TOR2 (TORC1-B)
CC (PubMed:12408816, PubMed:12631735). Interacts with PIB2; following
CC activation of PIB2 by glutamine or cysteine (PubMed:34535752,
CC PubMed:29698392, PubMed:28483912). TORC1 binds to and is inhibited by
CC FKBP-rapamycin (PubMed:12408816, PubMed:7606777).
CC {ECO:0000269|PubMed:12408816, ECO:0000269|PubMed:12631735,
CC ECO:0000269|PubMed:28483912, ECO:0000269|PubMed:29698392,
CC ECO:0000269|PubMed:34535752, ECO:0000269|PubMed:7606777}.
CC -!- INTERACTION:
CC P35169; P53233: FMP48; NbExp=3; IntAct=EBI-19374, EBI-9664;
CC P35169; P20081: FPR1; NbExp=4; IntAct=EBI-19374, EBI-6961;
CC P35169; P38873: KOG1; NbExp=7; IntAct=EBI-19374, EBI-24864;
CC P35169; P38691: KSP1; NbExp=2; IntAct=EBI-19374, EBI-9937;
CC P35169; P41318: LST8; NbExp=5; IntAct=EBI-19374, EBI-28598;
CC P35169; P34072: MKS1; NbExp=3; IntAct=EBI-19374, EBI-10978;
CC P35169; P36003: NNK1; NbExp=3; IntAct=EBI-19374, EBI-9796;
CC P35169; P22211: NPR1; NbExp=2; IntAct=EBI-19374, EBI-12207;
CC P35169; Q03656: SKY1; NbExp=2; IntAct=EBI-19374, EBI-9800;
CC P35169; Q08921: TCO89; NbExp=4; IntAct=EBI-19374, EBI-37395;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10973982,
CC ECO:0000269|PubMed:12631735}; Peripheral membrane protein
CC {ECO:0000269|PubMed:10973982, ECO:0000269|PubMed:12631735}; Cytoplasmic
CC side {ECO:0000269|PubMed:10973982, ECO:0000269|PubMed:12631735}.
CC Vacuole membrane {ECO:0000269|PubMed:12631735,
CC ECO:0000269|PubMed:28483912, ECO:0000269|PubMed:29698392,
CC ECO:0000269|PubMed:32801125}; Peripheral membrane protein
CC {ECO:0000269|PubMed:12631735}; Cytoplasmic side
CC {ECO:0000269|PubMed:12631735}. Note=Also localizes to membranous
CC structures both proximal to, yet distinct from, the plasma membrane as
CC well as within the cell interior, probably endosomal or Golgi membranes
CC (PubMed:10973982). Localization to the vacuolar membrane is dependent
CC upon PIB2 and GTR1 (PubMed:29698392). {ECO:0000269|PubMed:10973982,
CC ECO:0000269|PubMed:29698392}.
CC -!- DISRUPTION PHENOTYPE: Increases cellular levels of glutamine and
CC alanine during high hydrostatic pressure (mechanical stress)
CC (PubMed:32801125). Sensitive to high hydrostatic pressure (mechanical
CC stress) (PubMed:32801125). {ECO:0000269|PubMed:32801125}.
CC -!- MISCELLANEOUS: It may act on another substrate or phosphorylate a
CC different position in the phosphatidylinositol ring.
CC -!- MISCELLANEOUS: Present with 589 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 is the initiator. {ECO:0000305}.
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DR EMBL; L19540; AAB66881.1; -; Genomic_DNA.
DR EMBL; X74857; CAA52849.1; -; Genomic_DNA.
DR EMBL; Z49566; CAA89594.1; -; Genomic_DNA.
DR EMBL; L47993; AAB39292.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08853.1; -; Genomic_DNA.
DR PIR; S57085; S57085.
DR RefSeq; NP_012600.1; NM_001181724.1.
DR PDB; 1W1N; NMR; -; A=2438-2470.
DR PDB; 2KIO; NMR; -; A=2438-2470.
DR PDB; 2KIT; NMR; -; A=2438-2470.
DR PDBsum; 1W1N; -.
DR PDBsum; 2KIO; -.
DR PDBsum; 2KIT; -.
DR AlphaFoldDB; P35169; -.
DR BMRB; P35169; -.
DR PCDDB; P35169; -.
DR SMR; P35169; -.
DR BioGRID; 33823; 462.
DR ComplexPortal; CPX-1715; TORC1 serine/threonine-protein kinase complex, TOR1 variant.
DR DIP; DIP-917N; -.
DR IntAct; P35169; 37.
DR MINT; P35169; -.
DR STRING; 4932.YJR066W; -.
DR iPTMnet; P35169; -.
DR MaxQB; P35169; -.
DR PaxDb; P35169; -.
DR PRIDE; P35169; -.
DR EnsemblFungi; YJR066W_mRNA; YJR066W; YJR066W.
DR GeneID; 853529; -.
DR KEGG; sce:YJR066W; -.
DR SGD; S000003827; TOR1.
DR VEuPathDB; FungiDB:YJR066W; -.
DR eggNOG; KOG0891; Eukaryota.
DR GeneTree; ENSGT00940000174195; -.
DR HOGENOM; CLU_000178_7_1_1; -.
DR InParanoid; P35169; -.
DR OMA; FSGRVVH; -.
DR BioCyc; YEAST:G3O-31699-MON; -.
DR BRENDA; 2.7.1.137; 984.
DR EvolutionaryTrace; P35169; -.
DR PRO; PR:P35169; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P35169; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0010008; C:endosome membrane; IDA:SGD.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IDA:SGD.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IDA:SGD.
DR GO; GO:0000139; C:Golgi membrane; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0031931; C:TORC1 complex; IPI:SGD.
DR GO; GO:0031932; C:TORC2 complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IMP:SGD.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:SGD.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:InterPro.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:SGD.
DR GO; GO:0034605; P:cellular response to heat; IGI:SGD.
DR GO; GO:0034599; P:cellular response to oxidative stress; IGI:SGD.
DR GO; GO:0031505; P:fungal-type cell wall organization; IMP:SGD.
DR GO; GO:0051321; P:meiotic cell cycle; IMP:SGD.
DR GO; GO:0031930; P:mitochondria-nucleus signaling pathway; IMP:SGD.
DR GO; GO:0010507; P:negative regulation of autophagy; IGI:SGD.
DR GO; GO:0016242; P:negative regulation of macroautophagy; IBA:GO_Central.
DR GO; GO:0044387; P:negative regulation of protein kinase activity by regulation of protein phosphorylation; IMP:SGD.
DR GO; GO:0042790; P:nucleolar large rRNA transcription by RNA polymerase I; IMP:SGD.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:SGD.
DR GO; GO:0006468; P:protein phosphorylation; IDA:CACAO.
DR GO; GO:0051726; P:regulation of cell cycle; IMP:SGD.
DR GO; GO:0001558; P:regulation of cell growth; IMP:SGD.
DR GO; GO:1905356; P:regulation of snRNA pseudouridine synthesis; IGI:SGD.
DR GO; GO:0090153; P:regulation of sphingolipid biosynthetic process; IMP:SGD.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IMP:SGD.
DR GO; GO:0007584; P:response to nutrient; IC:ComplexPortal.
DR GO; GO:0042254; P:ribosome biogenesis; IMP:SGD.
DR GO; GO:0031929; P:TOR signaling; IMP:SGD.
DR GO; GO:0006413; P:translational initiation; IMP:SGD.
DR Gene3D; 1.10.1070.11; -; 1.
DR Gene3D; 1.20.120.150; -; 1.
DR Gene3D; 1.25.10.10; -; 4.
DR IDEAL; IID50246; -.
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 PANTHER; PTHR11139:SF9; PTHR11139:SF9; 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 3D-structure; ATP-binding; Cell cycle; Cell membrane; Kinase; Membrane;
KW Nucleotide-binding; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Transferase; Vacuole.
FT CHAIN 1..2470
FT /note="Serine/threonine-protein kinase TOR1"
FT /id="PRO_0000088813"
FT REPEAT 114..151
FT /note="HEAT 1"
FT /evidence="ECO:0000255"
FT REPEAT 248..286
FT /note="HEAT 2"
FT /evidence="ECO:0000255"
FT REPEAT 627..664
FT /note="HEAT 3"
FT /evidence="ECO:0000255"
FT REPEAT 663..701
FT /note="HEAT 4"
FT /evidence="ECO:0000255"
FT REPEAT 746..784
FT /note="HEAT 5"
FT /evidence="ECO:0000255"
FT REPEAT 787..826
FT /note="HEAT 6"
FT /evidence="ECO:0000255"
FT REPEAT 829..870
FT /note="HEAT 7"
FT /evidence="ECO:0000255"
FT REPEAT 907..946
FT /note="HEAT 8"
FT /evidence="ECO:0000255"
FT REPEAT 949..987
FT /note="HEAT 9"
FT /evidence="ECO:0000255"
FT REPEAT 1108..1147
FT /note="HEAT 10"
FT /evidence="ECO:0000255"
FT DOMAIN 1331..1919
FT /note="FAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00534"
FT REPEAT 1869..1907
FT /note="HEAT 11"
FT /evidence="ECO:0000255"
FT DOMAIN 2093..2408
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT DOMAIN 2438..2470
FT /note="FATC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00535"
FT REGION 1775..2157
FT /note="Interaction with FKBP-rapamycin"
FT /evidence="ECO:0000269|PubMed:7606777"
FT REGION 2099..2105
FT /note="G-loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 2272..2280
FT /note="Catalytic loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 2292..2317
FT /note="Activation loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT MUTAGEN 1972
FT /note="S->A: No effect."
FT /evidence="ECO:0000269|PubMed:7606777,
FT ECO:0000269|PubMed:8413204"
FT MUTAGEN 1972
FT /note="S->E,I: Confers resistance to rapamycin. Abolishes
FT interaction with FKBP-rapamycin."
FT /evidence="ECO:0000269|PubMed:7606777,
FT ECO:0000269|PubMed:8413204"
FT MUTAGEN 1972
FT /note="S->N: In DRR1-27; confers resistance to rapamycin."
FT /evidence="ECO:0000269|PubMed:7606777,
FT ECO:0000269|PubMed:8413204"
FT MUTAGEN 1972
FT /note="S->R: In DRR1-1; confers resistance to rapamycin.
FT Abolishes interaction with FKBP-rapamycin."
FT /evidence="ECO:0000269|PubMed:7606777,
FT ECO:0000269|PubMed:8413204"
FT MUTAGEN 2176
FT /note="W->R: Sensitive to high hydrostatic pressure
FT (mechanical stress)."
FT /evidence="ECO:0000269|PubMed:32801125"
FT MUTAGEN 2275
FT /note="D->A: Abolishes protein kinase activity."
FT /evidence="ECO:0000269|PubMed:10436010"
FT MUTAGEN 2276
FT /note="R->P: Abolishes rapamycin-resistance of mutants E-
FT 1972; I-1972 and R-1972."
FT /evidence="ECO:0000269|PubMed:7606777"
FT MUTAGEN 2294
FT /note="D->E: Abolishes rapamycin-resistance of mutants E-
FT 1972; I-1972 and R-1972."
FT /evidence="ECO:0000269|PubMed:7606777"
FT CONFLICT 58
FT /note="D -> G (in Ref. 1; AAB66881)"
FT /evidence="ECO:0000305"
FT CONFLICT 115
FT /note="V -> I (in Ref. 1; AAB66881)"
FT /evidence="ECO:0000305"
FT CONFLICT 133
FT /note="S -> N (in Ref. 1; AAB66881)"
FT /evidence="ECO:0000305"
FT CONFLICT 231
FT /note="A -> R (in Ref. 2; CAA52849)"
FT /evidence="ECO:0000305"
FT CONFLICT 396
FT /note="N -> K (in Ref. 1; AAB66881 and 2; CAA52849)"
FT /evidence="ECO:0000305"
FT CONFLICT 547
FT /note="N -> S (in Ref. 1; AAB66881 and 2; CAA52849)"
FT /evidence="ECO:0000305"
FT CONFLICT 675
FT /note="T -> I (in Ref. 2; CAA52849)"
FT /evidence="ECO:0000305"
FT CONFLICT 1292
FT /note="G -> E (in Ref. 2; CAA52849)"
FT /evidence="ECO:0000305"
FT CONFLICT 1436
FT /note="G -> A (in Ref. 2; CAA52849)"
FT /evidence="ECO:0000305"
FT CONFLICT 1468
FT /note="A -> R (in Ref. 1; AAB66881 and 2; CAA52849)"
FT /evidence="ECO:0000305"
FT CONFLICT 1469..1471
FT /note="WGL -> GGS (in Ref. 2; CAA52849)"
FT /evidence="ECO:0000305"
FT CONFLICT 1478..1479
FT /note="EQ -> DE (in Ref. 2; CAA52849)"
FT /evidence="ECO:0000305"
FT CONFLICT 1590
FT /note="V -> I (in Ref. 2; CAA52849)"
FT /evidence="ECO:0000305"
FT CONFLICT 1632..1642
FT /note="NDPSLPNTFKA -> TILVYQIRSKP (in Ref. 2; CAA52849)"
FT /evidence="ECO:0000305"
FT CONFLICT 1640
FT /note="F -> V (in Ref. 1; AAB66881)"
FT /evidence="ECO:0000305"
FT CONFLICT 1844
FT /note="L -> S (in Ref. 2; CAA52849)"
FT /evidence="ECO:0000305"
FT CONFLICT 2202
FT /note="H -> Q (in Ref. 1; AAB66881)"
FT /evidence="ECO:0000305"
FT CONFLICT 2414
FT /note="K -> R (in Ref. 1; AAB66881 and 2; CAA52849)"
FT /evidence="ECO:0000305"
FT HELIX 2444..2460
FT /evidence="ECO:0007829|PDB:1W1N"
SQ SEQUENCE 2470 AA; 281140 MW; ACB1781B9963BB1E CRC64;
MEPHEEQIWK SKLLKAANND MDMDRNVPLA PNLNVNMNMK MNASRNGDEF GLTSSRFDGV
VIGSNGDVNF KPILEKIFRE LTSDYKEERK LASISLFDLL VSLEHELSIE EFQAVSNDIN
NKILELVHTK KTSTRVGAVL SIDTLISFYA YTERLPNETS RLAGYLRGLI PSNDVEVMRL
AAKTLGKLAV PGGTYTSDFV EFEIKSCLEW LTASTEKNSF SSSKPDHAKH AALLIITALA
ENCPYLLYQY LNSILDNIWR ALRDPHLVIR IDASITLAKC LSTLRNRDPQ LTSQWVQRLA
TSCEYGFQVN TLECIHASLL VYKEILFLKD PFLNQVFDQM CLNCIAYENH KAKMIREKIY
QIVPLLASFN PQLFAGKYLH QIMDNYLEIL TNAPANKIPH LKDDKPQILI SIGDIAYEVG
PDIAPYVKQI LDYIEHDLQT KFKFRKKFEN EIFYCIGRLA VPLGPVLGKL LNRNILDLMF
KCPLSDYMQE TFQILTERIP SLGPKINDEL LNLVCSTLSG TPFIQPGSPM EIPSFSRERA
REWRNKNILQ KTGESNDDNN DIKIIIQAFR MLKNIKSRFS LVEFVRIVAL SYIEHTDPRV
RKLAALTSCE IYVKDNICKQ TSLHSLNTVS EVLSKLLAIT IADPLQDIRL EVLKNLNPCF
DPQLAQPDNL RLLFTALHDE SFNIQSVAME LVGRLSSVNP AYVIPSIRKI LLELLTKLKF
STSSREKEET ASLLCTLIRS SKDVAKPYIE PLLNVLLPKF QDTSSTVAST ALRTIGELSV
VGGEDMKIYL KDLFPLIIKT FQDQSNSFKR EAALKALGQL AASSGYVIDP LLDYPELLGI
LVNILKTENS QNIRRQTVTL IGILGAIDPY RQKEREVTST TDISTEQNAP PIDIALLMQG
MSPSNDEYYT TVVIHCLLKI LKDPSLSSYH TAVIQAIMHI FQTLGLKCVS FLDQIIPTIL
DVMRTCSQSL LEFYFQQLCS LIIIVRQHIR PHVDSIFQAI KDFSSVAKLQ ITLVSVIEAI
SKALEGEFKR LVPLTLTLFL VILENDKSSD KVLSRRVLRL LESFGPNLEG YSHLITPKIV
QMAEFTSGNL QRSAIITIGK LAKDVDLFEM SSRIVHSLLR VLSSTTSDEL SKVIMNTLSL
LLIQMGTSFA IFIPVINEVL MKKHIQHTIY DDLTNRILNN DVLPTKILEA NTTDYKPAEQ
MEAADAGVAK LPINQSVLKS AWNSSQQRTK EDWQEWSKRL SIQLLKESPS HALRACSNLA
SMYYPLAKEL FNTAFACVWT ELYSQYQEDL IGSLCIALSS PLNPPEIHQT LLNLVEFMEH
DDKALPIPTQ SLGEYAERCH AYAKALHYKE IKFIKEPENS TIESLISINN QLNQTDAAIG
ILKHAQQHHS LQLKETWFEK LERWEDALHA YNEREKAGDT SVSVTLGKMR SLHALGEWEQ
LSQLAARKWK VSKLQTKKLI APLAAGAAWG LGEWDMLEQY ISVMKPKSPD KEFFDAILYL
HKNDYDNASK HILNARDLLV TEISALINES YNRAYSVIVR TQIITEFEEI IKYKQLPPNS
EKKLHYQNLW TKRLLGCQKN VDLWQRVLRV RSLVIKPKQD LQIWIKFANL CRKSGRMRLA
NKALNMLLEG GNDPSLPNTF KAPPPVVYAQ LKYIWATGAY KEALNHLIGF TSRLAHDLGL
DPNNMIAQSV KLSSASTAPY VEEYTKLLAR CFLKQGEWRI ATQPNWRNTN PDAILGSYLL
ATHFDKNWYK AWHNWALANF EVISMVQEET KLNGGKNDDD DDTAVNNDNV RIDGSILGSG
SLTINGNRYP LELIQRHVVP AIKGFFHSIS LLETSCLQDT LRLLTLLFNF GGIKEVSQAM
YEGFNLMKIE NWLEVLPQLI SRIHQPDPTV SNSLLSLLSD LGKAHPQALV YPLTVAIKSE
SVSRQKAALS IIEKIRIHSP VLVNQAELVS HELIRVAVLW HELWYEGLED ASRQFFVEHN
IEKMFSTLEP LHKHLGNEPQ TLSEVSFQKS FGRDLNDAYE WLNNYKKSKD INNLNQAWDI
YYNVFRKITR QIPQLQTLDL QHVSPQLLAT HDLELAVPGT YFPGKPTIRI AKFEPLFSVI
SSKQRPRKFS IKGSDGKDYK YVLKGHEDIR QDSLVMQLFG LVNTLLKNDS ECFKRHLDIQ
QYPAIPLSPK SGLLGWVPNS DTFHVLIREH RDAKKIPLNI EHWVMLQMAP DYENLTLLQK
IEVFTYALDN TKGQDLYKIL WLKSRSSETW LERRTTYTRS LAVMSMTGYI LGLGDRHPSN
LMLDRITGKV IHIDFGDCFE AAILREKYPE KVPFRLTRML TYAMEVSGIE GSFRITCENV
MRVLRDNKES LMAILEAFAL DPLIHWGFDL PPQKLTEQTG IPLPLINPSE LLRKGAITVE
EAANMEAEQQ NETKNARAML VLRRITDKLT GNDIKRFNEL DVPEQVDKLI QQATSIERLC
QHYIGWCPFW
