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 02-SEP-2026, entry version 229. 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%3c869::aid-yea964%3e3.0.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] {ECO:0000305} RP ACTIVITY REGULATION, AND SUBCELLULAR LOCATION. RC STRAIN=ATCC 200060 / W303 {ECO:0000303|PubMed:28993463}; RX PubMed=28993463; DOI=10.1242/jcs.207910; RA Varlakhanova N.V., Mihalevic M.J., Bernstein K.A., Ford M.G.J.; RT "Pib2 and the EGO complex are both required for activation of TORC1."; RL J. Cell Sci. 130:3878-3890(2017). RN [24] 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 [25] 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 [26] 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 [27] 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 [28] RP FUNCTION. RX PubMed=36691768; DOI=10.15252/embj.2022112344; RA Shetty S., Hofstetter J., Battaglioni S., Ritz D., Hall M.N.; RT "TORC1 phosphorylates and inhibits the ribosome preservation factor Stm1 to RT activate dormant ribosomes."; RL EMBO J. 42:e112344-e112344(2023). RN [29] 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:28993463, PubMed:7606777, CC PubMed:8741837, PubMed:9539725, PubMed:9843498). In nutrient-rich CC conditions, responsible for the phosphorylation of AGC S6 kinase (S6K) CC YPK3, 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). Activates dormant CC ribosomes by mediating phosphorylation of STM1, leading to STM1 CC inactivation and reactivation of translation (PubMed:36691768). 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:28993463, ECO:0000269|PubMed:36691768, CC ECO:0000269|PubMed:7606777, ECO:0000269|PubMed:8741837, CC ECO:0000269|PubMed:9539725, ECO:0000269|PubMed:9843498}. CC -!- CATALYTIC ACTIVITY: CC Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + CC H(+); 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=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + CC ADP + H(+); Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA- CC COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; CC Evidence={ECO:0000269|PubMed:10436010, 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:28993463, ECO:0000269|PubMed:29698392, CC 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:28483912, CC PubMed:29698392, PubMed:34535752). 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:28993463, CC ECO:0000269|PubMed:29698392, ECO:0000269|PubMed:32801125}; Peripheral CC membrane protein {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:28993463, PubMed:29698392). CC {ECO:0000269|PubMed:10973982, ECO:0000269|PubMed:28993463, 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; 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 AlphaFoldDB; P35169; -. DR BMRB; P35169; -. DR PCDDB; P35169; -. DR SMR; P35169; -. DR BioGRID; 33823; 506. DR ComplexPortal; CPX-1715; TORC1 serine/threonine-protein kinase complex, TOR1 variant. DR DIP; DIP-917N; -. DR FunCoup; P35169; 1239. DR IntAct; P35169; 40. DR MINT; P35169; -. DR STRING; 4932.YJR066W; -. DR GlyGen; P35169; 1 site. DR iPTMnet; P35169; -. DR PaxDb; 4932-YJR066W; -. DR PeptideAtlas; P35169; -. DR EnsemblFungi; YJR066W_mRNA; YJR066W; YJR066W. DR GeneID; 853529; -. DR KEGG; sce:YJR066W; -. DR AGR; SGD:S000003827; -. DR SGD; S000003827; TOR1. DR VEuPathDB; FungiDB:YJR066W; -. DR eggNOG; KOG0891; Eukaryota. DR HOGENOM; CLU_000178_7_1_1; -. DR InParanoid; P35169; -. DR OMA; MWLRFVS; -. DR OrthoDB; 381190at2759; -. DR BioCyc; YEAST:G3O-31699-MONOMER; -. DR BRENDA; 2.7.1.137; 984. DR BioGRID-ORCS; 853529; 2 hits in 13 CRISPR screens. 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: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:0038201; C:TOR complex; IBA:GO_Central. DR GO; GO:0031931; C:TORC1 complex; IPI:SGD. DR GO; GO:0005774; C:vacuolar membrane; EXP:UniProtKB. DR GO; GO:0004672; F:protein kinase activity; IMP:SGD. DR GO; GO:0106310; F:protein serine kinase activity; EXP:UniProtKB. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB. DR GO; GO:0044877; F:protein-containing complex binding; IEA:InterPro. DR GO; GO:0034605; P:cellular response to heat; IGI:SGD. DR GO; GO:0006995; P:cellular response to nitrogen starvation; IGI:SGD. DR GO; GO:0034599; P:cellular response to oxidative stress; IGI:SGD. DR GO; GO:0006974; P:DNA damage response; IMP: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: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:0051726; P:regulation of cell cycle; IMP:SGD. DR GO; GO:0001558; P:regulation of cell growth; NAS:ComplexPortal. 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; NAS:ComplexPortal. DR GO; GO:0042254; P:ribosome biogenesis; IMP:SGD. DR GO; GO:0031929; P:TOR signaling; IMP:SGD. DR GO; GO:0038202; P:TORC1 signaling; IBA:GO_Central. DR GO; GO:0038203; P:TORC2 signaling; IBA:GO_Central. DR GO; GO:0006413; P:translational initiation; IMP:SGD. DR CDD; cd05169; PIKKc_TOR; 1. DR FunFam; 1.10.1070.11:FF:000020; Serine/threonine-protein kinase TOR; 1. DR FunFam; 1.20.120.150:FF:000001; Serine/threonine-protein kinase TOR; 1. DR FunFam; 1.25.10.10:FF:000371; Serine/threonine-protein kinase TOR; 1. DR FunFam; 1.25.10.10:FF:000601; Serine/threonine-protein kinase TOR; 1. DR FunFam; 1.25.10.10:FF:000786; Serine/threonine-protein kinase TOR; 1. DR FunFam; 3.30.1010.10:FF:000006; Serine/threonine-protein kinase TOR; 1. DR Gene3D; 1.20.120.150; FKBP12-rapamycin binding domain; 1. DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 4. DR Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic domain; 1. DR IDEAL; IID50246; -. DR InterPro; IPR011989; ARM-like. DR InterPro; IPR016024; ARM-type_fold. DR InterPro; IPR050517; DDR_Repair_Kinase. DR InterPro; IPR003152; FATC_dom. DR InterPro; IPR009076; FRB_dom. DR InterPro; IPR036738; FRB_sf. DR InterPro; IPR057564; HEAT_ATR. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR024585; mTOR_dom. 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_cat. DR PANTHER; PTHR11139; ATAXIA TELANGIECTASIA MUTATED ATM -RELATED; 1. DR PANTHER; PTHR11139:SF9; SERINE_THREONINE-PROTEIN KINASE MTOR; 1. DR Pfam; PF02259; FAT; 1. DR Pfam; PF02260; FATC; 1. DR Pfam; PF08771; FRB_dom; 1. DR Pfam; PF23593; HEAT_ATR; 1. DR Pfam; PF11865; mTOR_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 SMART; SM01345; Rapamycin_bind; 1. DR SUPFAM; SSF48371; ARM repeat; 2. DR SUPFAM; SSF47212; FKBP12-rapamycin-binding domain of FKBP-rapamycin-associated protein (FRAP); 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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. DR PDBsum; 1W1N; -. DR PDBsum; 2KIO; -. DR PDBsum; 2KIT; -. 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 FT E-1972; I-1972 and R-1972." FT /evidence="ECO:0000269|PubMed:7606777" FT MUTAGEN 2294 FT /note="D->E: Abolishes rapamycin-resistance of mutants FT E-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 //