TOR2_YEAST
ID TOR2_YEAST Reviewed; 2474 AA.
AC P32600; D6VX00;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=Serine/threonine-protein kinase TOR2;
DE EC=2.7.1.67;
DE EC=2.7.11.1;
DE AltName: Full=Dominant rapamycin resistance protein 2;
DE AltName: Full=Phosphatidylinositol 4-kinase TOR2;
DE Short=PI4-kinase TOR2;
DE Short=PI4K TOR2;
DE Short=PtdIns-4-kinase TOR2;
DE AltName: Full=Target of rapamycin kinase 2;
DE AltName: Full=Temperature-sensitive CSG2 suppressor protein 14;
GN Name=TOR2; Synonyms=DRR2, TSC14; OrderedLocusNames=YKL203C;
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].
RC STRAIN=JK9-3D;
RX PubMed=8387896; DOI=10.1016/0092-8674(93)90144-f;
RA Kunz J., Henriquez R., Schneider U., Deuter-Reinhard M., Movva N.,
RA Hall M.N.;
RT "Target of rapamycin in yeast, TOR2, is an essential phosphatidylinositol
RT kinase homolog required for G1 progression.";
RL Cell 73:585-596(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
RN [3]
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 [4]
RP FUNCTION.
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 [5]
RP FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-1975 AND ASP-2279, AND
RP CATALYTIC ACTIVITY.
RX PubMed=8846782; DOI=10.1002/j.1460-2075.1995.tb00277.x;
RA Cardenas M.E., Heitman J.;
RT "FKBP12-rapamycin target TOR2 is a vacuolar protein with an associated
RT phosphatidylinositol-4 kinase activity.";
RL EMBO J. 14:5892-5907(1995).
RN [6]
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 [7]
RP FUNCTION.
RX PubMed=8943012; DOI=10.1073/pnas.93.24.13780;
RA Schmidt A., Kunz J., Hall M.N.;
RT "TOR2 is required for organization of the actin cytoskeleton in yeast.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:13780-13785(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 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 [13]
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 [14]
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 [15]
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 [16]
RP SUBCELLULAR LOCATION, SUBUNIT, AND INTERACTION WITH 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 [17]
RP FUNCTION IN RECEPTOR ENDOCYTOSIS, AND MUTAGENESIS OF GLY-2129.
RX PubMed=14593073; DOI=10.1091/mbc.e03-05-0323;
RA deHart A.K.A., Schnell J.D., Allen D.A., Tsai J.-Y., Hicke L.;
RT "Receptor internalization in yeast requires the Tor2-Rho1 signaling
RT pathway.";
RL Mol. Biol. Cell 14:4676-4684(2003).
RN [18]
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 [19]
RP FUNCTION, AND PHOSPHORYLATION OF SLM1-SLM2.
RX PubMed=15372071; DOI=10.1038/sj.emboj.7600384;
RA Audhya A., Loewith R., Parsons A.B., Gao L., Tabuchi M., Zhou H., Boone C.,
RA Hall M.N., Emr S.D.;
RT "Genome-wide lethality screen identifies new PI4,5P2 effectors that
RT regulate the actin cytoskeleton.";
RL EMBO J. 23:3747-3757(2004).
RN [20]
RP SUBUNIT, AND INTERACTION WITH LST8 AND TSC11.
RX PubMed=16002396; DOI=10.1074/jbc.m505553200;
RA Wullschleger S., Loewith R., Oppliger W., Hall M.N.;
RT "Molecular organization of target of rapamycin complex 2.";
RL J. Biol. Chem. 280:30697-30704(2005).
RN [21]
RP INTERACTION WITH SLM1 AND SLM2.
RX PubMed=15689497; DOI=10.1091/mbc.e04-07-0564;
RA Fadri M., Daquinag A., Wang S., Xue T., Kunz J.;
RT "The pleckstrin homology domain proteins Slm1 and Slm2 are required for
RT actin cytoskeleton organization in yeast and bind phosphatidylinositol-4,5-
RT bisphosphate and TORC2.";
RL Mol. Biol. Cell 16:1883-1900(2005).
RN [22]
RP FUNCTION, PHOSPHORYLATION OF YPK2, AND MUTAGENESIS OF ASP-2298.
RX PubMed=16055732; DOI=10.1128/mcb.25.16.7239-7248.2005;
RA Kamada Y., Fujioka Y., Suzuki N.N., Inagaki F., Wullschleger S.,
RA Loewith R., Hall M.N., Ohsumi Y.;
RT "Tor2 directly phosphorylates the AGC kinase Ypk2 to regulate actin
RT polarization.";
RL Mol. Cell. Biol. 25:7239-7248(2005).
RN [23]
RP FUNCTION, AND INTERACTION WITH SLM1.
RX PubMed=16959779; DOI=10.1074/jbc.m604244200;
RA Mulet J.M., Martin D.E., Loewith R., Hall M.N.;
RT "Mutual antagonism of TOR and calcineurin signaling.";
RL J. Biol. Chem. 281:33000-33007(2006).
RN [24]
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 [25]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [26]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-10, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [27]
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 [28]
RP INTERACTION WITH PIB2, AND 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).
CC -!- FUNCTION: Phosphatidylinositol 3-kinase homolog, component of both
CC TORC1 and TORC2. TORC1 regulates multiple cellular processes to control
CC cell growth in response to environmental signals. Nutrient limitation
CC and environmental stress signals cause inactivation of TORC1. Active
CC TORC1 positively controls ribosome biogenesis via control of rRNA,
CC ribosomal protein and tRNA gene expression, and rRNA processing. TORC1
CC positively controls protein biosynthesis by regulation of mRNA
CC stability, translation initiation factor activity, and high-affinity
CC amino acid permeases that serve to provide amino acids for use by the
CC translation machinery. TORC1 also promotes growth by sequestering a
CC number of nutrient and general stress-responsive transcription factors
CC in the cytoplasm. TORC1 negatively controls macroautophagy, a process
CC to recycle surplus cytoplasmic mass under nutrient starvation
CC conditions. TORC1 controls many of these processes via TIP41-TAP42-
CC mediated inhibition of the type 2A-related phosphatases PP2A and SIT4
CC (PubMed:10198052, PubMed:10329624, PubMed:10604478, PubMed:11741537,
CC PubMed:15620355, PubMed:7606777, PubMed:8741837, PubMed:9539725,
CC PubMed:9843498). In nutrient-rich conditions, responsible for the
CC phosphorylation of AGC S6 kinase (S6K) YPK3, activating YPK3 kinase
CC activity and promoting phosphorylation of ribosomal protein S6
CC (PubMed:25767889). Phosphorylates kinase SCH9 at 6 amino acids in the
CC C-terminus, activating SCH9 kinase activity to properly regulate
CC ribosome biogenesis, translation initiation, and entry into stationary
CC phase (PubMed:17560372). TORC2 regulates cell cycle-dependent
CC polarization of the actin-cytoskeleton, cell wall integrity, and
CC receptor endocytosis. TORC2 controls polarity of the actin
CC cytoskeleton, which is required for orienting the secretory pathway
CC toward discrete growth sites, via the RHO1/PKC1/MAPK cell integrity
CC pathway by activating the RHO1 guanine nucleotide exchange factor ROM2.
CC TORC2 phosphorylates the AGC kinase YPK2, an upstream effector of the
CC cell integrity pathway. TORC2 negatively regulates calcineurin-
CC dependent stress signaling via phosphorylation of its effector SLM1-
CC SLM2 (PubMed:14593073, PubMed:15372071, PubMed:16055732,
CC PubMed:16959779, PubMed:8846782, PubMed:8943012).
CC {ECO:0000269|PubMed:10198052, ECO:0000269|PubMed:10329624,
CC ECO:0000269|PubMed:10604478, ECO:0000269|PubMed:11741537,
CC ECO:0000269|PubMed:14593073, ECO:0000269|PubMed:15372071,
CC ECO:0000269|PubMed:15620355, ECO:0000269|PubMed:16055732,
CC ECO:0000269|PubMed:16959779, ECO:0000269|PubMed:17560372,
CC ECO:0000269|PubMed:25767889, ECO:0000269|PubMed:7606777,
CC ECO:0000269|PubMed:8741837, ECO:0000269|PubMed:8846782,
CC ECO:0000269|PubMed:8943012, ECO:0000269|PubMed:9539725,
CC 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:8846782};
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:8846782};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + ATP = a
CC 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate) + ADP +
CC H(+); Xref=Rhea:RHEA:19877, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57880, ChEBI:CHEBI:58178, ChEBI:CHEBI:456216;
CC EC=2.7.1.67; Evidence={ECO:0000269|PubMed:8846782};
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). TORC1 binds to and is inhibited by
CC FKBP-rapamycin (PubMed:12408816). Interacts with PIB2; following
CC activation of PIB2 by glutamine (PubMed:29698392). The target of
CC rapamycin complex 2 (TORC2) is composed of at least AVO1, AVO2, BIT61,
CC LST8, TOR2 and TSC11 (PubMed:12408816, PubMed:12631735,
CC PubMed:16002396, PubMed:16959779). TORC2 likely forms a homodimer
CC (PubMed:16002396). Contrary to TORC1, TORC2 does not bind to and is not
CC sensitive to FKBP-rapamycin (PubMed:12408816). Interacts with SLM1 and
CC SLM2 (PubMed:15689497, PubMed:16959779). {ECO:0000269|PubMed:12408816,
CC ECO:0000269|PubMed:12631735, ECO:0000269|PubMed:15689497,
CC ECO:0000269|PubMed:16002396, ECO:0000269|PubMed:16959779,
CC ECO:0000269|PubMed:29698392}.
CC -!- INTERACTION:
CC P32600; Q08236: AVO1; NbExp=4; IntAct=EBI-19385, EBI-29284;
CC P32600; Q04749: AVO2; NbExp=4; IntAct=EBI-19385, EBI-28131;
CC P32600; P47041: BIT61; NbExp=2; IntAct=EBI-19385, EBI-25889;
CC P32600; P20081: FPR1; NbExp=3; IntAct=EBI-19385, EBI-6961;
CC P32600; P41318: LST8; NbExp=7; IntAct=EBI-19385, EBI-28598;
CC P32600; Q04372: TAP42; NbExp=4; IntAct=EBI-19385, EBI-18926;
CC P32600; P40061: TSC11; NbExp=5; IntAct=EBI-19385, EBI-22621;
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:8846782}; Peripheral membrane protein
CC {ECO:0000269|PubMed:12631735, ECO:0000269|PubMed:8846782}; Cytoplasmic
CC side {ECO:0000269|PubMed:12631735, ECO:0000269|PubMed:8846782}.
CC Note=Also localizes to membranous structures both proximal to, yet
CC distinct from, the plasma membrane as well as within the cell interior,
CC probably endosomal or Golgi membranes. {ECO:0000269|PubMed:10973982}.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. {ECO:0000305}.
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DR EMBL; X71416; CAA50548.1; -; Genomic_DNA.
DR EMBL; Z28203; CAA82048.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA08966.1; -; Genomic_DNA.
DR PIR; S38040; S38040.
DR RefSeq; NP_012719.2; NM_001179768.1.
DR PDB; 6EMK; EM; 8.00 A; A/C=1-2474.
DR PDBsum; 6EMK; -.
DR AlphaFoldDB; P32600; -.
DR SMR; P32600; -.
DR BioGRID; 33920; 471.
DR ComplexPortal; CPX-1716; TORC1 serine/threonine-protein kinase complex, TOR2 variant.
DR ComplexPortal; CPX-1717; TORC2 complex.
DR DIP; DIP-2332N; -.
DR IntAct; P32600; 24.
DR MINT; P32600; -.
DR STRING; 4932.YKL203C; -.
DR iPTMnet; P32600; -.
DR MaxQB; P32600; -.
DR PaxDb; P32600; -.
DR PRIDE; P32600; -.
DR EnsemblFungi; YKL203C_mRNA; YKL203C; YKL203C.
DR GeneID; 853632; -.
DR KEGG; sce:YKL203C; -.
DR SGD; S000001686; TOR2.
DR VEuPathDB; FungiDB:YKL203C; -.
DR eggNOG; KOG0891; Eukaryota.
DR GeneTree; ENSGT00940000174195; -.
DR HOGENOM; CLU_000178_7_1_1; -.
DR InParanoid; P32600; -.
DR OMA; DPYKHQQ; -.
DR BioCyc; YEAST:G3O-31962-MON; -.
DR BRENDA; 2.7.1.137; 984.
DR Reactome; R-SCE-1257604; PIP3 activates AKT signaling.
DR Reactome; R-SCE-3371571; HSF1-dependent transactivation.
DR Reactome; R-SCE-389357; CD28 dependent PI3K/Akt signaling.
DR Reactome; R-SCE-5218920; VEGFR2 mediated vascular permeability.
DR Reactome; R-SCE-6804757; Regulation of TP53 Degradation.
DR Reactome; R-SCE-9639288; Amino acids regulate mTORC1.
DR PRO; PR:P32600; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P32600; protein.
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:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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; IPI:SGD.
DR GO; GO:0004430; F:1-phosphatidylinositol 4-kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0007010; P:cytoskeleton organization; IMP:SGD.
DR GO; GO:0030950; P:establishment or maintenance of actin cytoskeleton polarity; 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:0045807; P:positive regulation of endocytosis; IMP:SGD.
DR GO; GO:2001108; P:positive regulation of Rho guanyl-nucleotide exchange factor activity; IMP:SGD.
DR GO; GO:0035025; P:positive regulation of Rho protein signal transduction; IMP:SGD.
DR GO; GO:0006468; P:protein phosphorylation; IDA:SGD.
DR GO; GO:0051726; P:regulation of cell cycle; IC:ComplexPortal.
DR GO; GO:0001558; P:regulation of cell growth; IC:ComplexPortal.
DR GO; GO:1905356; P:regulation of snRNA pseudouridine synthesis; 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 Gene3D; 1.10.1070.11; -; 1.
DR Gene3D; 1.20.120.150; -; 1.
DR Gene3D; 1.25.10.10; -; 3.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR024585; DUF3385_TOR.
DR InterPro; IPR003152; FATC_dom.
DR InterPro; IPR009076; FRB_dom.
DR InterPro; IPR036738; FRB_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000403; PI3/4_kinase_cat_dom.
DR InterPro; IPR036940; PI3/4_kinase_cat_sf.
DR InterPro; IPR018936; PI3/4_kinase_CS.
DR InterPro; IPR003151; PIK-rel_kinase_FAT.
DR InterPro; IPR014009; PIK_FAT.
DR InterPro; IPR026683; TOR.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR11139: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; 3.
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; Phosphoprotein; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Transferase; Vacuole.
FT CHAIN 1..2474
FT /note="Serine/threonine-protein kinase TOR2"
FT /id="PRO_0000088815"
FT REPEAT 588..626
FT /note="HEAT 1"
FT REPEAT 636..674
FT /note="HEAT 2"
FT REPEAT 676..710
FT /note="HEAT 3"
FT REPEAT 756..793
FT /note="HEAT 4"
FT REPEAT 797..835
FT /note="HEAT 5"
FT REPEAT 841..879
FT /note="HEAT 6"
FT REPEAT 917..955
FT /note="HEAT 7"
FT REPEAT 1039..1076
FT /note="HEAT 8"
FT REPEAT 1079..1116
FT /note="HEAT 9"
FT REPEAT 1118..1155
FT /note="HEAT 10"
FT REPEAT 1292..1331
FT /note="HEAT 11"
FT DOMAIN 1338..1922
FT /note="FAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00534"
FT DOMAIN 2097..2421
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT DOMAIN 2442..2474
FT /note="FATC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00534,
FT ECO:0000255|PROSITE-ProRule:PRU00535"
FT REGION 1..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2103..2109
FT /note="G-loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 2276..2284
FT /note="Catalytic loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 2296..2321
FT /note="Activation loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..60
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 10
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MUTAGEN 1975
FT /note="S->I: In TOR2-1; confers resistance to rapamycin."
FT /evidence="ECO:0000269|PubMed:8846782"
FT MUTAGEN 2129
FT /note="G->R: Causes defect in receptor endocytosis."
FT /evidence="ECO:0000269|PubMed:14593073"
FT MUTAGEN 2279
FT /note="D->A: Loss of function."
FT /evidence="ECO:0000269|PubMed:8846782"
FT MUTAGEN 2298
FT /note="D->E: Loss of kinase activity."
FT /evidence="ECO:0000269|PubMed:16055732"
FT CONFLICT 1473
FT /note="Missing (in Ref. 2; CAA82048)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2474 AA; 281568 MW; F2349690146058CF CRC64;
MNKYINKYTT PPNLLSLRQR AEGKHRTRKK LTHKSHSHDD EMSTTSNTDS NHNGPNDSGR
VITGSAGHIG KISFVDSELD TTFSTLNLIF DKLKSDVPQE RASGANELST TLTSLAREVS
AEQFQRFSNS LNNKIFELIH GFTSSEKIGG ILAVDTLISF YLSTEELPNQ TSRLANYLRV
LIPSSDIEVM RLAANTLGRL TVPGGTLTSD FVEFEVRTCI DWLTLTADNN SSSSKLEYRR
HAALLIIKAL ADNSPYLLYP YVNSILDNIW VPLRDAKLII RLDAAVALGK CLTIIQDRDP
ALGKQWFQRL FQGCTHGLSL NTNDSVHATL LVFRELLSLK APYLRDKYDD IYKSTMKYKE
YKFDVIRREV YAILPLLAAF DPAIFTKKYL DRIMVHYLRY LKNIDMNAAN NSDKPFILVS
IGDIAFEVGS SISPYMTLIL DNIREGLRTK FKVRKQFEKD LFYCIGKLAC ALGPAFAKHL
NKDLLNLMLN CPMSDHMQET LMILNEKIPS LESTVNSRIL NLLSISLSGE KFIQSNQYDF
NNQFSIEKAR KSRNQSFMKK TGESNDDITD AQILIQCFKM LQLIHHQYSL TEFVRLITIS
YIEHEDSSVR KLAALTSCDL FIKDDICKQT SVHALHSVSE VLSKLLMIAI TDPVAEIRLE
ILQHLGSNFD PQLAQPDNLR LLFMALNDEI FGIQLEAIKI IGRLSSVNPA YVVPSLRKTL
LELLTQLKFS NMPKKKEESA TLLCTLINSS DEVAKPYIDP ILDVILPKCQ DASSAVASTA
LKVLGELSVV GGKEMTRYLK ELMPLIINTF QDQSNSFKRD AALTTLGQLA ASSGYVVGPL
LDYPELLGIL INILKTENNP HIRRGTVRLI GILGALDPYK HREIEVTSNS KSSVEQNAPS
IDIALLMQGV SPSNDEYYPT VVIHNLMKIL NDPSLSIHHT AAIQAIMHIF QNLGLRCVSF
LDQIIPGIIL VMRSCPPSQL DFYFQQLGSL ISIVKQHIRP HVEKIYGVIR EFFPIIKLQI
TIISVIESIS KALEGEFKRF VPETLTFFLD ILENDQSNKR IVPIRILKSL VTFGPNLEDY
SHLIMPIVVR MTEYSAGSLK KISIITLGRL AKNINLSEMS SRIVQALVRI LNNGDRELTK
ATMNTLSLLL LQLGTDFVVF VPVINKALLR NRIQHSVYDQ LVNKLLNNEC LPTNIIFDKE
NEVPERKNYE DEMQVTKLPV NQNILKNAWY CSQQKTKEDW QEWIRRLSIQ LLKESPSACL
RSCSSLVSVY YPLARELFNA SFSSCWVELQ TSYQEDLIQA LCKALSSSEN PPEIYQMLLN
LVEFMEHDDK PLPIPIHTLG KYAQKCHAFA KALHYKEVEF LEEPKNSTIE ALISINNQLH
QTDSAIGILK HAQQHNELQL KETWYEKLQR WEDALAAYNE KEAAGEDSVE VMMGKLRSLY
ALGEWEELSK LASEKWGTAK PEVKKAMAPL AAGAAWGLEQ WDEIAQYTSV MKSQSPDKEF
YDAILCLHRN NFKKAEVHIF NARDLLVTEL SALVNESYNR AYNVVVRAQI IAELEEIIKY
KKLPQNSDKR LTMRETWNTR LLGCQKNIDV WQRILRVRSL VIKPKEDAQV RIKFANLCRK
SGRMALAKKV LNTLLEETDD PDHPNTAKAS PPVVYAQLKY LWATGLQDEA LKQLINFTSR
MAHDLGLDPN NMIAQSVPQQ SKRVPRHVED YTKLLARCFL KQGEWRVCLQ PKWRLSNPDS
ILGSYLLATH FDNTWYKAWH NWALANFEVI SMLTSVSKKK QEGSDASSVT DINEFDNGMI
GVNTFDAKEV HYSSNLIHRH VIPAIKGFFH SISLSESSSL QDALRLLTLW FTFGGIPEAT
QAMHEGFNLI QIGTWLEVLP QLISRIHQPN QIVSRSLLSL LSDLGKAHPQ ALVYPLMVAI
KSESLSRQKA ALSIIEKMRI HSPVLVDQAE LVSHELIRMA VLWHEQWYEG LDDASRQFFG
EHNTEKMFAA LEPLYEMLKR GPETLREISF QNSFGRDLND AYEWLMNYKK SKDVSNLNQA
WDIYYNVFRK IGKQLPQLQT LELQHVSPKL LSAHDLELAV PGTRASGGKP IVKISKFEPV
FSVISSKQRP RKFCIKGSDG KDYKYVLKGH EDIRQDSLVM QLFGLVNTLL QNDAECFRRH
LDIQQYPAIP LSPKSGLLGW VPNSDTFHVL IREHREAKKI PLNIEHWVML QMAPDYDNLT
LLQKVEVFTY ALNNTEGQDL YKVLWLKSRS SETWLERRTT YTRSLAVMSM TGYILGLGDR
HPSNLMLDRI TGKVIHIDFG DCFEAAILRE KFPEKVPFRL TRMLTYAMEV SGIEGSFRIT
CENVMKVLRD NKGSLMAILE AFAFDPLINW GFDLPTKKIE EETGIQLPVM NANELLSNGA
ITEEEVQRVE NEHKNAIRNA RAMLVLKRIT DKLTGNDIRR FNDLDVPEQV DKLIQQATSV
ENLCQHYIGW CPFW
