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Serine/threonine-protein kinase TOR2 (EC 2.7.1.67) (EC 2.7.11.1) (Dominant rapamycin resistance protein 2) (Phosphatidylinositol 4-kinase TOR2) (PI4-kinase TOR2) (PI4K TOR2) (PtdIns-4-kinase TOR2) (Target of rapamycin kinase 2) (Temperature-sensitive CSG2 suppressor protein 14)

 TOR2_YEAST              Reviewed;        2474 AA.
P32600; D6VX00;
01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
09-JAN-2007, sequence version 3.
12-SEP-2018, entry version 174.
RecName: Full=Serine/threonine-protein kinase TOR2;
EC=2.7.1.67;
EC=2.7.11.1;
AltName: Full=Dominant rapamycin resistance protein 2;
AltName: Full=Phosphatidylinositol 4-kinase TOR2;
Short=PI4-kinase TOR2;
Short=PI4K TOR2;
Short=PtdIns-4-kinase TOR2;
AltName: Full=Target of rapamycin kinase 2;
AltName: Full=Temperature-sensitive CSG2 suppressor protein 14;
Name=TOR2; Synonyms=DRR2, TSC14; OrderedLocusNames=YKL203C;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=JK9-3D;
PubMed=8387896; DOI=10.1016/0092-8674(93)90144-F;
Kunz J., Henriquez R., Schneider U., Deuter-Reinhard M., Movva N.,
Hall M.N.;
"Target of rapamycin in yeast, TOR2, is an essential
phosphatidylinositol kinase homolog required for G1 progression.";
Cell 73:585-596(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=8196765; DOI=10.1038/369371a0;
Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M.,
Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C.,
Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G.,
Zimmermann J., Haasemann M., Becker I., Mewes H.-W.;
"Complete DNA sequence of yeast chromosome XI.";
Nature 369:371-378(1994).
[3]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[4]
FUNCTION.
PubMed=7606777; DOI=10.1016/0092-8674(95)90058-6;
Zheng X.-F., Florentino D., Chen J., Crabtree G.R., Schreiber S.L.;
"TOR kinase domains are required for two distinct functions, only one
of which is inhibited by rapamycin.";
Cell 82:121-130(1995).
[5]
FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-1975 AND ASP-2279,
AND CATALYTIC ACTIVITY.
PubMed=8846782;
Cardenas M.E., Heitman J.;
"FKBP12-rapamycin target TOR2 is a vacuolar protein with an associated
phosphatidylinositol-4 kinase activity.";
EMBO J. 14:5892-5907(1995).
[6]
FUNCTION.
PubMed=8741837; DOI=10.1091/mbc.7.1.25;
Barbet N.C., Schneider U., Helliwell S.B., Stansfield I., Tuite M.F.,
Hall M.N.;
"TOR controls translation initiation and early G1 progression in
yeast.";
Mol. Biol. Cell 7:25-42(1996).
[7]
FUNCTION.
PubMed=8943012; DOI=10.1073/pnas.93.24.13780;
Schmidt A., Kunz J., Hall M.N.;
"TOR2 is required for organization of the actin cytoskeleton in
yeast.";
Proc. Natl. Acad. Sci. U.S.A. 93:13780-13785(1996).
[8]
FUNCTION.
PubMed=9843498; DOI=10.1093/emboj/17.23.6924;
Schmidt A., Beck T., Koller A., Kunz J., Hall M.N.;
"The TOR nutrient signalling pathway phosphorylates NPR1 and inhibits
turnover of the tryptophan permease.";
EMBO J. 17:6924-6931(1998).
[9]
FUNCTION.
PubMed=9539725; DOI=10.1073/pnas.95.8.4264;
Berset C., Trachsel H., Altmann M.;
"The TOR (target of rapamycin) signal transduction pathway regulates
the stability of translation initiation factor eIF4G in the yeast
Saccharomyces cerevisiae.";
Proc. Natl. Acad. Sci. U.S.A. 95:4264-4269(1998).
[10]
FUNCTION.
PubMed=10329624; DOI=10.1093/emboj/18.10.2782;
Jiang Y., Broach J.R.;
"Tor proteins and protein phosphatase 2A reciprocally regulate Tap42
in controlling cell growth in yeast.";
EMBO J. 18:2782-2792(1999).
[11]
FUNCTION.
PubMed=10198052; DOI=10.1091/mbc.10.4.987;
Powers T., Walter P.;
"Regulation of ribosome biogenesis by the rapamycin-sensitive TOR-
signaling pathway in Saccharomyces cerevisiae.";
Mol. Biol. Cell 10:987-1000(1999).
[12]
FUNCTION.
PubMed=10604478; DOI=10.1038/45287;
Beck T., Hall M.N.;
"The TOR signalling pathway controls nuclear localization of nutrient-
regulated transcription factors.";
Nature 402:689-692(1999).
[13]
SUBCELLULAR LOCATION.
PubMed=10973982; DOI=10.1074/jbc.M007296200;
Kunz J., Schneider U., Howald I., Schmidt A., Hall M.N.;
"HEAT repeats mediate plasma membrane localization of Tor2p in
yeast.";
J. Biol. Chem. 275:37011-37020(2000).
[14]
FUNCTION.
PubMed=11741537; DOI=10.1016/S1097-2765(01)00386-0;
Jacinto E., Guo B., Arndt K.T., Schmelzle T., Hall M.N.;
"TIP41 interacts with TAP42 and negatively regulates the TOR signaling
pathway.";
Mol. Cell 8:1017-1026(2001).
[15]
SUBUNIT.
PubMed=12408816; DOI=10.1016/S1097-2765(02)00636-6;
Loewith R., Jacinto E., Wullschleger S., Lorberg A., Crespo J.L.,
Bonenfant D., Oppliger W., Jenoe P., Hall M.N.;
"Two TOR complexes, only one of which is rapamycin sensitive, have
distinct roles in cell growth control.";
Mol. Cell 10:457-468(2002).
[16]
SUBCELLULAR LOCATION, SUBUNIT, AND INTERACTION WITH LST8.
PubMed=12631735; DOI=10.1091/mbc.E02-09-0609;
Wedaman K.P., Reinke A., Anderson S., Yates J.R. III, McCaffery J.M.,
Powers T.;
"Tor kinases are in distinct membrane-associated protein complexes in
Saccharomyces cerevisiae.";
Mol. Biol. Cell 14:1204-1220(2003).
[17]
FUNCTION IN RECEPTOR ENDOCYTOSIS, AND MUTAGENESIS OF GLY-2129.
PubMed=14593073; DOI=10.1091/mbc.E03-05-0323;
deHart A.K.A., Schnell J.D., Allen D.A., Tsai J.-Y., Hicke L.;
"Receptor internalization in yeast requires the Tor2-Rho1 signaling
pathway.";
Mol. Biol. Cell 14:4676-4684(2003).
[18]
FUNCTION.
PubMed=15620355; DOI=10.1016/j.cell.2004.11.047;
Martin D.E., Soulard A., Hall M.N.;
"TOR regulates ribosomal protein gene expression via PKA and the
forkhead transcription factor FHL1.";
Cell 119:969-979(2004).
[19]
FUNCTION, AND PHOSPHORYLATION OF SLM1-SLM2.
PubMed=15372071; DOI=10.1038/sj.emboj.7600384;
Audhya A., Loewith R., Parsons A.B., Gao L., Tabuchi M., Zhou H.,
Boone C., Hall M.N., Emr S.D.;
"Genome-wide lethality screen identifies new PI4,5P2 effectors that
regulate the actin cytoskeleton.";
EMBO J. 23:3747-3757(2004).
[20]
SUBUNIT, AND INTERACTION WITH LST8 AND TSC11.
PubMed=16002396; DOI=10.1074/jbc.M505553200;
Wullschleger S., Loewith R., Oppliger W., Hall M.N.;
"Molecular organization of target of rapamycin complex 2.";
J. Biol. Chem. 280:30697-30704(2005).
[21]
INTERACTION WITH SLM1 AND SLM2.
PubMed=15689497; DOI=10.1091/mbc.E04-07-0564;
Fadri M., Daquinag A., Wang S., Xue T., Kunz J.;
"The pleckstrin homology domain proteins Slm1 and Slm2 are required
for actin cytoskeleton organization in yeast and bind
phosphatidylinositol-4,5-bisphosphate and TORC2.";
Mol. Biol. Cell 16:1883-1900(2005).
[22]
FUNCTION, PHOSPHORYLATION OF YPK2, AND MUTAGENESIS OF ASP-2298.
PubMed=16055732; DOI=10.1128/MCB.25.16.7239-7248.2005;
Kamada Y., Fujioka Y., Suzuki N.N., Inagaki F., Wullschleger S.,
Loewith R., Hall M.N., Ohsumi Y.;
"Tor2 directly phosphorylates the AGC kinase Ypk2 to regulate actin
polarization.";
Mol. Cell. Biol. 25:7239-7248(2005).
[23]
FUNCTION, AND INTERACTION WITH SLM1.
PubMed=16959779; DOI=10.1074/jbc.M604244200;
Mulet J.M., Martin D.E., Loewith R., Hall M.N.;
"Mutual antagonism of TOR and calcineurin signaling.";
J. Biol. Chem. 281:33000-33007(2006).
[24]
FUNCTION.
PubMed=17560372; DOI=10.1016/j.molcel.2007.04.020;
Urban J., Soulard A., Huber A., Lippman S., Mukhopadhyay D.,
Deloche O., Wanke V., Anrather D., Ammerer G., Riezman H.,
Broach J.R., De Virgilio C., Hall M.N., Loewith R.;
"Sch9 is a major target of TORC1 in Saccharomyces cerevisiae.";
Mol. Cell 26:663-674(2007).
[25]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[26]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-10, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
[27]
FUNCTION.
PubMed=25767889; DOI=10.1371/journal.pone.0120250;
Gonzalez A., Shimobayashi M., Eisenberg T., Merle D.A., Pendl T.,
Hall M.N., Moustafa T.;
"TORC1 promotes phosphorylation of ribosomal protein S6 via the AGC
kinase Ypk3 in Saccharomyces cerevisiae.";
PLoS ONE 10:E0120250-E0120250(2015).
-!- FUNCTION: Phosphatidylinositol 3-kinase homolog, component of both
TORC1 and TORC2. TORC1 regulates multiple cellular processes to
control cell growth in response to environmental signals. Nutrient
limitation and environmental stress signals cause inactivation of
TORC1. Active TORC1 positively controls ribosome biogenesis via
control of rRNA, ribosomal protein and tRNA gene expression, and
rRNA processing. TORC1 positively controls protein biosynthesis by
regulation of mRNA stability, translation initiation factor
activity, and high-affinity amino acid permeases that serve to
provide amino acids for use by the translation machinery. TORC1
also promotes growth by sequestering a number of nutrient and
general stress-responsive transcription factors in the cytoplasm.
TORC1 negatively controls macroautophagy, a process to recycle
surplus cytoplasmic mass under nutrient starvation conditions.
TORC1 controls many of these processes via TIP41-TAP42-mediated
inhibition of the type 2A-related phosphatases PP2A and SIT4
(PubMed:10198052, PubMed:10329624, PubMed:10604478,
PubMed:11741537, PubMed:15620355, PubMed:7606777, PubMed:8741837,
PubMed:9539725, PubMed:9843498). In nutrient rich conditions,
responsible for the phosphorylation of AGC S6 kinase (S6K) YPK3,
activating YPK3 kinase activity and promoting phosphorylation of
ribosomal protein S6 (PubMed:25767889). Phosphorylates kinase SCH9
at 6 amino acids in the C-terminus, activating SCH9 kinase
activity to properly regulate ribosome biogenesis, translation
initiation, and entry into stationary phase (PubMed:17560372).
TORC2 regulates cell cycle-dependent polarization of the actin-
cytoskeleton, cell wall integrity, and receptor endocytosis. TORC2
controls polarity of the actin cytoskeleton, which is required for
orienting the secretory pathway toward discrete growth sites, via
the RHO1/PKC1/MAPK cell integrity pathway by activating the RHO1
guanine nucleotide exchange factor ROM2. TORC2 phosphorylates the
AGC kinase YPK2, an upstream effector of the cell integrity
pathway. TORC2 negatively regulates calcineurin-dependent stress
signaling via phosphorylation of its effector SLM1-SLM2
(PubMed:14593073, PubMed:15372071, PubMed:16055732,
PubMed:16959779, PubMed:8846782, PubMed:8943012).
{ECO:0000269|PubMed:10198052, ECO:0000269|PubMed:10329624,
ECO:0000269|PubMed:10604478, ECO:0000269|PubMed:11741537,
ECO:0000269|PubMed:14593073, ECO:0000269|PubMed:15372071,
ECO:0000269|PubMed:15620355, ECO:0000269|PubMed:16055732,
ECO:0000269|PubMed:16959779, ECO:0000269|PubMed:17560372,
ECO:0000269|PubMed:25767889, ECO:0000269|PubMed:7606777,
ECO:0000269|PubMed:8741837, ECO:0000269|PubMed:8846782,
ECO:0000269|PubMed:8943012, ECO:0000269|PubMed:9539725,
ECO:0000269|PubMed:9843498}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
{ECO:0000269|PubMed:8846782}.
-!- CATALYTIC ACTIVITY: ATP + 1-phosphatidyl-1D-myo-inositol = ADP +
1-phosphatidyl-1D-myo-inositol 4-phosphate.
{ECO:0000269|PubMed:8846782}.
-!- SUBUNIT: The target of rapamycin complex 1 (TORC1) is composed of
at least KOG1, LST8, TCO89 and either TOR1 (TORC1-A) or TOR2
(TORC1-B). TORC1 binds to and is inhibited by FKBP-rapamycin. The
target of rapamycin complex 2 (TORC2) is composed of at least
AVO1, AVO2, BIT61, LST8, TOR2 and TSC11. TORC2 likely forms a
homodimer. Contrary to TORC1, TORC2 does not bind to and is not
sensitive to FKBP-rapamycin. Interacts with SLM1 and SLM2.
{ECO:0000269|PubMed:12408816, ECO:0000269|PubMed:12631735,
ECO:0000269|PubMed:15689497, ECO:0000269|PubMed:16002396,
ECO:0000269|PubMed:16959779}.
-!- INTERACTION:
Q08236:AVO1; NbExp=4; IntAct=EBI-19385, EBI-29284;
Q04749:AVO2; NbExp=4; IntAct=EBI-19385, EBI-28131;
P47041:BIT61; NbExp=2; IntAct=EBI-19385, EBI-25889;
P20081:FPR1; NbExp=3; IntAct=EBI-19385, EBI-6961;
P41318:LST8; NbExp=7; IntAct=EBI-19385, EBI-28598;
Q04372:TAP42; NbExp=4; IntAct=EBI-19385, EBI-18926;
P40061:TSC11; NbExp=5; IntAct=EBI-19385, EBI-22621;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10973982,
ECO:0000269|PubMed:12631735}; Peripheral membrane protein
{ECO:0000269|PubMed:10973982, ECO:0000269|PubMed:12631735};
Cytoplasmic side {ECO:0000269|PubMed:10973982,
ECO:0000269|PubMed:12631735}. Vacuole membrane
{ECO:0000269|PubMed:12631735, ECO:0000269|PubMed:8846782};
Peripheral membrane protein {ECO:0000269|PubMed:12631735,
ECO:0000269|PubMed:8846782}; Cytoplasmic side
{ECO:0000269|PubMed:12631735, ECO:0000269|PubMed:8846782}.
Note=Also localizes to membranous structures both proximal to, yet
distinct from, the plasma membrane as well as within the cell
interior, probably endosomal or Golgi membranes.
{ECO:0000269|PubMed:10973982}.
-!- SIMILARITY: Belongs to the PI3/PI4-kinase family. {ECO:0000305}.
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EMBL; X71416; CAA50548.1; -; Genomic_DNA.
EMBL; Z28203; CAA82048.1; -; Genomic_DNA.
EMBL; BK006944; DAA08966.1; -; Genomic_DNA.
PIR; S38040; S38040.
RefSeq; NP_012719.2; NM_001179768.1.
PDB; 6EMK; EM; 8.00 A; A/C=1-2474.
PDBsum; 6EMK; -.
ProteinModelPortal; P32600; -.
SMR; P32600; -.
BioGrid; 33920; 461.
ComplexPortal; CPX-1716; TORC1 complex variant 2.
ComplexPortal; CPX-1717; TORC2 complex.
DIP; DIP-2332N; -.
IntAct; P32600; 24.
MINT; P32600; -.
STRING; 4932.YKL203C; -.
iPTMnet; P32600; -.
MaxQB; P32600; -.
PaxDb; P32600; -.
PRIDE; P32600; -.
EnsemblFungi; YKL203C; YKL203C; YKL203C.
GeneID; 853632; -.
KEGG; sce:YKL203C; -.
EuPathDB; FungiDB:YKL203C; -.
SGD; S000001686; TOR2.
GeneTree; ENSGT00920000149522; -.
HOGENOM; HOG000163215; -.
InParanoid; P32600; -.
KO; K07203; -.
OMA; SSHQGLM; -.
OrthoDB; EOG092C00HJ; -.
BioCyc; YEAST:G3O-31962-MONOMER; -.
BRENDA; 2.7.1.137; 984.
PRO; PR:P32600; -.
Proteomes; UP000002311; Chromosome XI.
GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IDA:SGD.
GO; GO:0000329; C:fungal-type vacuole membrane; IDA:SGD.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0005886; C:plasma membrane; IDA:SGD.
GO; GO:0031931; C:TORC1 complex; IPI:SGD.
GO; GO:0031932; C:TORC2 complex; IPI:SGD.
GO; GO:0004430; F:1-phosphatidylinositol 4-kinase activity; IEA:UniProtKB-EC.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:SGD.
GO; GO:0044877; F:protein-containing complex binding; IEA:InterPro.
GO; GO:0030037; P:actin filament reorganization involved in cell cycle; TAS:SGD.
GO; GO:0007010; P:cytoskeleton organization; IMP:SGD.
GO; GO:0006281; P:DNA repair; IBA:GO_Central.
GO; GO:0030950; P:establishment or maintenance of actin cytoskeleton polarity; IMP:SGD.
GO; GO:0010507; P:negative regulation of autophagy; IGI:SGD.
GO; GO:0045807; P:positive regulation of endocytosis; IMP:SGD.
GO; GO:2001108; P:positive regulation of Rho guanyl-nucleotide exchange factor activity; IMP:SGD.
GO; GO:0035025; P:positive regulation of Rho protein signal transduction; IMP:SGD.
GO; GO:0006468; P:protein phosphorylation; IDA:SGD.
GO; GO:0051726; P:regulation of cell cycle; TAS:SGD.
GO; GO:0001558; P:regulation of cell growth; TAS:SGD.
GO; GO:1905356; P:regulation of snRNA pseudouridine synthesis; IMP:SGD.
GO; GO:0042254; P:ribosome biogenesis; IMP:SGD.
GO; GO:0007165; P:signal transduction; TAS:SGD.
GO; GO:0031929; P:TOR signaling; IMP:SGD.
Gene3D; 1.10.1070.11; -; 1.
Gene3D; 1.20.120.150; -; 1.
Gene3D; 1.25.10.10; -; 3.
Gene3D; 1.25.40.10; -; 1.
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.
InterPro; IPR011990; TPR-like_helical_dom_sf.
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; 9.
SUPFAM; SSF56112; SSF56112; 3.
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;
3D-structure; ATP-binding; Cell cycle; Cell membrane;
Complete proteome; Kinase; Membrane; Nucleotide-binding;
Phosphoprotein; Reference proteome; Repeat;
Serine/threonine-protein kinase; Transferase; Vacuole.
CHAIN 1 2474 Serine/threonine-protein kinase TOR2.
/FTId=PRO_0000088815.
REPEAT 588 626 HEAT 1.
REPEAT 636 674 HEAT 2.
REPEAT 676 710 HEAT 3.
REPEAT 756 793 HEAT 4.
REPEAT 797 835 HEAT 5.
REPEAT 841 879 HEAT 6.
REPEAT 917 955 HEAT 7.
REPEAT 1039 1076 HEAT 8.
REPEAT 1079 1116 HEAT 9.
REPEAT 1118 1155 HEAT 10.
REPEAT 1292 1331 HEAT 11.
DOMAIN 1338 1922 FAT. {ECO:0000255|PROSITE-
ProRule:PRU00534}.
DOMAIN 2123 2441 PI3K/PI4K. {ECO:0000255|PROSITE-
ProRule:PRU00269}.
DOMAIN 2442 2474 FATC. {ECO:0000255|PROSITE-
ProRule:PRU00534, ECO:0000255|PROSITE-
ProRule:PRU00535}.
MOD_RES 10 10 Phosphothreonine.
{ECO:0000244|PubMed:19779198}.
MUTAGEN 1975 1975 S->I: In TOR2-1; confers resistance to
rapamycin. {ECO:0000269|PubMed:8846782}.
MUTAGEN 2129 2129 G->R: Causes defect in receptor
endocytosis.
{ECO:0000269|PubMed:14593073}.
MUTAGEN 2279 2279 D->A: Loss of function.
{ECO:0000269|PubMed:8846782}.
MUTAGEN 2298 2298 D->E: Loss of kinase activity.
{ECO:0000269|PubMed:16055732}.
CONFLICT 1473 1473 Missing (in Ref. 2; CAA82048).
{ECO:0000305}.
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


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