GenomeNet

Database: UniProt
Entry: P32600
LinkDB: P32600
Original site: P32600 
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   11-JUN-2014, entry version 132.
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;
OC   Saccharomycetes; 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
RT   phosphatidylinositol 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.,
RA   Bossier P., 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.,
RA   Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G.,
RA   Zimmermann J., Haasemann M., 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.,
RA   Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and
RT   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
RT   of which is inhibited by rapamycin.";
RL   Cell 82:121-130(1995).
RN   [5]
RP   FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-1975 AND ASP-2279,
RP   AND CATALYTIC ACTIVITY.
RX   PubMed=8846782;
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
RT   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
RT   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
RT   the stability of translation initiation factor eIF4G in the yeast
RT   Saccharomyces 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
RT   in 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-
RT   signaling 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
RT   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
RT   distinct 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
RT   forkhead 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.,
RA   Boone C., 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
RT   for actin cytoskeleton organization in yeast and bind
RT   phosphatidylinositol-4,5-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   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
RT   phosphoproteome analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [25]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-10, AND IDENTIFICATION
RP   BY 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
RT   insights into evolution.";
RL   Science 325:1682-1686(2009).
CC   -!- FUNCTION: Phosphatidylinositol 3-kinase homolog, component of both
CC       TORC1 and TORC2. TORC1 regulates multiple cellular processes to
CC       control cell growth in response to environmental signals. Nutrient
CC       limitation and environmental stress signals cause inactivation of
CC       TORC1. Active TORC1 positively controls ribosome biogenesis via
CC       control of rRNA, ribosomal protein and tRNA gene expression, and
CC       rRNA processing. TORC1 positively controls protein biosynthesis by
CC       regulation of mRNA stability, translation initiation factor
CC       activity, and high-affinity amino acid permeases that serve to
CC       provide amino acids for use by the translation machinery. TORC1
CC       also promotes growth by sequestering a number of nutrient and
CC       general stress-responsive transcription factors in the cytoplasm.
CC       TORC1 negatively controls macroautophagy, a process to recycle
CC       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       TORC2 regulates cell cycle-dependent polarization of the actin-
CC       cytoskeleton, cell wall integrity, and receptor endocytosis. TORC2
CC       controls polarity of the actin cytoskeleton, which is required for
CC       orienting the secretory pathway toward discrete growth sites, via
CC       the RHO1/PKC1/MAPK cell integrity pathway by activating the RHO1
CC       guanine nucleotide exchange factor ROM2. TORC2 phosphorylates the
CC       AGC kinase YPK2, an upstream effector of the cell integrity
CC       pathway. TORC2 negatively regulates calcineurin-dependent stress
CC       signaling via phosphorylation of its effector SLM1-SLM2.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- CATALYTIC ACTIVITY: ATP + 1-phosphatidyl-1D-myo-inositol = ADP +
CC       1-phosphatidyl-1D-myo-inositol 4-phosphate.
CC   -!- SUBUNIT: The target of rapamycin complex 1 (TORC1) is composed of
CC       at least KOG1, LST8, TCO89 and either TOR1 (TORC1-A) or TOR2
CC       (TORC1-B). TORC1 binds to and is inhibited by FKBP-rapamycin. The
CC       target of rapamycin complex 2 (TORC2) is composed of at least
CC       AVO1, AVO2, BIT61, LST8, TOR2 and TSC11. TORC2 likely forms a
CC       homodimer. Contrary to TORC1, TORC2 does not bind to and is not
CC       sensitive to FKBP-rapamycin. Interacts with SLM1 and SLM2.
CC   -!- INTERACTION:
CC       Q08236:AVO1; NbExp=4; IntAct=EBI-19385, EBI-29284;
CC       Q04749:AVO2; NbExp=4; IntAct=EBI-19385, EBI-28131;
CC       P47041:BIT61; NbExp=2; IntAct=EBI-19385, EBI-25889;
CC       P41318:LST8; NbExp=7; IntAct=EBI-19385, EBI-28598;
CC       Q04372:TAP42; NbExp=4; IntAct=EBI-19385, EBI-18926;
CC       P40061:TSC11; NbExp=5; IntAct=EBI-19385, EBI-22621;
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein;
CC       Cytoplasmic side. Vacuole membrane; Peripheral membrane protein;
CC       Cytoplasmic side. Note=Also localizes to membranous structures
CC       both proximal to, yet distinct from, the plasma membrane as well
CC       as within the cell interior, probably endosomal or Golgi
CC       membranes.
CC   -!- SIMILARITY: Belongs to the PI3/PI4-kinase family.
CC   -!- SIMILARITY: Contains 1 FAT domain.
CC   -!- SIMILARITY: Contains 1 FATC domain.
CC   -!- SIMILARITY: Contains 11 HEAT repeats.
CC   -!- SIMILARITY: Contains 1 PI3K/PI4K domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
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   ProteinModelPortal; P32600; -.
DR   SMR; P32600; 1405-1447, 1955-2420, 2442-2474.
DR   BioGrid; 33920; 250.
DR   DIP; DIP-2332N; -.
DR   IntAct; P32600; 24.
DR   MINT; MINT-2843476; -.
DR   STRING; 4932.YKL203C; -.
DR   MaxQB; P32600; -.
DR   PaxDb; P32600; -.
DR   PeptideAtlas; P32600; -.
DR   EnsemblFungi; YKL203C; YKL203C; YKL203C.
DR   GeneID; 853632; -.
DR   KEGG; sce:YKL203C; -.
DR   CYGD; YKL203c; -.
DR   SGD; S000001686; TOR2.
DR   eggNOG; COG5032; -.
DR   GeneTree; ENSGT00720000108744; -.
DR   HOGENOM; HOG000163215; -.
DR   KO; K07203; -.
DR   OMA; TYKQNIG; -.
DR   OrthoDB; EOG7Z3FCR; -.
DR   BioCyc; YEAST:G3O-31962-MONOMER; -.
DR   BRENDA; 2.7.1.137; 984.
DR   NextBio; 974511; -.
DR   PRO; PR:P32600; -.
DR   Genevestigator; P32600; -.
DR   GO; GO:0005737; C:cytoplasm; 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: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:0008144; F:drug binding; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:SGD.
DR   GO; GO:0030037; P:actin filament reorganization involved in cell cycle; TAS:SGD.
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: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:GOC.
DR   GO; GO:0051726; P:regulation of cell cycle; TAS:SGD.
DR   GO; GO:0001558; P:regulation of cell growth; TAS:SGD.
DR   GO; GO:0042254; P:ribosome biogenesis; IMP:SGD.
DR   GO; GO:0007165; P:signal transduction; TAS:SGD.
DR   GO; GO:0031929; P:TOR signaling; IMP:SGD.
DR   Gene3D; 1.10.1070.11; -; 3.
DR   Gene3D; 1.25.10.10; -; 6.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR024585; DUF3385_TOR.
DR   InterPro; IPR003152; FATC.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000403; PI3/4_kinase_cat_dom.
DR   InterPro; IPR018936; PI3/4_kinase_CS.
DR   InterPro; IPR003151; PIK-rel_kinase_FAT.
DR   InterPro; IPR014009; PIK_FAT.
DR   InterPro; IPR009076; Rapamycin-bd_dom.
DR   Pfam; PF11865; DUF3385; 1.
DR   Pfam; PF02259; FAT; 1.
DR   Pfam; PF02260; FATC; 1.
DR   Pfam; PF00454; PI3_PI4_kinase; 1.
DR   Pfam; PF08771; Rapamycin_bind; 1.
DR   SMART; SM00146; PI3Kc; 1.
DR   SUPFAM; SSF47212; SSF47212; 1.
DR   SUPFAM; SSF48371; SSF48371; 9.
DR   SUPFAM; SSF56112; SSF56112; 3.
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   ATP-binding; Cell cycle; Cell membrane; Complete proteome; Kinase;
KW   Membrane; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW   Repeat; Serine/threonine-protein kinase; Transferase; Vacuole.
FT   CHAIN         1   2474       Serine/threonine-protein kinase TOR2.
FT                                /FTId=PRO_0000088815.
FT   REPEAT      588    626       HEAT 1.
FT   REPEAT      636    674       HEAT 2.
FT   REPEAT      676    710       HEAT 3.
FT   REPEAT      756    793       HEAT 4.
FT   REPEAT      797    835       HEAT 5.
FT   REPEAT      841    879       HEAT 6.
FT   REPEAT      917    955       HEAT 7.
FT   REPEAT     1039   1076       HEAT 8.
FT   REPEAT     1079   1116       HEAT 9.
FT   REPEAT     1118   1155       HEAT 10.
FT   REPEAT     1292   1331       HEAT 11.
FT   DOMAIN     1338   1922       FAT.
FT   DOMAIN     2123   2441       PI3K/PI4K.
FT   DOMAIN     2442   2474       FATC.
FT   MOD_RES      10     10       Phosphothreonine.
FT   MUTAGEN    1975   1975       S->I: In TOR2-1; confers resistance to
FT                                rapamycin.
FT   MUTAGEN    2129   2129       G->R: Causes defect in receptor
FT                                endocytosis.
FT   MUTAGEN    2279   2279       D->A: Loss of function.
FT   MUTAGEN    2298   2298       D->E: Loss of kinase activity.
FT   CONFLICT   1473   1473       Missing (in Ref. 2; CAA82048).
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
//
DBGET integrated database retrieval system