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LMPD Database

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LMP007158

UniProt Annotations

Entry Information

Gene Name	phosphatidylinositol kinase-related protein kinase TOR2
Protein Entry	TOR2_YEAST
UniProt ID	P32600
Species	Yeast (S288c)

Comments

Comment type	Description
Catalytic Activity	ATP + 1-phosphatidyl-1D-myo-inositol = ADP + 1-phosphatidyl-1D-myo-inositol 4-phosphate. {ECO:0000269\|PubMed:8846782}.
Catalytic Activity	ATP + a protein = ADP + a phosphoprotein. {ECO:0000269\|PubMed:8846782}.
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. 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. {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:7606777, ECO:0000269\|PubMed:8741837, ECO:0000269\|PubMed:8846782, ECO:0000269\|PubMed:8943012, ECO:0000269\|PubMed:9539725, ECO:0000269\|PubMed:9843498}.
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; 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;
Similarity	Belongs to the PI3/PI4-kinase family. {ECO:0000305}.
Similarity	Contains 11 HEAT repeats. {ECO:0000305}.
Similarity	Contains 1 FATC domain. {ECO:0000255\|PROSITE- ProRule:PRU00535}.
Similarity	Contains 1 FAT domain. {ECO:0000255\|PROSITE- ProRule:PRU00534}.
Similarity	Contains 1 PI3K/PI4K domain. {ECO:0000255\|PROSITE- ProRule:PRU00269}.
Subcellular Location	Cell membrane; Peripheral membrane protein; Cytoplasmic side. Vacuole membrane; Peripheral membrane protein; Cytoplasmic side. 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.
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}.