TCO89_YEAST
ID TCO89_YEAST Reviewed; 799 AA.
AC Q08921; D6W3I8;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Target of rapamycin complex 1 subunit TCO89;
DE Short=TORC1 subunit TCO89;
DE AltName: Full=89 kDa TOR complex 1 protein;
GN Name=TCO89; OrderedLocusNames=YPL180W;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [2]
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 [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [4]
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 [5]
RP FUNCTION, IDENTIFICATION IN TORC1, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP SUBCELLULAR LOCATION.
RX PubMed=14736892; DOI=10.1074/jbc.m313062200;
RA Reinke A., Anderson S., McCaffery J.M., Yates J.R. III, Aronova S., Chu S.,
RA Fairclough S., Iverson C., Wedaman K.P., Powers T.;
RT "TOR complex 1 includes a novel component, Tco89p (YPL180w), and cooperates
RT with Ssd1p to maintain cellular integrity in Saccharomyces cerevisiae.";
RL J. Biol. Chem. 279:14752-14762(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-107, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-52; SER-107; SER-144 AND
RP SER-707, AND 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-52; THR-82; SER-84; SER-115;
RP SER-203; SER-215; SER-290; SER-397 AND SER-575, AND IDENTIFICATION BY MASS
RP 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 [10]
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).
RN [11]
RP DISRUPTION PHENOTYPE.
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).
CC -!- FUNCTION: Component of TORC1, which regulates multiple cellular
CC processes to control cell growth in response to environmental signals.
CC Nutrient limitation and environmental stress signals cause inactivation
CC of TORC1. Active TORC1 positively controls ribosome biogenesis via
CC control of rRNA, ribosomal protein and tRNA gene expression, and rRNA
CC processing. TORC1 positively controls protein biosynthesis by
CC regulation of mRNA stability, translation initiation factor activity,
CC and high-affinity amino acid permeases that serve to provide amino
CC acids for use by the translation machinery. TORC1 also promotes growth
CC by sequestering a number of nutrient and general stress-responsive
CC transcription factors in the cytoplasm. TORC1 negatively controls
CC macroautophagy, a process to recycle surplus cytoplasmic mass under
CC nutrient starvation conditions. {ECO:0000269|PubMed:14736892}.
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:14736892). Interacts with PIB2; following activation of PIB2 by
CC glutamine or cysteine (PubMed:29698392). TORC1 binds to and is
CC inhibited by FKBP-rapamycin (PubMed:14736892).
CC {ECO:0000269|PubMed:14736892, ECO:0000269|PubMed:29698392}.
CC -!- INTERACTION:
CC Q08921; P25293: NAP1; NbExp=2; IntAct=EBI-37395, EBI-11850;
CC Q08921; P35169: TOR1; NbExp=4; IntAct=EBI-37395, EBI-19374;
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 both
CC proximal to, yet distinct from, the plasma membrane as well as within
CC the cell interior, probably endosomal or Golgi membranes.
CC -!- DISRUPTION PHENOTYPE: Abnormal activation of TORC1 signaling
CC (PubMed:32801125). Abnormal punctate localization of TOR1
CC (PubMed:32801125). Sensitive to high hydrostatic pressure (mechanical
CC stress) (PubMed:32801125). {ECO:0000269|PubMed:32801125}.
CC -!- MISCELLANEOUS: Present with 243 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the TORC subunit TCO89 family. {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; Z73536; CAA97887.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11254.1; -; Genomic_DNA.
DR PIR; S65192; S65192.
DR RefSeq; NP_015145.1; NM_001183994.1.
DR AlphaFoldDB; Q08921; -.
DR SMR; Q08921; -.
DR BioGRID; 36002; 203.
DR ComplexPortal; CPX-1715; TORC1 serine/threonine-protein kinase complex, TOR1 variant.
DR ComplexPortal; CPX-1716; TORC1 serine/threonine-protein kinase complex, TOR2 variant.
DR DIP; DIP-5347N; -.
DR IntAct; Q08921; 22.
DR MINT; Q08921; -.
DR STRING; 4932.YPL180W; -.
DR iPTMnet; Q08921; -.
DR MaxQB; Q08921; -.
DR PaxDb; Q08921; -.
DR PRIDE; Q08921; -.
DR EnsemblFungi; YPL180W_mRNA; YPL180W; YPL180W.
DR GeneID; 855922; -.
DR KEGG; sce:YPL180W; -.
DR SGD; S000006101; TCO89.
DR VEuPathDB; FungiDB:YPL180W; -.
DR eggNOG; ENOG502QR2V; Eukaryota.
DR HOGENOM; CLU_023420_0_0_1; -.
DR InParanoid; Q08921; -.
DR OMA; RISHEYT; -.
DR BioCyc; YEAST:G3O-34075-MON; -.
DR PRO; PR:Q08921; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q08921; protein.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IDA:SGD.
DR GO; GO:0000306; C:extrinsic component of vacuolar membrane; IDA:SGD.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IDA:SGD.
DR GO; GO:0031931; C:TORC1 complex; IPI:SGD.
DR GO; GO:0031505; P:fungal-type cell wall organization; IMP:SGD.
DR GO; GO:0006071; P:glycerol metabolic process; IMP:SGD.
DR GO; GO:0051726; P:regulation of cell cycle; IC:ComplexPortal.
DR GO; GO:0001558; P:regulation of cell growth; IPI:SGD.
DR GO; GO:0007584; P:response to nutrient; IC:ComplexPortal.
DR GO; GO:0009651; P:response to salt stress; IMP:SGD.
DR GO; GO:0031929; P:TOR signaling; IC:SGD.
DR InterPro; IPR018857; TORC1_cplx_su_TCO89.
DR Pfam; PF10452; TCO89; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Membrane; Phosphoprotein; Reference proteome; Vacuole.
FT CHAIN 1..799
FT /note="Target of rapamycin complex 1 subunit TCO89"
FT /id="PRO_0000271786"
FT REGION 18..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 97..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 201..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 324..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 418..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 538..568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 663..685
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..243
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 256..274
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 329..350
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..367
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 368..390
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..432
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 436..457
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 460..476
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 52
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 82
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 84
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 104
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 107
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956"
FT MOD_RES 115
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 144
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 203
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 215
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 290
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 397
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 575
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 707
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
SQ SEQUENCE 799 AA; 88845 MW; 7243C08F4C74633D CRC64;
MVHRGRTLKS DTDVTSLNAS TVSHQSKPFR QFSTRSRAKS NASFKGLRRV LTHDGTLDND
YFNKHNVSQK CKSSDALFRK RTISGLNMTA LTRVKSNQGK RSASFHSPVH NTLLSPKNSS
HSNTGTAGFG LKPRRSKSTQ SVLSLRDAQE SKKSESTTDE EVECFSEDNI EDGKVNNDKV
IAEHVMPEEK KNVQQLNQNE LQSPDSIDEQ EEDKSGTDGK ENHRAVSLPL PHLSSNNYFG
ESSHSIEHQK DGETSPSSIE TKLNATSVIN EEGQSKVTKE ADIDDLSSHS QNLRASLVKA
GDNISEAPYD KEKKILDVGN TLAAHKSNQK PSHSDEQFDQ EDHIDAPRSN SSRKSDSSFM
SLRRQSSKQH KLLNEEEDLI KPDDISSAGT KDIEGHSLLE NYAPNMILSQ STGVERRFEN
SSSIQNSLGN EIHDSGEHMA SGDTFNELDD GKLRKSKKNG GRSQLGQNIP NSQSTFPTIA
NIGSKDNNVP QHNFSTSISS LTNNLRRAAP ESFHGSRMNN IFHKKGNQNL LLRSNDLNKN
SAAPASPLSN EHITSSTNSG SDANRQSNSG AKFNSFAQFL KSDGIDAESR TQRKLWLQRE
NSIMDLSSQN DGSDSIFMAG NIDAKREFER ISHEYSNVKR FYNPLDEALL RVQPIITGNA
NNIRKKSHND AQSIAHSSSD TDHKDEDDLL FTNYDKKFDD LYPHLASAKI QAVLSGIWKS
ESYLFNKDVN PINKNRTTST NHSVGHTASQ NARNLLRGPM GSSTTLHHQR VINSLQPTTR
AVNRRMENVG YMHTQPQQR
