TCO89_SCHPO
ID TCO89_SCHPO Reviewed; 451 AA.
AC O74428; Q7LL02;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1999, sequence version 2.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Target of rapamycin complex 1 subunit tco89 {ECO:0000303|PubMed:18076573};
DE Short=TORC1 subunit tco89;
GN Name=tco89 {ECO:0000303|PubMed:18076573};
GN ORFNames=SPCC162.12 {ECO:0000312|PomBase:SPCC162.12}, SPCC1753.06c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [3]
RP IDENTIFICATION IN THE TORC1 COMPLEX, PHOSPHORYLATION AT SER-70, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18076573; DOI=10.1111/j.1365-2443.2007.01141.x;
RA Hayashi T., Hatanaka M., Nagao K., Nakaseko Y., Kanoh J., Kokubu A.,
RA Ebe M., Yanagida M.;
RT "Rapamycin sensitivity of the Schizosaccharomyces pombe tor2 mutant and
RT organization of two highly phosphorylated TOR complexes by specific and
RT common subunits.";
RL Genes Cells 12:1357-1370(2007).
CC -!- FUNCTION: Component of TORC1, which regulates multiple cellular
CC processes to control cell growth in response to environmental signals.
CC Tor2 is essential for growth. Nutrient limitation and environmental
CC stress signals cause inactivation of TORC1. Active TORC1 positively
CC controls cell growth and ribosome biogenesis by regulating ribosomal
CC protein gene expression. TORC1 negatively controls G1 cell-cycle
CC arrest, sexual development and amino acid uptake. Represses mating,
CC meiosis and sporulation efficiency by interfering with the functions of
CC the transcription factor ste11 and the meiosis-promoting RNA-binding
CC protein mei2. {ECO:0000305|PubMed:18076573}.
CC -!- SUBUNIT: The target of rapamycin complex 1 (TORC1) is composed of at
CC least mip1, pop3/wat1, tco89, toc1 and tor2.
CC {ECO:0000269|PubMed:18076573}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
CC Note=Localizes at the barrier septum.
CC -!- PTM: Either Thr-10, Ser-11, Ser-12, Ser-13 or Thr-14 and Ser-214 or
CC Ser-215 and Ser-247 or Ser-249 are phosphorylated as well.
CC {ECO:0000269|PubMed:18076573}.
CC -!- SIMILARITY: Belongs to the TORC subunit TCO89 family. {ECO:0000305}.
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DR EMBL; CU329672; CAA22780.1; -; Genomic_DNA.
DR PIR; T41129; T41129.
DR RefSeq; NP_588232.1; NM_001023222.2.
DR AlphaFoldDB; O74428; -.
DR BioGRID; 275567; 42.
DR IntAct; O74428; 1.
DR STRING; 4896.SPCC162.12.1; -.
DR iPTMnet; O74428; -.
DR MaxQB; O74428; -.
DR PaxDb; O74428; -.
DR PRIDE; O74428; -.
DR EnsemblFungi; SPCC162.12.1; SPCC162.12.1:pep; SPCC162.12.
DR GeneID; 2538993; -.
DR KEGG; spo:SPCC162.12; -.
DR PomBase; SPCC162.12; tco89.
DR VEuPathDB; FungiDB:SPCC162.12; -.
DR HOGENOM; CLU_534367_0_0_1; -.
DR OMA; REIVYEF; -.
DR PRO; PR:O74428; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0032153; C:cell division site; HDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0031931; C:TORC1 complex; IDA:PomBase.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR GO; GO:0038202; P:TORC1 signaling; IC:PomBase.
DR InterPro; IPR018857; TORC1_cplx_su_TCO89.
DR Pfam; PF10452; TCO89; 3.
PE 1: Evidence at protein level;
KW Cell cycle; Cytoplasm; Meiosis; Phosphoprotein; Reference proteome;
KW Sporulation.
FT CHAIN 1..451
FT /note="Target of rapamycin complex 1 subunit tco89"
FT /id="PRO_0000304086"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 122..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 176..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 362..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..162
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..264
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 362..421
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 70
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18076573"
SQ SEQUENCE 451 AA; 49212 MW; 01D0A3FB3ED99305 CRC64;
MERPSLSRRT SSSTVSTDGE GVYSRSTKER KRNFIVNSRL KRGGGHVRVN RSGRLGSVTM
RPSALTRAHS QNPNSSLVNN SSAVSHLTKQ RSLNDLHELN GPKHVAKNGL IPLTQRKPNC
VWDDAPVDND STAGNLDSDS ALPTPSVTTN EAADSSRASS PVTRVVAVHD NKKKIINSNI
SNAPPFNNTD VQASARPPAA GQDDSAADAS TTKSSPVHNE VMAEPLPHSN NREVTQATNQ
PKWQIHSGSD IASEPPTLSR GNSLSLLANR KVPSTNVKKS QAELYDLGSS TSRTQQKLLI
QRASSKFDIV EDDMDTNPSK RFSNPHTKHI MDLVRTQYRN VLRTRELIPE FLEKIRSSYS
NNQNFDSQNA FNTSAAGTAG TREETISNGQ NGIVASAETS KKDDGVQSAS LNASMSARSH
ARQRSIHVPK TRKDTDYESI HQKLLQLWSQ G
