TOC1_SCHPO
ID TOC1_SCHPO Reviewed; 430 AA.
AC Q9HDW0;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 78.
DE RecName: Full=Target of rapamycin complex 1 subunit toc1 {ECO:0000303|PubMed:18076573};
DE Short=TORC1 subunit toc1;
GN Name=toc1 {ECO:0000303|PubMed:18076573};
GN ORFNames=SPBP18G5.03 {ECO:0000312|PomBase:SPBP18G5.03};
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, AND IDENTIFICATION BY MASS
RP 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).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-204 AND SER-399, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
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}.
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DR EMBL; CU329671; CAC21491.1; -; Genomic_DNA.
DR RefSeq; NP_595993.1; NM_001021900.2.
DR AlphaFoldDB; Q9HDW0; -.
DR SMR; Q9HDW0; -.
DR BioGRID; 277822; 38.
DR IntAct; Q9HDW0; 1.
DR STRING; 4896.SPBP18G5.03.1; -.
DR iPTMnet; Q9HDW0; -.
DR MaxQB; Q9HDW0; -.
DR PaxDb; Q9HDW0; -.
DR PRIDE; Q9HDW0; -.
DR EnsemblFungi; SPBP18G5.03.1; SPBP18G5.03.1:pep; SPBP18G5.03.
DR GeneID; 2541310; -.
DR KEGG; spo:SPBP18G5.03; -.
DR PomBase; SPBP18G5.03; toc1.
DR VEuPathDB; FungiDB:SPBP18G5.03; -.
DR HOGENOM; CLU_638031_0_0_1; -.
DR OMA; PMTIQSS; -.
DR PRO; PR:Q9HDW0; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0031931; C:TORC1 complex; IPI: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; IPI:PomBase.
PE 1: Evidence at protein level;
KW Cell cycle; Cytoplasm; Meiosis; Phosphoprotein; Reference proteome;
KW Sporulation.
FT CHAIN 1..430
FT /note="Target of rapamycin complex 1 subunit toc1"
FT /id="PRO_0000304016"
FT MOD_RES 204
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 399
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 430 AA; 48792 MW; F1EE640B81904606 CRC64;
MQLQSPFGDG ISCECLNIRV LGIPNETKHQ WIFVPRDLIK IKIYSLLQIC KAENCSAVAC
RGCNLCILAV QGNIEISEEP QKLFQEENVK VYIYDSAISL SSVRASFPIS ELGIRMDIIK
ARAEPREDEI RASFSSLVNK EIKRTVEELL LSKRSTNRLS LLAFMRNQQL NYEAYETKLL
EDASTIEKSL EKEVKTIYDS NIASPKESSD AIDADHAMID ESRSTQRRKS KPKKHVAFTD
EYQVAFSDKP GKYFNQPMQY SKQFKLDNPD YEASSDSLND IENLSTLTFR SDEELEFDFD
TNNINNNKSG DSLEMSTTIP SDEENEDFTS KVDAMEIHSG SLPLNIDSSP IFTNHSPSSS
LSSESSFEAS PSSFVDRKNR WIQMLKKADE HSRSIQARSM GYVLSDDLDN SKAFRPYKQS
FLAQGWKSLN