WAT1_SCHPO
ID WAT1_SCHPO Reviewed; 314 AA.
AC O74184;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 144.
DE RecName: Full=Target of rapamycin complex subunit wat1 {ECO:0000305|PubMed:18076573};
DE Short=TORC subunit wat1;
DE AltName: Full=WD repeat-containing protein pop3;
GN Name=pop3 {ECO:0000303|PubMed:11686295};
GN Synonyms=wat1 {ECO:0000303|PubMed:9108274};
GN ORFNames=SPBC21B10.05c {ECO:0000312|PomBase:SPBC21B10.05c};
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 [GENOMIC DNA].
RX PubMed=9108274; DOI=10.1007/s004380050400;
RA Kemp J.T., Balasubramanian M.K., Gould K.L.;
RT "A wat1 mutant of fission yeast is defective in cell morphology.";
RL Mol. Gen. Genet. 254:127-138(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND INTERACTION WITH PRP2.
RC STRAIN=972 / ATCC 24843;
RX PubMed=11686295; DOI=10.1242/jcs.114.16.2911;
RA Ochotorena I.L., Hirata D., Kominami K., Potashkin J., Sahin F.,
RA Wentz-Hunter K., Gould K.L., Sato K., Yoshida Y., Vardy L., Toda T.;
RT "Conserved Wat1/Pop3 WD-repeat protein of fission yeast secures genome
RT stability through microtubule integrity and may be involved in mRNA
RT maturation.";
RL J. Cell Sci. 114:2911-2920(2001).
RN [3]
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 [4]
RP FUNCTION, AND INTERACTION WITH TOR1 AND TOR2.
RX PubMed=17046992; DOI=10.1242/jcs.03241;
RA Alvarez B., Moreno S.;
RT "Fission yeast Tor2 promotes cell growth and represses cell
RT differentiation.";
RL J. Cell Sci. 119:4475-4485(2006).
RN [5]
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 [6]
RP IDENTIFICATION IN THE TORC1 AND THE TORC2 COMPLEXES, PHOSPHORYLATION AT
RP SER-141, AND 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).
RN [7]
RP FUNCTION, AND INTERACTION WITH TOR1 AND TOR2.
RX PubMed=17261596; DOI=10.1128/mcb.01039-06;
RA Matsuo T., Otsubo Y., Urano J., Tamanoi F., Yamamoto M.;
RT "Loss of the TOR kinase Tor2 mimics nitrogen starvation and activates the
RT sexual development pathway in fission yeast.";
RL Mol. Cell. Biol. 27:3154-3164(2007).
CC -!- FUNCTION: component of both TORC1 and TORC2, which regulate multiple
CC cellular processes to control cell growth in response to environmental
CC signals. Nutrient limitation and environmental stress signals cause
CC inactivation of TORC1. Active TORC1 positively controls cell growth and
CC ribosome biogenesis by regulating ribosomal protein gene expression.
CC TORC1 negatively controls G1 cell-cycle arrest, sexual development and
CC amino acid uptake. Represses mating, meiosis and sporulation efficiency
CC by interfering with the functions of the transcription factor ste11 and
CC the meiosis-promoting RNA-binding protein mei2. TORC2 is required for
CC cell survival under various stress conditions. TORC2 positively
CC controls G1 cell-cycle arrest, sexual development and amino acid
CC uptake. Positively regulates amino acid uptake through the control of
CC expression of amino acid permeases (PubMed:17046992, PubMed:18076573,
CC PubMed:17261596). May play a role in mRNA maturation as a coupling
CC protein between splicing and synthesis and/or stabilization.
CC {ECO:0000269|PubMed:11686295, ECO:0000269|PubMed:17046992,
CC ECO:0000269|PubMed:17261596, ECO:0000269|PubMed:18076573}.
CC -!- SUBUNIT: The target of rapamycin complex 1 (TORC1) is composed of at
CC least mip1, pop3/wat1, tco89, toc1 and tor2. The target of rapamycin
CC complex 2 (TORC2) is composed of at least bit61, pop3/wat1, sin1, ste20
CC and tor1 (PubMed:17046992, PubMed:18076573, PubMed:17261596). Interacts
CC with prp2 (PubMed:11686295). {ECO:0000269|PubMed:11686295,
CC ECO:0000269|PubMed:17046992, ECO:0000269|PubMed:17261596,
CC ECO:0000269|PubMed:18076573}.
CC -!- INTERACTION:
CC O74184; P36629: prp2; NbExp=4; IntAct=EBI-1564139, EBI-1024157;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the WD repeat LST8 family. {ECO:0000305}.
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DR EMBL; AB016895; BAA32427.1; -; Genomic_DNA.
DR EMBL; CU329671; CAB57925.1; -; Genomic_DNA.
DR PIR; T39922; T39922.
DR RefSeq; NP_595682.1; NM_001021577.2.
DR AlphaFoldDB; O74184; -.
DR SMR; O74184; -.
DR BioGRID; 277170; 17.
DR IntAct; O74184; 5.
DR STRING; 4896.SPBC21B10.05c.1; -.
DR iPTMnet; O74184; -.
DR PaxDb; O74184; -.
DR EnsemblFungi; SPBC21B10.05c.1; SPBC21B10.05c.1:pep; SPBC21B10.05c.
DR GeneID; 2540645; -.
DR KEGG; spo:SPBC21B10.05c; -.
DR PomBase; SPBC21B10.05c; pop3.
DR VEuPathDB; FungiDB:SPBC21B10.05c; -.
DR eggNOG; KOG0315; Eukaryota.
DR HOGENOM; CLU_000288_57_5_1; -.
DR InParanoid; O74184; -.
DR OMA; VQRNYKH; -.
DR PhylomeDB; O74184; -.
DR Reactome; R-SPO-1257604; PIP3 activates AKT signaling.
DR Reactome; R-SPO-3371571; HSF1-dependent transactivation.
DR Reactome; R-SPO-389357; CD28 dependent PI3K/Akt signaling.
DR Reactome; R-SPO-5218920; VEGFR2 mediated vascular permeability.
DR Reactome; R-SPO-6804757; Regulation of TP53 Degradation.
DR Reactome; R-SPO-9639288; Amino acids regulate mTORC1.
DR PRO; PR:O74184; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0031931; C:TORC1 complex; IDA:PomBase.
DR GO; GO:0031932; C:TORC2 complex; IDA:PomBase.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IMP:PomBase.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR GO; GO:0031929; P:TOR signaling; IBA:GO_Central.
DR GO; GO:0038202; P:TORC1 signaling; EXP:PomBase.
DR GO; GO:0038203; P:TORC2 signaling; EXP:PomBase.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR037588; MLST8.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR19842; PTHR19842; 1.
DR Pfam; PF00400; WD40; 5.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 3.
DR PROSITE; PS50082; WD_REPEATS_2; 5.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cytoplasm; Meiosis; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Sporulation; WD repeat.
FT CHAIN 1..314
FT /note="Target of rapamycin complex subunit wat1"
FT /id="PRO_0000051141"
FT REPEAT 1..35
FT /note="WD 1"
FT REPEAT 38..76
FT /note="WD 2"
FT REPEAT 81..120
FT /note="WD 3"
FT REPEAT 122..161
FT /note="WD 4"
FT REPEAT 165..204
FT /note="WD 5"
FT REPEAT 213..252
FT /note="WD 6"
FT REPEAT 257..296
FT /note="WD 7"
FT MOD_RES 141
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18076573"
SQ SEQUENCE 314 AA; 35133 MW; DC6D1275BDF1E086 CRC64;
MSVQYPPQHS VLLVSSGYDH TIRFWEALSG ICSRTIQHAD SQVNRLCISP DKKFLAAAGN
PHVRLYDINT SSQMPLMTFE GHTNNVTAIA FHCDGKWLAT SSEDGTVKVW DMRAPSVQRN
YDHKSPVNDL LIHPNQGELL SCDQSGRVRA WDLGENSCTH ELIPEEDVPM SSITVGSDGS
MLIAGNNKGN CYVWRMLNHQ GASLLQPVVK FQAHQRYITR CVLSPDVKHL ATCSADATVN
IWSTEDMSFM LERRLQGHQR WVWDCAFSAD STYLVTASSD HVARLWELSS GETIRQYSGH
HKAAVCVALN DYQI
