BIT61_SCHPO
ID BIT61_SCHPO Reviewed; 422 AA.
AC O74547;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Target of rapamycin complex 2 subunit bit61 {ECO:0000303|PubMed:18076573};
DE Short=TORC2 subunit bit61;
GN Name=bit61 {ECO:0000303|PubMed:18076573};
GN ORFNames=SPCC777.08c {ECO:0000312|PomBase:SPCC777.08c};
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 TORC2 COMPLEX, PHOSPHORYLATION AT SER-109 AND
RP SER-132, 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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-201, AND IDENTIFICATION BY
RP 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 TORC2, which regulates multiple cellular
CC processes to control cell growth in response to environmental signals.
CC TORC2 is required for cell survival under various stress conditions.
CC TORC2 positively controls G1 cell-cycle arrest, sexual development and
CC amino acid uptake. Positively regulates amino acid uptake through the
CC control of expression of amino acid permeases.
CC {ECO:0000305|PubMed:18076573}.
CC -!- SUBUNIT: The target of rapamycin complex 2 (TORC2) is composed of at
CC least bit61, pop3/wat1, sin1, ste20 and tor1.
CC {ECO:0000269|PubMed:18076573}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
CC -!- PTM: Either Thr-23, Thr-25 or Ser-26 and Ser-78 or Ser-79 are
CC phosphorylated as well. {ECO:0000269|PubMed:18076573}.
CC -!- SIMILARITY: Belongs to the BIT61 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; CU329672; CAA20712.1; -; Genomic_DNA.
DR PIR; T11714; T11714.
DR RefSeq; NP_588254.1; NM_001023244.2.
DR AlphaFoldDB; O74547; -.
DR BioGRID; 275537; 10.
DR IntAct; O74547; 1.
DR STRING; 4896.SPCC777.08c.1; -.
DR iPTMnet; O74547; -.
DR MaxQB; O74547; -.
DR PaxDb; O74547; -.
DR PRIDE; O74547; -.
DR EnsemblFungi; SPCC777.08c.1; SPCC777.08c.1:pep; SPCC777.08c.
DR GeneID; 2538963; -.
DR KEGG; spo:SPCC777.08c; -.
DR PomBase; SPCC777.08c; bit61.
DR VEuPathDB; FungiDB:SPCC777.08c; -.
DR eggNOG; ENOG502RZ40; Eukaryota.
DR HOGENOM; CLU_650803_0_0_1; -.
DR InParanoid; O74547; -.
DR OMA; PFNGQWP; -.
DR Reactome; R-SPO-1257604; PIP3 activates AKT signaling.
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 PRO; PR:O74547; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0031932; C:TORC2 complex; IDA:PomBase.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0038203; P:TORC2 signaling; IPI:PomBase.
DR InterPro; IPR013745; Bit61/PRR5.
DR PANTHER; PTHR32428; PTHR32428; 2.
DR Pfam; PF08539; HbrB; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cytoplasm; Meiosis; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..422
FT /note="Target of rapamycin complex 2 subunit bit61"
FT /id="PRO_0000352803"
FT REGION 48..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..87
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 109
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18076573"
FT MOD_RES 132
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18076573"
FT MOD_RES 201
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 422 AA; 46863 MW; FDEE90C6C2AE9BE2 CRC64;
MVGRGSFSST SSASSINWIP KNTKTSIESV SNTISLSENG QNQDLETVTT KESNVGDSDT
TENIKSPFNG QWPFSRRSSQ SSSHPVFEET HWSKHSKRPG KLNVLTPTSP SNVNAEVQSI
STKTQLSLLN LSPHKHKKPK DGLDLSALQK TLNGSRNFLR GRRDAGGIFG ASIPQSLVTN
QIINGFGAAS LAFAKLGKVR SPLEGRFNLV PISADETWLI VESEVCSLYS GEALHYSLED
LNGILILHLQ ALIRDTKMNE FVGHLETLFR KATKCLSDSL SPVPEELFLN RIIETWLFFF
SSVLPYVQGV FLPIKTKLFD EQEKTQLPYE VNEFCSTNRE KLNVHRLALM TFRDYMVLPI
ANRIQICIGR AESAENALDN AGEVFARLFQ ILSLLASVRT NDSKEQEITN LATKVRCLLI
AS
