RICTR_SCHPO
ID RICTR_SCHPO Reviewed; 1309 AA.
AC Q09743;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 25-MAY-2022, entry version 155.
DE RecName: Full=Target of rapamycin complex 2 subunit ste20 {ECO:0000305|PubMed:18076573};
DE Short=TORC2 subunit ste20;
GN Name=ste20 {ECO:0000303|PubMed:10467002};
GN ORFNames=SPBC12C2.02c {ECO:0000312|PomBase:SPBC12C2.02c};
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], AND FUNCTION.
RX PubMed=10467002; DOI=10.1007/s002940050456;
RA Hilti N., Baumann D., Schweingruber A.M., Bigler P., Schweingruber M.E.;
RT "Gene ste20 controls amiloride sensitivity and fertility in
RT Schizosaccharomyces pombe.";
RL Curr. Genet. 35:585-592(1999).
RN [2]
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 [3]
RP INTERACTION WITH TOR1.
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 [4]
RP IDENTIFICATION IN THE TORC2 COMPLEX, PHOSPHORYLATION AT SER-151 AND
RP THR-1203, 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 [5]
RP INTERACTION WITH TOR1.
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 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:0000269|PubMed:10467002, 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:17046992, ECO:0000269|PubMed:17261596,
CC ECO:0000269|PubMed:18076573}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- PTM: Either Ser-203 or Ser-204 are phosphorylated as well.
CC {ECO:0000269|PubMed:18076573}.
CC -!- SIMILARITY: Belongs to the RICTOR family. {ECO:0000305}.
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DR EMBL; AJ223984; CAA11758.1; -; Genomic_DNA.
DR EMBL; CU329671; CAA90815.1; -; Genomic_DNA.
DR PIR; T39379; T39379.
DR RefSeq; NP_596021.1; NM_001021929.2.
DR AlphaFoldDB; Q09743; -.
DR SMR; Q09743; -.
DR BioGRID; 276393; 200.
DR STRING; 4896.SPBC12C2.02c.1; -.
DR iPTMnet; Q09743; -.
DR MaxQB; Q09743; -.
DR PaxDb; Q09743; -.
DR PRIDE; Q09743; -.
DR EnsemblFungi; SPBC12C2.02c.1; SPBC12C2.02c.1:pep; SPBC12C2.02c.
DR GeneID; 2539845; -.
DR KEGG; spo:SPBC12C2.02c; -.
DR PomBase; SPBC12C2.02c; ste20.
DR VEuPathDB; FungiDB:SPBC12C2.02c; -.
DR eggNOG; KOG3694; Eukaryota.
DR HOGENOM; CLU_001013_1_1_1; -.
DR InParanoid; Q09743; -.
DR OMA; RYVRAGC; -.
DR PhylomeDB; Q09743; -.
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:Q09743; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005938; C:cell cortex; IDA:PomBase.
DR GO; GO:0032153; C:cell division site; HDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0005829; C:cytosol; IDA:PomBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; IMP:PomBase.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR011072; HR1_rho-bd.
DR InterPro; IPR036274; HR1_rpt_sf.
DR InterPro; IPR028268; Pianissimo_fam.
DR InterPro; IPR028267; Pianissimo_N.
DR InterPro; IPR029453; Rictor_IV.
DR InterPro; IPR029451; RICTOR_M.
DR InterPro; IPR029452; RICTOR_V.
DR PANTHER; PTHR13298; PTHR13298; 1.
DR Pfam; PF02185; HR1; 1.
DR Pfam; PF14663; RasGEF_N_2; 1.
DR Pfam; PF14666; RICTOR_M; 1.
DR Pfam; PF14664; RICTOR_N; 1.
DR Pfam; PF14668; RICTOR_V; 1.
DR SMART; SM00742; Hr1; 1.
DR SMART; SM01307; RICTOR_M; 1.
DR SMART; SM01308; RICTOR_N; 1.
DR SMART; SM01310; RICTOR_V; 1.
DR SUPFAM; SSF46585; SSF46585; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS51860; REM_1; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Coiled coil; Meiosis; Membrane; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..1309
FT /note="Target of rapamycin complex 2 subunit ste20"
FT /id="PRO_0000072263"
FT TRANSMEM 285..305
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 392..412
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 504..524
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 564..584
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 926..946
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 984..1004
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 24..110
FT /note="REM-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01207"
FT REGION 105..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 183..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 151
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18076573"
FT MOD_RES 1203
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18076573"
SQ SEQUENCE 1309 AA; 147413 MW; 33EEA6794DBC6A82 CRC64;
MKPVRRGQTD TALDISSHAK TNGDFIKKMN TTDSKRLKLL EDLKGKLEVE CKIRDGAETL
LQVFDTNFKK ETKERKEMLK KKCTDELESS KKKIEELVSS IESFQGENGE AKTGSTSLTR
SASATVSRKS SLQEKYSTRF SYKAGCSDSC SVTVSGTGEL IGPTRNAHSN LTPTVIQRID
FENVNEKNNS SSEDTQPNGK RPSSLQSNFS QFPLNPWLDN IYKACLEGSM KDVIDSSNNL
CEYLHEHSDP AYAKNFSLIT PTILSMLELN VSEVTASVYR LLRHLFLDAT AFSCCQMLNL
PWILSKSLLS GTDAYQIERE QAFRLIRTLY FLSSTEGHED YLSGITRTII SICEHVSDVS
RGIAVETLIE LMIIRPKILF KANGLRVLMI SLIDGSISEN LAASAALALV YLLDDPESAC
YVNLPYDIGI LLSPFTSSSS RDTFNSSEEQ SEQAAKAMKS SAKVASVLLN SWSGLLALST
NDFQALRSIV DTLRVPSFAP RSDVIDLFFL IFQVEYSSWS ESFLAGKRLT VVKNQAVSND
DNINMVNIPD GSNKKYMSLR QHFTAVLLFI FLELGLVESI VCMIRASDDP SASRKATYLL
GEVLRLSDEL LPIHLGAKIQ SLPSLFNMAS QFTAEDRFVA TSVLQSIESL NRVKFHSATQ
PFSQTTSLLF KEQKTDGSFR GQRQVEHVKL KMGMQIDDSH FRSMLAETNV LATKNYQKWR
WDTLVQIMEG PLLSPKRIDE TLRTTKFMRR LLAFYKPFSN RFSSIQNTKP NQKFIKVGCL
VFRTLLANPE GVKYLSESKV IKQIAESLSQ IDGYSEQVSE PIFSNSRLQK TLTHGYFPML
KVLSSQKEGH AIMERWRIFT TLYHLTELRN RDDLIIIFLT NLDYRLEGHT RIIFSKALNT
GQQAVRLTAT KHLAALINSE SANDNLNHWA ISLLIFQLYD PCLEVCKTAV KVLNEVCARN
ENLLAQVVQL QPSLAHLGEI GSPLLLRFLA TTVGFHYLSE INFIEHELDN WYHHRNIDYV
DLLEQNFFLS FVSNLKIIDK KNNEPDENIL PLHFYGELVK SPQGCEVLES SGHFESFMGT
LVEFYDKPLG NEAIRQLKSA LWAIGNIGKT DQGITFLINH DTIPLIVKYA ENSLIPTVRG
TAYFVLGLIS RTSKGVEILE SLHWYSLMSL MGTSQGICIP RHAGQVLSTP RRNVEFVNER
VPTPEFSSLL SSLTNSEREV IRLVSNLSNH VLTNESARQL TKIRSKNAKV FSSKRLVKAC
MTILGKFHYR VQIQQFVFEL FPYSVLLSSS TSQDLNESPS RPNNLSISA
