TSC11_YEAST
ID TSC11_YEAST Reviewed; 1430 AA.
AC P40061; D3DM00;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Target of rapamycin complex 2 subunit TSC11;
DE Short=TORC2 subunit TSC11;
DE AltName: Full=Adheres voraciously to TOR2 protein 3;
DE AltName: Full=Temperature-sensitive CSG2 suppressor protein 11;
GN Name=TSC11; Synonyms=AVO3; OrderedLocusNames=YER093C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 967-1430.
RC STRAIN=ATCC 204508 / S288c;
RA Korch C., Mountain H.A., Wenzlau J.M.;
RT "Structure and regulation of MET6, the vitamin B12-independent methionine
RT synthase gene of Saccharomyces cerevisiae.";
RL Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP IDENTIFICATION IN TORC2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=12408816; DOI=10.1016/s1097-2765(02)00636-6;
RA Loewith R., Jacinto E., Wullschleger S., Lorberg A., Crespo J.L.,
RA Bonenfant D., Oppliger W., Jenoe P., Hall M.N.;
RT "Two TOR complexes, only one of which is rapamycin sensitive, have distinct
RT roles in cell growth control.";
RL Mol. Cell 10:457-468(2002).
RN [5]
RP SUBCELLULAR LOCATION, IDENTIFICATION IN TORC2, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=12631735; DOI=10.1091/mbc.e02-09-0609;
RA Wedaman K.P., Reinke A., Anderson S., Yates J.R. III, McCaffery J.M.,
RA Powers T.;
RT "Tor kinases are in distinct membrane-associated protein complexes in
RT Saccharomyces cerevisiae.";
RL Mol. Biol. Cell 14:1204-1220(2003).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [7]
RP SUBUNIT, INTERACTION WITH TOR2, AND PHOSPHORYLATION.
RX PubMed=16002396; DOI=10.1074/jbc.m505553200;
RA Wullschleger S., Loewith R., Oppliger W., Hall M.N.;
RT "Molecular organization of target of rapamycin complex 2.";
RL J. Biol. Chem. 280:30697-30704(2005).
RN [8]
RP FUNCTION.
RX PubMed=15809876; DOI=10.1007/s00294-005-0570-8;
RA Ho H.-L., Shiau Y.-S., Chen M.-Y.;
RT "Saccharomyces cerevisiae TSC11/AVO3 participates in regulating cell
RT integrity and functionally interacts with components of the Tor2 complex.";
RL Curr. Genet. 47:273-288(2005).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-84, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19; SER-81; SER-87 AND
RP SER-141, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Essential component of TORC2, which regulates cell cycle-
CC dependent polarization of the actin-cytoskeleton and cell wall
CC integrity. TORC2 controls polarity of the actin cytoskeleton, which is
CC required for orienting the secretory pathway toward discrete growth
CC sites, via the RHO1/PKC1/MAPK cell integrity pathway. TSC11 may exert
CC its functions through two distinct mechanisms, one mediated by AVO1 and
CC the other mediated by AVO2 and SLM1. {ECO:0000269|PubMed:15809876}.
CC -!- SUBUNIT: The target of rapamycin complex 2 (TORC2) is composed of at
CC least AVO1, AVO2, BIT61, LST8, TOR2 and TSC11. TORC2 likely forms a
CC homodimer. Contrary to TORC1, TORC2 does not bind to and is not
CC sensitive to FKBP-rapamycin. TSC11 binds to the N-terminal HEAT repeat
CC region in TOR2 and is required for TORC2 integrity by tethering AVO1
CC and AVO2 to the complex. {ECO:0000269|PubMed:12408816,
CC ECO:0000269|PubMed:12631735, ECO:0000269|PubMed:16002396}.
CC -!- INTERACTION:
CC P40061; P41318: LST8; NbExp=2; IntAct=EBI-22621, EBI-28598;
CC P40061; P32600: TOR2; NbExp=5; IntAct=EBI-22621, EBI-19385;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12631735};
CC Peripheral membrane protein {ECO:0000269|PubMed:12631735}; Cytoplasmic
CC side {ECO:0000269|PubMed:12631735}. Vacuole membrane
CC {ECO:0000269|PubMed:12631735}; Peripheral membrane protein
CC {ECO:0000269|PubMed:12631735}; Cytoplasmic side
CC {ECO:0000269|PubMed:12631735}.
CC -!- PTM: Phosphorylated by TOR2; when part of TORC2.
CC {ECO:0000269|PubMed:16002396}.
CC -!- MISCELLANEOUS: Present with 1840 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the RICTOR family. {ECO:0000305}.
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DR EMBL; U18839; AAB64648.1; -; Genomic_DNA.
DR EMBL; U32508; AAB60298.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07754.1; -; Genomic_DNA.
DR PIR; S50596; S50596.
DR RefSeq; NP_011018.1; NM_001178984.1.
DR AlphaFoldDB; P40061; -.
DR SMR; P40061; -.
DR BioGRID; 36838; 631.
DR ComplexPortal; CPX-1717; TORC2 complex.
DR DIP; DIP-4957N; -.
DR IntAct; P40061; 10.
DR MINT; P40061; -.
DR STRING; 4932.YER093C; -.
DR iPTMnet; P40061; -.
DR MaxQB; P40061; -.
DR PaxDb; P40061; -.
DR PRIDE; P40061; -.
DR EnsemblFungi; YER093C_mRNA; YER093C; YER093C.
DR GeneID; 856828; -.
DR KEGG; sce:YER093C; -.
DR SGD; S000000895; TSC11.
DR VEuPathDB; FungiDB:YER093C; -.
DR eggNOG; KOG3694; Eukaryota.
DR GeneTree; ENSGT00390000002096; -.
DR HOGENOM; CLU_001013_1_1_1; -.
DR InParanoid; P40061; -.
DR OMA; QAIISCV; -.
DR BioCyc; YEAST:G3O-30260-MON; -.
DR Reactome; R-SCE-1257604; PIP3 activates AKT signaling.
DR Reactome; R-SCE-389357; CD28 dependent PI3K/Akt signaling.
DR Reactome; R-SCE-5218920; VEGFR2 mediated vascular permeability.
DR Reactome; R-SCE-6804757; Regulation of TP53 Degradation.
DR PRO; PR:P40061; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P40061; protein.
DR GO; GO:0005829; C:cytosol; HDA:SGD.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031932; C:TORC2 complex; IPI:SGD.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR GO; GO:0030950; P:establishment or maintenance of actin cytoskeleton polarity; IMP:SGD.
DR GO; GO:0031505; P:fungal-type cell wall organization; IMP:SGD.
DR GO; GO:0001558; P:regulation of cell growth; IPI:SGD.
DR GO; GO:0030148; P:sphingolipid biosynthetic process; IMP:SGD.
DR GO; GO:0031929; P:TOR signaling; IC:SGD.
DR GO; GO:0038203; P:TORC2 signaling; IBA:GO_Central.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
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; 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; SM01307; RICTOR_M; 1.
DR SMART; SM01308; RICTOR_N; 1.
DR SMART; SM01310; RICTOR_V; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Coiled coil; Guanine-nucleotide releasing factor; Membrane;
KW Phosphoprotein; Reference proteome; Vacuole.
FT CHAIN 1..1430
FT /note="Target of rapamycin complex 2 subunit TSC11"
FT /id="PRO_0000202640"
FT DOMAIN 995..1100
FT /note="N-terminal Ras-GEF"
FT REGION 1..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 182..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 91..180
FT /evidence="ECO:0000255"
FT COMPBIAS 186..206
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..225
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..279
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 81
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 84
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 87
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 141
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 1430 AA; 164368 MW; 07BB5D75BA204E50 CRC64;
MSIPHSAKQS SPLSSRRRSV TNTTPLLTPR HSRDNSSTQI SSAKNITSSS PSTITNESSK
RNKQNLVLST SFISTKRLEN SAPSPTSPLM ARRTRSTMTK ALLNLKAEIN NQYQELARLR
KKKDDIEHLR DSTISDIYSG SYSTNHLQKH SMRIRANTQL REIDNSIKRV EKHIFDLKQQ
FDKKRQRSLT TSSSIKADVG SIRNDDGQNN DSEELGDHDS LTDQVTLDDE YLTTPTSGTE
RNSQQNLNRN STVNSRNNEN HSTLSIPDLD GSNKVNLTGD TEKDLGDLEN ENQIFTSTTT
EAATWLVSDY MQSFQEKNVN PDFIAQKANG LVTLLKEHSE IRKDLVLTSF MSSIQNLLLN
GNKLIAASAY RVCRYLINSS IFIDELLELR LDAFIIISLA KDNSFQIERE QALKMVRRFI
EYNNGVTQGI MQAIISCVEK PEDSLRHMAL ETLLELCFVA PEMVKECRGM RVIEGFLQDY
TSFSLASVIL DTILQLMATH KTRQHFLEDF NVSVLTTVFS DTNTKSNVNV EKMQNASTLI
SITLNSYNGF MLFSNNNFKP LKQLVSFFQI PICAQYLIDI FLDVLKIKPL PYKPRGRHSH
SFKPIPSQYY KECMSVNQRL ALIVLILENS EFVPHLLELL NEEDRDDHLV AKGRYLLTEY
FNLRMNLVDK KYTSVSKPIY KENFTYVNET FQFKKIAYKM NRNRNTIGMS GIDYAQNIKS
FSKNIKENTL LREVDDFRFR RMVYDSKVLQ TKDFTRWNWN IINELLEGPL LNKKQLEELV
KSTKFIRRLL VFYRPLRLRF SNVNKGAKLS QKYVQVGCQF FKTLTATPEG MKILMDDTKI
IPQLASLMFR AMEGNISGNI FNKNKLREKI IFGYFKFIGI LTQSKNGVHI LTRWNFFTVI
YKMFQFESKL GLEFLLLTIP ELDLKYSSHC RVIIGKALVV ANEKVRIEAT KHIGDKLKEL
LSTKESDLKL KANKVKLQQF KMEMLTRQLY DLSPSVVAVA DQALYECIVA GNGSEELGTS
FRMFLNQMVF IRSPILFELL SRPYGFQLLN EINFVKEERD SWLSKKNIEY VHIVEEFLKK
NESINAKSLT FQQKSRLPLH FYESLTKTED GILLLSQTGD LVTFMNVIKK YVNGNNMATV
ENAKEILDLK AALWCVGFIG STELGIGLLD NYSLVEDIIE VAYNASVTSV RFTAFYVLGL
ISMTREGCEI LDEMGWNCCV SVQDEPIGIA LPNRLDRFLS YNEHKWSAFG EYSDEMIVFN
KSDGDLIEKC LPIEFDLDKL LKEKDTAENP LNEKIITNKY DNDITSQTIT VSGENSSLFA
NEGLSSPYVT QYRNDDDSIE SKVLHIVSQL GNHILSNHAV KEITEINNKY GPRLFENEKM
FFKVFNMMSK YRFKPHVRKF LCGLFINNRA LENVIRHDNK RDKRPANFTR
