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   27-MAR-2024, entry version 185.
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; 633.
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; 4932-YER093C; -.
DR   PeptideAtlas; P40061; -.
DR   EnsemblFungi; YER093C_mRNA; YER093C; YER093C.
DR   GeneID; 856828; -.
DR   KEGG; sce:YER093C; -.
DR   AGR; SGD:S000000895; -.
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   OrthoDB; 90320at2759; -.
DR   BioCyc; YEAST:G3O-30260-MONOMER; -.
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   BioGRID-ORCS; 856828; 0 hits in 10 CRISPR screens.
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; NAS:ComplexPortal.
DR   GO; GO:0038203; P:TORC2 signaling; IBA:GO_Central.
DR   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 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; CYTOSOLIC REGULATOR PIANISSIMO; 1.
DR   PANTHER; PTHR13298:SF11; RAPAMYCIN-INSENSITIVE COMPANION OF MTOR; 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; SM01303; RasGEF_N_2; 1.
DR   SMART; SM01307; RICTOR_M; 1.
DR   SMART; SM01308; RICTOR_N; 1.
DR   SMART; SM01310; RICTOR_V; 1.
DR   SUPFAM; SSF48371; ARM repeat; 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
//