BIT61_YEAST
ID BIT61_YEAST Reviewed; 543 AA.
AC P47041; D6VWC4;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Target of rapamycin complex 2 subunit BIT61;
DE Short=TORC2 subunit BIT61;
DE AltName: Full=61 kDa binding partner of TOR2 protein;
GN Name=BIT61; OrderedLocusNames=YJL058C; ORFNames=J1141;
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=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
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].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
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 [5]
RP FUNCTION, IDENTIFICATION IN TORC2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=14736892; DOI=10.1074/jbc.m313062200;
RA Reinke A., Anderson S., McCaffery J.M., Yates J.R. III, Aronova S., Chu S.,
RA Fairclough S., Iverson C., Wedaman K.P., Powers T.;
RT "TOR complex 1 includes a novel component, Tco89p (YPL180w), and cooperates
RT with Ssd1p to maintain cellular integrity in Saccharomyces cerevisiae.";
RL J. Biol. Chem. 279:14752-14762(2004).
RN [6]
RP INTERACTION WITH SLM1 AND SLM2.
RX PubMed=15689497; DOI=10.1091/mbc.e04-07-0564;
RA Fadri M., Daquinag A., Wang S., Xue T., Kunz J.;
RT "The pleckstrin homology domain proteins Slm1 and Slm2 are required for
RT actin cytoskeleton organization in yeast and bind phosphatidylinositol-4,5-
RT bisphosphate and TORC2.";
RL Mol. Biol. Cell 16:1883-1900(2005).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-144, 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 [8]
RP IDENTIFICATION BY 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-58; SER-59; SER-139 AND
RP SER-144, 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: Component of TORC2, which regulates cell cycle-dependent
CC polarization of the actin-cytoskeleton and cell wall integrity. TORC2
CC controls polarity of the actin cytoskeleton, which is required for
CC orienting the secretory pathway toward discrete growth sites, via the
CC RHO1/PKC1/MAPK cell integrity pathway. {ECO:0000269|PubMed:14736892}.
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. {ECO:0000269|PubMed:14736892}.
CC -!- INTERACTION:
CC P47041; P32600: TOR2; NbExp=2; IntAct=EBI-25889, EBI-19385;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein;
CC Cytoplasmic side. Vacuole membrane {ECO:0000305}; Peripheral membrane
CC protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC -!- MISCELLANEOUS: Present with 1960 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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; Z49333; CAA89349.1; -; Genomic_DNA.
DR EMBL; AY693068; AAT93087.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08740.1; -; Genomic_DNA.
DR PIR; S56830; S56830.
DR RefSeq; NP_012477.1; NM_001181491.1.
DR AlphaFoldDB; P47041; -.
DR BioGRID; 33696; 99.
DR ComplexPortal; CPX-1717; TORC2 complex.
DR DIP; DIP-1444N; -.
DR IntAct; P47041; 16.
DR MINT; P47041; -.
DR STRING; 4932.YJL058C; -.
DR iPTMnet; P47041; -.
DR MaxQB; P47041; -.
DR PaxDb; P47041; -.
DR PRIDE; P47041; -.
DR EnsemblFungi; YJL058C_mRNA; YJL058C; YJL058C.
DR GeneID; 853388; -.
DR KEGG; sce:YJL058C; -.
DR SGD; S000003594; BIT61.
DR VEuPathDB; FungiDB:YJL058C; -.
DR eggNOG; ENOG502RZ40; Eukaryota.
DR GeneTree; ENSGT00940000176511; -.
DR HOGENOM; CLU_037144_0_0_1; -.
DR InParanoid; P47041; -.
DR OMA; HYLLAVF; -.
DR BioCyc; YEAST:G3O-31521-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:P47041; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P47041; protein.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0031932; C:TORC2 complex; IDA:SGD.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030950; P:establishment or maintenance of actin cytoskeleton polarity; IPI:SGD.
DR GO; GO:0031505; P:fungal-type cell wall organization; IPI:SGD.
DR GO; GO:0001558; P:regulation of cell growth; IPI:SGD.
DR GO; GO:0031929; P:TOR signaling; IC:ComplexPortal.
DR GO; GO:0038203; P:TORC2 signaling; IBA:GO_Central.
DR InterPro; IPR013745; Bit61/PRR5.
DR PANTHER; PTHR32428; PTHR32428; 1.
DR Pfam; PF08539; HbrB; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Membrane; Phosphoprotein; Reference proteome; Vacuole.
FT CHAIN 1..543
FT /note="Target of rapamycin complex 2 subunit BIT61"
FT /id="PRO_0000203060"
FT REGION 93..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 58
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 59
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 139
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 144
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
SQ SEQUENCE 543 AA; 60841 MW; 99F0F96840311F4B CRC64;
MTAEDILLRE RTSTTTQRPV NSEQYLNVQL ATAPVKNFQT TSEISRQTLV DTSNDDVYSI
KNLKGSRNPI SPSVSNVGFQ SIFHTVDHPR SKVSVASNHS LRSNDNASAA TSKSGSSQIG
ESHSVDTVEC SNNLSKKLSS DAISITQKSL HSTPSGRYMK GKASGFFNRR NRAHTTISSD
PASFLTDSST LHNSSHSFRN VIKNFFQNKS HRHIGQDAIE PAIPNSLSKF LHSSYGRHKS
PSQFIHTNAG QLVDSGTSVY SLNVNPSGVN PNTIVEDPLS GTDPASPNPV SMLHDLLRNL
PSLEANYKHF NSQELTTLTN NIWNIFCSNV AELFRTQRIW KLRAKIENFN EVLEFYCILK
TDPRVTHSGM NRIISDLKEF LVSSLYNLEN QIVFNYSNED TINNALKRLG VIWRIFYQEV
YYDLAAVLLP LDQSIREDGN STVLKSGNES RTHINGNYSI GFLLLMCFRD SIVLPCYENF
VNSNDGISKS FQLYIFNQEE ESNVTETDKL TLLQCFGILS TIQSNDRNQR IIEELLAGIR
MSI
