ID   RTS3_YEAST              Reviewed;         263 AA.
AC   P53289; D6VUU0; Q7ZA12;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   27-MAR-2024, entry version 143.
DE   RecName: Full=Protein phosphatase type 2A regulatory subunit RTS3;
GN   Name=RTS3; OrderedLocusNames=YGR161C;
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 [GENOMIC DNA], AND VARIANTS ILE-20 AND SER-201.
RA   Reis V.C.B., Torres F.A.G.;
RT   "Polymorphism detected in the yeast ORF YGR161C.";
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9290212;
RX   DOI=10.1002/(sici)1097-0061(19970915)13:11<1077::aid-yea152>3.0.co;2-y;
RA   Rieger M., Brueckner M., Schaefer M., Mueller-Auer S.;
RT   "Sequence analysis of 203 kilobases from Saccharomyces cerevisiae
RT   chromosome VII.";
RL   Yeast 13:1077-1090(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169869;
RA   Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA   Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA   Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA   Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA   Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA   Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA   Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA   Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA   Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA   Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA   Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA   Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA   Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA   Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA   Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA   Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA   Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA   Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA   Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA   Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA   Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA   Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL   Nature 387:81-84(1997).
RN   [4]
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   [5]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(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   FUNCTION.
RX   PubMed=14566057; DOI=10.1073/pnas.2132527100;
RA   Samanta M.P., Liang S.;
RT   "Predicting protein functions from redundancies in large-scale protein
RT   interaction networks.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:12579-12583(2003).
RN   [8]
RP   FUNCTION.
RX   PubMed=16713564; DOI=10.1016/j.cell.2006.03.038;
RA   Queralt E., Lehane C., Novak B., Uhlmann F.;
RT   "Downregulation of PP2A(Cdc55) phosphatase by separase initiates mitotic
RT   exit in budding yeast.";
RL   Cell 125:719-732(2006).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-192, 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   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-172; SER-214 AND SER-238, AND
RP   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).
RN   [11]
RP   FUNCTION.
RX   PubMed=21360731; DOI=10.1002/yea.1830;
RA   Hood-DeGrenier J.K.;
RT   "Identification of phosphatase 2A-like Sit4-mediated signalling and
RT   ubiquitin-dependent protein sorting as modulators of caffeine sensitivity
RT   in S. cerevisiae.";
RL   Yeast 28:189-204(2011).
CC   -!- FUNCTION: May be a component of a protein phosphatase type 2A (PP2A)
CC       complex. Negatively regulates SIT4 phosphatase, a modulators of
CC       caffeine sensitivity. {ECO:0000269|PubMed:14566057,
CC       ECO:0000269|PubMed:16713564, ECO:0000269|PubMed:21360731}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC       {ECO:0000269|PubMed:14562095}.
CC   -!- MISCELLANEOUS: Present with 2100 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
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DR   EMBL; AY301067; AAP48998.1; -; Genomic_DNA.
DR   EMBL; Z72946; CAA97175.1; -; Genomic_DNA.
DR   EMBL; BK006941; DAA08251.1; -; Genomic_DNA.
DR   PIR; S64472; S64472.
DR   RefSeq; NP_011677.3; NM_001181290.3.
DR   AlphaFoldDB; P53289; -.
DR   SMR; P53289; -.
DR   BioGRID; 33408; 115.
DR   DIP; DIP-6319N; -.
DR   IntAct; P53289; 15.
DR   MINT; P53289; -.
DR   STRING; 4932.YGR161C; -.
DR   iPTMnet; P53289; -.
DR   MaxQB; P53289; -.
DR   PaxDb; 4932-YGR161C; -.
DR   PeptideAtlas; P53289; -.
DR   EnsemblFungi; YGR161C_mRNA; YGR161C; YGR161C.
DR   GeneID; 853065; -.
DR   KEGG; sce:YGR161C; -.
DR   AGR; SGD:S000003393; -.
DR   SGD; S000003393; RTS3.
DR   VEuPathDB; FungiDB:YGR161C; -.
DR   eggNOG; ENOG502SBUT; Eukaryota.
DR   HOGENOM; CLU_1058272_0_0_1; -.
DR   InParanoid; P53289; -.
DR   OrthoDB; 2015436at2759; -.
DR   BioCyc; YEAST:G3O-30860-MONOMER; -.
DR   BioGRID-ORCS; 853065; 6 hits in 10 CRISPR screens.
DR   PRO; PR:P53289; -.
DR   Proteomes; UP000002311; Chromosome VII.
DR   RNAct; P53289; Protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0005634; C:nucleus; HDA:SGD.
PE   1: Evidence at protein level;
KW   Cytoplasm; Nucleus; Phosphoprotein; Reference proteome.
FT   CHAIN           1..263
FT                   /note="Protein phosphatase type 2A regulatory subunit RTS3"
FT                   /id="PRO_0000202835"
FT   REGION          1..62
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          149..176
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        10..24
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        44..61
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        154..176
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         172
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         192
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MOD_RES         214
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         238
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   VARIANT         20
FT                   /note="V -> I"
FT                   /evidence="ECO:0000269|Ref.1"
FT   VARIANT         201
FT                   /note="P -> S"
FT                   /evidence="ECO:0000269|Ref.1"
SQ   SEQUENCE   263 AA;  29263 MW;  BA31D32B9ADF02AB CRC64;
     MIATSRAVNM NKESKHKKAV AKPCRERQTS VTRAMRPAVA RDPRRLSTSS SPSSSPMSAQ
     RRLSREEIIN EMEKEQDAIV VRLLREIETL KEENSRLKNQ LHHPVPARRS SPFFEGESAI
     LDDDDCNYGY TLDTPKLKLT DGASRHTVLP LTPKDSMTHI SHSARRSSRN ASISNGTSIS
     DTIFPIETKI HSAPTTNRNL PSADLPHHTL LPRSLSGISS SDLTESGALL HDRRRRSSNY
     SLDGSNSLKA DLMAKRFQTG SLK
//