TOS3_YEAST
ID TOS3_YEAST Reviewed; 560 AA.
AC P43637; D6VTX4;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Serine/threonine-protein kinase TOS3;
DE EC=2.7.11.1;
DE AltName: Full=Target of SBF protein 3;
GN Name=TOS3; OrderedLocusNames=YGL179C; ORFNames=G1618;
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].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=7668046; DOI=10.1002/yea.320110808;
RA Coglievina M., Bertani I., Klima R., Zaccaria P., Bruschi C.V.;
RT "The DNA sequence of a 7941 bp fragment of the left arm of chromosome VII
RT of Saccharomyces cerevisiae contains four open reading frames including the
RT multicopy suppressor gene of the pop2 mutation and a putative
RT serine/threonine protein kinase gene.";
RL Yeast 11:767-774(1995).
RN [2]
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 [3]
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 [4]
RP FUNCTION.
RX PubMed=11062466; DOI=10.1038/81576;
RA Zhu H., Klemic J.F., Chang S., Bertone P., Casamayor A., Klemic K.G.,
RA Smith D., Gerstein M., Reed M.A., Snyder M.;
RT "Analysis of yeast protein kinases using protein chips.";
RL Nat. Genet. 26:283-289(2000).
RN [5]
RP FUNCTION.
RX PubMed=12906789; DOI=10.1016/s0960-9822(03)00459-7;
RA Sutherland C.M., Hawley S.A., McCartney R.R., Leech A., Stark M.J.R.,
RA Schmidt M.C., Hardie D.G.;
RT "Elm1p is one of three upstream kinases for the Saccharomyces cerevisiae
RT SNF1 complex.";
RL Curr. Biol. 13:1299-1305(2003).
RN [6]
RP AUTOPHOSPHORYLATION, AND PHOSPHORYLATION OF GAL83; MIG1 AND SIP2.
RX PubMed=12748292; DOI=10.1128/mcb.23.11.3909-3917.2003;
RA Nath N., McCartney R.R., Schmidt M.C.;
RT "Yeast Pak1 kinase associates with and activates Snf1.";
RL Mol. Cell. Biol. 23:3909-3917(2003).
RN [7]
RP PHOSPHORYLATION OF SNF1.
RX PubMed=12847291; DOI=10.1073/pnas.1533136100;
RA Hong S.-P., Leiper F.C., Woods A., Carling D., Carlson M.;
RT "Activation of yeast Snf1 and mammalian AMP-activated protein kinase by
RT upstream kinases.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:8839-8843(2003).
RN [8]
RP FUNCTION.
RX PubMed=15340085; DOI=10.1128/mcb.24.18.8255-8263.2004;
RA Hedbacker K., Hong S.-P., Carlson M.;
RT "Pak1 protein kinase regulates activation and nuclear localization of Snf1-
RT Gal83 protein kinase.";
RL Mol. Cell. Biol. 24:8255-8263(2004).
RN [9]
RP FUNCTION.
RX PubMed=16054096; DOI=10.1016/j.cmet.2005.06.005;
RA Woods A., Dickerson K., Heath R., Hong S.-P., Momcilovic M.,
RA Johnstone S.R., Carlson M., Carling D.;
RT "Ca2+/calmodulin-dependent protein kinase kinase-beta acts upstream of AMP-
RT activated protein kinase in mammalian cells.";
RL Cell Metab. 2:21-33(2005).
RN [10]
RP FUNCTION.
RX PubMed=15824893; DOI=10.1007/s00294-005-0576-2;
RA McCartney R.R., Rubenstein E.M., Schmidt M.C.;
RT "Snf1 kinase complexes with different beta subunits display stress-
RT dependent preferences for the three Snf1-activating kinases.";
RL Curr. Genet. 47:335-344(2005).
RN [11]
RP FUNCTION.
RX PubMed=15879520; DOI=10.1128/ec.4.5.861-866.2005;
RA Kim M.-D., Hong S.-P., Carlson M.;
RT "Role of Tos3, a Snf1 protein kinase kinase, during growth of Saccharomyces
RT cerevisiae on nonfermentable carbon sources.";
RL Eukaryot. Cell 4:861-866(2005).
RN [12]
RP FUNCTION.
RX PubMed=16201971; DOI=10.1042/bj20051213;
RA Elbing K., McCartney R.R., Schmidt M.C.;
RT "Purification and characterization of the three Snf1-activating kinases of
RT Saccharomyces cerevisiae.";
RL Biochem. J. 393:797-805(2006).
RN [13]
RP FUNCTION, AND DOMAIN.
RX PubMed=16607009; DOI=10.1128/ec.5.4.620-627.2006;
RA Rubenstein E.M., McCartney R.R., Schmidt M.C.;
RT "Regulatory domains of Snf1-activating kinases determine pathway
RT specificity.";
RL Eukaryot. Cell 5:620-627(2006).
RN [14]
RP FUNCTION.
RX PubMed=16835226; DOI=10.1074/jbc.m604399200;
RA Momcilovic M., Hong S.-P., Carlson M.;
RT "Mammalian TAK1 activates Snf1 protein kinase in yeast and phosphorylates
RT AMP-activated protein kinase in vitro.";
RL J. Biol. Chem. 281:25336-25343(2006).
RN [15]
RP FUNCTION.
RX PubMed=17438333; DOI=10.1074/jbc.m700146200;
RA Hong S.-P., Carlson M.;
RT "Regulation of snf1 protein kinase in response to environmental stress.";
RL J. Biol. Chem. 282:16838-16845(2007).
CC -!- FUNCTION: One of the three SNF1 protein kinases (with SAK1 and ELM1)
CC which are required for growth on nonfermentable carbon sources and
CC nonpreferred sugars and for response to environmental stress. Activates
CC SNF1 by phosphorylation of its activation-loop 'Thr-210'. Required for
CC the regulation by SNF1 of the transcription of a large set of genes,
CC the modification the activity of metabolic enzymes, and the control of
CC various nutrient-responsive cellular developmental processes.
CC Phosphorylates also GAL83, MIG1 and SIP2. {ECO:0000269|PubMed:11062466,
CC ECO:0000269|PubMed:12906789, ECO:0000269|PubMed:15340085,
CC ECO:0000269|PubMed:15824893, ECO:0000269|PubMed:15879520,
CC ECO:0000269|PubMed:16054096, ECO:0000269|PubMed:16201971,
CC ECO:0000269|PubMed:16607009, ECO:0000269|PubMed:16835226,
CC ECO:0000269|PubMed:17438333}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- DOMAIN: The C-terminus (residues 351 to 560) is required for efficient
CC SNF1 pathway signaling. {ECO:0000269|PubMed:16607009}.
CC -!- PTM: Autophosphorylated. {ECO:0000269|PubMed:12748292,
CC ECO:0000269|PubMed:12847291}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; X83690; CAA58659.1; -; Genomic_DNA.
DR EMBL; Z72701; CAA96891.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA07935.1; -; Genomic_DNA.
DR PIR; S57252; S57252.
DR RefSeq; NP_011336.3; NM_001181044.3.
DR AlphaFoldDB; P43637; -.
DR SMR; P43637; -.
DR BioGRID; 33075; 143.
DR DIP; DIP-5033N; -.
DR IntAct; P43637; 6.
DR STRING; 4932.YGL179C; -.
DR iPTMnet; P43637; -.
DR PaxDb; P43637; -.
DR PRIDE; P43637; -.
DR EnsemblFungi; YGL179C_mRNA; YGL179C; YGL179C.
DR GeneID; 852696; -.
DR KEGG; sce:YGL179C; -.
DR SGD; S000003147; TOS3.
DR VEuPathDB; FungiDB:YGL179C; -.
DR eggNOG; KOG0585; Eukaryota.
DR GeneTree; ENSGT00940000161828; -.
DR HOGENOM; CLU_484098_0_0_1; -.
DR InParanoid; P43637; -.
DR OMA; VTSDFGC; -.
DR BioCyc; YEAST:G3O-30666-MON; -.
DR Reactome; R-SCE-111932; CaMK IV-mediated phosphorylation of CREB.
DR Reactome; R-SCE-442729; CREB1 phosphorylation through the activation of CaMKII/CaMKK/CaMKIV cascasde.
DR Reactome; R-SCE-9619229; Activation of RAC1 downstream of NMDARs.
DR PRO; PR:P43637; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P43637; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; HDA:SGD.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:SGD.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:1900180; P:regulation of protein localization to nucleus; IMP:SGD.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Stress response;
KW Transferase.
FT CHAIN 1..560
FT /note="Serine/threonine-protein kinase TOS3"
FT /id="PRO_0000086126"
FT DOMAIN 50..344
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 189
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 56..64
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 79
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 560 AA; 62091 MW; EFFA0C5ED58B5466 CRC64;
MVLLKEPVQP LPRSSLLYNN ASNSSSRIKE TRKVKLLYNP LTKRQILNNF EILATLGNGQ
YGKVKLARDL GTGALVAIKI LNRFEKRSGY SLQLKVENPR VNQEIEVMKR CHHENVVELY
EILNDPESTK VYLVLEYCSR GPVKWCPENK MEIKAVGPSI LTFQQSRKVV LDVVSGLEYL
HSQGITHRDI KPSNLLISSN GTVKISDFGV AMSTATGSTN IQSSHEQLLK SRALGTPAFF
APELCSTEKE YSCSSAIDIW SLGVTIYCLL FGKLPFNANS GLELFDSIIN KPLEFPSYEE
MLNGATSGIT MEEYTDAKDL LKKLLQKDPD KRIKLADIKV HPFMCHYGKS DAASVLTNLE
TFHELKVSPP SSCKRVELVS LPVNSSFASL DSVYMENFDH NNLRTGADRN STYSPSIYDA
NTLSPSAYHN IGSRESSYSS FSSFTSSTAF ASQISIQDAP AIGDQQCLIG ESGSSLRVNS
CEFPQYTTMS PVGEYPFEST EASLSSTLTP VGNVPQRIKA HLVEGKSNSK DDLRIEADAS
LVFEASDAQR TRRRMSLYKL
