ID   PRR1_YEAST              Reviewed;         518 AA.
AC   P28708; D6VXH3;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   27-MAR-2024, entry version 186.
DE   RecName: Full=Serine/threonine-protein kinase PRR1;
DE            EC=2.7.11.1;
DE   AltName: Full=Pheromone response regulator 1;
GN   Name=PRR1; OrderedLocusNames=YKL116C; ORFNames=YKL516;
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].
RX   PubMed=1561835; DOI=10.1002/yea.320080207;
RA   Jacquier A., Legrain P., Dujon B.;
RT   "Sequence of a 10.7 kb segment of yeast chromosome XI identifies the APN1
RT   and the BAF1 loci and reveals one tRNA gene and several new open reading
RT   frames including homologs to RAD2 and kinases.";
RL   Yeast 8:121-132(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8196765; DOI=10.1038/369371a0;
RA   Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA   Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA   Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA   Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA   Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA   Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA   Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA   Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA   Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA   Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA   Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA   Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA   Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA   Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA   Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA   Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA   Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA   Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA   Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA   van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA   von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA   Becker I., Mewes H.-W.;
RT   "Complete DNA sequence of yeast chromosome XI.";
RL   Nature 369:371-378(1994).
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=11337509; DOI=10.1074/jbc.m103436200;
RA   Burchett S.A., Scott A., Errede B., Dohlman H.G.;
RT   "Identification of novel pheromone-response regulators through systematic
RT   overexpression of 120 protein kinases in yeast.";
RL   J. Biol. Chem. 276:26472-26478(2001).
RN   [6]
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   [7]
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   [8]
RP   CATALYTIC ACTIVITY.
RX   PubMed=16319894; DOI=10.1038/nature04187;
RA   Ptacek J., Devgan G., Michaud G., Zhu H., Zhu X., Fasolo J., Guo H.,
RA   Jona G., Breitkreutz A., Sopko R., McCartney R.R., Schmidt M.C.,
RA   Rachidi N., Lee S.-J., Mah A.S., Meng L., Stark M.J.R., Stern D.F.,
RA   De Virgilio C., Tyers M., Andrews B., Gerstein M., Schweitzer B.,
RA   Predki P.F., Snyder M.;
RT   "Global analysis of protein phosphorylation in yeast.";
RL   Nature 438:679-684(2005).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132, 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-132, 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-132, AND IDENTIFICATION BY
RP   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   [12]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC   -!- FUNCTION: Protein kinase that functions as a regulator in the
CC       pheromone-induced mating pathway downstream of mitogen-activated
CC       protein kinase (MAPK) FUS3. Diminishes transcriptional induction of
CC       genes in response to pheromone signaling. {ECO:0000269|PubMed:11062466,
CC       ECO:0000269|PubMed:11337509}.
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         Evidence={ECO:0000269|PubMed:16319894};
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; Evidence={ECO:0000269|PubMed:16319894};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC   -!- MISCELLANEOUS: Present with 1510 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC       protein kinase family. NIM1 subfamily. {ECO:0000305}.
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DR   EMBL; S93804; AAB21999.1; -; Genomic_DNA.
DR   EMBL; Z28115; CAA81955.1; -; Genomic_DNA.
DR   EMBL; BK006944; DAA09043.1; -; Genomic_DNA.
DR   PIR; S27381; S27381.
DR   RefSeq; NP_012806.1; NM_001179682.1.
DR   AlphaFoldDB; P28708; -.
DR   SMR; P28708; -.
DR   BioGRID; 34019; 194.
DR   DIP; DIP-1919N; -.
DR   IntAct; P28708; 7.
DR   MINT; P28708; -.
DR   STRING; 4932.YKL116C; -.
DR   iPTMnet; P28708; -.
DR   MaxQB; P28708; -.
DR   PaxDb; 4932-YKL116C; -.
DR   PeptideAtlas; P28708; -.
DR   EnsemblFungi; YKL116C_mRNA; YKL116C; YKL116C.
DR   GeneID; 853744; -.
DR   KEGG; sce:YKL116C; -.
DR   AGR; SGD:S000001599; -.
DR   SGD; S000001599; PRR1.
DR   VEuPathDB; FungiDB:YKL116C; -.
DR   eggNOG; KOG0586; Eukaryota.
DR   HOGENOM; CLU_032736_0_0_1; -.
DR   InParanoid; P28708; -.
DR   OMA; PCDMIMS; -.
DR   OrthoDB; 5395166at2759; -.
DR   BioCyc; YEAST:G3O-31900-MONOMER; -.
DR   BioGRID-ORCS; 853744; 0 hits in 13 CRISPR screens.
DR   PRO; PR:P28708; -.
DR   Proteomes; UP000002311; Chromosome XI.
DR   RNAct; P28708; Protein.
DR   GO; GO:0005938; C:cell cortex; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; HDA: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; IBA:GO_Central.
DR   GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR   GO; GO:0031138; P:negative regulation of conjugation with cellular fusion; IMP:SGD.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:SGD.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0019236; P:response to pheromone; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR016240; Ser/Thr_kin_YKL116c_prd.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR44167; OVARIAN-SPECIFIC SERINE/THREONINE-PROTEIN KINASE LOK-RELATED; 1.
DR   PANTHER; PTHR44167:SF8; OVARIAN-SPECIFIC SERINE_THREONINE-PROTEIN KINASE LOK; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   PIRSF; PIRSF000609; Ser/Thr_PK_YKL116c_prd; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 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   Acetylation; ATP-binding; Cytoplasm; Kinase; Nucleotide-binding;
KW   Pheromone response; Phosphoprotein; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..518
FT                   /note="Serine/threonine-protein kinase PRR1"
FT                   /id="PRO_0000086149"
FT   DOMAIN          192..508
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          1..59
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        22..48
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        354
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         198..206
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         225
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   MOD_RES         132
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
SQ   SEQUENCE   518 AA;  58956 MW;  4AEB19FAA27671B6 CRC64;
     MDEYSSIYSQ PKTPRLKQEG FPDSIGDQHE KALIDENGEE DKKMASTEGT TGDSRSTPLT
     VSIPTFENVQ ALPTPMTYTP LSPGNLSMSP IDQSSLNIPK RRSHARLLDD MLSVTQPNQR
     VVSELIAPAN LSPQRVVSLP TVTEEALVND SVDSDNYTKE PYFPESSSST EKCDDDIFQG
     FLLDHWDRPL LWKKVRPIGS GNFSTVLLYE LMDQSNPKLK QVAVKRLKYP EELSNVEQIN
     TSLRYKETLS RLENSLTREL QVLKSLNHPC IVKLLGINNP IFVTSKKPLC DLIIKTPRAL
     PPCDMIMSYC PAGDLLAAVM ARNGRLEAWL IQRIFTEVVL AVKYLHENSI IHRDLKLENI
     LLKYSFDDIN SFRDSPIYCK QNFIELADFG LCKKIENNEM CTARCGSEDY VSPEILMGVP
     YDGHLSDTWA LGVILYSLFE DRLPFDPPPN ASARQRSRAT SHRIARFDWR WYRLSDYKTN
     VGKQIVENTL TRKNQRWSIN EIYESPFVKT IADTLSFS
//