PRR1_YEAST
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 03-AUG-2022, entry version 179.
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 regulator in the pheromone-
CC induced mating pathway downstream of mitogen-activated protein kinase
CC (MAPK) FUS3. Diminishes transcriptional induction of genes in response
CC 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; 169.
DR DIP; DIP-1919N; -.
DR IntAct; P28708; 7.
DR MINT; P28708; -.
DR STRING; 4932.YKL116C; -.
DR iPTMnet; P28708; -.
DR MaxQB; P28708; -.
DR PaxDb; P28708; -.
DR PRIDE; P28708; -.
DR EnsemblFungi; YKL116C_mRNA; YKL116C; YKL116C.
DR GeneID; 853744; -.
DR KEGG; sce:YKL116C; -.
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 BioCyc; YEAST:G3O-31900-MON; -.
DR PRO; PR:P28708; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P28708; protein.
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:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0019236; P:response to pheromone; IEA:UniProtKB-KW.
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 Pfam; PF00069; Pkinase; 1.
DR PIRSF; PIRSF000609; Ser/Thr_PK_YKL116c_prd; 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 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
