PRR2_YEAST
ID PRR2_YEAST Reviewed; 699 AA.
AC Q12310; D6VRE0;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Serine/threonine-protein kinase PRR2;
DE EC=2.7.11.1;
DE AltName: Full=Pheromone response regulator 2;
GN Name=PRR2; OrderedLocusNames=YDL214C; ORFNames=D1014;
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=9046097;
RX DOI=10.1002/(sici)1097-0061(199702)13:2<163::aid-yea54>3.0.co;2-4;
RA Bahr A., Moeller-Rieker S., Hankeln T., Kraemer C., Protin U.,
RA Schmidt E.R.;
RT "The nucleotide sequence of a 39 kb segment of yeast chromosome IV: 12 new
RT open reading frames, nine known genes and one gene for Gly-tRNA.";
RL Yeast 13:163-169(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(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 INDUCTION.
RX PubMed=10940301; DOI=10.1074/jbc.m004235200;
RA Bertram P.G., Choi J.H., Carvalho J., Ai W., Zeng C., Chan T.-F.,
RA Zheng X.F.S.;
RT "Tripartite regulation of Gln3p by TOR, Ure2p, and phosphatases.";
RL J. Biol. Chem. 275:35727-35733(2000).
RN [5]
RP CATALYTIC ACTIVITY.
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 [6]
RP FUNCTION, AND MUTAGENESIS OF LYS-390.
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 [7]
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).
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: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:11062466, 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:11062466,
CC ECO:0000269|PubMed:16319894};
CC -!- INDUCTION: By the macrolide rapamycin in a TOR-dependent manner.
CC {ECO:0000269|PubMed:10940301}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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; X99000; CAA67476.1; -; Genomic_DNA.
DR EMBL; Z74262; CAA98792.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11650.1; -; Genomic_DNA.
DR PIR; S67773; S67773.
DR RefSeq; NP_010067.1; NM_001180274.1.
DR AlphaFoldDB; Q12310; -.
DR SMR; Q12310; -.
DR BioGRID; 31831; 87.
DR DIP; DIP-1640N; -.
DR IntAct; Q12310; 6.
DR MINT; Q12310; -.
DR STRING; 4932.YDL214C; -.
DR iPTMnet; Q12310; -.
DR PaxDb; Q12310; -.
DR PRIDE; Q12310; -.
DR EnsemblFungi; YDL214C_mRNA; YDL214C; YDL214C.
DR GeneID; 851312; -.
DR KEGG; sce:YDL214C; -.
DR SGD; S000002373; PRR2.
DR VEuPathDB; FungiDB:YDL214C; -.
DR eggNOG; KOG0590; Eukaryota.
DR GeneTree; ENSGT00940000176633; -.
DR HOGENOM; CLU_000288_82_4_1; -.
DR InParanoid; Q12310; -.
DR BioCyc; YEAST:G3O-29596-MON; -.
DR PRO; PR:Q12310; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q12310; protein.
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; 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; Pheromone response;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..699
FT /note="Serine/threonine-protein kinase PRR2"
FT /id="PRO_0000262752"
FT DOMAIN 361..653
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 168..193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 484
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 367..375
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 390
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MUTAGEN 390
FT /note="K->R: Abolishes kinase activity."
FT /evidence="ECO:0000269|PubMed:11337509"
SQ SEQUENCE 699 AA; 78939 MW; BB178BCE735D6086 CRC64;
MSLSRILRYN QRNNKTTASL TAEHAYSDNW AYSVSLGDPT SVGVNMAAKT GEALNKSYDS
VFSSLPVADS VPRTDFTASS RDDENTDVQK LTTSWMEKID TKMPENISKI DSNIISSPMV
SKVEARFIVP KGRLRKNSTD FTSSFSNSLS LPKSYGKLIF FTSKKNSSST KKNLANDISD
NKHNNNSSNT IGHNIPVTTA TATCDEIACT STEHEYNVYE EERMFTTRVY SLEDSVSSLS
TNPLDDTYSE AVQVNTRHIE DTESTAHIRK HSYTTSLSSI KRLFKITSFS NNNSNSCDHQ
ESTVADDCAI SSSLKETTSS PVSTGSFSLM IENEDSDRDQ IIQALYSNIE ASTDLVSRKY
RDLDVVLGEG SGGKVKLVQR VLDNKVFALK EYRSKKKRES ERKYIKNIIS EYCIASTLKN
PNICETLEIL YEKGKIFQIL EYCEYDLFSL VMSEKMHYEE ICCLFKQLIN GVKYLHDIGL
SHRDLKLDNC VVTRRGILKL IDFGASSVFH YPLSSQMIEA NGIVGSDPYL SPEVFYFNEY
DPRALDVWSV GIIFFCMITR RFPWKYPKVK DVQFKAFCSG RGVSSFKDLV TRPATDDSNN
YDNDGYEEGV IDMGPNFILH RLPEETHKIM RRILEVSPFR RITINGILQD GWIKEIETCQ
VVGAASPNEA SLRIINKGNH IHTNIDQRYA HIGGLHQRT
