KDX1_YEAST
ID KDX1_YEAST Reviewed; 433 AA.
AC P36005; D6VX38;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Serine/threonine-protein kinase KDX1;
DE EC=2.7.11.1;
DE AltName: Full=Kinase dead X-talker protein 1;
DE AltName: Full=MPK1-like protein kinase 1;
GN Name=KDX1; Synonyms=MLP1; OrderedLocusNames=YKL161C; ORFNames=YKL615;
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 204508 / S288c;
RX PubMed=8091859; DOI=10.1002/yea.320100005;
RA Vandenbol M., Bolle P.-A., Dion C., Portetelle D., Hilger F.;
RT "DNA sequencing of a 36.2 kb fragment located between the FAS1 and LAP loci
RT of chromosome XI of Saccharomyces cerevisiae.";
RL Yeast 10:S35-S40(1994).
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, AND INTERACTION WITH RLM1.
RX PubMed=9111331; DOI=10.1128/mcb.17.5.2615;
RA Watanabe Y., Takaesu G., Hagiwara M., Irie K., Matsumoto K.;
RT "Characterization of a serum response factor-like protein in Saccharomyces
RT cerevisiae, Rlm1, which has transcriptional activity regulated by the Mpk1
RT (Slt2) mitogen-activated protein kinase pathway.";
RL Mol. Cell. Biol. 17:2615-2623(1997).
RN [5]
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 [6]
RP INDUCTION.
RX PubMed=18055054; DOI=10.1016/j.jbiotec.2007.10.006;
RA Rodriguez-Pena J.M., Diez-Muniz S., Nombela C., Arroyo J.;
RT "A yeast strain biosensor to detect cell wall-perturbing agents.";
RL J. Biotechnol. 133:311-317(2008).
RN [7]
RP FUNCTION.
RX PubMed=20489023; DOI=10.1126/science.1176495;
RA Breitkreutz A., Choi H., Sharom J.R., Boucher L., Neduva V., Larsen B.,
RA Lin Z.Y., Breitkreutz B.J., Stark C., Liu G., Ahn J., Dewar-Darch D.,
RA Reguly T., Tang X., Almeida R., Qin Z.S., Pawson T., Gingras A.C.,
RA Nesvizhskii A.I., Tyers M.;
RT "A global protein kinase and phosphatase interaction network in yeast.";
RL Science 328:1043-1046(2010).
CC -!- FUNCTION: Serine/threonine-protein kinase involved in the SLT2 mitogen-
CC activated (MAP) kinase signaling pathway that regulates cell wall
CC integrity. May also be involved in the mating pheromone and the CWI
CC MAPK pathways. {ECO:0000269|PubMed:11062466,
CC ECO:0000269|PubMed:20489023, ECO:0000269|PubMed:9111331}.
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 -!- SUBUNIT: Interacts with RLM1. {ECO:0000269|PubMed:9111331}.
CC -!- INDUCTION: Accumulates in large amounts when cell wall integrity is
CC compromised. {ECO:0000269|PubMed:18055054}.
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; Z26877; CAA81493.1; -; Genomic_DNA.
DR EMBL; Z28161; CAA82003.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09004.1; -; Genomic_DNA.
DR PIR; S37790; S37790.
DR RefSeq; NP_012761.1; NM_001179727.1.
DR AlphaFoldDB; P36005; -.
DR SMR; P36005; -.
DR BioGRID; 33977; 103.
DR DIP; DIP-6316N; -.
DR IntAct; P36005; 26.
DR MINT; P36005; -.
DR STRING; 4932.YKL161C; -.
DR iPTMnet; P36005; -.
DR PaxDb; P36005; -.
DR PRIDE; P36005; -.
DR EnsemblFungi; YKL161C_mRNA; YKL161C; YKL161C.
DR GeneID; 853696; -.
DR KEGG; sce:YKL161C; -.
DR SGD; S000001644; KDX1.
DR VEuPathDB; FungiDB:YKL161C; -.
DR eggNOG; KOG0660; Eukaryota.
DR GeneTree; ENSGT00940000176702; -.
DR HOGENOM; CLU_000288_181_1_1; -.
DR InParanoid; P36005; -.
DR OMA; TERCIFR; -.
DR BioCyc; YEAST:G3O-31929-MON; -.
DR Reactome; R-SCE-3214858; RMTs methylate histone arginines.
DR Reactome; R-SCE-69231; Cyclin D associated events in G1.
DR Reactome; R-SCE-75815; Ubiquitin-dependent degradation of Cyclin D.
DR Reactome; R-SCE-9754119; Drug-mediated inhibition of CDK4/CDK6 activity.
DR PRO; PR:P36005; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P36005; protein.
DR GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0030332; F:cyclin binding; IBA:GO_Central.
DR GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0010389; P:regulation of G2/M transition of mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
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; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..433
FT /note="Serine/threonine-protein kinase KDX1"
FT /id="PRO_0000086150"
FT DOMAIN 23..318
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 153
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 29..37
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 55
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 433 AA; 49633 MW; BC27B76B7DB95822 CRC64;
MATDTERCIF RAFGQDFILN KHFHLTGKIG RGSHSLICSS TYTESNEETH VAIRKIPNAF
GNKLSCKRTL RELKLLRHLR GHPNIVWLFD TDIVFYPNGA LNGVYLYEEL MECDLSQIIR
SEQRLEDAHF QSFIYQILCA LKYIHSANVL HCDLKPKNLL VNSDCQLKIC NFGLSCSYSE
NHKVNDGFIK GYITSIWYKA PEILLNYQEC TKAVDIWSTG CILAELLGRK PMFEGKDYVD
HLNHILQILG TPPEETLQEI ASQKVYNYIF QFGNIPGRSF ESILPGANPE ALELLKKMLE
FDPKKRITVE DALEHPYLSM WHDIDEEFSC QKTFRFEFEH IESMAELGNE VIKEVFDFRK
VVRKHPISGD SPSSSLSLED AIPQEVVQVH PSRKVLPSYS PEFSYVSQLP SLTTTQPYQN
LMGISSNSFQ GVN
