PKH3_YEAST
ID PKH3_YEAST Reviewed; 898 AA.
AC Q03306; D6VT91;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Serine/threonine-protein kinase PKH3;
DE EC=2.7.11.1;
DE AltName: Full=Pkb-activating kinase homolog 3;
GN Name=PKH3; OrderedLocusNames=YDR466W;
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 [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 [2]
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 [3]
RP FUNCTION.
RX PubMed=10567559; DOI=10.1128/mcb.19.12.8344;
RA Inagaki M., Schmelzle T., Yamaguchi K., Irie K., Hall M.N., Matsumoto K.;
RT "PDK1 homologs activate the Pkc1-mitogen-activated protein kinase pathway
RT in yeast.";
RL Mol. Cell. Biol. 19:8344-8352(1999).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-696, 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-753 AND SER-871, AND
RP IDENTIFICATION BY 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).
CC -!- FUNCTION: Serine/threonine-protein kinase which may phosphorylate the
CC same targets substrates as PKH1 and PKH2, 2 upstream activators of
CC PKC1. {ECO:0000269|PubMed:10567559, ECO:0000269|PubMed:11062466}.
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 -!- INTERACTION:
CC Q03306; Q04439: MYO5; NbExp=2; IntAct=EBI-37683, EBI-11687;
CC Q03306; P37304: PAM1; NbExp=3; IntAct=EBI-37683, EBI-12870;
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; U33050; AAB64902.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12301.1; -; Genomic_DNA.
DR PIR; S69634; S69634.
DR RefSeq; NP_010754.1; NM_001180774.1.
DR AlphaFoldDB; Q03306; -.
DR SMR; Q03306; -.
DR BioGRID; 32520; 131.
DR DIP; DIP-8781N; -.
DR IntAct; Q03306; 17.
DR MINT; Q03306; -.
DR STRING; 4932.YDR466W; -.
DR iPTMnet; Q03306; -.
DR MaxQB; Q03306; -.
DR PaxDb; Q03306; -.
DR PRIDE; Q03306; -.
DR EnsemblFungi; YDR466W_mRNA; YDR466W; YDR466W.
DR GeneID; 852077; -.
DR KEGG; sce:YDR466W; -.
DR SGD; S000002874; PKH3.
DR VEuPathDB; FungiDB:YDR466W; -.
DR eggNOG; KOG0592; Eukaryota.
DR HOGENOM; CLU_008400_0_0_1; -.
DR InParanoid; Q03306; -.
DR OMA; CSKRHII; -.
DR BioCyc; YEAST:G3O-29994-MON; -.
DR PRO; PR:Q03306; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q03306; 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:0000196; P:cell wall integrity MAPK cascade; IGI:SGD.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; HDA:SGD.
DR CDD; cd05581; STKc_PDK1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR039046; PDPK1.
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; Transferase.
FT CHAIN 1..898
FT /note="Serine/threonine-protein kinase PKH3"
FT /id="PRO_0000086554"
FT DOMAIN 11..293
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 435..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 675..850
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 446..484
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 695..721
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 735..830
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 138
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 17..25
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 41
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 696
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 753
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 871
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 898 AA; 100476 MW; 44715C40DD26B89E CRC64;
MTSRKRSPHD FIFKEELGHG SYSTVFKALD KKSPNKIYAI KVCSKKHIIK EAKVKYVTIE
KNTMNLLAQK HHAGIIKLYY TFHDEENLYF VLDFAPGGEL LSLLHKMGTF NDIWTRHFTA
QLIDALEFIH SHGIIHRDLK PENVLLDRDG RLMITDFGAA ATIDPSLSGD SAKFNSDSNG
SKDNQNCASF VGTAEYVSPE LLLYNQCGYG SDIWALGCMI YQFVQGQPPF RGENELKTFE
KIVALDYPWG PNNRINNSTS PINPLVINLV QKILVIEVNE RISLEQIKRH PYFSKVDWND
KIKIWRGIWQ SQGQSLQQTT LGLPNIPQNI LPTRQLHVID TPARSIQITK QKRKKPTKIS
NTTSSIVVWR KRLGISTGKD DLGTVPSTTP AVTAPNDTNV LTNTAAHSTA NIALPPNSQS
NQVKRAQLVA PNRIPPKVPV INDNVRNKSI PRTKPNVPPL QTSSIPQKLS TSSASSALSA
PSTEIRNQDL THTLDGRNSI DIHVLKQDYV FIYGIPYEHE GPAMSLNSYN KIDNDLITSL
VAQHKEELKN SESFLQVLTL KKSGMLSYKN TVMEGNDDQE NKEHQMANIE DTDLSMYDFE
FNELTRKGFL ILEKYKNRIW FISLPSYSTL SKIPFNAVKS STINNNENWV DCFFRARQLL
EEKQILDKIS NVSFDSKASS EPSSPPPISR KERPLSIGNN VTTLSYTAKN GSQNNAPQND
NVGEEKPFRI PSSTKDRPGA NSTPSSRHPR VLSSNNAGET PKKMNGRLPN SAPSTNTYTN
GSVPAFNHRP STNVGNNKHN ILTSKKQGSS VFSPSSSTTK PQIKTTGYRQ PTPSPPLPQM
EFPTTREKYS APSNMVISSS RYEVLHTLNN SQTNFDREIA SRGASAAFRS LQKSKKKK
