KAPC_YEAST
ID KAPC_YEAST Reviewed; 398 AA.
AC P05986; D6VX33;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 2.
DT 03-AUG-2022, entry version 209.
DE RecName: Full=cAMP-dependent protein kinase type 3;
DE Short=PKA 3;
DE EC=2.7.11.11;
GN Name=TPK3; Synonyms=PKA3; OrderedLocusNames=YKL166C; ORFNames=YKL630;
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=3036373; DOI=10.1016/0092-8674(87)90223-6;
RA Toda T., Cameron S., Sass P., Zoller M., Wigler M.;
RT "Three different genes in S. cerevisiae encode the catalytic subunits of
RT the cAMP-dependent protein kinase.";
RL Cell 50:277-287(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091858; DOI=10.1002/yea.320100004;
RA Vandenbol M., Bolle P.-A., Dion C., Portetelle D., Hilger F.;
RT "Sequencing and analysis of a 20.5 kb DNA segment located on the left arm
RT of yeast chromosome XI.";
RL Yeast 10:S25-S33(1994).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 344-398.
RX PubMed=1544898; DOI=10.1016/s0021-9258(18)42745-7;
RA Fearon K., Mason T.L.;
RT "Structure and function of MRP20 and MRP49, the nuclear genes for two
RT proteins of the 54 S subunit of the yeast mitochondrial ribosome.";
RL J. Biol. Chem. 267:5162-5170(1992).
RN [6]
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [8]
RP IDENTIFICATION BY 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-55, 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).
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=2.7.11.11;
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=2.7.11.11;
CC -!- ACTIVITY REGULATION: Activated by cAMP.
CC -!- INTERACTION:
CC P05986; P07278: BCY1; NbExp=4; IntAct=EBI-9470, EBI-9475;
CC -!- MISCELLANEOUS: Present with 1590 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. cAMP subfamily. {ECO:0000305}.
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DR EMBL; M17074; AAA35166.1; -; Genomic_DNA.
DR EMBL; Z26878; CAA81521.1; -; Genomic_DNA.
DR EMBL; Z28166; CAA82008.1; -; Genomic_DNA.
DR EMBL; M81697; AAA34791.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA08999.1; -; Genomic_DNA.
DR PIR; S37996; OKBYC3.
DR RefSeq; NP_012755.1; NM_001179732.1.
DR AlphaFoldDB; P05986; -.
DR SMR; P05986; -.
DR BioGRID; 33971; 322.
DR ComplexPortal; CPX-571; cAMP-dependent protein kinase complex variant 3.
DR ComplexPortal; CPX-573; cAMP-dependent protein kinase complex variant 5.
DR ComplexPortal; CPX-574; cAMP-dependent protein kinase complex variant 6.
DR DIP; DIP-550N; -.
DR IntAct; P05986; 28.
DR MINT; P05986; -.
DR STRING; 4932.YKL166C; -.
DR iPTMnet; P05986; -.
DR MaxQB; P05986; -.
DR PaxDb; P05986; -.
DR PRIDE; P05986; -.
DR EnsemblFungi; YKL166C_mRNA; YKL166C; YKL166C.
DR GeneID; 853688; -.
DR KEGG; sce:YKL166C; -.
DR SGD; S000001649; TPK3.
DR VEuPathDB; FungiDB:YKL166C; -.
DR eggNOG; KOG0616; Eukaryota.
DR GeneTree; ENSGT00940000176357; -.
DR HOGENOM; CLU_000288_63_5_1; -.
DR InParanoid; P05986; -.
DR OMA; GNARYNK; -.
DR BioCyc; YEAST:G3O-31934-MON; -.
DR BRENDA; 2.7.11.11; 984.
DR Reactome; R-SCE-163615; PKA activation.
DR Reactome; R-SCE-164378; PKA activation in glucagon signalling.
DR Reactome; R-SCE-180024; DARPP-32 events.
DR Reactome; R-SCE-432040; Vasopressin regulates renal water homeostasis via Aquaporins.
DR Reactome; R-SCE-442720; CREB1 phosphorylation through the activation of Adenylate Cyclase.
DR Reactome; R-SCE-5610787; Hedgehog 'off' state.
DR Reactome; R-SCE-5687128; MAPK6/MAPK4 signaling.
DR Reactome; R-SCE-9634597; GPER1 signaling.
DR Reactome; R-SCE-983231; Factors involved in megakaryocyte development and platelet production.
DR PRO; PR:P05986; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P05986; protein.
DR GO; GO:0005952; C:cAMP-dependent protein kinase complex; IGI:SGD.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0010494; C:cytoplasmic stress granule; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0000932; C:P-body; IDA:SGD.
DR GO; GO:0004679; F:AMP-activated protein kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004691; F:cAMP-dependent protein kinase activity; IDA:SGD.
DR GO; GO:0004672; F:protein kinase activity; HDA:SGD.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0007005; P:mitochondrion organization; IMP:SGD.
DR GO; GO:0010607; P:negative regulation of cytoplasmic mRNA processing body assembly; IGI:SGD.
DR GO; GO:2000766; P:negative regulation of cytoplasmic translation; IMP:SGD.
DR GO; GO:0010737; P:protein kinase A signaling; IGI:SGD.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0007265; P:Ras protein signal transduction; IGI:SGD.
DR InterPro; IPR000961; AGC-kinase_C.
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; PS51285; AGC_KINASE_CTER; 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; cAMP; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..398
FT /note="cAMP-dependent protein kinase type 3"
FT /id="PRO_0000086071"
FT DOMAIN 88..342
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 343..398
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT ACT_SITE 211
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 94..102
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 117
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 55
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CONFLICT 4
FT /note="D -> E (in Ref. 1; AAA35166)"
FT /evidence="ECO:0000305"
FT CONFLICT 208
FT /note="I -> T (in Ref. 1; AAA35166)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 398 AA; 45977 MW; 4ADDE8E63032B313 CRC64;
MYVDPMNNNE IRKLSITAKT ETTPDNVGQD IPVNAHSVHE ECSSNTPVEI NGRNSGKLKE
EASAGICLVK KPMLQYRDTS GKYSLSDFQI LRTLGTGSFG RVHLIRSNHN GRFYALKTLK
KHTIVKLKQV EHTNDERRML SIVSHPFIIR MWGTFQDSQQ VFMVMDYIEG GELFSLLRKS
QRFPNPVAKF YAAEVCLALE YLHSKDIIYR DLKPENILLD KNGHIKITDF GFAKYVPDVT
YTLCGTPDYI APEVVSTKPY NKSVDWWSFG VLIYEMLAGY TPFYNSNTMK TYENILNAEL
KFPPFFHPDA QDLLKKLITR DLSERLGNLQ NGSEDVKNHP WFNEVIWEKL LARYIETPYE
PPIQQGQGDT SQFDRYPEEE FNYGIQGEDP YMDLMKEF
