ID KAPA_YEAST Reviewed; 397 AA. AC P06244; D6VW23; P11595; Q2VQW1; DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot. DT 21-SEP-2011, sequence version 3. DT 27-MAR-2024, entry version 230. DE RecName: Full=cAMP-dependent protein kinase type 1; DE Short=PKA 1; DE EC=2.7.11.11; DE AltName: Full=CDC25-suppressing protein kinase; DE AltName: Full=PK-25; GN Name=TPK1; Synonyms=PKA1, SRA3; OrderedLocusNames=YJL164C; GN ORFNames=J0541; 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]. RX PubMed=3546292; DOI=10.1016/s0021-9258(18)61539-x; RA Lisziewicz J., Godany A., Foerster H.-H., Kuentzel H.; RT "Isolation and nucleotide sequence of a Saccharomyces cerevisiae protein RT kinase gene suppressing the cell cycle start mutation cdc25."; RL J. Biol. Chem. 262:2549-2553(1987). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2823100; DOI=10.1128/mcb.7.8.2653-2663.1987; RA Cannon J.F., Tatchell K.; RT "Characterization of Saccharomyces cerevisiae genes encoding subunits of RT cyclic AMP-dependent protein kinase."; RL Mol. Cell. Biol. 7:2653-2663(1987). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x; RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C., RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D., RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J., RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C., RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E., RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T., RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B., RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R., RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N., RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H., RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.; RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X."; RL EMBO J. 15:2031-2049(1996). RN [5] RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 79-86. 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 [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-82. RC STRAIN=ATCC 208353 / W303-1A; RX PubMed=15905473; DOI=10.1093/nar/gki583; RA Zhang Z., Dietrich F.S.; RT "Mapping of transcription start sites in Saccharomyces cerevisiae using 5' RT SAGE."; RL Nucleic Acids Res. 33:2838-2851(2005). RN [7] 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 [8] 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 [9] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [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). RN [10] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 81-397. RX PubMed=11368172; DOI=10.1006/abbi.2000.2241; RA Mashhoon N., Carmel G., Pflugrath J.W., Kuret J.; RT "Structure of the unliganded cAMP-dependent protein kinase catalytic RT subunit from Saccharomyces cerevisiae."; RL Arch. Biochem. Biophys. 387:11-19(2001). 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 P06244; P07278: BCY1; NbExp=7; IntAct=EBI-9458, EBI-9475; CC P06244; P39717: GPB2; NbExp=3; IntAct=EBI-9458, EBI-20711; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus CC {ECO:0000269|PubMed:14562095}. CC -!- MISCELLANEOUS: Present with 4320 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}. CC -!- SEQUENCE CAUTION: CC Sequence=AAA35088.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; 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; M17072; AAA35164.1; -; Genomic_DNA. DR EMBL; J02665; AAA34877.1; -; Genomic_DNA. DR EMBL; M17224; AAA35088.1; ALT_INIT; Genomic_DNA. DR EMBL; Z49439; CAA89459.1; -; Genomic_DNA. DR EMBL; AY899257; AAX83942.1; -; mRNA. DR EMBL; BK006943; DAA08639.2; -; Genomic_DNA. DR PIR; JC1034; OKBYC1. DR RefSeq; NP_012371.2; NM_001181597.2. DR PDB; 1FOT; X-ray; 2.80 A; A=81-397. DR PDBsum; 1FOT; -. DR AlphaFoldDB; P06244; -. DR SMR; P06244; -. DR BioGRID; 33595; 454. DR ComplexPortal; CPX-536; cAMP-dependent protein kinase complex variant 1. DR ComplexPortal; CPX-572; cAMP-dependent protein kinase complex variant 4. DR ComplexPortal; CPX-573; cAMP-dependent protein kinase complex variant 5. DR DIP; DIP-548N; -. DR ELM; P06244; -. DR IntAct; P06244; 28. DR MINT; P06244; -. DR STRING; 4932.YJL164C; -. DR iPTMnet; P06244; -. DR MaxQB; P06244; -. DR PaxDb; 4932-YJL164C; -. DR PeptideAtlas; P06244; -. DR EnsemblFungi; YJL164C_mRNA; YJL164C; YJL164C. DR GeneID; 853275; -. DR KEGG; sce:YJL164C; -. DR AGR; SGD:S000003700; -. DR SGD; S000003700; TPK1. DR VEuPathDB; FungiDB:YJL164C; -. DR eggNOG; KOG0616; Eukaryota. DR GeneTree; ENSGT00940000176357; -. DR HOGENOM; CLU_000288_63_5_1; -. DR InParanoid; P06244; -. DR OMA; HINNECS; -. DR OrthoDB; 10768at2759; -. DR BioCyc; YEAST:G3O-31604-MONOMER; -. 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-9634597; GPER1 signaling. DR Reactome; R-SCE-983231; Factors involved in megakaryocyte development and platelet production. DR BioGRID-ORCS; 853275; 0 hits in 13 CRISPR screens. DR EvolutionaryTrace; P06244; -. DR PRO; PR:P06244; -. DR Proteomes; UP000002311; Chromosome X. DR RNAct; P06244; Protein. DR GO; GO:0005952; C:cAMP-dependent protein kinase complex; IDA:SGD. DR GO; GO:0000785; C:chromatin; IDA:SGD. DR GO; GO:0005737; C:cytoplasm; IDA:SGD. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0005634; C:nucleus; 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:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0010607; P:negative regulation of cytoplasmic mRNA processing body assembly; IGI:SGD. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:0010737; P:protein kinase A signaling; IGI:SGD. DR GO; GO:0007265; P:Ras protein signal transduction; IMP:SGD. DR GO; GO:0016241; P:regulation of macroautophagy; IMP:SGD. DR CDD; cd05580; STKc_PKA_like; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. 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 PANTHER; PTHR24353:SF73; CAMP-DEPENDENT PROTEIN KINASE TYPE 1-RELATED; 1. DR PANTHER; PTHR24353; CYCLIC NUCLEOTIDE-DEPENDENT PROTEIN KINASE; 1. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00133; S_TK_X; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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 3D-structure; Acetylation; ATP-binding; cAMP; Cell cycle; Cell division; KW Cytoplasm; Kinase; Nucleotide-binding; Nucleus; Reference proteome; KW Serine/threonine-protein kinase; Transferase. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:22814378" FT CHAIN 2..397 FT /note="cAMP-dependent protein kinase type 1" FT /id="PRO_0000086046" FT DOMAIN 87..341 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT DOMAIN 342..397 FT /note="AGC-kinase C-terminal" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618" FT REGION 1..60 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 10..54 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 210 FT /note="Proton acceptor" FT BINDING 93..101 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 116 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT MOD_RES 2 FT /note="N-acetylserine" FT /evidence="ECO:0007744|PubMed:22814378" FT CONFLICT 79..86 FT /note="SGKYSLQD -> VGSIVYKN (in Ref. 3; AAA35088 and 4; FT CAA89459)" FT /evidence="ECO:0000305" FT CONFLICT 164..171 FT /note="MDYIEGGE -> ILKVER (in Ref. 3; AAA35088)" FT /evidence="ECO:0000305" FT CONFLICT 180..181 FT /note="QR -> KD (in Ref. 3; AAA35088)" FT /evidence="ECO:0000305" FT CONFLICT 188..190 FT /note="KFY -> QIF (in Ref. 3; AAA35088)" FT /evidence="ECO:0000305" FT HELIX 84..86 FT /evidence="ECO:0007829|PDB:1FOT" FT STRAND 87..95 FT /evidence="ECO:0007829|PDB:1FOT" FT STRAND 100..106 FT /evidence="ECO:0007829|PDB:1FOT" FT TURN 107..109 FT /evidence="ECO:0007829|PDB:1FOT" FT STRAND 112..119 FT /evidence="ECO:0007829|PDB:1FOT" FT HELIX 120..125 FT /evidence="ECO:0007829|PDB:1FOT" FT HELIX 129..140 FT /evidence="ECO:0007829|PDB:1FOT" FT STRAND 150..155 FT /evidence="ECO:0007829|PDB:1FOT" FT STRAND 157..164 FT /evidence="ECO:0007829|PDB:1FOT" FT HELIX 172..178 FT /evidence="ECO:0007829|PDB:1FOT" FT HELIX 184..202 FT /evidence="ECO:0007829|PDB:1FOT" FT TURN 203..205 FT /evidence="ECO:0007829|PDB:1FOT" FT HELIX 213..215 FT /evidence="ECO:0007829|PDB:1FOT" FT STRAND 216..218 FT /evidence="ECO:0007829|PDB:1FOT" FT STRAND 224..226 FT /evidence="ECO:0007829|PDB:1FOT" FT TURN 246..248 FT /evidence="ECO:0007829|PDB:1FOT" FT HELIX 251..254 FT /evidence="ECO:0007829|PDB:1FOT" FT HELIX 263..277 FT /evidence="ECO:0007829|PDB:1FOT" FT HELIX 287..296 FT /evidence="ECO:0007829|PDB:1FOT" FT HELIX 307..316 FT /evidence="ECO:0007829|PDB:1FOT" FT TURN 321..323 FT /evidence="ECO:0007829|PDB:1FOT" FT TURN 329..332 FT /evidence="ECO:0007829|PDB:1FOT" FT HELIX 333..336 FT /evidence="ECO:0007829|PDB:1FOT" FT HELIX 339..341 FT /evidence="ECO:0007829|PDB:1FOT" FT HELIX 346..350 FT /evidence="ECO:0007829|PDB:1FOT" FT HELIX 391..393 FT /evidence="ECO:0007829|PDB:1FOT" SQ SEQUENCE 397 AA; 46076 MW; D4E5C30D7F11458B CRC64; MSTEEQNGGG QKSLDDRQGE ESQKGETSER ETTATESGNE SKSVEKEGGE TQEKPKQPHV TYYNEEQYKQ FIAQARVTSG KYSLQDFQIL RTLGTGSFGR VHLIRSRHNG RYYAMKVLKK EIVVRLKQVE HTNDERLMLS IVTHPFIIRM WGTFQDAQQI FMIMDYIEGG ELFSLLRKSQ RFPNPVAKFY AAEVCLALEY LHSKDIIYRD LKPENILLDK NGHIKITDFG FAKYVPDVTY TLCGTPDYIA PEVVSTKPYN KSIDWWSFGI LIYEMLAGYT PFYDSNTMKT YEKILNAELR FPPFFNEDVK DLLSRLITRD LSQRLGNLQN GTEDVKNHPW FKEVVWEKLL SRNIETPYEP PIQQGQGDTS QFDKYPEEDI NYGVQGEDPY ADLFRDF //