KAPA_YEAST
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 03-AUG-2022, entry version 222.
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; 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};
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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; 438.
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; P06244; -.
DR PRIDE; P06244; -.
DR EnsemblFungi; YJL164C_mRNA; YJL164C; YJL164C.
DR GeneID; 853275; -.
DR KEGG; sce:YJL164C; -.
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; HKETNQF; -.
DR BioCyc; YEAST:G3O-31604-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 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: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: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; IMP:SGD.
DR GO; GO:0016241; P:regulation of macroautophagy; IMP: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; SM00133; S_TK_X; 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 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
