KAPB_SCHPO
ID KAPB_SCHPO Reviewed; 512 AA.
AC P40376;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=cAMP-dependent protein kinase catalytic subunit;
DE EC=2.7.11.11;
GN Name=pka1; Synonyms=tpk; ORFNames=SPBC106.10;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7828877; DOI=10.1016/0378-1119(94)90659-9;
RA Yu G., Li J., Young D.;
RT "The Schizosaccharomyces pombe pka1 gene, encoding a homolog of cAMP-
RT dependent protein kinase.";
RL Gene 151:215-220(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8144551; DOI=10.1016/s0021-9258(17)36928-4;
RA Maeda T., Watanabe Y., Kunitomo H., Yamamoto M.;
RT "Cloning of the pka1 gene encoding the catalytic subunit of the cAMP-
RT dependent protein kinase in Schizosaccharomyces pombe.";
RL J. Biol. Chem. 269:9632-9637(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-356, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
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. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. cAMP subfamily. {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; U08622; AAA70165.1; -; mRNA.
DR EMBL; D23667; BAA04891.1; -; Genomic_DNA.
DR EMBL; CU329671; CAB53726.1; -; Genomic_DNA.
DR PIR; A54400; A54400.
DR RefSeq; NP_595159.1; NM_001021068.2.
DR AlphaFoldDB; P40376; -.
DR SMR; P40376; -.
DR BioGRID; 276331; 56.
DR STRING; 4896.SPBC106.10.1; -.
DR iPTMnet; P40376; -.
DR MaxQB; P40376; -.
DR PaxDb; P40376; -.
DR PRIDE; P40376; -.
DR EnsemblFungi; SPBC106.10.1; SPBC106.10.1:pep; SPBC106.10.
DR GeneID; 2539781; -.
DR KEGG; spo:SPBC106.10; -.
DR PomBase; SPBC106.10; pka1.
DR VEuPathDB; FungiDB:SPBC106.10; -.
DR eggNOG; KOG0616; Eukaryota.
DR HOGENOM; CLU_000288_63_3_1; -.
DR InParanoid; P40376; -.
DR OMA; QEDPPRY; -.
DR PhylomeDB; P40376; -.
DR BRENDA; 2.7.11.11; 5613.
DR Reactome; R-SPO-163615; PKA activation.
DR Reactome; R-SPO-164378; PKA activation in glucagon signalling.
DR Reactome; R-SPO-180024; DARPP-32 events.
DR Reactome; R-SPO-432040; Vasopressin regulates renal water homeostasis via Aquaporins.
DR Reactome; R-SPO-442720; CREB1 phosphorylation through the activation of Adenylate Cyclase.
DR Reactome; R-SPO-5610787; Hedgehog 'off' state.
DR Reactome; R-SPO-9634597; GPER1 signaling.
DR Reactome; R-SPO-983231; Factors involved in megakaryocyte development and platelet production.
DR PRO; PR:P40376; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005952; C:cAMP-dependent protein kinase complex; IPI:PomBase.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; IDA:PomBase.
DR GO; GO:0000324; C:fungal-type vacuole; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0004679; F:AMP-activated protein kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; ISM:PomBase.
DR GO; GO:0004691; F:cAMP-dependent protein kinase activity; IGI:PomBase.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:PomBase.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IMP:PomBase.
DR GO; GO:0010619; P:adenylate cyclase-activating glucose-activated G protein-coupled receptor signaling pathway; IMP:PomBase.
DR GO; GO:2000766; P:negative regulation of cytoplasmic translation; EXP:PomBase.
DR GO; GO:0045721; P:negative regulation of gluconeogenesis; IMP:PomBase.
DR GO; GO:0010515; P:negative regulation of induction of conjugation with cellular fusion; IMP:PomBase.
DR GO; GO:0061987; P:negative regulation of transcription from RNA polymerase II promoter by glucose; IMP:PomBase.
DR GO; GO:0031117; P:positive regulation of microtubule depolymerization; EXP:PomBase.
DR GO; GO:0046827; P:positive regulation of protein export from nucleus; IMP:PomBase.
DR GO; GO:0010737; P:protein kinase A signaling; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
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 ATP-binding; cAMP; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..512
FT /note="cAMP-dependent protein kinase catalytic subunit"
FT /id="PRO_0000086047"
FT DOMAIN 201..456
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 457..512
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT REGION 1..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 118..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..137
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..166
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 324
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 207..215
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 230
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 356
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 512 AA; 57578 MW; AF3547557AADDD84 CRC64;
MDTTAVASKG STNVGSSTDT LSTSASLHPS MNAGSVNEYS EQQRHGTNSF NGKPSVHDSV
GSDASVSNGH NNHNESSLWT SGIPKALEEA TKSKKPDSLV STSTSGCASA HSVGYQNIDN
LIPSPLPESA SRSSSQSSHQ RHSRDGRGEL GSEHGERRSA MDGLRDRHIR KVRVSQLLDL
QRRRIRPADH TTKDRYGIQD FNFLQTLGTG SFGRVHLVQS NHNRLYYAIK VLEKKKIVDM
KQIEHTCDER YILSRVQHPF ITILWGTFQD AKNLFMVMDF AEGGELFSLL RKCHRFPEKV
AKFYAAEVIL ALDYLHHNQI VYRDLKPENL LLDRFGHLKI VDFGFAKRVS TSNCCTLCGT
PDYLAPEIIS LKPYNKAADW WSLGILIFEM LAGYPPFYSE NPMKLYENIL EGKVNYPSYF
SPASIDLLSH LLQRDITCRY GNLKDGSMDI IMHPWFRDIS WDKILTRKIE VPYVPPIQAG
MGDSSQFDAY ADVATDYGTS EDPEFTSIFK DF
