KAPR_SCHPO
ID KAPR_SCHPO Reviewed; 412 AA.
AC P36600; O14272;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2001, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=cAMP-dependent protein kinase regulatory subunit;
DE Short=PKA regulatory subunit;
GN Name=cgs1; ORFNames=SPAC8C9.03;
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 [GENOMIC DNA].
RX PubMed=1657594; DOI=10.1002/j.1460-2075.1991.tb04945.x;
RA Devoti J., Seydoux G., Beach D., McLeod M.;
RT "Interaction between ran1+ protein kinase and cAMP dependent protein kinase
RT as negative regulators of fission yeast meiosis.";
RL EMBO J. 10:3759-3768(1991).
RN [2]
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104, 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 -!- SUBUNIT: Tetramer, composed of 2 regulatory (R) and 2 catalytic (C)
CC subunits. In the presence of cAMP it dissociates into 2 active
CC monomeric C subunits and an R dimer.
CC -!- SIMILARITY: Belongs to the cAMP-dependent kinase regulatory chain
CC family. {ECO:0000305}.
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DR EMBL; S64905; AAB20314.1; -; Genomic_DNA.
DR EMBL; CU329670; CAB16291.2; -; Genomic_DNA.
DR PIR; S18634; S18634.
DR PIR; T39140; T39140.
DR RefSeq; NP_594274.1; NM_001019697.2.
DR AlphaFoldDB; P36600; -.
DR SMR; P36600; -.
DR BioGRID; 279773; 22.
DR STRING; 4896.SPAC8C9.03.1; -.
DR iPTMnet; P36600; -.
DR MaxQB; P36600; -.
DR PaxDb; P36600; -.
DR PRIDE; P36600; -.
DR EnsemblFungi; SPAC8C9.03.1; SPAC8C9.03.1:pep; SPAC8C9.03.
DR GeneID; 2543351; -.
DR KEGG; spo:SPAC8C9.03; -.
DR PomBase; SPAC8C9.03; cgs1.
DR VEuPathDB; FungiDB:SPAC8C9.03; -.
DR eggNOG; KOG1113; Eukaryota.
DR HOGENOM; CLU_018310_0_1_1; -.
DR InParanoid; P36600; -.
DR OMA; YDNWSPP; -.
DR PhylomeDB; P36600; -.
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:P36600; -.
DR Proteomes; UP000002485; Chromosome I.
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; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0030552; F:cAMP binding; IMP:PomBase.
DR GO; GO:0004862; F:cAMP-dependent protein kinase inhibitor activity; IMP:PomBase.
DR GO; GO:0034236; F:protein kinase A catalytic subunit binding; IBA:GO_Central.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IMP:PomBase.
DR GO; GO:0042149; P:cellular response to glucose starvation; IDA:PomBase.
DR GO; GO:0110034; P:negative regulation of adenylate cyclase-activating glucose-activated G protein-coupled receptor signaling pathway; IC:PomBase.
DR GO; GO:2000480; P:negative regulation of cAMP-dependent protein kinase activity; IBA:GO_Central.
DR GO; GO:0046827; P:positive regulation of protein export from nucleus; IMP:PomBase.
DR CDD; cd00038; CAP_ED; 2.
DR Gene3D; 2.60.120.10; -; 2.
DR InterPro; IPR012198; cAMP_dep_PK_reg_su.
DR InterPro; IPR003117; cAMP_dep_PK_reg_su_I/II_a/b.
DR InterPro; IPR018490; cNMP-bd-like.
DR InterPro; IPR018488; cNMP-bd_CS.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR Pfam; PF00027; cNMP_binding; 2.
DR Pfam; PF02197; RIIa; 1.
DR PIRSF; PIRSF000548; PK_regulatory; 1.
DR SMART; SM00100; cNMP; 2.
DR SMART; SM00394; RIIa; 1.
DR SUPFAM; SSF51206; SSF51206; 2.
DR PROSITE; PS00888; CNMP_BINDING_1; 2.
DR PROSITE; PS00889; CNMP_BINDING_2; 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 2.
PE 1: Evidence at protein level;
KW cAMP; cAMP-binding; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Repeat.
FT CHAIN 1..412
FT /note="cAMP-dependent protein kinase regulatory subunit"
FT /id="PRO_0000205414"
FT REGION 1..142
FT /note="Dimerization and phosphorylation"
FT REGION 392..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 101..105
FT /note="Pseudophosphorylation motif"
FT BINDING 143..277
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="1"
FT /ligand_note="high affinity"
FT BINDING 224
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="1"
FT /ligand_note="high affinity"
FT BINDING 233
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="1"
FT /ligand_note="high affinity"
FT BINDING 278..412
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="2"
FT /ligand_note="low affinity"
FT BINDING 344
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="2"
FT /ligand_note="low affinity"
FT BINDING 353
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="2"
FT /ligand_note="low affinity"
FT MOD_RES 104
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT CONFLICT 274
FT /note="E -> Q (in Ref. 1; AAB20314)"
FT /evidence="ECO:0000305"
FT CONFLICT 295
FT /note="Q -> L (in Ref. 1; AAB20314)"
FT /evidence="ECO:0000305"
FT CONFLICT 326
FT /note="Missing (in Ref. 1; AAB20314)"
FT /evidence="ECO:0000305"
FT CONFLICT 336
FT /note="L -> Q (in Ref. 1; AAB20314)"
FT /evidence="ECO:0000305"
FT CONFLICT 356
FT /note="T -> P (in Ref. 1; AAB20314)"
FT /evidence="ECO:0000305"
FT CONFLICT 397
FT /note="E -> K (in Ref. 1; AAB20314)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 412 AA; 46468 MW; CA6D4D53D308EF2B CRC64;
MSFEEVYEEL KALVDEQNPS DVLQFCYDFF GEKLKAERSV FRRGDTITES FSDGDESDFL
SELNDMVAGP EAIGPDAKYV PELGGLKEMN VSYPQNYNLL RRQSVSTESM NPSAFALETK
RTFPPKDPED LKRLKRSVAG NFLFKNLDEE HYNEVLNAMT EKRIGEAGVA VIVQGAVGDY
FYIVEQGEFD VYKRPELNIT PEEVLSSGYG NYITTISPGE YFGELALMYN APRAASVVSK
TPNNVIYALD RTSFRRIVFE NAYRQRMLYE SLLEEVPILS SLDKYQRQKI ADALQTVVYQ
AGSIVIRQGD IGNQFYLIED GEAEVVKNGK GVVVTLTKGD YFGELALIHE TVRNATVQAK
TRLKLATFDK PTFNRLLGNA IDLMRNQPRA RMGMDNEYGD QSLHRSPPST KA
