ID   KAPR_APLCA              Reviewed;         378 AA.
AC   P31319;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=cAMP-dependent protein kinase regulatory subunit;
DE   AltName: Full=N4 subunit of protein kinase A;
OS   Aplysia californica (California sea hare).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Heterobranchia; Euthyneura; Tectipleura; Aplysiida; Aplysioidea;
OC   Aplysiidae; Aplysia.
OX   NCBI_TaxID=6500;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1310865; DOI=10.1016/0896-6273(92)90304-v;
RA   Bergold P.J., Beushausen S.A., Sacktor T.C., Cheley S., Bayley H.,
RA   Schwartz J.H.;
RT   "A regulatory subunit of the cAMP-dependent protein kinase down-regulated
RT   in aplysia sensory neurons during long-term sensitization.";
RL   Neuron 8:387-397(1992).
CC   -!- SUBUNIT: The inactive form of the enzyme is composed of two regulatory
CC       chains and two catalytic chains. Activation by cAMP produces two active
CC       catalytic monomers and a regulatory dimer that binds four cAMP
CC       molecules.
CC   -!- PTM: The pseudophosphorylation site binds to the substrate-binding
CC       region of the catalytic chain but is not phosphorylated. The
CC       physiological significance of phosphorylations by other kinases is
CC       unclear.
CC   -!- SIMILARITY: Belongs to the cAMP-dependent kinase regulatory chain
CC       family. {ECO:0000305}.
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DR   EMBL; X62382; CAA44246.1; -; mRNA.
DR   PIR; JH0590; OKGAR1.
DR   RefSeq; NP_001191582.1; NM_001204653.1.
DR   AlphaFoldDB; P31319; -.
DR   SMR; P31319; -.
DR   GeneID; 100533363; -.
DR   OrthoDB; 1047290at2759; -.
DR   GO; GO:0005952; C:cAMP-dependent protein kinase complex; IEA:InterPro.
DR   GO; GO:0030552; F:cAMP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008603; F:cAMP-dependent protein kinase regulator activity; IEA:InterPro.
DR   GO; GO:0001932; P:regulation of protein phosphorylation; IEA:InterPro.
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; 2.
DR   PROSITE; PS50042; CNMP_BINDING_3; 2.
PE   2: Evidence at transcript level;
KW   Acetylation; cAMP; cAMP-binding; Nucleotide-binding; Phosphoprotein;
KW   Repeat.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..378
FT                   /note="cAMP-dependent protein kinase regulatory subunit"
FT                   /id="PRO_0000205393"
FT   REGION          2..133
FT                   /note="Dimerization and phosphorylation"
FT   REGION          56..96
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           93..97
FT                   /note="Pseudophosphorylation motif"
FT   COMPBIAS        56..79
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         134..251
FT                   /ligand="3',5'-cyclic AMP"
FT                   /ligand_id="ChEBI:CHEBI:58165"
FT                   /ligand_label="1"
FT   BINDING         199
FT                   /ligand="3',5'-cyclic AMP"
FT                   /ligand_id="ChEBI:CHEBI:58165"
FT                   /ligand_label="1"
FT   BINDING         208
FT                   /ligand="3',5'-cyclic AMP"
FT                   /ligand_id="ChEBI:CHEBI:58165"
FT                   /ligand_label="1"
FT   BINDING         252..378
FT                   /ligand="3',5'-cyclic AMP"
FT                   /ligand_id="ChEBI:CHEBI:58165"
FT                   /ligand_label="2"
FT   BINDING         323
FT                   /ligand="3',5'-cyclic AMP"
FT                   /ligand_id="ChEBI:CHEBI:58165"
FT                   /ligand_label="2"
FT   BINDING         332
FT                   /ligand="3',5'-cyclic AMP"
FT                   /ligand_id="ChEBI:CHEBI:58165"
FT                   /ligand_label="2"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         98
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   378 AA;  42737 MW;  4982603DF922CF71 CRC64;
     MAANTDEEQS LKECEAYVQK HNIQQLLKEC IVQLVVNKPE SPLAFLRDHF DRLEKEQVAK
     EKSKSATPPS DEKEEDMSST PPQMHPAMNK RMRRGAVSAE VYREEDAAQY VKKVVPKDYK
     TMAALSKAIS KNVLFSHLDD NERSDIFDAM FPVHRHAGEV IIQQGDEGDN FYVIDQGEVD
     VYVNNVHVTS IGEGGSFGEL ALIYGTPRAA TVKAKTDVKL WGIDRDSYRR ILMGSTIRKR
     KIYEDFLSKV SILENLDKWE RLTVADALEP VQFEDKEEIV RQGEPGEDFF IILEGSAAVL
     QRRSENEEPV EVGRLGPSDY FGEIALLLDR PRAATVVARG PLKCVKLDRA RFERVLGPCS
     DILKRNISQY NSFVSLSV