KAPR_STRPU
ID KAPR_STRPU Reviewed; 369 AA.
AC Q26619;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=cAMP-dependent protein kinase type II regulatory subunit;
OS Strongylocentrotus purpuratus (Purple sea urchin).
OC Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Echinoidea;
OC Euechinoidea; Echinacea; Camarodonta; Echinidea; Strongylocentrotidae;
OC Strongylocentrotus.
OX NCBI_TaxID=7668;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Testis;
RA Rankin T.L., Dangott L.J.;
RT "Regulatory subunit type II of cyclic AMP-dependent protein kinase
RT localized in sea urchin spermatozoa.";
RL Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the cAMP-dependent kinase regulatory chain
CC family. {ECO:0000305}.
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DR EMBL; U19887; AAA61966.1; -; mRNA.
DR RefSeq; NP_999688.1; NM_214523.1.
DR AlphaFoldDB; Q26619; -.
DR SMR; Q26619; -.
DR STRING; 7668.SPU_018419-tr; -.
DR EnsemblMetazoa; NM_214523; NP_999688; LOC373288.
DR GeneID; 373288; -.
DR KEGG; spu:373288; -.
DR eggNOG; KOG1113; Eukaryota.
DR HOGENOM; CLU_018310_2_0_1; -.
DR OMA; YDNWSPP; -.
DR OrthoDB; 1047290at2759; -.
DR PhylomeDB; Q26619; -.
DR Proteomes; UP000007110; Unassembled WGS sequence.
DR GO; GO:0005952; C:cAMP-dependent protein kinase complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0030552; F:cAMP binding; IBA:GO_Central.
DR GO; GO:0004862; F:cAMP-dependent protein kinase inhibitor activity; IBA:GO_Central.
DR GO; GO:0034236; F:protein kinase A catalytic subunit binding; IBA:GO_Central.
DR GO; GO:2000480; P:negative regulation of cAMP-dependent protein kinase activity; IBA:GO_Central.
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; 1.
DR PROSITE; PS00889; CNMP_BINDING_2; 2.
DR PROSITE; PS50042; CNMP_BINDING_3; 2.
PE 2: Evidence at transcript level;
KW cAMP; cAMP-binding; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Repeat.
FT CHAIN 1..369
FT /note="cAMP-dependent protein kinase type II regulatory
FT subunit"
FT /id="PRO_0000205398"
FT REGION 1..120
FT /note="Dimerization and phosphorylation"
FT /evidence="ECO:0000250"
FT REGION 56..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 121..238
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="1"
FT BINDING 186
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 195
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 239..365
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="2"
FT BINDING 313
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 322
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT MOD_RES 81
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 369 AA; 41789 MW; 30FCECC13D8C26A5 CRC64;
MNFEIPEGLT DLLQDFTVAV LREKPSDLVE FASSYFAKLQ ENNISLGGKR GVTFTAPEDA
ESDIDDEPPE LPKNRYARRK SVCAEKYDPE ADNDTDTQKL VYPKSDEQRA RLTEAVKNIL
LFRALDEKQM QEVIDAMFEK KTTPGDHVID QGDDGDNFYV IDRGEYDIFV NDNKVGAYKD
SGSFGELALM YNTPRAATIA ATTDGILWAL DRVSFRRIVL KNAAKKRRIY EELLEKVSIF
KSLEPYERMN LADALVTRTY EDGDCIIAQG DGADGCYFIE AGQCRIAMKS ERSDNPDEEK
EVAIYNQGQY FGELALLTNK PRAASVYAVE DVDCLLDVNA FERLLGPCMD IMKRNIEHYE
QETSRLFGK