KAP3_BOVIN
ID KAP3_BOVIN Reviewed; 418 AA.
AC P31322;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=cAMP-dependent protein kinase type II-beta regulatory subunit;
GN Name=PRKAR2B;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=2254332; DOI=10.1016/s0021-9258(18)45811-5;
RA Luo Z., Shafit-Zagardo B., Erlichman J.;
RT "Identification of the MAP2- and P75-binding domain in the regulatory
RT subunit (RII beta) of type II cAMP-dependent protein kinase. Cloning and
RT expression of the cDNA for bovine brain RII beta.";
RL J. Biol. Chem. 265:21804-21810(1990).
CC -!- FUNCTION: Regulatory subunit of the cAMP-dependent protein kinases
CC involved in cAMP signaling in cells. Type II regulatory chains mediate
CC membrane association by binding to anchoring proteins, including the
CC MAP2 kinase.
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. Interacts with PRKACA and PRKACB. Interacts with the
CC phosphorylated form of PJA2. Forms a complex composed of PRKAR2B, GSK3B
CC and GSKIP through GSKIP interaction; facilitates PKA-induced
CC phosphorylation and regulates GSK3B activity.
CC {ECO:0000250|UniProtKB:P31323}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane
CC {ECO:0000250}. Note=Colocalizes with PJA2 in the cytoplasm and at the
CC cell membrane. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Four types of regulatory chains are found: I-alpha,
CC I-beta, II-alpha, and II-beta. Their expression varies among tissues
CC and is in some cases constitutive and in others inducible.
CC -!- PTM: Phosphorylated by the activated catalytic chain.
CC -!- SIMILARITY: Belongs to the cAMP-dependent kinase regulatory chain
CC family. {ECO:0000305}.
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DR EMBL; J05692; AAA30755.1; -; mRNA.
DR PIR; A36528; OKBOR2.
DR RefSeq; NP_777074.1; NM_174649.2.
DR AlphaFoldDB; P31322; -.
DR SMR; P31322; -.
DR BioGRID; 159716; 1.
DR DIP; DIP-547N; -.
DR STRING; 9913.ENSBTAP00000019916; -.
DR ChEMBL; CHEMBL2111446; -.
DR DrugCentral; P31322; -.
DR iPTMnet; P31322; -.
DR PaxDb; P31322; -.
DR PeptideAtlas; P31322; -.
DR GeneID; 282463; -.
DR KEGG; bta:282463; -.
DR CTD; 5577; -.
DR eggNOG; KOG1113; Eukaryota.
DR InParanoid; P31322; -.
DR OrthoDB; 1047290at2759; -.
DR PRO; PR:P31322; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005952; C:cAMP-dependent protein kinase complex; IEA:InterPro.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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 cAMP; cAMP-binding; Cell membrane; Cytoplasm; Membrane; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..418
FT /note="cAMP-dependent protein kinase type II-beta
FT regulatory subunit"
FT /id="PRO_0000205389"
FT REGION 2..153
FT /note="Dimerization and phosphorylation"
FT REGION 45..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 154..275
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="1"
FT BINDING 223
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="1"
FT BINDING 232
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="1"
FT BINDING 276..418
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="2"
FT BINDING 352
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="2"
FT BINDING 361
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="2"
FT MOD_RES 69
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P31323"
FT MOD_RES 83
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P31323"
FT MOD_RES 85
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P31323"
FT MOD_RES 114
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P31323"
SQ SEQUENCE 418 AA; 46336 MW; 669CE065D0455D3F CRC64;
MSIEIPAGLT ELLQGFTVEV LRHQPADLLE FALQHFTRLQ EENERKGTAR FGHEGRTWGD
AGAAGGGGTP SKGVNFAEEP RHSDSENGEE EEEEAADAGA FNAPVINRFT RRASVCAEAY
NPDEEEDDAE SRIIHPKTDD QRNRLQEACK DILLFKNLDP EQMSQVLDAM FEKLVKEGEH
VIDQGDDGDN FYVIDRGTFD IYVKCDGVGR CVGNYDNRGS FGELALMYNT PRAATITATS
PGALWGLDRV TFRRIIVKNN AKKRKMYESF IESLPFLKSL EVSERLKVVD VIGTKVYNDG
EQIIAQGDSA DSFFIVESGE VKITMKRKGK SEVEENGAVE IARCSRGQYF GELALVTNKP
RAASAHAIGT VKCLAMDVQA FERLLGPCME IMKRNIATYE EQLVALFGTN MDIVEPTA
