KAP2_PIG
ID KAP2_PIG Reviewed; 155 AA.
AC P05207;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=cAMP-dependent protein kinase type II-alpha regulatory subunit;
DE Flags: Fragment;
GN Name=PRKAR2A;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2431926; DOI=10.1016/0014-5793(86)81114-0;
RA Hemmings B.A., Schwarz M., Adavani S.R., Jans D.A.;
RT "Expression cloning of a cDNA encoding the type II regulatory subunit of
RT the cAMP-dependent protein kinase.";
RL FEBS Lett. 209:219-222(1986).
RN [2]
RP PROTEIN SEQUENCE OF 37-42, AND PHOSPHORYLATION AT SER-41.
RC TISSUE=Skeletal muscle;
RX PubMed=225318; DOI=10.1016/s0021-9258(19)86801-1;
RA Potter R.L., Taylor S.S.;
RT "Correlation of the cAMP binding domain with a site of autophosphorylation
RT on the regulatory subunit of cAMP-dependent protein kinase II from porcine
RT skeletal muscle.";
RL J. Biol. Chem. 254:9000-9005(1979).
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 AKAP4 and CBFA2T3 (By similarity). Interacts
CC with the phosphorylated form of PJA2 (By similarity). Interacts with
CC MYRIP; this interaction may link PKA to components of the exocytosis
CC machinery, thus facilitating exocytosis, including insulin release (By
CC similarity). Forms a complex composed of PRKAR2A, GSK3B and GSKIP
CC through GSKIP interaction; facilitates PKA-induced phosphorylation and
CC regulates GSK3B activity (By similarity). Interacts with ADCY8;
CC inhibits adenylate cyclase activity through PKA phosphorylation (By
CC similarity). {ECO:0000250, ECO:0000250|UniProtKB:P13861}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane
CC {ECO:0000250}. Note=Colocalizes with PJA2 in the cytoplasm and the cell
CC 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 {ECO:0000269|PubMed:225318}.
CC -!- SIMILARITY: Belongs to the cAMP-dependent kinase regulatory chain
CC family. {ECO:0000305}.
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DR EMBL; X04709; CAA28414.1; -; mRNA.
DR PIR; A25652; A25652.
DR AlphaFoldDB; P05207; -.
DR SMR; P05207; -.
DR STRING; 9823.ENSSSCP00000012116; -.
DR iPTMnet; P05207; -.
DR PaxDb; P05207; -.
DR PeptideAtlas; P05207; -.
DR PRIDE; P05207; -.
DR eggNOG; KOG1113; Eukaryota.
DR InParanoid; P05207; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005952; C:cAMP-dependent protein kinase complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IMP:AgBase.
DR GO; GO:0042585; C:germinal vesicle; IMP:AgBase.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; IMP:AgBase.
DR GO; GO:1904146; P:positive regulation of meiotic cell cycle process involved in oocyte maturation; IMP:AgBase.
DR GO; GO:1903538; P:regulation of meiotic cell cycle process involved in oocyte maturation; IMP:AgBase.
DR CDD; cd00038; CAP_ED; 1.
DR Gene3D; 2.60.120.10; -; 1.
DR InterPro; IPR018490; cNMP-bd-like.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR SUPFAM; SSF51206; SSF51206; 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 1.
PE 1: Evidence at protein level;
KW cAMP; cAMP-binding; Cell membrane; Cytoplasm; Direct protein sequencing;
KW Membrane; Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN <1..>155
FT /note="cAMP-dependent protein kinase type II-alpha
FT regulatory subunit"
FT /id="PRO_0000205387"
FT REGION <1..81
FT /note="Dimerization and phosphorylation"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 82..>155
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="1"
FT BINDING 150
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="1"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13861"
FT MOD_RES 22
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13861"
FT MOD_RES 41
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000269|PubMed:225318"
FT NON_TER 1
FT NON_TER 155
SQ SEQUENCE 155 AA; 17706 MW; A3047AD60EF6AFAC CRC64;
SGSQDLEPSS GLVTDAIADS ESEDDEDLDV PIPSRFDRRV SVCAETYNPD EEEEDTDPRV
IHPKTDQQRC RLQEACKDIL LFKNLDQEQL SQVLDAMFER TVKVDEHVID QRDDGDNFYV
IERGTYDILV TKDNQTRSVG QYDNHGSFGE LALMY
