KAPCB_PIG
ID KAPCB_PIG Reviewed; 351 AA.
AC P05383;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=cAMP-dependent protein kinase catalytic subunit beta;
DE Short=PKA C-beta;
DE EC=2.7.11.11;
GN Name=PRKACB;
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] OF 14-251.
RX PubMed=2441988; DOI=10.1111/j.1432-1033.1987.tb13326.x;
RA Adavani S.R., Schwarz M., Showers M.O., Maurer R.A., Hemmings B.A.;
RT "Multiple mRNA species code for the catalytic subunit of the cAMP-dependent
RT protein kinase from LLC-PK1 cells. Evidence for two forms of the catalytic
RT subunit.";
RL Eur. J. Biochem. 167:221-226(1987).
RN [2]
RP PROTEIN SEQUENCE OF 2-8; 10-22 AND 30-47, MYRISTOYLATION AT GLY-2, AND
RP DEAMIDATION AT ASN-3.
RX PubMed=9521123; DOI=10.1002/pro.5560070227;
RA Jedrzejewski P.T., Girod A., Tholey A., Koenig N., Thullner S., Kinzel V.,
RA Bossemeyer D.;
RT "A conserved deamidation site at Asn 2 in the catalytic subunit of
RT mammalian cAMP-dependent protein kinase detected by capillary LC-MS and
RT tandem mass spectrometry.";
RL Protein Sci. 7:457-469(1998).
RN [3]
RP DEAMIDATION AT ASN-3, AND SUBCELLULAR LOCATION.
RX PubMed=10684253; DOI=10.1083/jcb.148.4.715;
RA Pepperkok R., Hotz-Wagenblatt A., Koenig N., Girod A., Bossemeyer D.,
RA Kinzel V.;
RT "Intracellular distribution of mammalian protein kinase A catalytic subunit
RT altered by conserved Asn2 deamidation.";
RL J. Cell Biol. 148:715-726(2000).
CC -!- FUNCTION: Mediates cAMP-dependent signaling triggered by receptor
CC binding to GPCRs. PKA activation regulates diverse cellular processes
CC such as cell proliferation, the cell cycle, differentiation and
CC regulation of microtubule dynamics, chromatin condensation and
CC decondensation, nuclear envelope disassembly and reassembly, as well as
CC regulation of intracellular transport mechanisms and ion flux.
CC Regulates the abundance of compartmentalized pools of its regulatory
CC subunits through phosphorylation of PJA2 which binds and ubiquitinates
CC these subunits, leading to their subsequent proteolysis. Phosphorylates
CC GPKOW which regulates its ability to bind RNA.
CC {ECO:0000250|UniProtKB:P22694}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.11;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.11;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- ACTIVITY REGULATION: Activated by cAMP. {ECO:0000250|UniProtKB:P22694}.
CC -!- SUBUNIT: A number of inactive tetrameric holoenzymes are produced by
CC the combination of homo- or heterodimers of the different regulatory
CC subunits associated with two catalytic subunits. cAMP causes the
CC dissociation of the inactive holoenzyme into a dimer of regulatory
CC subunits bound to four cAMP and two free monomeric catalytic subunits.
CC Interacts with PRKAR1A and PRKAR2B (By similarity). The cAMP-dependent
CC protein kinase catalytic subunit binds PJA2. Interacts with GPKOW.
CC {ECO:0000250|UniProtKB:P05132, ECO:0000250|UniProtKB:P22694}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane
CC {ECO:0000250}. Membrane {ECO:0000250|UniProtKB:P22694}; Lipid-anchor
CC {ECO:0000250|UniProtKB:P22694}. Nucleus {ECO:0000250}.
CC Note=Translocates into the nucleus (monomeric catalytic subunit). The
CC inactive holoenzyme is found in the cytoplasm. {ECO:0000250}.
CC -!- PTM: Asn-3 is deaminated to Asp in more than 25% of the proteins,
CC giving rise to 2 major isoelectric variants, called CB and CA
CC respectively (0.4 pH unit change). Deamidation proceeds via the so-
CC called beta-aspartyl shift mechanism and yields either 'D-Asp-2'
CC (major) or 'D-isoAsp-2' (minor), in addition to L-isomers. Deamidation
CC occurs after the addition of myristate. The Asn-3 form reaches a
CC significantly larger nuclear/cytoplasmic ratio than the 'Asp-2' form.
CC {ECO:0000269|PubMed:10684253, ECO:0000269|PubMed:9521123}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. cAMP subfamily. {ECO:0000305}.
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DR EMBL; X05998; CAA29415.1; -; mRNA.
DR PIR; S00085; S00085.
DR AlphaFoldDB; P05383; -.
DR SMR; P05383; -.
DR iPTMnet; P05383; -.
DR PeptideAtlas; P05383; -.
DR PRIDE; P05383; -.
DR InParanoid; P05383; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004679; F:AMP-activated protein kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0004691; F:cAMP-dependent protein kinase activity; ISS:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0010737; P:protein kinase A signaling; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR CDD; cd14209; STKc_PKA; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR044109; STKc_PKA.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; cAMP; Cell membrane; Cytoplasm; Direct protein sequencing;
KW Kinase; Lipoprotein; Membrane; Myristate; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9521123"
FT CHAIN 2..351
FT /note="cAMP-dependent protein kinase catalytic subunit
FT beta"
FT /id="PRO_0000086062"
FT DOMAIN 44..298
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 299..351
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT ACT_SITE 167
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 50..58
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 73
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 3
FT /note="Deamidated asparagine; partial"
FT /evidence="ECO:0000269|PubMed:10684253,
FT ECO:0000269|PubMed:9521123"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05132"
FT MOD_RES 69
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P68181"
FT MOD_RES 140
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05132"
FT MOD_RES 198
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P05132"
FT MOD_RES 322
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P68182"
FT MOD_RES 331
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P05132"
FT MOD_RES 339
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P68182"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:9521123"
SQ SEQUENCE 351 AA; 40594 MW; 384A1EB1FC198B61 CRC64;
MGNAATAKKG SEVESVKEFL AKAKEDFLKK WENPAPNNAG LEDFERKKTL GTGSFGRVML
VKHKATEQYY AMKILDKQKV VKLKQIEHTL NEKRILQAVN FPFLVRLEFS FKDNSNLYMV
MEYVPGGEMF SHLRRIGRFS EPHARFYAAQ IVLTFEYLHS LDLIYRDLKP ENLLIDHQGY
IQVTDFGFAK RVKGRTWTLC GTPEYLAPEI ILSKGYNKAV DWWALGVLIY EMAAGYPPFF
ADQPIQIYEK IVSGKVRFPS HFSSDLKDLL RNLLQVDLTK RFGNLKNGVS DIKTHKWFAT
TDWIAIYQRK VEAPFIPKFR GSGDTSNFDD YEEEDIRVSI TEKCGKEFCE F
