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cAMP-dependent protein kinase catalytic subunit alpha (PKA C-alpha) (EC 2.7.11.11)

 KAPCA_CRIGR             Reviewed;         351 AA.
P25321;
01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
25-OCT-2017, entry version 116.
RecName: Full=cAMP-dependent protein kinase catalytic subunit alpha;
Short=PKA C-alpha;
EC=2.7.11.11;
Name=PRKACA;
Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Cricetidae; Cricetinae; Cricetulus.
NCBI_TaxID=10029;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1645343;
Howard P., Day K.H., Kim K.E., Richardson J., Thomas J., Abraham I.,
Fleischmann R.D., Gottesman M.M., Maurer R.A.;
"Decreased catalytic subunit mRNA levels and altered catalytic subunit
mRNA structure in a cAMP-resistant Chinese hamster ovary cell line.";
J. Biol. Chem. 266:10189-10195(1991).
-!- FUNCTION: Phosphorylates a large number of substrates in the
cytoplasm and the nucleus. Regulates the abundance of
compartmentalized pools of its regulatory subunits through
phosphorylation of PJA2 which binds and ubiquitinates these
subunits, leading to their subsequent proteolysis. Phosphorylates
CDC25B, ABL1, NFKB1, CLDN3, PSMC5/RPT6, PJA2, RYR2, RORA and VASP.
RORA is activated by phosphorylation. Required for glucose-
mediated adipogenic differentiation increase and osteogenic
differentiation inhibition from osteoblasts. Involved in the
regulation of platelets in response to thrombin and collagen;
maintains circulating platelets in a resting state by
phosphorylating proteins in numerous platelet inhibitory pathways
when in complex with NF-kappa-B (NFKB1 and NFKB2) and I-kappa-B-
alpha (NFKBIA), but thrombin and collagen disrupt these complexes
and free active PRKACA stimulates platelets and leads to platelet
aggregation by phosphorylating VASP. Prevents the
antiproliferative and anti-invasive effects of alpha-
difluoromethylornithine in breast cancer cells when activated.
RYR2 channel activity is potentiated by phosphorylation in
presence of luminal Ca(2+), leading to reduced amplitude and
increased frequency of store overload-induced Ca(2+) release
(SOICR) characterized by an increased rate of Ca(2+) release and
propagation velocity of spontaneous Ca(2+) waves, despite reduced
wave amplitude and resting cytosolic Ca(2+). PSMC5/RPT6 activation
by phosphorylation stimulates proteasome. Negatively regulates
tight junctions (TJs) in ovarian cancer cells via CLDN3
phosphorylation. NFKB1 phosphorylation promotes NF-kappa-B p50-p50
DNA binding. Involved in embryonic development by down-regulating
the Hedgehog (Hh) signaling pathway that determines embryo pattern
formation and morphogenesis. Prevents meiosis resumption in
prophase-arrested oocytes via CDC25B inactivation by
phosphorylation. May also regulate rapid eye movement (REM) sleep
in the pedunculopontine tegmental (PPT) (By similarity).
Phosphorylates APOBEC3G and AICDA (By similarity). Phosphorylates
HSF1; this phosphorylation promotes HSF1 nuclear localization and
transcriptional activity upon heat shock (By similarity).
{ECO:0000250, ECO:0000250|UniProtKB:P17612}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- ENZYME REGULATION: Allosterically activated by various compounds,
including ATP. Activated by cAMP; the nucleotide acts as a dynamic
and allosteric activator by coupling the two lobes of apo PKA,
enhancing the enzyme dynamics synchronously and priming it for
catalysis.
-!- SUBUNIT: A number of inactive tetrameric holoenzymes are produced
by the combination of homo- or heterodimers of the different
regulatory subunits associated with two catalytic subunits. cAMP
causes the dissociation of the inactive holoenzyme into a dimer of
regulatory subunits bound to four cAMP and two free monomeric
catalytic subunits. Activates cAMP-sensitive PKAI and PKAII
holoenzymes by interacting with regulatory subunit (R) of PKA,
PRKAR1A/PKR1 and PRKAR2A/PKR2, respectively. Interacts with NFKB1,
NFKB2 and NFKBIA in platelets; these interactions are disrupted by
thrombin and collagen. Binds to ABL1 in spermatozoa and with
CDC25B in oocytes (By similarity). Interacts with APOBEC3G and
AICDA (By similarity). Interacts with RAB13; downstream effector
of RAB13 involved in tight junction assembly (By similarity).
Found in a complex at least composed of MROH2B, PRKACA and TCP11
(By similarity). Interacts with MROH2B (By similarity). Interacts
with TCP11 (By similarity). Interacts with HSF1 (By similarity).
{ECO:0000250, ECO:0000250|UniProtKB:P05132,
ECO:0000250|UniProtKB:P17612}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus
{ECO:0000250}. Cell membrane {ECO:0000250}. Mitochondrion
{ECO:0000250}. Membrane {ECO:0000250|UniProtKB:P17612}; Lipid-
anchor {ECO:0000250|UniProtKB:P17612}. Cell projection, cilium,
flagellum {ECO:0000250|UniProtKB:P05132}. Cytoplasmic vesicle,
secretory vesicle, acrosome {ECO:0000250|UniProtKB:P05132}.
Note=Translocates into the nucleus (monomeric catalytic subunit).
The inactive holoenzyme is found in the cytoplasm. Distributed
throughout the cytoplasm in meiotically incompetent oocytes.
Associated to mitochondrion as meiotic competence is acquired.
Aggregates around the germinal vesicles (GV) at the immature GV
stage oocytes (By similarity). Expressed in the midpiece region of
the sperm flagellum (By similarity). Colocalizes with MROH2B and
TCP11 on the acrosome and tail regions in round spermatids and
spermatozoa regardless of the capacitation status of the sperm (By
similarity). Colocalizes with HSF1 in nuclear stress bodies (nSBs)
upon heat shock (By similarity). {ECO:0000250,
ECO:0000250|UniProtKB:P05132, ECO:0000250|UniProtKB:P17612}.
-!- TISSUE SPECIFICITY: Ubiquitously expressed in mammalian tissues.
-!- PTM: Asn-3 is partially deaminated to Asp giving rise to 2 major
isoelectric variants, called CB and CA respectively.
{ECO:0000250}.
-!- PTM: Autophosphorylated. Phosphorylation is enhanced by vitamin
K(2). Phosphorylated on threonine and serine residues.
Phosphorylation on Thr-198 is required for full activity (By
similarity). {ECO:0000250}.
-!- PTM: Phosphorylated at Tyr-331 by activated receptor tyrosine
kinases EGFR and PDGFR; this increases catalytic efficienncy.
{ECO:0000250}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
protein kinase family. cAMP subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; M63311; AAA37010.1; -; mRNA.
PIR; B40384; OKHYCA.
PDB; 4WIH; X-ray; 1.14 A; A=1-351.
PDBsum; 4WIH; -.
ProteinModelPortal; P25321; -.
SMR; P25321; -.
PRIDE; P25321; -.
Ensembl; ENSCGRT00001021270; ENSCGRP00001017026; ENSCGRG00001017184.
HOVERGEN; HBG108317; -.
BRENDA; 2.7.11.11; 1309.
GO; GO:0001669; C:acrosomal vesicle; ISS:UniProtKB.
GO; GO:0005952; C:cAMP-dependent protein kinase complex; IEA:Ensembl.
GO; GO:0005813; C:centrosome; IEA:Ensembl.
GO; GO:0097546; C:ciliary base; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; IEA:Ensembl.
GO; GO:0043197; C:dendritic spine; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
GO; GO:0045171; C:intercellular bridge; IEA:Ensembl.
GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
GO; GO:0031594; C:neuromuscular junction; IEA:Ensembl.
GO; GO:0016607; C:nuclear speck; IEA:Ensembl.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
GO; GO:0044853; C:plasma membrane raft; IEA:Ensembl.
GO; GO:0036126; C:sperm flagellum; ISS:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004691; F:cAMP-dependent protein kinase activity; ISS:UniProtKB.
GO; GO:0000287; F:magnesium ion binding; IEA:Ensembl.
GO; GO:0030145; F:manganese ion binding; IEA:Ensembl.
GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
GO; GO:0034237; F:protein kinase A regulatory subunit binding; IEA:Ensembl.
GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; IEA:Ensembl.
GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
GO; GO:0071333; P:cellular response to glucose stimulus; IEA:Ensembl.
GO; GO:0034605; P:cellular response to heat; ISS:UniProtKB.
GO; GO:0071374; P:cellular response to parathyroid hormone stimulus; IEA:Ensembl.
GO; GO:0001707; P:mesoderm formation; IEA:Ensembl.
GO; GO:0050804; P:modulation of chemical synaptic transmission; IEA:Ensembl.
GO; GO:0006397; P:mRNA processing; IEA:Ensembl.
GO; GO:1901621; P:negative regulation of smoothened signaling pathway involved in dorsal/ventral neural tube patterning; IEA:Ensembl.
GO; GO:0001843; P:neural tube closure; IEA:Ensembl.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IEA:Ensembl.
GO; GO:0018107; P:peptidyl-threonine phosphorylation; IEA:Ensembl.
GO; GO:0071158; P:positive regulation of cell cycle arrest; IEA:Ensembl.
GO; GO:0046827; P:positive regulation of protein export from nucleus; IEA:Ensembl.
GO; GO:0046777; P:protein autophosphorylation; IEA:Ensembl.
GO; GO:2000810; P:regulation of bicellular tight junction assembly; IEA:Ensembl.
GO; GO:0045667; P:regulation of osteoblast differentiation; IEA:Ensembl.
GO; GO:0061136; P:regulation of proteasomal protein catabolic process; IEA:Ensembl.
GO; GO:0070613; P:regulation of protein processing; IEA:Ensembl.
GO; GO:0048240; P:sperm capacitation; IEA:Ensembl.
InterPro; IPR000961; AGC-kinase_C.
InterPro; IPR011009; Kinase-like_dom.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00069; Pkinase; 1.
SMART; SM00133; S_TK_X; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS51285; AGC_KINASE_CTER; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
3D-structure; ATP-binding; cAMP; Cell membrane; Cell projection;
Cytoplasm; Cytoplasmic vesicle; Kinase; Lipoprotein; Membrane;
Mitochondrion; Myristate; Nucleotide-binding; Nucleus; Phosphoprotein;
Serine/threonine-protein kinase; Transferase.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P00517}.
CHAIN 2 351 cAMP-dependent protein kinase catalytic
subunit alpha.
/FTId=PRO_0000086051.
DOMAIN 44 298 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 299 351 AGC-kinase C-terminal.
NP_BIND 50 58 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 122 128 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 169 172 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 167 167 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 73 73 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 3 3 Deamidated asparagine. {ECO:0000250}.
MOD_RES 11 11 Phosphoserine; by autocatalysis.
{ECO:0000250|UniProtKB:P05132}.
MOD_RES 49 49 Phosphothreonine.
{ECO:0000250|UniProtKB:P17612}.
MOD_RES 140 140 Phosphoserine.
{ECO:0000250|UniProtKB:P05132}.
MOD_RES 196 196 Phosphothreonine.
{ECO:0000250|UniProtKB:P17612}.
MOD_RES 198 198 Phosphothreonine; by PDPK1.
{ECO:0000250|UniProtKB:P00517}.
MOD_RES 202 202 Phosphothreonine.
{ECO:0000250|UniProtKB:P17612}.
MOD_RES 331 331 Phosphotyrosine.
{ECO:0000250|UniProtKB:P05132}.
MOD_RES 339 339 Phosphoserine.
{ECO:0000250|UniProtKB:P00517}.
LIPID 2 2 N-myristoyl glycine.
{ECO:0000250|UniProtKB:P17612}.
HELIX 3 32 {ECO:0000244|PDB:4WIH}.
HELIX 41 43 {ECO:0000244|PDB:4WIH}.
STRAND 44 52 {ECO:0000244|PDB:4WIH}.
STRAND 54 63 {ECO:0000244|PDB:4WIH}.
TURN 64 66 {ECO:0000244|PDB:4WIH}.
STRAND 69 76 {ECO:0000244|PDB:4WIH}.
HELIX 77 82 {ECO:0000244|PDB:4WIH}.
HELIX 86 98 {ECO:0000244|PDB:4WIH}.
STRAND 107 112 {ECO:0000244|PDB:4WIH}.
STRAND 114 122 {ECO:0000244|PDB:4WIH}.
HELIX 129 136 {ECO:0000244|PDB:4WIH}.
HELIX 141 160 {ECO:0000244|PDB:4WIH}.
HELIX 170 172 {ECO:0000244|PDB:4WIH}.
STRAND 173 175 {ECO:0000244|PDB:4WIH}.
STRAND 181 183 {ECO:0000244|PDB:4WIH}.
HELIX 203 205 {ECO:0000244|PDB:4WIH}.
HELIX 208 211 {ECO:0000244|PDB:4WIH}.
HELIX 219 234 {ECO:0000244|PDB:4WIH}.
HELIX 244 253 {ECO:0000244|PDB:4WIH}.
HELIX 264 273 {ECO:0000244|PDB:4WIH}.
TURN 278 280 {ECO:0000244|PDB:4WIH}.
TURN 286 289 {ECO:0000244|PDB:4WIH}.
HELIX 290 293 {ECO:0000244|PDB:4WIH}.
HELIX 296 298 {ECO:0000244|PDB:4WIH}.
HELIX 303 307 {ECO:0000244|PDB:4WIH}.
TURN 345 350 {ECO:0000244|PDB:4WIH}.
SEQUENCE 351 AA; 40620 MW; 84333CD0B439F356 CRC64;
MGNAAAAKKG SEQESVKEFL AKAKEEFLKK WESPSQNTAQ LDHFDRIKTL GTGSFGRVML
VKHKETGNHY AMKILDKQKV VKLKQIEHTL NEKRILQAVN FPFLVKLEFS FKDNSNLYMV
MEYVPGGEMF SHLRRIGRFS EPHARFYAAQ IVLTFEYLHS LDLIYRDLKP ENLLIDQQGY
IQVTDFGFAK RVKGRTWTLC GTPEYLAPEI ILSKGYNKAV DWWALGVLIY EMAAGYPPFF
ADQPIQIYEK IVSGKVRFPS HFSSDLKDLL RNLLQVDLTK RFGNLKNGVN DIKNHKWFAT
TDWIAIYQRK VEAPFIPKFK GPGDTSNFDD YEEEEIRVSI NEKCGKEFTE F


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