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

 KAPCA_SHEEP             Reviewed;         351 AA.
Q9MZD9; Q9MZD8;
15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
12-SEP-2018, entry version 117.
RecName: Full=cAMP-dependent protein kinase catalytic subunit alpha;
Short=PKA C-alpha;
EC=2.7.11.11;
Name=PRKACA;
Ovis aries (Sheep).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Caprinae; Ovis.
NCBI_TaxID=9940;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
TISSUE=Testis;
PubMed=10982398; DOI=10.1091/mbc.11.9.3031;
San Agustin J.T., Wilkerson C.G., Witman G.B.;
"The unique catalytic subunit of sperm cAMP-dependent protein kinase
is the product of an alternative C-alpha mRNA expressed specifically
in spermatogenic cells.";
Mol. Biol. Cell 11:3031-3044(2000).
[2]
PARTIAL PROTEIN SEQUENCE (ISOFORM 2).
TISSUE=Sperm;
PubMed=9733793; DOI=10.1074/jbc.273.38.24874;
San Agustin J.T., Leszyk J.D., Nuwaysir L.M., Witman G.B.;
"The catalytic subunit of the cAMP-dependent protein kinase of ovine
sperm flagella has a unique amino-terminal sequence.";
J. Biol. Chem. 273:24874-24883(1998).
-!- 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. Regulates negatively
tight junction (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. Isoform 2 phosphorylates and
activates ABL1 in sperm flagellum to promote spermatozoa
capacitation (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.
-!- ACTIVITY 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. The cAMP-dependent protein kinase catalytic
subunit binds PJA2. Both isoforms 1 and 2 forms activate 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 isoform 2 and TCP11 (By similarity). Interacts with
MROH2B (By similarity). Interacts with HSF1 (By similarity).
Isoform 2 interacts with TCP11 (By similarity). {ECO:0000250,
ECO:0000250|UniProtKB:P05132, ECO:0000250|UniProtKB:P17612}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane
{ECO:0000250}. Nucleus {ECO:0000250}. Mitochondrion {ECO:0000250}.
Membrane {ECO:0000250|UniProtKB:P17612}; Lipid-anchor
{ECO:0000250|UniProtKB:P17612}. 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). Colocalizes
with HSF1 in nuclear stress bodies (nSBs) upon heat shock (By
similarity). {ECO:0000250, ECO:0000250|UniProtKB:P17612}.
-!- SUBCELLULAR LOCATION: Isoform 2: Cell projection, cilium,
flagellum {ECO:0000250|UniProtKB:P05132}. Cytoplasmic vesicle,
secretory vesicle, acrosome {ECO:0000250|UniProtKB:P05132}.
Note=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). {ECO:0000250,
ECO:0000250|UniProtKB:P05132}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=C alpha1;
IsoId=Q9MZD9-1; Sequence=Displayed;
Note=Predominant somatic isoform.;
Name=2; Synonyms=Cs;
IsoId=Q9MZD9-2; Sequence=VSP_008016;
Note=Sperm specific.;
-!- TISSUE SPECIFICITY: Isoform 2 is sperm specific.
-!- 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; AF238979; AAF76423.1; -; mRNA.
EMBL; AF238980; AAF76424.1; -; mRNA.
RefSeq; NP_001009234.1; NM_001009234.1. [Q9MZD9-1]
UniGene; Oar.786; -.
ProteinModelPortal; Q9MZD9; -.
SMR; Q9MZD9; -.
PRIDE; Q9MZD9; -.
GeneID; 443094; -.
KEGG; oas:443094; -.
CTD; 5566; -.
HOVERGEN; HBG108317; -.
KO; K04345; -.
Proteomes; UP000002356; Unplaced.
GO; GO:0001669; C:acrosomal vesicle; ISS:UniProtKB.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0036126; C:sperm flagellum; ISS:UniProtKB.
GO; GO:0097225; C:sperm midpiece; ISS:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004691; F:cAMP-dependent protein kinase activity; IEA:UniProtKB-EC.
GO; GO:0034237; F:protein kinase A regulatory subunit binding; IEA:InterPro.
GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
GO; GO:0071333; P:cellular response to glucose stimulus; IEA:InterPro.
GO; GO:0034605; P:cellular response to heat; ISS:UniProtKB.
GO; GO:0010737; P:protein kinase A signaling; IEA:InterPro.
InterPro; IPR000961; AGC-kinase_C.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR039035; PKA_C-alpha.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
PANTHER; PTHR24353:SF82; PTHR24353:SF82; 1.
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;
Alternative splicing; ATP-binding; cAMP; Cell membrane;
Cell projection; Cilium; Complete proteome; Cytoplasm;
Cytoplasmic vesicle; Direct protein sequencing; Flagellum; Kinase;
Lipoprotein; Membrane; Mitochondrion; Myristate; Nucleotide-binding;
Nucleus; Phosphoprotein; Reference proteome;
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_0000086056.
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 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}.
VAR_SEQ 1 15 MGNAAAAKKGSEQES -> MASNPND (in isoform
2). {ECO:0000303|PubMed:10982398}.
/FTId=VSP_008016.
SEQUENCE 351 AA; 40590 MW; 260F2ADF5F86335B CRC64;
MGNAAAAKKG SEQESVKEFL AKAKEDFLKK WENPAQNTAH LDQFERIKTL GTGSFGRVML
VKHTETGNHY 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 NEKCGKEFSE F


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