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Protein kinase C alpha type (PKC-A) (PKC-alpha) (EC 2.7.11.13)

 KPCA_RABIT              Reviewed;         672 AA.
P10102;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
22-NOV-2017, entry version 163.
RecName: Full=Protein kinase C alpha type;
Short=PKC-A;
Short=PKC-alpha;
EC=2.7.11.13;
Name=PRKCA;
Oryctolagus cuniculus (Rabbit).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae;
Oryctolagus.
NCBI_TaxID=9986;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
PubMed=3808073; DOI=10.1038/325161a0;
Ohno S., Kawasaki H., Imajoh S., Suzuki K., Inagaki M., Yokokura H.,
Sakoh T., Hidaka H.;
"Tissue-specific expression of three distinct types of rabbit protein
kinase C.";
Nature 325:161-166(1987).
[2]
REVIEW.
PubMed=3045562; DOI=10.1038/334661a0;
Nishizuka Y.;
"The molecular heterogeneity of protein kinase C and its implications
for cellular regulation.";
Nature 334:661-665(1988).
-!- FUNCTION: Calcium-activated, phospholipid- and diacylglycerol
(DAG)-dependent serine/threonine-protein kinase that is involved
in positive and negative regulation of cell proliferation,
apoptosis, differentiation, migration and adhesion, cardiac
hypertrophy, angiogenesis, platelet function and inflammation, by
directly phosphorylating targets such as RAF1, BCL2, CSPG4,
TNNT2/CTNT, or activating signaling cascades involving MAPK1/3
(ERK1/2) and RAP1GAP. Depending on the cell type, is involved in
cell proliferation and cell growth arrest by positive and negative
regulation of the cell cycle. Can promote cell growth by
phosphorylating and activating RAF1, which mediates the activation
of the MAPK/ERK signaling cascade, and/or by up-regulating CDKN1A,
which facilitates active cyclin-dependent kinase (CDK) complex
formation. In cells stimulated by the phorbol ester PMA, can
trigger a cell cycle arrest program which is associated with the
accumulation of the hyper-phosphorylated growth-suppressive form
of RB1 and induction of the CDK inhibitors CDKN1A and CDKN1B.
Depending on the cell type, exhibits anti-apoptotic function and
protects cells from apoptosis by suppressing the p53/TP53-mediated
activation of IGFBP3, or mediates anti-apoptotic action by
phosphorylating BCL2. During macrophage differentiation induced by
macrophage colony-stimulating factor (CSF1), is translocated to
the nucleus and is associated with macrophage development. After
wounding, translocates from focal contacts to lamellipodia and
participates in the modulation of desmosomal adhesion. Plays a
role in cell motility by phosphorylating CSPG4, which induces
association of CSPG4 with extensive lamellipodia at the cell
periphery and polarization of the cell accompanied by increases in
cell motility. During chemokine-induced CD4(+) T cell migration,
phosphorylates CDC42-guanine exchange factor DOCK8 resulting in
its dissociation from LRCH1 and the activation of GTPase CDC42.
Negatively regulates myocardial contractility and positively
regulates angiogenesis, platelet aggregation and thrombus
formation in arteries. Mediates hypertrophic growth of neonatal
cardiomyocytes, in part through a MAPK1/3 (ERK1/2)-dependent
signaling pathway, and upon PMA treatment, is required to induce
cardiomyocyte hypertrophy up to heart failure and death, by
increasing protein synthesis, protein-DNA ratio and cell surface
area. Regulates cardiomyocyte function by phosphorylating cardiac
troponin T (TNNT2/CTNT), which induces significant reduction in
actomyosin ATPase activity, myofilament calcium sensitivity and
myocardial contractility. In angiogenesis, is required for full
endothelial cell migration, adhesion to vitronectin (VTN), and
vascular endothelial growth factor A (VEGFA)-dependent regulation
of kinase activation and vascular tube formation. Involved in the
stabilization of VEGFA mRNA at post-transcriptional level and
mediates VEGFA-induced cell proliferation. In the regulation of
calcium-induced platelet aggregation, mediates signals from the
CD36/GP4 receptor for granule release, and activates the integrin
heterodimer ITGA2B-ITGB3 through the RAP1GAP pathway for adhesion.
During response to lipopolysaccharides (LPS), may regulate
selective LPS-induced macrophage functions involved in host
defense and inflammation. But in some inflammatory responses, may
negatively regulate NF-kappa-B-induced genes, through IL1A-
dependent induction of NF-kappa-B inhibitor alpha (NFKBIA/IKBA).
Upon stimulation with 12-O-tetradecanoylphorbol-13-acetate (TPA),
phosphorylates EIF4G1, which modulates EIF4G1 binding to MKNK1 and
may be involved in the regulation of EIF4E phosphorylation.
Phosphorylates KIT, leading to inhibition of KIT activity.
Phosphorylates ATF2 which promotes cooperation between ATF2 and
JUN, activating transcription. {ECO:0000250|UniProtKB:P17252}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
Evidence={ECO:0000250|UniProtKB:P05696};
Note=Binds 3 Ca(2+) ions per subunit. The ions are bound to the C2
domain. {ECO:0000250|UniProtKB:P05696};
-!- ENZYME REGULATION: Classical (or conventional) PKCs (PRKCA, PRKCB
and PRKCG) are activated by calcium and diacylglycerol (DAG) in
the presence of phosphatidylserine. Three specific sites; Thr-497
(activation loop of the kinase domain), Thr-638 (turn motif) and
Ser-657 (hydrophobic region), need to be phosphorylated for its
full activation.
-!- SUBUNIT: Interacts with ADAP1/CENTA1, CSPG4 and PRKCABP. Binds to
CAVIN2 in the presence of phosphatidylserine. Interacts with PICK1
(via PDZ domain). Interacts with TRIM41. Recruited in a circadian
manner into a nuclear complex which also includes BMAL1 and RACK1.
{ECO:0000250|UniProtKB:P05696, ECO:0000250|UniProtKB:P17252,
ECO:0000250|UniProtKB:P20444}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane
{ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
Mitochondrion membrane {ECO:0000250}; Peripheral membrane protein
{ECO:0000250}. Nucleus {ECO:0000250}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
protein kinase family. PKC subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X04796; CAA28483.1; -; mRNA.
PIR; C26037; KIRBC.
RefSeq; NP_001095194.1; NM_001101724.1.
UniGene; Ocu.3268; -.
ProteinModelPortal; P10102; -.
SMR; P10102; -.
STRING; 9986.ENSOCUP00000025402; -.
PRIDE; P10102; -.
GeneID; 100037720; -.
KEGG; ocu:100037720; -.
CTD; 5578; -.
eggNOG; KOG0694; Eukaryota.
eggNOG; ENOG410XNPH; LUCA.
HOGENOM; HOG000233022; -.
HOVERGEN; HBG108317; -.
InParanoid; P10102; -.
KO; K02677; -.
BRENDA; 2.7.11.13; 1749.
Proteomes; UP000001811; Unplaced.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; ISS:UniProtKB.
GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004697; F:protein kinase C activity; IEA:UniProtKB-EC.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
GO; GO:0034351; P:negative regulation of glial cell apoptotic process; ISS:UniProtKB.
GO; GO:0045766; P:positive regulation of angiogenesis; ISS:UniProtKB.
GO; GO:0010613; P:positive regulation of cardiac muscle hypertrophy; ISS:UniProtKB.
GO; GO:0045785; P:positive regulation of cell adhesion; ISS:UniProtKB.
GO; GO:0030335; P:positive regulation of cell migration; ISS:UniProtKB.
GO; GO:2000707; P:positive regulation of dense core granule biogenesis; ISS:UniProtKB.
GO; GO:0010595; P:positive regulation of endothelial cell migration; ISS:UniProtKB.
GO; GO:0001938; P:positive regulation of endothelial cell proliferation; ISS:UniProtKB.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
GO; GO:0031666; P:positive regulation of lipopolysaccharide-mediated signaling pathway; ISS:UniProtKB.
GO; GO:0045651; P:positive regulation of macrophage differentiation; ISS:UniProtKB.
GO; GO:0045931; P:positive regulation of mitotic cell cycle; ISS:UniProtKB.
GO; GO:0090330; P:regulation of platelet aggregation; ISS:UniProtKB.
CDD; cd00029; C1; 2.
CDD; cd05615; STKc_cPKC_alpha; 1.
Gene3D; 2.60.40.150; -; 1.
InterPro; IPR000961; AGC-kinase_C.
InterPro; IPR000008; C2_dom.
InterPro; IPR035892; C2_domain_sf.
InterPro; IPR034663; cPKC_alpha.
InterPro; IPR020454; DAG/PE-bd.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR002219; PE/DAG-bd.
InterPro; IPR017892; Pkinase_C.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR014375; Protein_kinase_C_a/b/g.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00130; C1_1; 2.
Pfam; PF00168; C2; 1.
Pfam; PF00069; Pkinase; 1.
Pfam; PF00433; Pkinase_C; 1.
PIRSF; PIRSF000550; PKC_alpha; 1.
PRINTS; PR00360; C2DOMAIN.
PRINTS; PR00008; DAGPEDOMAIN.
SMART; SM00109; C1; 2.
SMART; SM00239; C2; 1.
SMART; SM00133; S_TK_X; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF49562; SSF49562; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS51285; AGC_KINASE_CTER; 1.
PROSITE; PS50004; C2; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PROSITE; PS00479; ZF_DAG_PE_1; 2.
PROSITE; PS50081; ZF_DAG_PE_2; 2.
2: Evidence at transcript level;
Acetylation; Angiogenesis; Apoptosis; ATP-binding; Calcium;
Cell adhesion; Cell membrane; Complete proteome; Cytoplasm; Kinase;
Membrane; Metal-binding; Mitochondrion; Nucleotide-binding; Nucleus;
Phosphoprotein; Reference proteome; Repeat;
Serine/threonine-protein kinase; Transferase; Zinc; Zinc-finger.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P17252}.
CHAIN 2 672 Protein kinase C alpha type.
/FTId=PRO_0000055681.
DOMAIN 172 260 C2. {ECO:0000255|PROSITE-
ProRule:PRU00041}.
DOMAIN 339 597 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 598 668 AGC-kinase C-terminal.
ZN_FING 36 86 Phorbol-ester/DAG-type 1.
{ECO:0000255|PROSITE-ProRule:PRU00226}.
ZN_FING 101 151 Phorbol-ester/DAG-type 2.
{ECO:0000255|PROSITE-ProRule:PRU00226}.
NP_BIND 345 353 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 463 463 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
METAL 186 186 Calcium 1; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P05696}.
METAL 187 187 Calcium 1.
{ECO:0000250|UniProtKB:P05696}.
METAL 187 187 Calcium 2.
{ECO:0000250|UniProtKB:P05696}.
METAL 193 193 Calcium 2.
{ECO:0000250|UniProtKB:P05696}.
METAL 246 246 Calcium 1.
{ECO:0000250|UniProtKB:P05696}.
METAL 246 246 Calcium 2.
{ECO:0000250|UniProtKB:P05696}.
METAL 247 247 Calcium 2; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P05696}.
METAL 248 248 Calcium 1.
{ECO:0000250|UniProtKB:P05696}.
METAL 248 248 Calcium 2.
{ECO:0000250|UniProtKB:P05696}.
METAL 248 248 Calcium 3.
{ECO:0000250|UniProtKB:P05696}.
METAL 252 252 Calcium 3; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P05696}.
METAL 254 254 Calcium 1.
{ECO:0000250|UniProtKB:P05696}.
METAL 254 254 Calcium 3.
{ECO:0000250|UniProtKB:P05696}.
BINDING 195 195 Inositol phosphate group.
{ECO:0000250|UniProtKB:P05696}.
BINDING 245 245 Inositol phosphate group.
{ECO:0000250|UniProtKB:P05696}.
BINDING 368 368 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:P17252}.
MOD_RES 10 10 Phosphoserine.
{ECO:0000250|UniProtKB:P17252}.
MOD_RES 226 226 Phosphoserine.
{ECO:0000250|UniProtKB:P17252}.
MOD_RES 319 319 Phosphoserine.
{ECO:0000250|UniProtKB:P05696}.
MOD_RES 497 497 Phosphothreonine; by PDPK1.
{ECO:0000250}.
MOD_RES 501 501 Phosphothreonine.
{ECO:0000250|UniProtKB:P05771}.
MOD_RES 628 628 N6-acetyllysine.
{ECO:0000250|UniProtKB:P17252}.
MOD_RES 631 631 Phosphothreonine; by autocatalysis.
{ECO:0000250|UniProtKB:P68403,
ECO:0000255}.
MOD_RES 638 638 Phosphothreonine; by autocatalysis.
{ECO:0000250|UniProtKB:P17252}.
MOD_RES 651 651 Phosphoserine.
{ECO:0000250|UniProtKB:P17252}.
MOD_RES 657 657 Phosphoserine.
{ECO:0000250|UniProtKB:P05771}.
MOD_RES 658 658 Phosphotyrosine; by SYK.
{ECO:0000250|UniProtKB:P20444}.
SEQUENCE 672 AA; 76782 MW; 3D311367D3577A77 CRC64;
MADVFPANDS TASQDVANRF ARKGALRQKN VHEVKDHKFI ARFFKQPTFC SHCTDFIWGF
GKQGFQCQVC CFVVHKRCHE FVTFSCPGAD KGPDTDDPRS KHKFKIHTYG SPTFCDHCGS
LLYGLIHQGM KCDTCDMNVH KQCVINVPSL CGMDHTEKRG RIYLKAEVTD EKLHVTVRDA
KNLIPMDPNG LSDPYVKLKL IPDPKNESKQ KTKTIRSTLN PQWNESFTFK LKPSDKDRRL
SVEIWDWDRT TRNDFMGSLS FGVSELMKMP ASGWYKLLNQ EEGEYYNVPI PEGDEDGNVE
LRQKFEKAKL GPAGNKVISP SEDRKQPSNN LDRVKLTDFN FLMVLGKGSF GKVMLADRKG
TEELYAIKIL KKDVVIQDDD VECTMVEKRV LALMDKPPFL TQLHSCFQTV DRLYFVMEYV
NGGDLMYHIQ QVGKFKEPQA VFYAAEISIG LFFLHKRGII YRDLKLDNVM LDSEGHIKIA
DFGMCKEHMM DGVTTRTFCG TPDYIAPEII AYQPYGKSVD WWAYGVLLYE MLAGQPPFDG
EDEDELFQSI MEHNVSYPKS LSKEAVSICK GLMTKHPAKR LGCGPEGERD VREHAFFRRI
DWEKLENREI QPPFKPKVCG KGAENFDKFF TRGQPVVTPP DQLVIANIDQ SDFEGFSYVN
PQFVHPILQS SV


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