protein kinase C-epsilon (PKC-N, PRKCE)

^[1]^[2]

Function

Ca+2-independent, phospholipid-dependent
serine/hreonine kinase
activated by diacylglycerol
forms a ternary complex with TRIM63 & GN2BL1
3 specific sites
- Thr-566 (activation loop of the kinase domain)
- Thr-710 (turn motif)
- Ser-729 (hydrophobic region) need to be phosphorylated for its full activation
phosphorylation on Thr-566 by PDPK1 triggers autophosphorylation on Ser-729
PDGF activates PKC epsilon^[2]

C1 domain, containing the phorbol ester/DAG-type region 1 is the diacylglycerol sensor
C2 domain is a non-Ca+2 binding domain
belongs to the protein kinase superfamily, AGC Ser/Thr protein kinase family, PKC subfamily
contains 1 AGC-kinase C-terminal domain
contains 1 C2 domain
contains 2 phorbol-ester/DAG-type Zn+2 fingers
contains 1 protein kinase domain

↑ UniProt http://www.uniprot.org/uniprot/Q02156.html
↑ ^2.0 ^2.1 Moriya S, Kazlauskas A, Akimoto K, Hirai S, Mizuno K, Takenawa T, Fukui Y, Watanabe Y, Ozaki S, Ohno S. Platelet-derived growth factor activates protein kinase C epsilon through redundant and independent signaling pathways involving phospholipase C gamma or phosphatidylinositol 3-kinase. Proc Natl Acad Sci U S A. 1996 Jan 9;93(1):151-5. PMID: https://www.ncbi.nlm.nih.gov/pubmed/8552594