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. 1992 Sep 24;1132(2):154-60.
doi: 10.1016/0167-4781(92)90006-l.

Sequence and expression of human protein kinase C-epsilon

P Basta  1 , M B Strickland, W Holmes, C R Loomis, L M Ballas, D J Burns
Affiliations

Sequence and expression of human protein kinase C-epsilon

P Basta et al. Biochim Biophys Acta. .

Abstract

Two human homologues of protein kinase C-epsilon (E1 and E2) were isolated from two distinct cDNA libraries. Sequence comparisons to PKC-epsilon cDNAs from several species indicated that each of these human epsilon clones contained cloning artifacts. Thus, a composite PKC-epsilon (E3) clone was derived from clones E1 and E2. Human PKC-epsilon (E3) has an overall sequence identity of 90-92% at the nucleotide level compared to the previously characterized mouse, rat and rabbit clones. At the amino acid level, the deduced human epsilon sequence shows a 98-99% identity with the mouse, rat and rabbit sequences. Expression of the human PKC-epsilon clone in Sf9 cells confirmed that the recombinant protein displayed protein kinase C activity and phorbol ester binding activity. The recombinant protein was also recognized by two distinct epsilon-specific polyclonal antibodies.

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