Nucleotide sequence of mouse EndoA cytokeratin cDNA reveals polypeptide characteristics of the type-II keratin subfamily

Abstract

EndoA cytokeratin (EndoA) belongs to a family of intermediate filaments (IFs) and is coordinately expressed with EndoB cytokeratin during early mouse embryogenesis. We have isolated and sequenced a cDNA from a library constructed from mRNA of parietal yolk sac-like cells, PYS-2, which are derived from mouse teratocarcinoma. Sequence analysis reveals that EndoA is composed of 490 amino acids, its Mr is 54,362, and it contains a central alpha-helical coiled-coil structure flanked by non-alpha-helical domains. The amino acid sequence of EndoA is highly homologous with human cytokeratin No. 8 (93%) and with bovine cytokeratin No. 8 (91%) not only in the central domain, but also in its tail portion, which is less conserved among other intermediate filaments. A comparison with the other cytokeratin proteins characterizes this polypeptide as a non-epidermal type of cytokeratin of the basic (type-II) subfamily. The C-terminal sequence of EndoA is identical to that of human and bovine cytokeratin No. 8 and also highly conserved in other intermediate filaments (desmin, vimentin, glial fibrillary acidic protein and EndoB). It suggests that these may be involved in interaction with some cell component(s), or in more general roles to form IFs. The N-terminal head region is rich in Ser residues including possible phosphorylation sites.