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A new type of fish antifreeze protein, designated here type IV, has been isolated from the longhorn sculpin, Myoxocephalus octodecimspinosis. Sequence analysis of the protein (LS-12) reveals that it contains 108 amino acids, is blocked at the N-terminus by a pyroglutamyl group and has a high (17%) content of glutamine; it is thus completely unrelated to the earlier described types I, II and III fish antifreeze proteins. Circular dichroism spectra and conformational analysis based on the sequence data indicate that LS-12 has a high helix content and probably folds as a four-helix bundle. LS-12 shows sequence similarity to certain plasma apolipoproteins known to have helix bundle structures, suggesting the possibility that LS-12 may have arisen by recruitment and mutation of a plasma apolipoprotein.
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Deng et al. (1997) studied this question.
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