“…Furthermore, although A1 and C1 are nonpolymorphic both these genes, along with E1, B3 (from group D), and five group B sequences (B2, B3, B4, 8 and 9, 1-29) were previously shown to have higher rates of nonsynonymous than synonymous substitution in the peptide binding region, indicating that they may all function to present peptide to T cells (Ellis et al 1995). Finally, while both A1 and C1 have the threonine-to-serine amino acid replacement at position 143 in the ␣ 2 domain, thought to be a marker of nonclassical class I genes, this change is also present in a number of classical class I sequences from cattle (Ellis et al 1996) and so may not be diagnostic of gene function or origin in all species. The status of A1 and C1 are therefore ambiguous, apparently being both nonpolymorphic yet with classical class I features and, so, do not appear to fulfill the standard criteria for either class Ia or class Ib genes (Hughes et al 1999).…”