The multifunctional prohormonc, proopiomclanocortin (POMC), is processsd in the melanotropc cells of the pituitary pars intprmedia at pairs of basic amino acid residues to give a number of pcptides, including a-melanophorc-stimulating hormone (o-MSH). This hormone causes skin darkening in amphibians during background adaptation. Here WC report the complete structure of XLWU~ILS IueGs prohonnonc convcrtasc PC?, the enzyme thought to be responsible for processing of POMC to a-MSH. A comparative structural analysis revealed an overall aminoacid sequence identity of85-87% between Xctt~pus PC2 and its mammalian counterparts, with the lowest degree ofidcntity in the signal peptidrsequcmx (28-368) and the region amino+zrmintil to the catalytic domain (59-608). The occurrence of a second, structurally different PC2 protein reflects the expression of two ,%'crro(l~rs PC2 penes. The expression pattern of PC2 in the XLWII~US pituitary gland of black-and white-adapted anhnals was found to be similar to that of POMC, namely high expression in active mclanotrope cells of black animals. This observation is in lint with a physiological role for PC2 in processing POMC to a-MSH.
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