Pigment Cell Res 1991 Feb 01;41:41-7. doi: 10.1111/j.1600-0749.1991.tb00312.x.

Complete sequence and expression of a cDNA encoding a chicken 115-kDa melanosomal matrix protein.

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A full-length cDNA clone encoding a 115-kDa melanosomal matrix protein (MMP115) was isolated from a cDNA library constructed from poly(A)+ RNA of the chicken pigmented epithelial cells. Sequence analysis showed that the cDNA encoded a polypeptide of 762 amino acids, including a hydrophobic signal peptide. There are no membrane-spanning regions, but there are five N-linked glycosylation signals. A cysteine- and histidine-rich domain is present near the C-terminus. A sequence of 24 amino acids is repeated three times in the polypeptide. A database search for homologies yielded no sequence similarities in other proteins. A plasmid containing the full-length cDNA was transferred into mouse cell lines by transfection. The transfected cells produced a protein that had the same size, 115 kDa, as the mature MMP115. When B16 mouse melanoma cells were transfected, the chicken MMP115 was expressed in the melanosomes. The presence of a specific sorting signal was suggested for localization of melanosomal proteins. Southern blot analysis has revealed that the homologues of the chicken MMP115 gene are found in many vertebrate genomes.

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