Abstract
This chapter focuses on collagen type XIX protein. Type XIX collagen is expressed in human rhabdomyosarcoma and fibroblast cell lines. It is only characterized at the complementary DNA (cDNA) and genomic levels and is a member of the fibril-associated collagens with interrupted triple helices (FACIT) collagens, which include type IX, XII, XIV, and XVI collagens. The predicted α1(XIX) chain comprises five collagenous domains (COL1–5), which range in size from 70 to 224 amino acids, and six noncollagenous domains (NC1–6), varying between 19 and 44 amino acids. Sequence comparison between cDNA and genomic clones indicates unusual alternative splicing events involving incomplete recognition at acceptor sites. However, it is not known whether the resulting truncated variants are functional. The molecular structure of type XIX collagen protein is unknown, and it has not been isolated. The chapter discusses the primary structure of the α1(XIX) chain and the structural and functional sites of type XIX collagen.
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