Alternative splicing of mouse alpha1(XIII) collagen RNAs results in at least 17 different transcripts, predicting alpha1(XIII) collagen chains with length varying between 651 and 710 amino acid residues.

@article{Peltonen1997AlternativeSO,
  title={Alternative splicing of mouse alpha1(XIII) collagen RNAs results in at least 17 different transcripts, predicting alpha1(XIII) collagen chains with length varying between 651 and 710 amino acid residues.},
  author={Sirkku A Peltonen and Marko Rehn and Taina Pihlajaniemi},
  journal={DNA and cell biology},
  year={1997},
  volume={16 2},
  pages={227-34}
}
The alpha1(XIII) collagen chain has three collagenous domains (COL1-COL3) and four noncollagenous domains (NC1-NC4). A hydrophobic sequence in the extreme amino-terminal noncollagenous domain suggests that type XIII collagen is a transmembrane protein. The alpha1(XIII) collagen RNA is characterized by complex alternative splicing. In this study, expression of the alpha1(XIII) collagen chain was detected in 12 mouse tissues using reverse transcription (RT) and the polymerase chain reaction (PCR… CONTINUE READING