Complete primary structure and genomic organization of the mouse Col14a1 gene

Donald R. Gerecke, Xianmin Meng, Bin Liu, David E. Birk

Research output: Contribution to journalArticlepeer-review

12 Scopus citations

Abstract

The entire mouse cDNA sequence for type XIV collagen was determined using overlapping PCR products. The 6456 nucleotide (nt) cDNA sequence contains a 5391-nt open reading frame encoding 1797 amino acid residues. The amino terminus has a 28-residue signal peptide that is followed by the mature polypeptide of 1769 amino acid residues with a calculated molecular mass of 193.2 kDa. The mouse α1(XIV) collagen chain is predicted to contain all the structural domains described for the polypeptide in chicken and human. These include fibronectin type III repeats, von Willebrand factor A domains, thrombospondin-N-terminal-like domains and two triple-helical domains similar to those of other collagen family members. The amino acid residue sequence of human α1(XIV) collagen showed an overall identity of 74% to the chicken sequence and 88% to the human sequence. The entire mouse genomic structure has been determined and is made up of 48 exons. Alternatively spliced forms of mouse type XIV, collagen were not identified corresponding to the findings for the human form.

Original languageEnglish (US)
Pages (from-to)209-216
Number of pages8
JournalMatrix Biology
Volume22
Issue number3
DOIs
StatePublished - May 2003

All Science Journal Classification (ASJC) codes

  • Molecular Biology

Keywords

  • Genomic organization
  • Mouse
  • Type XIV collagen
  • cDNA sequence

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