Structural and phylogenetic analyses of RGD-CAP/beta ig-h3, a fasciclin-like adhesion protein expressed in chick chondrocytes

Biochim Biophys Acta. 1998 Feb 11;1395(3):288-92. doi: 10.1016/s0167-4781(97)00172-3.


A cDNA for RGD-CAP/beta ig-h3 was cloned from a chick embryo chondrocyte cDNA library. The deduced amino acid sequence showed that the chick RGD-CAP/beta ig-h3 is 76-77% identical with human, mouse and pig forms of the protein, and 43% identical with human and mouse osteoblast specific factor 2 (OSF2). RGD-CAP/beta ig-h3 contained four internal repeat domains and two highly conserved sequences (H1 and H2) in each repeat. Chick RGD-CAP/beta ig-h3, as well as the mammalian RGD-CAP/beta ig-h3, contained an RGD sequence, which may serve as a recognition sequence for integrins, in the fourth repeat. Database searches revealed that the H1 and H2 sequences are conserved in some secreted or membrane proteins of several species including mammals, insects, sea urchins, plants, yeast and bacteria. Phylogenetic analysis showed that a portion of the common ancestor gene for RGD-CAP/beta ig-h3 and OSF2 was duplicated to form four repeat domains before the separation of the genes followed by the divergence of vertebrate species.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Cartilage / enzymology
  • Cartilage / metabolism*
  • Cell Adhesion Molecules / chemistry*
  • Chick Embryo
  • Chickens / genetics*
  • Conserved Sequence
  • Extracellular Matrix Proteins*
  • Humans
  • Mice
  • Molecular Sequence Data
  • Neoplasm Proteins / biosynthesis
  • Neoplasm Proteins / chemistry
  • Neoplasm Proteins / genetics*
  • Phylogeny*
  • Sequence Alignment
  • Sequence Homology, Amino Acid
  • Swine
  • Transforming Growth Factor beta*


  • Cell Adhesion Molecules
  • Extracellular Matrix Proteins
  • Neoplasm Proteins
  • Transforming Growth Factor beta
  • betaIG-H3 protein

Associated data

  • GENBANK/AB005553