Collagens represent a large family of extracellular matrix glycoproteins.
Members of this family include the fibrillar collagens, which are involved in
the formation of striated fibrils. Fibril-forming or fibrillar collagens are
one of the most ancient families of extracellular matrix molecules being found
throughout the metazoan kingdom from the simplest (porifera (sponges)) to the
most complex animals (vertebrates). Fibrillar collagens form the major
structural elements in extracellular matrices as diverse as the evolutionarily
"primitive" mesoglea of cnidarians to the highly specialized connective
tissues of vertebrates (e.g. bone, cartilage, skin, and tendon). Molecular
features shared by all members of this family include a highly conserved C-terminal non-collagenous (NC1) domain or C-propeptide and a long collagenous
domain of ~1000 amino acid residues. The NC1 domain is the most conserved part
of fibrillar collagens from invertebrates to vertebrates (types I-III, V, XI,
XXIV and XXVII) [1,2,3]. Fibrillar collagen NC1 domains have also been
identified in choanoflagelates, which are considered the closest relatives of
The profile we developed covers the entire fibrillar collagen NC1 domain.
Boot-Handford R.P. Tuckwell D.S. Plumb D.A. Rock C.F. Poulsom R.
A novel and highly conserved collagen (pro(alpha)1(XXVII)) with a unique expression pattern and unusual molecular characteristics establishes a new clade within the vertebrate fibrillar collagen family.
King N. Westbrook M.J. Young S.L. Kuo A. Abedin M. Chapman J. Fairclough S. Hellsten U. Isogai Y. Letunic I. Marr M. Pincus D. Putnam N. Rokas A. Wright K.J. Zuzow R. Dirks W. Good M. Goodstein D. Lemons D. Li W. Lyons J.B. Morris A. Nichols S. Richter D.J. Salamov A. JGI Sequencing Bork P. Lim W.A. Manning G. Miller W.T. McGinnis W. Shapiro H. Tjian R. Grigoriev I.V. Rokhsar D.
The genome of the choanoflagellate Monosiga brevicollis and the origin of metazoans.
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