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PROSITE documentation PDOC51461 [for PROSITE entry PS51461]

Fibrillar collagen C-terminal non-collagenous (NC1) domain profile





Description

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 metazoans [4,5].

The profile we developed covers the entire fibrillar collagen NC1 domain.

Last update:

July 2009 / First entry.

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Technical section

PROSITE method (with tools and information) covered by this documentation:

NC1_FIB, PS51461; Fibrillar collagen C-terminal non-collagenous (NC1) domain profile  (MATRIX)


References

1AuthorsSicot F.-X. Exposito J.-Y. Masselot M. Garrone R. Deutsch J. Gaill F.
TitleCloning of an annelid fibrillar-collagen gene and phylogenetic analysis of vertebrate and invertebrate collagens.
SourceEur. J. Biochem. 246:50-58(1997).
PubMed ID9210465

2AuthorsExposito J.-Y. Cluzel C. Lethias C. Garrone R.
TitleTracing the evolution of vertebrate fibrillar collagens from an ancestral alpha chain.
SourceMatrix Biol. 19:275-279(2000).
PubMed ID10936452

3AuthorsBoot-Handford R.P. Tuckwell D.S. Plumb D.A. Rock C.F. Poulsom R.
TitleA 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.
SourceJ. Biol. Chem. 278:31067-31077(2003).
PubMed ID12766169
DOI10.1074/jbc.M212889200

4AuthorsKing 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.
TitleThe genome of the choanoflagellate Monosiga brevicollis and the origin of metazoans.
SourceNature 451:783-788(2008).
PubMed ID18273011
DOI10.1038/nature06617

5AuthorsExposito J.-Y. Larroux C. Cluzel C. Valcourt U. Lethias C. Degnan B.M.
TitleDemosponge and sea anemone fibrillar collagen diversity reveals the early emergence of A/C clades and the maintenance of the modular structure of type V/XI collagens from sponge to human.
SourceJ. Biol. Chem. 283:28226-28235(2008).
PubMed ID18697744
DOI10.1074/jbc.M804573200



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