The function of this domain is unknown. It is found in the N-terminal region of nematode cuticle collagens. Cuticle is a tough elastic structure secreted by hypodermal cells and is primarily composed of collagen proteins (PUBMED:7828882).
The function of this domain is unknown. It is found in the N-terminal region of nematode cuticle collagens (see IPR008160 ). Cuticle is a tough elastic structure secreted by hypodermal cells and is primarily composed of collagen proteins [ (PUBMED:2753356) (PUBMED:7828882) ].
There are 5235 Col_cuticle_N domains in 5107 proteins in SMART's nrdb database.
Click on the following links for more information.
Evolution (species in which this domain is found)
Taxonomic distribution of proteins containing Col_cuticle_N domain.
This tree includes only several representative species. The complete taxonomic breakdown of all proteins with Col_cuticle_N domain is also avaliable.
Click on the protein counts, or double click on taxonomic names to display all proteins containing Col_cuticle_N domain in the selected taxonomic class.
Literature (relevant references for this domain)
Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.
Identification and analysis of a cuticular collagen-encoding gene from theplant-parasitic nematode Meloidogyne incognita.
Gene. 1994; 151: 237-42
Display abstract
The vast majority of proteins in the nematode cuticle are collagens.Cuticular collagen-encoding genes (col) have been described for the animalparasites Ascaris suum and Haemonchus contortus and for the free-livingCaenorhabditis elegans. The proteins encoded by all these genes seem tohave the same basic structure, indicating that there is a conservedsubfamily of cuticular col in these nematodes. In this paper, we describethe identification and characterization of a cDNA (Lemmi 5) whichcorresponds to a cuticular col of the plant-parasitic nematode Meloidogyneincognita. The derived protein structure is very similar to the basicstructure of the C. elegans cuticular collagens. Using PCR technology, wehave shown the presence of Lemmi 5-related sequences in the genome ofDitylenchus destructor. Our data strongly support the existence of acuticular col subfamily which is highly conserved in the phylum Nemata.
Sequence comparisons of developmentally regulated collagen genes ofCaenorhabditis elegans.
Gene. 1989; 76: 331-44
Display abstract
Collagen genes col-6, col-7 (partial), col-8, col-14 and col-19 from thenematode Caenorhabditis elegans were sequenced, and compared to thepreviously sequenced genes col-1 and col-2. The genes are between 1.0 and1.2 kb in length, and each includes one or two short introns. Thepresumptive promoter regions contain sequences similar to the eukaryoticTATA promoter element. Two distinct, conserved sequences were found in thepresumptive promoter regions of, respectively, the dauer larva-specificgenes col-2 and col-6, and the primarily adult-specific genes col-7 andcol-19. The domain structures of the collagen polypeptides are similar:each polypeptide contains two triple-helix forming (Gly-X-Y)n domains, oneof 30-33 amino acids (aa), and the other of 127-132 aa. The latter domainis interrupted by one to three short (2-8 aa) non-(Gly-X-Y)n segments thatoccur at relatively conserved locations in each polypeptide. Sets ofcysteine residues flank the (Gly-X-Y)n domains in all of the polypeptides.The genes can be placed into three families based upon amino acid sequencesimilarities. Genes within a family do not always exhibit similardevelopmental expression programs, suggesting that structural andregulatory regions of the genes have evolved separately. The codon usagein the genes is highly asymmetrical, with adenine appearing in the thirdposition of 85% of the glycine codons, and 93% of the proline codons.
Links (links to other resources describing this domain)
