Summary
Cuticle and basement membrane collagens are extracellular matrix components encoded by a family of about 160 genes known to be expressed to which this gene belongs. Collagens have short interrupted blocks of Gly-X-Y sequence flanked by conserved cysteine residues, akin to vertebrate fibril-associated collagens with interrupted triple helix, and are thought to form trimers or higher order polymers. They can be grouped into subfamilies according to homology (Johnstone, 2000). The Caenorhabditis elegans cuticle is a complex multilayered extracellular matrix, consisting predominantly of cuticle collagens and synthesised by the underlying epidermal cell layer (called hypodermis). It is secreted five times during development, in embryos and before each molt. During cuticle synthesis, the genes are expressed in a distinct temporal series, reiterated at each molt, and the temporal groups contribute distinct discrete substructure of the extracellular matrix: The early group of cuticle collagen genes is required for the formation of annuli, it includes DPY-2, 3, 7, 8 and 10, and peaks in mRNA abundance about 4 h before the new cuticle is secreted; these 5 proteins localise in the annuli of the outermost layer of cuticle, right above the actin bundles in the epidermal cell. The intermediate group includes DPY-5 and DPY-13, peaks about 2 hours later, and these collagens go below and in between the annuli (McMahon et al, 2003). For a small number of collagen genes, with no distinctive sequence feature, but certainly critical to assembly or function of the extracellular matrix, such as the DPY genes above, loss of function causes a change in body shape (dumpy, squat or long), or leads to animals that roll when moving (alae helically twisted), or to male ray morphology defects. Some collagens that participate in the inner basement membranes are essential for viability, or play a critical role in synaptogenesis, muscle attachment, cell migration and process guidance. But most other collagens probably have a redundant role, since loss of their function is apparently wild type, and alleles with visible effects in these genes are gain of function mutations. [Main specialists: Iain Johnstone and Jim Kramer; Don Riddle, Ann Rose, Bob Horvitz, Sidney Brenner][Wormbase] dpy-13 encodes a member of the collagen superfamily containing 20 copies of the collagen triple helix repeat; transcipt levels oscillate, peaking once during each larval stage.
Wormbase predicts one model.

AceView summary
According to AceView, this gene is expressed at high level, 2.8 times the average gene in this release, mostly from L2 larvae to adult [Kohara cDNAs], in the intermediate group, peaking about 2 hours before cuticle secretion [Johnstone et al, 1996]. The sequence of this gene is defined by 37 cDNA clones. We annotate structural defects or features in 17 cDNA clones.
The gene contains 2 distinct gt-ag introns. Transcription produces one mRNA. There are 2 validated alternative polyadenylation sites (see the diagram).
The spliced mRNA putatively encodes a good protein, containing domains collagen triple helix repeat, nematode cuticle collagen, N-terminal [Pfam], a vacuolar domain [Psort2].
Function: There are 9 articles specifically referring to this gene in PubMed. In addition we point below to 49 abstracts. This gene is associated to a phenotype (DumPY : shorter than wild-type). Proteins are expected to have molecular function (structural constituent of cuticle) and to localize in nucleus.

Please quote: AceView: a comprehensive cDNA-supported gene and transcripts annotation, Genome Biology 2006, 7(Suppl 1):S12

Map: This gene dpy-13 maps on chomosome IV at position +0.00 (interpolated). In AceView, it covers 1.10 kb, from 4235608 to 4236708 (WS190), on the direct strand.
Links to: WormBase, NextDB, RNAiDB.
as Other names: The gene is also known dpy-16, in Wormgenes/AceView by its positional name 4F1, in Wormbase by its cosmid.number name F30B5.1, in NextDB, the Nematode expression pattern database, as CEYK1902.

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