Description: Homo sapiens cadherin 17, LI cadherin (liver-intestine) (CDH17), transcript variant 1, mRNA. RefSeq Summary (NM_004063): This gene is a member of the cadherin superfamily, genes encoding calcium-dependent, membrane-associated glycoproteins. The encoded protein is cadherin-like, consisting of an extracellular region, containing 7 cadherin domains, and a transmembrane region but lacking the conserved cytoplasmic domain. The protein is a component of the gastrointestinal tract and pancreatic ducts, acting as an intestinal proton-dependent peptide transporter in the first step in oral absorption of many medically important peptide-based drugs. The protein may also play a role in the morphological organization of liver and intestine. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Jan 2009]. Transcript (Including UTRs) Position: hg19 chr8:95,139,394-95,220,815 Size: 81,422 Total Exon Count: 18 Strand: - Coding Region Position: hg19 chr8:95,140,468-95,206,913 Size: 66,446 Coding Exon Count: 17
ID:CAD17_HUMAN DESCRIPTION: RecName: Full=Cadherin-17; AltName: Full=Intestinal peptide-associated transporter HPT-1; AltName: Full=Liver-intestine cadherin; Short=LI-cadherin; Flags: Precursor; FUNCTION: Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. LI-cadherin may have a role in the morphological organization of liver and intestine. Involved in intestinal peptide transport. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein (Potential). TISSUE SPECIFICITY: Expressed in the gastrointestinal tract and pancreatic duct. Not detected in kidney, lung, liver, brain, adrenal gland and skin. SIMILARITY: Contains 7 cadherin domains.
The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.
ModBase Predicted Comparative 3D Structure on Q12864
Front
Top
Side
The pictures above may be empty if there is no ModBase structure for the protein. The ModBase structure frequently covers just a fragment of the protein. You may be asked to log onto ModBase the first time you click on the pictures. It is simplest after logging in to just click on the picture again to get to the specific info on that model.
Orthologous Genes in Other Species
Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.