|CD167b||DDR2 (discoidin domain receptor family, member 2)|
|Molecule Type||Antigen Expression||Molecular Weight|
Min / Max
|Non-lineage Restricted Molecule|
Type 1 glycoprotein
|130 / 130|
|CD167b is widely expressed but has high expression in skeletal and heart muscle, kidney,|
skin and lung, and at less levels in brain, placenta, liver and pancreas.
|MOLECULAR FAMILY NAME: Belongs to the tyrosine kinase family.|
CD167b is a single-pass type-1 855 aa glycoprotein. It is a tripartite structure which contains an 155 aa discoidin extracellular domain followed by a 200 aa stalk and contains a F5/8 type C domain and a VIII-like domain, a transmembrane domain and cytoplasmic domain which has a juxtamembrane region and a catalytic tyrosine region. CD167b belongs to a subfamily of tyrosine kinase receptors with a homology region to the Dictyostelium discoideum protein discoidin I in their extracellular domain. There are 2 members that have been identified as CD167a (DDR1) and CD167b ( DDR2). During the cell aggregation of Dictyostelium, the related molecule is secreted and functions as a lectin. It is thought to be important in the maintenance of morphology, cytoskeletal organization, and the ability to align with other cells during aggregation. The discoidin domain in the extracellular regions, CD167a and CD167b, are thought to play a role in cell-cell contact and in cell adhesion signaling pathways. In both CD167a and b, ligand binding is thought to trigger receptor dimerization, which would enable transphosphorylation of tyrosine residues.
Discoidin domains, also called Factor VIII-homology or DS domains, are found in a variety of other proteins. Transmembrane proteins with the discoidin domain are CD167b, neurexin, and neuropilin, A5 antigen in Xenopus. Secreted proteins with the discoidin domain are blood clotting factor 5, blood clotting factor 8, AEBP1, MFG-E8, BA46, Del-1, and XLRS-1. The kinase domain has high homology to mammalian TrkA, B and C, and to the marine sponge tyrosine kinase receptor GCTK from Geodia cydonium.
POST-TRANSCRIPTIONAL MODIFICATION: No information.
POST-TRANSLATIONAL MODIFICATION: No information.
|LIGANDS AND MOLECULES ASSOCIATED WITH CD167b |
CD167b binds fibrillar collagens type-1-3 and 5.
Receptor tyrosine kinases (RTKs) play a role in the communication of cells with their microenvironment. CD167b is a tyrosine kinase activated by triple helical fibrillar glycosylated collagen. When activated CD167b induces the expression of MMP1 and MMP2. It is involved in the regulation of cell proliferation and ECM remodeling mediated by metalloprotease MMP1 (collagenase 1) and MMP2 (gelatinase A). These molecules are involved in the regulation of cell growth, differentiation and metabolism. The biomedical mechanism by which RTKs transduce signals across the membrane has been shown to be a ligand induced receptor oligomerization and subsequent intracellular phosphorylation. This autophosphorylation leads to phosphorylation of cytosolic targets as well as association with other molecules, which are involved in pleiotropic effects of signal transduction. CD167b functions as an adhesion molecule and is a collagen recept that mediates fibroblast migration and proliferation. Various types of collagen have been identified as the cognate ligands for both DDR's. CD167a and CD167b autophosphorylation is achieved by all collagens tested, type 1-type 6. CD167b is only activated by fibrillar collagens especially type 1 and 3.
PROTEINS AND DNA ELEMENTS WHICH REGULATE TRANSCRIPTION OF CD167b: No information.
SUBSTRATES: No information.
ENZYMES WHICH MODIFY CD167b: No information.
Database accession numbers
Revised June 25, 2008