CDH5

Developmental stage

Expressed in endothelial cells of allantois/umbilical vessels at 8.5 dpc (at protein level). During hemangioblast differentiation, expressed in hemogenic endothelium cells and down-regulated in nascent blood precursors.

Domain

Three calcium ions are usually bound at the interface of each cadherin domain and rigidify the connections, imparting a strong curvature to the full-length ectodomain.

Function

Cadherins are calcium-dependent cell adhesion proteins (By similarity). They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types (By similarity). This cadherin may play an important role in endothelial cell biology through control of the cohesion and organization of the intercellular junctions (PubMed:9220534, PubMed:20332120). It associates with alpha-catenin forming a link to the cytoskeleton (By similarity). Acts in concert with KRIT1 and PALS1 to establish and maintain correct endothelial cell polarity and vascular lumen (PubMed:27466317). These effects are mediated by recruitment and activation of the Par polarity complex and RAP1B (By similarity). Required for activation of PRKCZ and for localization of phosphorylated PRKCZ, PARD3, TIAM1 and RAP1B to the cell junction (By similarity).

Post-translational modifications

Phosphorylated on tyrosine residues by KDR/VEGFR-2. Dephosphorylated by PTPRB.

O-glycosylated.

Tissue specificity

Expressed in postnatal endothelial cells of the retinal vascular plexus (at protein level).

Cellular localization

• Cell junction
• Cell membrane
• Single-pass type I membrane protein
• Found at cell-cell boundaries and probably at cell-matrix boundaries. KRIT1 and CDH5 reciprocally regulate their localization to endothelial cell-cell junctions (By similarity).

Alternative names

• Cadherin-5
• Vascular endothelial cadherin
• VE-cadherin
• Cdh5

Database links

• entrezGene:12562
• swissprot:P55284

Target type

Proteins

Molecular weight

87903Da