| Primary Identifier | IPR003551 | Type | Family |
| Short Name | Claudin5 |
| description | Claudins form the paracellular tight junction seal in epithelial tissues. In humans, 24 claudins (claudin 1-24) have been identified. Their ability to polymerise and form strands is affected by the cell types [, , ]. They can also form heteropolymers with each other within and between tight junction strands []. Most of the claudins (claudin-12 being the exception) have a C-terminal PDZ-binding motif that can interact with other PDZ domain proteins, such as scaffolding protein, ZO-1, -2 and -3 []. They also interact with non-tight junction proteins, such as cell adhesion proteins EpCam and tetraspanins and the signaling proteins, ephrin A and B and their receptors, EphA and EphB [].Claudin-5 was originally termed lung-specific membrane protein, brainendothelial cell clone 1 protein (BEC1), and transmembrane protein deletedin velo-cardio-facial syndrome (TMVCF). It was reclassified as claudin-5on the basis of cDNA sequence similarity with claudins-1 and -2, and antibody studies that showed it to be expressed at tight junctions []. Claudin-5 may play an important role in development, since the gene is frequently deleted in velo-cardio-facial/DiGeorge syndrome patients []. |
