CLDN4

The protein encoded by this intronless gene belongs to the claudin family. Claudins are integral membrane proteins that are components of the epithelial cell tight junctions, which regulate movement of solutes and ions through the paracellular space. This protein is a high-affinity receptor for Clostridium perfringens enterotoxin (CPE) and may play a role in internal organ development and function during pre- and postnatal life. This gene is deleted in Williams-Beuren syndrome, a neurodevelopmental disorder affecting multiple systems. [provided by RefSeq, Sep 2013]

Claudin 4

Channel-forming tight junction protein that mediates paracellular chloride transport in the kidney. Plays a critical role in the paracellular reabsorption of filtered chloride in the kidney collecting ducts. Claudins play a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity.

Bicellular tight junction assembly Source: GO_Central
Calcium-independent cell-cell adhesion via plasma membrane cell-adhesion molecules Source: UniProtKB
Cell adhesion Source: GO_Central
Chloride transport Source: UniProtKB-KW
Circadian rhythm Source: Ensembl
Establishment of skin barrier Source: UniProtKB
Female pregnancy Source: Ensembl
Positive regulation of cell migration Source: ARUK-UCL
Positive regulation of metallopeptidase activity Source: ARUK-UCL
Positive regulation of wound healing Source: ARUK-UCL
Regulation of cell morphogenesis Source: ARUK-UCL
Renal absorption Source: UniProtKB
Response to progesterone Source: Ensembl

Cell membrane; Tight junction. CLDN4 is required for tight junction localization in the kidney.

CLDN4 is located in the Williams-Beuren syndrome (WBS) critical region. WBS results from a hemizygous deletion of several genes on chromosome 7q11.23, thought to arise as a consequence of unequal crossing over between highly homologous low-copy repeat sequences flanking the deleted region.

Cytoplasmic: 1-7
Helical: 8-28
Extracellular: 29-81
Helical: 82-102
Cytoplasmic: 103-117
Helical: 118-138
Extracellular: 139-160
Helical: 161-181
Cytoplasmic: 182-209

Phosphorylated. Phosphorylation by EPHA2 is stimulated by EFNA1 and alters interaction with TJP1.