The WSC domain is a putative carbohydrate binding domain of about 90 amino acids. The domain is named after yeast WSC1-WSC4 (cell wall integrity and stress response components 1-4) proteins, which each contain a single WSC domain. The WSC domain can also be found as more copies in tandem or in combination with other domains, such as PKD (see <PDOC50093>), LDL-receptor class A (see<PDOC00929>), C-type lectin (see <PDOC00537>); kringle (see <PDOC00020>), CUB (see <PDOC00908>); FN3 (see <PDOC50853>) and protein kinase (see <PDOC00100>). The WSC domain contains eight conserved cysteine residues which are predicted to form disulfide bridges [1].

Some proteins known to contain a WSC domain:

• Mammalian polycystin-1 (PKD1), which forms a calcium-regulated ion channel with PKD2. Defects in PKD1 are the cause of autosomal dominant polycystic kidney disease type I.
• Baker's yeast SLG1/WSC1, WSC2 and WSC3 proteins, which may act as sensors of environmental stress.
• Baker's yeast WSC4, which is implicated in protein translocation to the endoplasmic reticulum.
• Mammalian kremen (kringle-containing protein marking the eye and the nose) proteins 1 and 2.
• Fruit fly xylosyltransferase oxt (EC 2.4.2.26), which is the first glycosyltransferase in the biosynthesis of glycosaminoglycan chains.
• Caenorhabditis elegans xylosyltransferase sqv-6 (EC 2.4.2.26).
• Fruit fly Wsck, a putative receptor with tyrosine-protein kinase activity (EC 2.7.10.1).
• Trichoderma harzianum β-1,3 exoglucanase, which contains 2 WSC domains in tandem.

The profile we developed covers the entire WSC domain.