Immunoglobulin Superfamily Member 8 (IGSF8) is a single-pass membrane protein. IGSF8 contains four Ig-like C2 type domains. The Ig-like C2-type domains 3 and 4 are required for interactions with CD81. IGSF8 may regulate proliferation and differentiation of keratinocytes. IGSF8 may participate in the regulation of neurite outgrowth and maintenance of the neural network in the adult brain. It also may play a role on integrin-dependent morphology and motility functions.
Progesterone Receptor B (PR-B) is a 118 kDa member of the NR3 subfamily within the nuclear hormone receptor family of proteins. It is expressed in female reproductive tissues as well as neurons throughout the CNS. PR-B is particularly important in the mammary gland where it mediates proliferative responses to progesterone.
Polymeric immunoglobulin receptor, also known asPIGR, is a member of the immunoglobulin superfamilyand aFc receptor. The ectodomain of this receptor consists of five units with homology to the variable units of immunoglobulins and a transmembrane region, which also has some homology to certain immunoglobulin variable regions. PIGR is expressed on several glandular epithelia including those of liver and breast. The deduced amino-acid sequence has a length of 764 residues and shows an overall similarity of 56% and 64% with the rabbit and rat counterpart. PIGR mediates transcellular transport of polymeric immunoglobulin molecules, and thus facilitates the secretion ofIgAandIgM. During this process, a cleavage occurs that separates the extracellular (known as the secretory component) from the transmembrane segment of PIGR.
Collagen alpha-1(III) chain (Col3a1) is a secreted protein and belongs to the fibrillar collagen family.It contains 1 fibrillar collagen NC1 domain and 1 VWFC domain. Collagen alpha-1(III) chain is a fibrillar collagen that is found in extensible connective tissues such as skin, lung, and the vascular system, frequently in association with type I collagen. The COL3A1 gene produces the components of type III collagen, called pro-alpha1(III) chains. Three copies of this chain combine to make a molecule of type III procollagen. These triple-stranded, rope-like procollagen molecules must be processed by enzymes outside the cell to remove extra protein segments from their ends. Once these molecules are processed, the collagen molecules arrange themselves into long, thin fibrils. Within these fibrils, the individual collagen molecules are cross-linked to one another. These cross-links result in the formation of very strong mature type III collagen fibrils, which are found in the spaces around cells.
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