Chloride intracellular channel protein 3 (CLIC3) is encoded by the CLIC3 gene. CLIC3 is a single-pass membrane protein which belongs to the chloride channel CLIC family. It contains one GST C-terminal domain and one GST N-terminal domain. Chloride intracellular channel protein 3 high expressed in the placental, lung and heart, low expressed in skeletal muscle, kidney and pancreas. Chloride intracellular channel protein 3 can insert into membranes and forms chloride ion channels, may participate in cellular growth control.
Chloride intracellular channel protein 4; also known as Intracellular chloride ion channel protein p64H1 and CLIC4; is a member of the chloride channel CLIC family. It contains oneGST C-terminal domain. CLIC4 is a member of a family of intracellular chloride channels. It is regulated by p53; c-Myc; and tumor necrosis factor-alpha. CLIC4 is detected in epithelial cells from colon; esophagus and kidney (at protein level). CLIC4 has alternate cellular functions like a potential role in angiogenesis or in maintaining apical-basolateral membrane polarity during mitosis and cytokinesis. CLIC4 could promote endothelial cell proliferation and regulate endothelial morphogenesis (tubulogenesis). Expression of CLIC4 is prominent in heart; kidney; placenta and skeletal muscle. Overexpression of CLIC4 in cancer cells inhibits tumor growth. Conversely; overexpression of CLIC4 in tumor stromal cells stimulates tumor growth. Thus; CLIC4 participates in normal and pathological processes and may serve as a useful target for therapies in disturbances of homeostasis and neoplastic transformation. Loss of CLIC4 in tumor cells and gain in tumor stroma is common to many human cancers and marks malignant progression. Up-regulation of CLIC4 in tumor stroma is coincident with myofibroblast conversion; generally a poor prognostic indicator. Reactivation and restoration of CLIC4 in tumor cells or the converse in tumor stromal cells could provide a novel approach to inhibit tumor growth.
Chloride Intracellular Channel Protein 4 (CLIC4) is a 253 amino acid single-pass membrane protein that localizes to both the nucleus and the cytoplasm and contains one GST C-terminal domain. CLIC4 is expressed in various tissues and exhibits an intracellular vesicular pattern in Panc-1 cells (pancreatic cancer cells). CLIC4 acts as a monomer which is able to form selective ion channels in target proteins; thus facilitating the transport of chloride and other ions. CLIC4 is believed to have a role in apoptosis and is able to translocate to the nucleus under stress conditions. CLIC4 has alternate cellular functions like a potential role in angiogenesis or in maintaining apical-basolateral membrane polarity during mitosis and cytokinesis.
Chloride Intracellular Channel Protein 5 (CLIC5) is a single-pass membrane protein which belongs to the chloride channel CLIC family. It contains one GST C-terminal domain. Chloride intracellular channels are involved in chloride ion transport within various subcellular compartments. CLIC5 can insert into membranes and form selective ion channels regulated by actin that may transport chloride ions. It may play a role in the regulation of transepithelial ion absorption and secretion. CLIC5 specifically associates with the cytoskeleton of placenta microvilli. CLIC5 is required for the development and/or maintenance of the proper glomerular endothelial cell and podocyte architecture.
Dual specificity protein kinase CLK3, also known as CDC-like kinase 3, and CLK3, is a member of CMGC Ser/Thr protein kinase family and Lammer subfamily. Mammalian CLK is the prototype for a family of dual specificity kinases (termed Lammer kinases) that have been conserved in evolution. CLK family members have shown to interact with, and phosphorylate, serine- and arginine-rich (SR) proteins of the spliceosomal complex, which is a part of the regulatory mechanism that enables the SR proteins to control RNA splicing. The three members of the CLK family of kinases (CLK1, CLK2, and CLK3) have been shown to undergo conserved alternative splicing to generate catalytically active and inactive isoforms. The human CLK2 and CLK3 are found within the nucleus and display dual-specificity kinase activity. The truncated isoforms, hCLK2(T) and hCLK3(T), colocalize with SR proteins in nuclear speckles. CLK3 may play a role in the development and progression of azoospermia.
CLM-9, also known as TREM4, is a receptor which belongs to the TREM family. The TREM family of receptors regulates the activity of various cell types of the immune system including neutrophils, monocyte/macrophages, microglia, and dendritic cells. CLM-9 may mediate L-selectin-dependent lymphocyte rollings. It binds SELL in a calcium dependent manner. CLM-9 also binds lymphocyte which suggests that it functions in lymphocyte adhesion. The major CLM-9 transcript is expressed highly in human heart, skeletal muscle, and placenta. The mouse protein has been shown to be expressed in capillary endothelial cells. Human CLM-9 mediates the uptake of human IgA2 and mouse IgM.
CMRF35-Like Molecule 9 (CD300LG) is a single-pass type I membrane protein which belongs to the CD300 family. CD300LG has one Ig-like V-type domain which mediates binding to lymphocyte. CD300LG is highly expressed in heart, skeletal muscle and placenta. CD300LG acts as a receptor which may mediate L-selectin-dependent lymphocyte rollings. CD300LG also binds SELL in a calcium dependent manner and lymphocyte. CD300LG may play a important role in molecular traffic across the capillary endothelium.
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