C-type lectin domain family 2 member D (CLEC2D), also known as lectin-like transcript 1 (LLT1) and osteoclast inhibitory lectin (OCIL), is a type II transmembrane C-type lectin receptor primarily expressed upon immune cell activation in T cells, B cells, NK cells, and plasmacytoid and monocyte-derived dendritic cells. CLEC2D interacts with NKR-P1A (KLRB1, CD161) on NK cells and some subsets of T cells, inhibiting NK cell cytotoxicity while alternatively inducing proliferation and IFNγ production in T cells. CLEC2D is also expressed by osteoblasts, inhibiting osteoclast formation and bone resorption.
Tetranectin binds to plasminogen and to isolated kringle 1. May be involved in the packaging of molecules destined for exocytosis.
Protease component of the Clp complex that cleaves peptides and various proteins in an ATP-dependent process. Has low peptidase activity in the absence of CLPX. The Clp complex can degrade CSN1S1, CSN2 and CSN3, as well as synthetic peptides (in vitro) and may be responsible for a fairly general and central housekeeping function rather than for the degradation of specific substrates. Cleaves PINK1 in the mitochondrion.
The protein encoded by this gene is a cofactor needed by pancreatic lipase for efficient dietary lipid hydrolysis. It binds to the C-terminal, non-catalytic domain of lipase, thereby stabilizing an active conformation and considerably increasing the overall hydrophobic binding site. The gene product allows lipase to anchor noncovalently to the surface of lipid micelles, counteracting the destabilizing influence of intestinal bile salts. This cofactor is only expressed in pancreatic acinar cells, suggesting regulation of expression by tissue-specific elements. Three transcript variants encoding different isoforms have been found for this gene.
Calsyntenins (calsyntenin-1, -2, -3) compose a family of neuronally expressed proteins that belong to the cadherin superfamily of cell adhesion molecules (PMID: 24966372; 12498782). Calsyntenin-1 (CLSTN1) is a proteolytically processed postsynaptic membrane protein with a cytoplasmic calcium-binding domain. By binding Ca2+, calsyntenin-1 may modulate Ca2+-mediated postsynaptic signals (PMID: 11161476). Calsyntenin-1 is a transmembrane cargo-docking protein for Kinesin-1-mediated vesicular transport (PMID: 16760430). It can mediate axonal transport of the amyloid precursor protein and regulate Aβ production
Clusterin, also known as complement-associated protein SP-40, Complement cytolysis inhibitor, Apolipoprotein J, Testosterone-repressed prostate message 2, Aging-associated gene 4 protein, CLU and APOJ, is a secreted protein which belongs to the clusterin family. Clusterin/Apolipoprotein J/Apo-J is an enigmatic glycoprotein with a nearly ubiquitous tissue distribution and an apparent involvement in biological processes ranging from mammary gland involution to neurodegeneration in Alzheimer's disease. Its major form, a heterodimer, is secreted and present in physiological fluids, but truncated forms targeted to the nucleus have also been identified. Clusterin/Apolipoprotein J/Apo-J is a widely distributed glycoprotein with a wide range of biologic properties. A prominent and defining feature of clusterin is its marked induction in such disease states as glomerulonephritis, cystic renal disease, renal tubular injury, neurodegenerative conditions, atherosclerosis, and myocardial infarction. Upregulation of clusterin mRNA and protein levels detected in diverse disease states and in in vitro systems have led to suggestions that it functions in membrane lipid recycling, in apoptotic cell death, and as a stress-induced secreted chaperone protein, amongst others.
Clusterin (CLU) also named as apolipoprotein J, is a multifunctional glycoprotein that is expressed ubiquitously in most tissues. Clusterin functions as a secreted chaperone protein that interacts with and stabilizes stress-induced proteins to prevent their precipitation. Research studies show that clusterin plays a protective role in Alzheimer’s disease by sequestering amyloid β (1-40) peptides to form long-lived, stable complexes, which prevents amyloid fibril formation.In addition to the secreted protein, several intracellular isoforms are localized to the nucleus, mitochondria, cytoplasm and ER. The subcellular distribution of these multiple isoforms leads to the diversity of clusterin functions. Additional studies report that clusterin is involved in membrane recycling, cell adhesion, cell proliferation, apoptosis, and tumor survival.
Transcription factor Maf (encoded by MAF) is a DNA-binding, leucine zipper-containing transcription factor that acts as a homodimer or as a heterodimer. Depending on the binding site and binding partner, the encoded protein can be a transcriptional activator or repressor. This protein plays a role in the regulation of several cellular processes, including embryonic lens fiber cell development, increased T-cell susceptibility to apoptosis, and chondrocyte terminal differentiation.
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