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Adipsin is the mouse homolog of the previously described human complement Factor D, a serine protease, which is now designated human Adipsin. Human Adipsin is highly expressed in and secreted by adipose tissue, and it has also been found in monocytes and macrophages. Rodent Adipsin has only been detected in high levels in adipose tissue. It has been shown that complement factor B, when complexed with activated complement component C3, is cleaved by Adipsin. While low expression of Adipsin ha

The protein encoded by this gene appears to be multifunctional. Along with PCBP-1 and hnRNPK, it is one of the major cellular poly(rC)-binding proteins. The encoded protein contains three K-homologous (KH) domains which may be involved in RNA binding. Together with PCBP-1, this protein also functions as a translational coactivator of poliovirus RNA via a sequence-specific interaction with stem-loop IV of the IRES, promoting poliovirus RNA replication by binding to its 5'-terminal cloverleaf s

The protein encoded by this gene is a member of the RAS superfamily which are small GTP/GDP-binding proteins with an average size of 200 amino acids. The RAS-related proteins of the RAB/YPT family may play a role in the transport of proteins from the endoplasmic reticulum to the Golgi and the plasma membrane. This protein shares 97%, 96%, and 51% similarity with the dog RAB8, mouse MEL, and mouse YPT1 proteins, respectively and contains the 4 GTP/GDP-binding sites that are present in all th

IGF2BP2 (insulin-like growth factor 2 mRNA binding protein 2) is also known as IGF2 mRNA-binding protein 2, IMP-2 (IGF-II mRNA-binding protein 2), VICKZ family member 2 or hepatocellular carcinoma autoantigen p62 and is a 556 amino acid protein. IGF2BP2 is expressed in a variety of tissues including heart, placenta, skeletal muscle, pancreas, fetal liver, lung, kidney, thymus and gonadal cells. IGF2BP2 is an RNA binding protein which may be involved in the regulation of mRNA translation and

The 78 kDa glucose regulated protein/BiP (GRP78) belongs to the family of ~70 kDa heat shock proteins (HSP 70). GRP78 is a resident protein of the endoplasmic reticulum (ER) and may associate transiently with a variety of newly synthesized secretory and membrane proteins or permanently with mutant or defective proteins that are incorrectly folded, thus preventing their export from the ER lumen. GRP78 is a highly conserved protein that is essential for cell viability. The highly conserved sequ