This gene encodes a member of the CCAAT/enhancer-binding protein (C/EBP) family of transcription factors. The protein functions as a dominant-negative inhibitor by forming heterodimers with other C/EBP members, such as C/EBP and LAP (liver activator protein), and preventing their DNA binding activity. The protein is implicated in adipogenesis and erythropoiesis, is activated by endoplasmic reticulum stress, and promotes apoptosis. Fusion of this gene and FUS on chromosome 16 or EWSR1 on chromosome 22 induced by translocation generates chimeric proteins in myxoid liposarcomas or Ewing sarcoma. Multiple alternatively spliced transcript variants encoding two isoforms with different length have been identified.
Chordin is a secreted glycoprotein that regulates dorsoventral patterning during gastrulation. Chordin functions as a bone morphogenetic protein (BMP) antagonist that blocks their ventralizing activity by binding to the BMPs and inhibiting their interaction with their receptors. Mouse Chordin cDNA encodes a 948 amino acid (aa) residue precursor protein with a putative 26 aa residue signal peptide. Chordin contains four internal cysteine-rich repeats (CRs) that are conserved in the spacing of their ten cysteine residues. The CRs of chordin, especially CR1 and CR3, have been shown to be the functional domains for BMP binding. These conserved CRs are present in an expanding family of secreted molecules that antagonize BMP signaling. Xolloid (an extracellular zinc metalloproteinase) can cleave chordin at two specific sites resulting in chordin fragments with lower BMP-affinity. Cleavage of the chordin/BMP complex can reverse the BMP antagonist activity of chordin. Mouse chordin is expressed at high levels in 7 day postcoitum mouse embryos. Chordin expression is also detected in multiple fetal and adult tissues, most notably liver and cerebellum, suggesting additional roles for chordin in organogenesis and homeostasis.
Human Chromogranin A (CHGA) an acidic protein and a member of the chromogranin/secretogranin family of neuroendocrine secretory proteins. It is located in secretory vesicles of neurons and endocrine cells such as islet beta cell secretory granules in pancreas. Chromogranin A expression has been oberserved in neuroendocrine tumors, medullary thyroid carcinoma, as well as carcinoid tumors.
The protein encoded by this gene is a member of the chromogranin/secretogranin family of neuroendocrine secretory proteins. It is found in secretory vesicles of neurons and endocrine cells. This gene product is a precursor to three biologically active peptides; vasostatin, pancreastatin, and parastatin. These peptides act as autocrine or paracrine negative modulators of the neuroendocrine system. Two other peptides, catestatin and chromofungin, have antimicrobial activity and antifungal activity, respectively. Two transcript variants encoding different isoforms have been found for this gene.
This gene encodes a member of the IAP family of proteins that inhibit apoptosis by binding to tumor necrosis factor receptor-associated factors TRAF1 and TRAF2, probably by interfering with activation of ICE-like proteases. The encoded protein inhibits apoptosis induced by serum deprivation but does not affect apoptosis resulting from exposure to menadione, a potent inducer of free radicals. It contains 3 baculovirus IAP repeats and a ring finger domain. Transcript variants encoding the same isoform have been identified.
Calcium and integrin-binding protein 2 (CIB2) belongs to a protein family with four known members, CIB1 through CIB4, which are characterized by multiple calcium-binding EF-hand domains. Sensorineural hearing loss is genetically heterogeneous. The mutations in CIB2, which encodes a calcium- and integrin-binding protein, are associated with nonsyndromic deafness (DFNB48) and Usher syndrome type 1J (USH1J). Furthermore, in zebrafish and Drosophila melanogaster, CIB2 is essential for the function and proper development of hair cells and retinal photoreceptor cells. We also show that CIB2 is a new member of the vertebrate Usher interactome. Variants in CIB2 can underlie either Usher syndrome type I (USH1J) or nonsyndromic hearing impairment (NSHI) (DFNB48). CIB2 is widely expressed in various human and animal tissues, mainly in skeletal muscle, nervous tissue, inner ear, and retina. The CIB2 protein is responsible for maintaining Ca(2+) homeostasis in cells and interacting with integrins-transmembrane receptors essential for cell adhesion, migration, and activation of signaling pathways. Calcium signaling pathway is crucial for signal transduction in the inner ear, and integrins regulate hair cell differentiation and maturation of the stereocilia.
Cold-induced RNA-binding protein (CIRBP) is a 172-residue, multifunctional sensor protein that was first isolated as a protein induced in mouse fibroblasts cultured at 32ºC. Conversely, CIRBP expression decreases in cells or tissues subjected to increased temperature. The CIRBP protein is composed of an amino-terminal RNA-binding domain and a carboxyl-terminal, glycine-rich domain. Stressful stimuli, such as hypoxia, heat shock, osmotic shock, or oxidative conditions, lead to translocation of CIRBP from the nucleus to cytoplasmic stress granules through a mechanism involving CIRBP methylation-dependent nuclear export. CIRBP plays a role in regulating apoptosis and preserving the stemness of neural stem cells at moderately low temperatures. Research studies demonstrate that CIRBP contributes to the regulation of circadian rhythm through post-translational modulation of CLOCK expression.
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