CD299 is also known as DC-SIGNR and CLEC4M, is a type II integral membrane protein. DC-SIGNR exists as a homotetramer, and the tandem repeat domain, also called neck domain, mediates oligermerization. Multiple human DC-SIGN/CD209 splice forms exist, generating both membrane-bound and soluble forms. DC-SIGNR is ragarded as a pathogen-recognition receptor involved in peripheral immune surveillance in liver, and probably mediate the endocytosis of pathogens which are subsequently degraded in lysosomal compartments. DC-SIGNR appears to selectively recognize and bind many viral surface glycoproteins containing high mannose N-linked oligosaccharides in a calcium-dependent manner, including HIV-1 gp12, HIV-2 gp12, SIV gp12, ebolavirus glycoproteins, HCV E2, and human SARS coronavirus protein S, as well as the cellular adhesion protein ICAM3. DC-SIGN/CD209 is expressed on dendritic cells (DC) and inflammatory macrophages and contributes to antigen presentation.
DCN1-Like Protein 1 is a protein containing 1 DCUN1 domain and 1 UBA-like domain. DCN1-Like Protein 1 contains part of an E3 Ubiquitin Ligase Complex for Neddylation. It is required for Neddylation of Cullin components of E3 Cullin-RING Ubiquitin Ligase complexes. It enhances the rate of Cullins Neddylation. DCN1-Like Protein 1 recruits the NEDD8-charged E2 Enzyme to the Cullin component. DCUN1D1 is involved in the release of inhibitory effects of CAND1 on the Cullin-RING Ligase E3 complex assembly and activity. It acts also as an oncogene facilitating malignant transformation and carcinogenic progression.
DCX (doublecortin, N-GST chimera)contains 2 doublecortin domains and belongs to the doublecortin family. It is highly expressed in neuronal cells of fetal brain, but not expressed in other fetal tissues. In the adult, it is highly expressed in the brain frontal lobe, but very low expression in other regions of brain, and not detected in heart, placenta, lung, liver, skeletal muscles, kidney and pancreas. DCX is a microtubule-associated protein required for initial steps of neuronal dispersion and cortex lamination during cerebral cortex development. It may act by competing with the putative neuronal protein kinase DCAMKL1 in binding to a target protein. DCX may in that way participate in a signaling pathway that is crucial for neuronal interaction before and during migration, possibly as part of a calcium ion-dependent signal transduction pathway. It may be part with LIS-1 of a overlapping, but distinct, signaling pathways that promote neuronal migration. Defects in DCX are the cause of lissencephaly X-linked type 1 and subcortical band heterotopia X-linked.
L-Xylulose Reductase is an enzyme that belongs to the Short-Chain Dehydrogenases/Reductases (SDR) family. L-Xylulose Reductase is responsible for the metabolism of Xylulose, converting it into Xylitol. L-Xylulose Reductase catalyzes the NADPH-dependent reduction of several Pentoses, Tetroses, Trioses, α-Dicarbonyl compounds and L-Xylulose. L-Xylulose Reductase participates in the Uronate Cycle of Glucose metabolism. It may play a role in the water absorption and cellular osmoregulation in the proximal renal tubules by producing Xylitol, an osmolyte, thereby preventing osmolytic stress from occurring in the renal tubules.
CHOP/GADD153, also known as DNA-damage-inducible transcript 3 (DDIT3), is a basic domain-leucine zipper(bZIP) transcription factor of C/EBP family. This protein has been shown to be up-regulated by several stresses, such as amino acid or glucose starvation, endoplasmic reticulum (ER) stress, osmotic stress and hypoxia. GADD153 protein may play a role in ER stress-mediated apoptosis and in disease including diabetes, brain ischemia and neurodegenerative disease. Recombinant GADD153 fused with His-tag, was expressed in E.coli and purified by conventional chromatography techniques.
The enzyme oligosaccharyltransferase (dolichyl-diphosphooligosaccharide-protein glycosyltransferase) (DDOST), or 48-kDa subunit (OST48) is one of the catalytic subunits in this complex, exerts a typical type I membrane topology, containing a large luminal domain, a hydrophobic transmembrane domain and a short cytosolic peptide tail. DDOST/OST48 catalyzes the transfer of a high-mannose oligosaccharide (GlcNac2Man9Glc3) from a dolichol-linked oligosaccharide donor (dolichol-P-GlcNac2Man9Glc3) onto the asparagine acceptor site within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains across the membrane of the endoplasmic reticulum. The mammalian oligosaccharyltransferase (OST) is an oligomeric complex composed of three type I transmembrane proteins of the endoplasmic reticulum: ribophorin I (RI), ribophorin II (RII), and OST48. OST48 is not a glycoprotein and is not recognized by antibodies to either ribophorin. Like ribophorins I and II, OST48 was found to be an integral membrane protein, with the majority of the polypeptide located within the lumen of the endoplasmic reticulum (ER). OST48 does not show significant amino acid sequence homology to either ribophorin I or II. It had been found that only the luminal domain of RI contains ER retention information. The dilysine motif in OST48 functions as an ER localization motif because OST48 in which the two lysine residues are replaced by serine (OST48ss) is no longer retained in the ER and is found instead also at the plasma membrane.
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