DPP4/CD26 is a type II transmembrane glycoprotein expressed ubiquitously in most tissues and different cell types. The protein has a short cytoplasmic domain, transmembrane domain, a flexible stalk fragment and extracellular fragment. Both the catalytic peptide hydrolase domain and the beta-propeller ligand binding domain are located in the extracellular fragment. DPP4/CD26 is a multifunctional protein that exists in both a membrane bound form as well as an extracellular soluble form. As a peptidase, it removes N-terminal dipeptides sequentially from proteins with a proline or alanine as the penultimate P1 amino acid. DPP4/CD26 has been shown to cleave a wide range of substrates including GLP-1, BNP, etc. In addition to its peptidase activity, DPP4/CD26 interacts with multiple important cell surface ligands, such as adenosine deaminase, fibronectin, and IGF2 receptor to influence processes like T cell activation, cell migration and proliferation.
The protein encoded by this gene is an enzyme that elongates the prenyl side-chain of coenzyme Q, or ubiquinone, one of the key elements in the respiratory chain. The gene product catalyzes the formation of all trans-polyprenyl pyrophosphates from isopentyl diphosphate in the assembly of polyisoprenoid side chains, the first step in coenzyme Q biosynthesis. The protein may be peripherally associated with the inner mitochondrial membrane, though no transit peptide has been definitively identified to date. Defects in this gene are a cause of coenzyme Q10 deficiency.
DPY30 domain containing 2 belongs to the dpy-30 family. Dumpy-30 family members act as determinants of male fertility and interaction partners of metal-responsive transcription factor 1 (MTF-1) in Drosophila. MTF-1 plays a key role in transition metal detoxification and homeostasis. It binds to metal response elements (MREs). Two candidate dMTF-1 interactors are related to the small regulatory protein Dumpy-30 (Dpy-30) of the worm C. elegans. Dpy-30 is the founding member of a protein family involved in chromatin modifications, notably histone methylation. Mutants affect mating type in yeast and male mating in C. elegans. As part of the MLL1/MLL complex, DPY30 domain containing 2 is involved in methylation and dimethylation at 'Lys-4' of histone H3. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. DPY30 domain containing 2 may also play an indirect or direct role in endosomal transport.
DR5, also known as CD262, TNFRSF10B, TRAILR2, TRICK2 and KILLER, is a widely expressed single-pass type I membrane protein belonging to the tumour necrosis factor receptor superfamily (TNFRSF). It is a receptor for TNF-related apoptosis-inducing ligand (TRAIL), which is a member of the tumor necrosis factor (TNF) family of cytokines and induces apoptosis in a wide variety of cells. DR5 contains two extracellular cysteine-rich repeats, typical for TNF receptor (TNFR) family members, and a cytoplasmic death domain (DD), through which DR5 is capable to transmit the apoptotic signal. In PDAC cells, especially Panc89 cells, it expresses additionally to the approximately 48 and 40 kDa forms of DR5, a faster migrating variant of DR5 of about 32 kDa. The TRAIL receptor 2 (death receptor 5, or DR5) forms receptor dimers in a ligand-dependent manner.
DROSHA(drosha ribonuclease III) Homo sapiens This gene encodes a ribonuclease (RNase) III double-stranded RNA-specific ribonuclease and subunit of the microprocessor protein complex, which catalyzes the initial processing step of microRNA (miRNA) synthesis. The encoded protein cleaves the stem loop structure from the primary microRNA (pri-miRNA) in the nucleus, yielding the precursor miRNA (pre-miRNA), which is then exported to the cytoplasm for further processing. In a human cell line lacking a functional copy of this gene, canonical miRNA synthesis is reduced. Somatic mutations in this gene have been observed in human patients with kidney cancer.
This gene encodes a member of the dynamin superfamily of GTPases. The encoded protein mediates mitochondrial and peroxisomal division, and is involved in developmentally regulated apoptosis and programmed necrosis. Dysfunction of this gene is implicated in several neurological disorders, including Alzheimer's disease. Mutations in this gene are associated with the autosomal dominant disorder, encephalopathy, lethal, due to defective mitochondrial and peroxisomal fission (EMPF). Alternative splicing results in multiple transcript variants encoding different isoforms.
DSC2 is a calcium-dependent glycoprotein that is a member of the desmocollin subfamily of the cadherin superfamily. Like other desmocollins, murine DSC2 has two products, Dsc2a and Dsc2b, produced by alternative splicing of a 46 bp exon which encodes 11 COOH-terminal aa followed by an in-frame stop codon. These desmosomal family members, along with the desmogleins, are found primarily in epithelial cells where they constitute the adhesive proteins of the desmosome cell-cell junction and are required for cell adhesion and desmosome formation. The desmosomal family members are arranged in two clusters on chromosome 18, occupying less than 650 kb combined. Mutations in DSC2 are associated with arrhythmogenic right ventricular dysplasia-11. DSC2 is Involved in the interaction of plaque proteins and intermediate filaments mediating cell-cell adhesion. DSC2 may contribute to epidermal cell positioning by mediating differential adhesiveness between cells that express different isoforms.
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