Thioredoxin domain-containing protein 15(TXNDC15) is a single-pass type I membrane protein. Mature Human TXNDC15 consists of a 289 amino acid (aa) extracellular region (ECD) with one thioredoxin domain, a 21 aa transmembrane domain, and a 18 aa cytoplasmic region. It has 2 isoforms produced by alternative splicing. Thioredoxins comprise a family of small proteins that, by catalyzing the oxidation of disulfide bonds, participate in redox reactions throughout the cell. Proteins that contain thioredoxin domains do not necessarily convey the oxidative properties of thioredoxins, but generally function as disulfide isomerases that enzymatically rearrange disulfide bonds found in various proteins.
Cell surface A33 antigen, also known as glycoprotein A33, is a single-pass type I membrane protein which is expressed in normal gastrointestinal epithelium and in 95% of colon cancers. GPA33 contains oneIg-like C2-type (immunoglobulin-like) domain and oneIg-like V-type (immunoglobulin-like) domain. The open reading frame encodes a 319-amino acid polypeptide having a putative secretory signal sequence and 3 potential glycosylation sites. The predicted mature protein has a 213-amino acid extracellular region, a single transmembrane domain, and a 62-amino acid intracellular tail. Intracellular traffic and recycling to the cell surface appear to play a major role in GPA33 function and to have an influence on its surface density superseding translational regulation. GPA33 has become a promising target of immunologic therapy strategies, but its biologic function and potential role in tumorigenesis are unknown. EpCAM protein and GPA33 mRNA expressions are specific and sensitive markers of Barrett's metaplasia (BM). GPA33 may also play a role in cell-cell recognition and signaling.
Thioredoxin reductase 1 (TXNRD1) which is a selenocysteine-containing protein is overexpressed in many malignancies. TXNRD1 plays a key role in regulating cell growth and transformation, and protects cells against oxidative damage. We investigated the association between TXNRD1 polymorphisms and ATDH susceptibility. Moreover, TXNRD1 is an essential selenium-containing enzyme involved in detoxification of reactive oxygen species (ROS) and redox signaling. And genetic variations in TXNRD1 favor the development of Drug-induced liver injury (DILI), which is the most common adverse drug reaction.
Axl (Ufo, Ark), Dtk (Sky, Tyro3, Rse, Brt) and Mer (human and mouse homologues of chicken cEyk)constitute a new receptor tyrosine kinase subfamily. The extracellular domain of these proteins contain two Ig-like motifs and two fibronectin type III motifs. This characteristic topology is also found in neural cell adhesion molecules and in receptor tyrosine phosphatases. All three receptors bind the vitamin K-dependent protein growth-arrest specific gene 6 (Gas6) which is structurally related to the anticoagulation factor protein S. The binding affinities for Gas6 is in the order of Axl > Dtk > Mer. Gas6 binding induces tyrosine phosphorylation and downstream signaling pathways that can lead to cell proliferation, migration, or the prevention of apoptosis. Dtk is widely expressed during embryonic development. In adults, Dtk is predominantly expressed in neurons in restricted regions of the brain.
Axl, also known as Ufo and Ark, is a widely expressed 140 kDa glycoprotein in the TAM receptor tyrosine kinase family. Axl binds the vitamin K-dependent protein Gas6 which triggers tyrosine autophosphorylation of the Axl cytoplasmic domain. Axl functions in dampening the immune response, regulating cytokine secretion, clearing apoptotic cells and debris, and maintaining cell survival. Axl is highly expressed in solid cancers and promotes in vivo tumorigenesis and tumor cell invasiveness. It also functions as a cellular entry receptor for Gas6-opsonized lentiviruses. Axl contributes to cell survival, migration, invasion, metastasis and chemosensitivity justify further investigation of Axl as novel therapeutic targets in cancer. The receptor tyrosine kinase AXL is thought to play a role in metastasis. The soluble AXL receptor as a therapeutic candidate agent for treatment of metastatic ovarian cancer. GAS6/AXL targeting as an effective strategy for inhibition of metastatic tumor progression in vivo.
UBA5 is a member of the ubiquitin-activating E1 family and UBA5 subfamily. Ubiquitin and ubiquitin-like proteins are recognized as covalently conjugated to various cellular substrates by a three-step enzymatic pathway. The ubiquitin-activating enzyme (E1) has a vital role in the first step of ubiquitination pathway to activate ubiquitin or ubiquitin-like proteins. UBA5 activates ubiquitin-fold modifier 1, a ubiquitin-like post-translational modifier protein, via the formation of a high-energy thioester bond. UBA5 is located primarily in cytoplasm, while it generally localizes to the nucleus in presence of SUMO2.
Ubiquitin-Associated Protein 1 (UBAP1) belongs to the UBA domain family. Members of this family are related to ubiquitin and the ubiquitination pathway. Because of their cytogenetic location, this UBA domain family member is being studied as a putative target for mutation in nasopharyngeal carcinomas. UBAP1 is highly expressed in the heart, brain, placenta, lung, skeletal muscle, liver, and pancreas. UBAP1 consists of two UBA domains and one UMA domain. The ubiquitin associated domain is throught to be a non-covalent ubiquitin binding domain, including a compact three helix bundle.
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