TNFSF12 is a cytokine that belongs to the tumor necrosis factor (TNF) ligand family. It is a ligand for the FN14/TWEAKR receptor. TNFSF12 has overlapping signaling functions with TNF, but displays a much wider tissue distribution. It can induce apoptosis via multiple pathways of cell death in a cell type-specific manner. It is also found that TNFSF12 promotes proliferation and migration of endothelial cells, and thus acts as a regulator of angiogenesis. TNFSF12 also is a weak inducer of apoptosis in some cell types and mediates NF-kappa-B activation.
Twinfilin-1; also known as Protein A6; Protein tyrosine kinase 9; TWF1 and PTK9; is a cytoplasm protein which belongs to theactin-binding proteins ADF family and Twinfilin subfamily. Twinfilin-1 (TWF1 / PTK9 ) is a highly conserved actin monomer-binding protein that regulates cytoskeletal dynamics in organisms from yeast to mammals. In addition to the mammalian twinfilin-1; a second protein with approximately 65% sequence identity to twinfilin-1 exists in mouse and humans. TWF1 / PTK9 is expressed at high levels in the colon; testis; ovary; prostate and lung. It is expressed at lower levels in the brain; bladder and heart. It is not detected in liver. TWF1 / PTK9 is an actin-binding protein involved in motile and morphological processes. It inhibits actin polymerization; likely by sequestering G-actin. By capping the barbed ends of filaments; it also regulates motility. TWF1 / PTK9 seems to play an important role in clathrin-mediated endocytosis and distribution of endocytic organelles.
Twisted Gastrulation Protein Homolog 1 (TWSG1) is a 22 kDa secreted protein that belongs to the twisted gastrulation protein family. Human TWSG1 is synthesized as a 223 aa precursor that contains a 25 aa signal peptide and a 198 aa mature chain. TWSG1 may be involved in dorsoventral axis formation. TWSG1 seems to antagonize BMP signaling by forming ternary complexes with CHRD and BMPs, thereby preventing BMPs from binding to their receptors.TWSG1 can inhibit BMP activity by binding directly to BMP proteins, and can act the anti-BMP function, partly mediated by cleavage and degradation of CHRD, which releases BMPs from ternary complexes. TWSG1 may be an important modulator of BMP-regulated cartilage development, chondrocyte differentiation and thymocyte development.
α-Taxilin belongs to the taxilin family. α-Taxilin exists in almost all tissues, with higher expression levels observed in the heart, kidney, liver, and pancreas. α-Taxilin binds to the C-terminal coiled coil region of syntaxin family members STX1A, STX3A, and STX4A, but not when these proteins are complexed with SNAP25, VAMP2 or STXBP1, suggesting that it interacts with syntaxins that do not form the SNARE complex. It is shown that α-Taxilin plays multiple roles in the generation and maintenance of neurons through modulation of the NAC-mediated translational machinary and/or the syntaxin-mediated vesicle traffic in the soma. In addition, α-Taxilin may be involved in intracellular vesicle traffic and potentially in calcium-dependent exocytosis in neuroendocrine cells.
Thioredoxin Domain-Containing Protein 12 belongs to the thioredoxin superfamily. In this family, proteins possess a thioredoxin fold with a consensus active-site sequence (CxxC) and have roles in redox regulation, defense against oxidative stress, refolding of disulfide-containing proteins, and regulation of transcription factors. TXNDC12 is widely expressed in many tissues and contains one thioredoxin domain.
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.
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