Anthrax Toxin Receptor 1 (ANTXR1) is a single-pass type I membrane protein that belongs to the ATR family. ANTXR1 contains one VWFA domain and binds PA through the VWA domain. ANTXR1 is highly expressed in tumor endothelial cells. ANTXR1 plays a role in cell attachment and migration. ANTXR1 interacts with extracellular matrix proteins and the actin cytoskeleton; it mediates adhesion of cells to type 1 collagen and gelatin; reorganization of the actin cytoskeleton and promotes cell spreading. It is also involved in the angiogenic response of cultured umbilical vein endothelial cells; up-regulated in cultured angiogenic umbilical vein endothelial cells. Defects in ANTXR1 are associated with susceptibility to hemangioma capillary infantile (HCI).
Telomeric repeat binding factor 1 (TRF1), also known as TERF1, the shelterin complex, which modulates the telomere structures. TRF1 protein structure contains a C-terminal Myb motif, a dimerization domain near its N-terminus and an acidic N-terminus. Pin2/TRF1 was originally identified as a protein bound to telomeric DNA (TRF1) and as a protein involved in mitotic regulation (Pin2). Pin2/TRF1 negatively regulates telomere length and importantly, its function is tightly regulated during the cell cycle, acting as an important regulator of mitosis. TRF1 can be bound and modulated by two nucleolar GTP-binding proteins, nucleostemin (NS) and guanine nucleotide binding protein-like 3-like (GNL3L), which exhibit apparently opposite effects on the protein degradation of TRF1. TRF1/TERF1 may has association with cancer. TRF1 may play a significant role in cell differentiation in non-small cell lung cancer (NSCLC). The expression level of TRF1 protein is significantly reduced in kidney cancer and the level is negatively correlated with malignant degree of the cancer. TRF1 expression in malignant gliomas cells, may play a role in the malignant progression of astroglial brain tumors.
Testin belongs to the prickle/espinas/testin family. Testin contains three LIM zinc-binding domains and one PET domain, TES as a scaffold protein that may have a role in cell adhesion, cell spreading and in the reorganization of the actin cytoskeleton. In addition, TES can also as a tumor suppressor, inhibits tumor cell growth, regulate the cell proliferation.TES interacts with many cytoskeletal proteins, such as Zyxin, Mena, Actin, Talin and VASP. The ability of TES to associate with alpha-actin, Zyxin and paxillin is dependent on the conformational state of the molecule.
CLM-9; also known as TREM4; is a receptor which belongs to the TREM family. The TREM family of receptors regulates the activity of various cell types of the immune system including neutrophils; monocyte/macrophages; microglia; and dendritic cells. CLM-9 may mediate L-selectin-dependent lymphocyte rollings. It binds SELL in a calcium dependent manner. CLM-9 also binds lymphocyte which suggests that it functions in lymphocyte adhesion. The major CLM-9 transcript is expressed highly in human heart; skeletal muscle; and placenta. The mouse protein has been shown to be expressed in capillary endothelial cells. Human CLM-9 mediates the uptake of human IgA2 and mouse IgM.
Bone Marrow Stromal Antigen 2 (BST2) is a single-pass type II membrane protein that belongs to the tetherin family. BST2 is predominantly expressed in the liver; lung; heart and placenta. BST2 is involved in the sorting of secreted proteins. BST2 is a human cellular protein which inhibits retrovirus infection by preventing the diffusion of virus particles after budding from infected cells. BST2 is initially discovered as an inhibitor to HIV-1 infection in the absence of Vpu; it has also been shown to inhibit the release of other viruses such as retroviruses; filoviruses; arenaviruses; and herpes viruses. BST2 may play a role in B-cell activation in rheumatoid arthritis.
TFAP2C, also known as AP2-GAMMA, is a member of the activating protein 2 family of transcription factors. AP-2 factors bind to the consensus sequence 5'-GCCNNNGGC-3' and activate genes involved in a large spectrum of important biological functions including proper eye, face, body wall, limb and neural tube development. They also suppress a number of genes including MCAM/MUC18, C/EBP alpha and MYC. TFAP2C may be prognostic indicators for patients with breast tumors. TFAP2C gene has been tested for association to diseases (Breast Neoplasms; Carcinoma) and proposed to participate in processes (cell-cell signaling, male gonad development, regulation of transcription from RNA polymerase II promoter). Proteins are expected to have molecular functions (DNA binding, protein binding, protein dimerization activity, transcription factor activity) and to localize in various compartments (membrane, nucleus).
Trefoil Factor 3 (TFF3), also known as Intestinal Trefoil Factor (ITF) and P1.B, is one of three structurally related secreted proteins that contain trefoil domains. These domains adopt a three-leaved conformation held together by conserved intrachain disulfide bonds. TFF3 is an approximately 7 kDa peptide that plays an important role in epithelial regeneration and wound healing. It can form disulfide-linked dimers or associate into disulfide-linked complexes with the intestinal mucous proteins FCGBP and MUC-2. TFF3 is expressed by epithelial goblet cells in the respiratory tract, biliary and breast ducts, small and large intestine, and cardia of the stomach. Following secretion, TFF3 can be retained in the overlying mucous layer. TFF3 is also expressed by chondrocytes during bone development. Mature human TFF3 shares 76% amino acid sequence identity with mouse and rat TFF3. TFF3 is up-regulated in response to a range of gastrointestinal epithelial disruptions. It promotes epithelial wound healing by inducing the migration of biliary, bronchial, and intestinal epithelial cells. TFF3 up-regulation is associated with and enhances tumor cell invasion and metastasis. It supports hypoxia-induced VEGF up-regulation in tumor cells and also promotes angiogenesis in non-tumor environments. Over-expression of TFF3 in type 2 diabetic mouse liver has been shown to improve glucose tolerance and insulin sensitivity.
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