The protein encoded by this gene is a member of the Toll-like receptor (TLR) family which plays a fundamental role in pathogen recognition and activation of innate immunity. TLRs are highly conserved from Drosophila to humans and share structural and functional similarities. They recognize pathogen-associated molecular patterns (PAMPs) that are expressed on infectious agents, and mediate the production of cytokines necessary for the development of effective immunity. The various TLRs exhibit different patterns of expression. This gene is expressed most abundantly in peripheral blood leukocytes, and mediates host response to Gram-positive bacteria and yeast via stimulation of NF-kappaB.
TLR4, also known as TLR-4, is a member of the Toll-like receptor (TLR) family, which plays a fundamental role in pathogen recognition and activation of innate immunity. TLRs are highly conserved from Drosophila to humans and share structural and functional similarities. They recognize pathogen-associated molecular patterns (PAMPs) that are expressed on infectious agents, and mediate the production of cytokines necessary for the development of effective immunity. TLR4 is most abundantly expressed in placenta, and in myelomonocytic subpopulation of the leukocytes. TLR 4 has also been designated as CD284 (cluster of differentiation 284). It has been implicated in signal transduction events induced by lipopolysaccharide (LPS) found in most gram-negative bacteria. TLR4 Cooperates with LY96 and CD14 to mediate the innate immune response to bacterial lipopolysaccharide (LPS). It acts via MYD88, TIRAP and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response. It is also involved in LPS-independent inflammatory responses triggered by Ni(2+).
TMED1 (Transmembrane Emp24 domain-containing protein 1) is a member of the TMED family of proteins (gene name TMED1). The TMED family of proteins are localized to membranes of the early secretory pathway, including the endoplasmic reticulum and Golgi, and function in vesicular protein trafficking. TMED1 is a 59 kDa monomer and has been reported to exist as homodimer. It contains 1 GOLD domain and is widely expressed. TMED1 is important in regulating innate immune signaling through its interaction with ST2L. Specifically, the GOLD domain in TMED1 interacts with the TIR domain of ST2L, a receptor for IL 33. This interaction promotes ST2L association with IL-33, allowing downstream signaling cascade activating MAP kinases, p38, and JNK. Studies have shown knockdown of TMED-1 in HUVECs impairs the IL-33 induced response resulting in reduction of IL-6 and IL-8 productions.
TMED1 belongs to the EMP24/GP25L family. It contains 1 GOLD domain and is widely expressed. TMED1 binds to its receptor IL1RL1 and results in the activation of DNA binding by nuclear factor NF-kappa-B or transcription from the IL8 promoter and most likely requires other proteins to elicit these activities. Dendritic cells from Peyer's patches (but not from spleen) express TMED1 in response to treatment with LPS. TMED1 may play a role in vesicular protein trafficking; mainly in the early secretory pathway. It may act as a cargo receptor at the lumenal side for incorporation of secretory cargo molecules into transport vesicles and may be involved in vesicle coat formation at the cytoplasmic side.
TMEM25 is a novel member of the immunoglobulin superfamily. Immunoglobulin superfamily members are implicated in immune responses, growth factor signaling, and cell adhesion. TMEM25 contains 1 Ig-like (immunoglobulin-like) domain and is a target of pharmacogenomics in the field of oncology and regenerative medicine. TMEM25 isoform 1, consisting of exons 1-9, encoded a 366-aa transmembrane protein. TMEM25 isoform 2, consisting of exons 1-4 and 6-9, encoded a 322-aa secreted protein. TMEM25 mRNA was expressed in brain, including cerebellar cortex and hippocampus, as well as in neuroblastoma, brain tumors, and gastric cancer. Human TMEM25 gene was located at the 11q23.3 oncogenomic recombination hotspot around the MLL amplicon and the neuroblastoma deleted region.
TMEM27 is a membrane protein. It has been proposed as a beta cell mass biomarker since it is cleaved and shed by pancreatic beta cells. Overexpression of TMEM27 leads to increased thymidine incorporation, whereas silencing of Tmem27 using RNAi results in a reduction of cell replication. Furthermore, transgenic mice with increased expression of Tmem27 in pancreatic beta cells exhibit increased beta cell mass. TMEM27 is also important for trafficking amino acid transporters to the apical brush border of proximal tubules.
TMIGD2 is a single-pass type I membrane protein, which contains one Ig-like (immunoglobulin-like) domain. It is widely expressed in many tissues, such as epithelial, endothelial cells and lung. However, it isn’t detected in thyroid, cerebellum, thymus and cerebral cortex. TMIGD2 can form homophilic interactions that could regulate cell-cell interaction. It Interacts with CACNB2, DST, MIA and NCKIPSD. It is shown that TMIGD2 plays a role in cell-cell interaction, cell migration, and angiogenesis.
Thymopentin is a member of the LEM family. Thymopentin is expressed in many tissues, highly in the adult thymus and fetal liver. The N-terminal contains two structurally independent domains, LEM domain and LEM-like domain. The C-terminal domain forms a four-stranded coiled coil. Thymopentin may be involved in the structural organization of the nucleus and in the post-mitotic nuclear assembly. It is associated with T-cell development and function. Meantime, Thymopentin plays an important role, together with LMNA, in the nuclear anchorage of RB1. Thymopoietin is participated in the induction of CD90 in the thymus.
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