T-Cell Membrane Protein 3 (TIM3) is a single-pass type I membrane protein that belongs to the TIM family of immunoglobulin superfamily. TIM3 includes a signal sequence (aa 1-21); an extracellular region (aa 22-202) with one Ig-like V-type domain; a transmembrane segment (aa 203-223); and a cytoplasmic domain (aa 224 - 301). TIM3 regulates macrophage activation; inhibits T-helper type 1 lymphocyte (Th1)-mediated auto- and alloimmune responses and promotes immunological tolerance. It may be also involved in T-cell homing and as a receptor for LGALS9.
Hepatitis A virus cellular receptor 2 (HAVCR2) is a single-pass type I membrane protein and it contains 1 Ig-like V-type (immunoglobulin-like) domain. The protein belongs to the immunoglobulin superfamily; and TIM family of proteins. The protein regulates macrophage activation. It inhibits T-helper type 1 lymphocyte (Th1)-mediated auto- and alloimmune responses and promotes immunological tolerance. It may be also involved in T-cell homing and it is receptor for LGALS9. CD4 (MIM 186940)-positive T helper lymphocytes can be divided into types 1 (Th1) and 2 (Th2) on the basis of their cytokine secretion patterns. Th1 cells and their associated cytokines are involved in cell-mediated immunity to intracellular pathogens and delayed-type hypersensitivity reactions; whereas Th2 cells are involved in the control of extracellular helminthic infections and the promotion of atopic and allergic diseases. The 2 types of cells also cross-regulate the functions of the other. TIM3 is a Th1-specific cell surface protein that regulates macrophage activation and enhances the severity of experimental autoimmune encephalomyelitis in mice.
T-cell Immunoglobulin and Mucin Domain-containing Protein 4(TIM-4) belongs to the immunoglobulin superfamily, is a member of the TIM family of immune regulating proteins. TIMs are type I transmembrane proteins with one Ig-like V domain and one Ser/Thr-rich mucin domain. Structurally, TIM-4 is distinguished from other TIMs by the presence of an RGD motif in its Ig domain and the lack of a site for tyrosine phosphorylation in its cytoplasmic tail. The mucin domain in TIM-4 is larger than in TIM-1 or TIM-3. TIM-4 is expressed by macrophages and mature dendritic cells but not by lymphocytes. it is Involved in regulating T-cell proliferation and lymphotoxin signaling.The interaction of TIM-4 with TIM-1 induces costimulatory and hyperproliferative signals in T cells. TIM-4 binds specifically to TIM-1 which is also the cellular receptor for the hepatitis A virus, and has been implicated in the development of asthma.
Mitochondrial intermembrane chaperone that participates in the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane. May also be required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer membrane. Acts as a chaperone-like protein that protects the hydrophobic precursors from aggregation and guide them through the mitochondrial intermembrane space.
Tissue Inhibitor of Metalloproteinases 1 (TIMP-1) is a member of TIMP family. The homologous proteins of TIMPs regulate the activity of matrix metalloproteinases (MMPs), including inhibition of active MMPs, proMMP activation, cell growth promotion, matrix binding, inhibition of angiogenesis and the induction of apoptosis. Timp-1 complexes with metalloproteinases (such as collagenases) and irreversibly inactivates them by binding to their catalytic zinc cofactor. It also mediates erythropoiesis in vitro, but, unlike IL-3, it is species-specific, stimulating the growth and differentiation of only human and murine erythroid progenitors. It is known to act on MMP-1, MMP-2, MMP-3, MMP-7, MMP-8, MMP-9, MMP-10, MMP-11, MMP-12, MMP-13, and MMP-16, without MMP-14.
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