Mitochondrial brown fat uncoupling protein 1 (UCP1, also Thermogenin and UCP) is a 33 kDa member of the mitochondrial carrier family of proteins. Human UCP1 are both 307 amino acids (aa) in length and contain three solcar repetitive regions and six transmembrane segments. UCP1 is found in brown adipose tissue, where it becomes activated by fatty acids and inhibited by nucleotides. It functions as a mitochondrial transporter that creates a proton leak across the inner mitochondrial membrane, uncoupling oxidative phosphorylation from ATP synthesis. As a result, energy is dissipated in the form of heat.
UCP are mitochondrial transporter proteins that create proton leaks across the inner mitochondrial membrane, thus uncoupling oxidative phosphorylation. As a result, energy is dissipated in the form of heat. May play a role in the modulation of tissue respiratory control. Participates in thermogenesis and energy balance.
Uteroglobin-Related Protein 1 (UGRP1) belongs to the secretoglobin family which has been suggested to play a role in lung inflammation and allergic diseases. UGRP1 is a 17 kDa secreted homodimeric protein that shows amino acid sequence similarity with uteroglobin. UGRP1 is expressed predominantly in the lung and low levels of expression are detected in the thyroid. Expression of UGRP1 in lung epithelial cells is enhanced by IL-10 and decreased through the activities of IL-9 and IL-5. UGRP1 interacts with the macrophage scavenger receptor with collagenous structure which is expressed by alveolar macrophages in the lung. It have suggested that UGRP1 may be involved in inflammation and pathogen clearance in the lung by binding to its receptor.
UL16-binding proteins (ULBP) or retinoic acid early transcripts-1 (RAET1) are ligands to the activating receptor; NKG2D. Ten members of the human ULBP/RAET1 gene family have been identified to encode for potentially functional proteins; and have tissue-specific expressions. ULBP1; also known as RAET1I and NKG2DL1; together with at least ULBP 2 and 3; are well-known ligands for NKG2D; and activate multiple signaling pathways in primary NK cells; resulting in the production of cytokines and chemokines. ULBP1 is expressed in T-cells; B-cells; erythroleukemia cell lines and in a wide range of tissues including heart; brain; lung; liver and bone marrow; as well as some tumor cells. As an unconventional member of the MHC class I family; ULBP1 function in immune responses; especially in cancer and infectious diseases. Unlike other ULBP members; ULBP1 is able to interact with soluble CMV glycoprotein UL16 in CMV infected cells. The interaction with UL16 blocked the interaction with the NKG2D receptor; and thus might escape the immune surveillance. Furthermore; UL16 also causes ULBP1 to be retained in the ER and cis-Golgi apparatus so that it does not reach the cell surface. The ULBP1 regulation may have implications for development of new therapeutic strategies against cancer cells.
NKG2D Ligand 2 (N2DL2) is a member of a family of cell-surface proteins. N2DL2 function as ligands for human cytomegalovirus glycoprotein UL16. N2DL2 is anchored to the membrane via a GPI-linkage. N2DL2 is bind to human NKG2D; an activating receptor expressed on NK cells; NKT cells; T cells. Engagement of NKG2D results in the activation of cytolytic activity and cytokine production by these effects cells. The ULBPs are expressed on some tumor cells and have been implicated in tumor surveillance.
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