Ubiquitin carboxyl-terminal hydrolase isozyme L1, also known as UCH-L1, Ubiquitin thioesterase L1, PGP9.5 and UCHL1, is a deubiqutinating enzyme with important functions in recycling of ubiquitin. Regulated proteolysis by the ubiquitin pathway has been implicated in control of the cell cycle, transcriptional activation, cell fate and growth, and synaptogenesis. The ubiquitin-proteasome system is involved in synaptic plasticity and is proposed to be part of a molecular switch that converts short-term synaptic potentiation to long-term changes in synaptic strength. UCHL1 is found in neuronal cell bodies and processes throughout the neocortex (at protein level). It is expressed in neurons and cells of the diffuse neuroendocrine system and their tumors. UCHL1 is weakly expressed in ovary. UCHL1 is a ubiquitin-protein hydrolase. It is involved both in the processing of ubiquitin precursors and of ubiquitinated proteins. This enzyme is a thiol protease that recognizes and hydrolyzes a peptide bond at the C-terminal glycine of ubiquitin. UCHL1 also binds to free monoubiquitin and may prevent its degradation in lysosomes. The homodimer of UCHL1 may have ATP-independent ubiquitin ligase activity. UCHL1 dysfunction has been associated with neurodegeneration in Parkinson's, Alzheimer's, and Huntington's disease patients. Reduced UCHL1 function may jeopardize the survival of CNS neurons.
Ubiquitin Carboxyl-Terminal Hydrolase Isozyme L1 (UCHL1) belongs to the Peptidase C12 family. UCHL1 is specifically expressed in the neurons and in cells of the diffuse neuroendocrine system. UCHL1 is a component of the ubiquitin system, which has a fundamental role in regulating various biological activities. UCHL1 is a thiol protease that recognizes and hydrolyzes a peptide bond at the C-terminal glycine of ubiquitin. UCHL1 also binds to free monoubiquitin and may prevent its degradation in lysosomes. The homodimer of UCHL1 may have ATP-independent ubiquitin ligase activity.
Ubiquitin carboxyl-terminal hydrolase isozyme L3, also known as UCH-L3, Ubiquitin thioesterase L3 and UCHL3, is a ubiquitin-protein hydrolase which belongs to thepeptidase C12 family. It is involved both in the processing of ubiquitin precursors and of ubiquitinated proteins. This enzyme is a thiol protease that recognizes and hydrolyzes a peptide bond at the C-terminal glycine of either ubiquitin or NEDD8. UCHL3 is highly expressed in heart, skeletal muscle, and testis. UCHL1 and UCHL3 are two of the deubiquitinating enzymes expressed in the brain. These phenotypes indicate the importance of UCHL1 and UCHL3 in the regulation of the central nervous system. UCHL3 functions as a de-ubiquitinating enzyme where lack of its hydrolase activity may result in the prominent accumulation of ubiquitinated proteins and subsequent induction of stress responses in skeletal muscle. UCHL3 has also been identified as a tumor-specific antigen in colon cancer.
Ubiquitin Carboxyl-Terminal Hydrolases (UCHs) are a family of cysteine hydrolases. They catalyze the hydrolysis of amides, thioesters and esters, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin. Up regulation of UCHL3 is associated with uterine cervical neoplasms. UCHL3 is implicated in age related cognitive disorders. UCHL3 also promotes adipogenesis and insulin signaling. In mice, UCHL3 knockout have been shown to be resistant to diet-induced obesity.
C10orf49 is a secreted protein which encoded by the UCMA gene. It is a member of the UCMA family. C10orf49 is predominantly expressed in resting chondrocytes. It may be involved in the negative control of osteogenic differentiation of osteochondrogenic precursor cells in peripheral zones of fetal cartilage and at the cartilage-bone interface.
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.
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