Harmonin, also known as Antigen NY-CO-38 / NY-CO-37, Autoimmune enteropathy-related antigen AIE-75, Protein PDZ-73, Renal carcinoma antigen NY-REN-3, Usher syndrome type-1C protein and USH1C, is a protein which is expressed in small intestine, colon, kidney, eye and weakly in pancreas. USH1C is expressed also in vestibule of the inner ear. USH1C contains 3PDZ (DHR) domains. USH1C may be involved in protein-protein interaction. Defects in USH1C are the cause of Usher syndrome type 1C (USH1C), also known as Usher syndrome type I Acadian variety. USH is a genetically heterogeneous condition characterized by the association of retinitis pigmentosa and sensorineural deafness. Age at onset and differences in auditory and vestibular function distinguish Usher syndrome type 1 (USH1), Usher syndrome type 2 (USH2) and Usher syndrome type 3 (USH3). Defects in USH1C are also the cause of deafness autosomal recessive type 18 (DFNB18) which is a form of sensorineural hearing loss. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information.
Ubiquitin Carboxyl-Terminal Hydrolase 14 (USP14) belongs to the ubiquitin-specific processing (USP) family which is a deubiquitinating enzyme (DUB) with His and Cys domains. USP14 located in the cytoplasm is a proteasome-associated deubiquitinase which releases ubiquitin from the proteasome targeted ubiquitinated proteins. USP14 acts also as a physiological inhibitor of endoplasmic reticulum-associated degradation (ERAD) under the non-stressed condition by inhibiting the degradation of unfolded endoplasmic reticulum proteins via interaction with ERN1. In addition, USP14 is indispensable for synaptic development and function at neuromuscular junctions, required for the degradation of the chemokine receptor CXCR4 which is critical for CXCL12-induced cell chemotaxis.
Ubiquitin carboxyl-terminal hydrolase 5, also known as Deubiquitinating enzyme 5, Isopeptidase T, Ubiquitin thiolesterase 5, Ubiquitin-specific-processing protease 5, ISOT and USP5, is a member of the peptidase C19 family. USP5 contains 2UBA domains and one UBP-type zinc finger. The UBP-type zinc finger domain interacts selectively with an unmodified C-terminus of the proximal ubiquitin. Both UBA domains are involved in polyubiquitin recognition. The UBP-type zinc finger domain crystallizes as a dimer linked by a disulfide bond between the Cys-195 residues of both molecules, but there is no evidence that the full-length USP5 exists as a dimer. USP5 cleaves linear and branched multiubiquitin polymers with a marked preference for branched polymers. USP5 is involved in unanchored 'Lys-48'-linked polyubiquitin disassembly. It binds linear and 'Lys-63'-linked polyubiquitin with a lower affinity. Knock-down of USP5 causes the accumulation of p53/TP53 and an increase in p53/TP53 transcriptional activity because the unanchored polyubiquitin that accumulates is able to compete with ubiquitinated p53/TP53 but not with MDM2 for proteasomal recognition.
Ubiquitin carboxyl-terminal hydrolase 7, also known as Ubiquitin thioesterase 7, Herpesvirus-associated ubiquitin-specific protease, Ubiquitin-specific-processing protease 7, USP7 and HAUSP, is a widely expressed protein which belongs to thepeptidase C19 family. USP7 is a member of the family of deubiquitinating enzymes. It is involved in the regulation of stress response pathways, epigenetic silencing and the progress of infections by DNA viruses. USP7 is a protein with a cysteine peptidase core, N- and C-terminal domains required for protein-protein interactions. USP7 contributes to epigenetic silencing of homeotic genes by Polycomb (Pc). USP7 cleaves ubiquitin fusion protein substrates. It deubiquitinates TP53/p53 and MDM2 and strongly stabilizes TP53 even in the presence of excess MDM2. USP7 also induces TP53-dependent cell growth repression and apoptosis. USP7 has key roles in the p53 pathway whereby it stabilizes both p53 and MDM2. Herpes simplex virus type 1 (HSV-1) regulatory protein ICP0 stimulates lytic infection and the reactivation of quiescent viral genomes. ICP0 interacts very strongly with USP7. USP7-mediated stabilization of ICP0 is dominant over ICP0-induced degradation of USP7 during productive HSV-1 infection. The biological significance of the ICP0-USP7 interaction may be most pronounced in natural infection situations, in which limited amounts of ICP0 are expressed.
Uteroglobin (UG); also known as Secretoglobin 1A member 1 (SCGB1A1); Blastokinin; Clara cell secretor protein (CCSP) or Clara cell-specific 10-kDa protein (CC10); is the founding member of the secretoglobin family of small; secreted; disulfide-bridged dimeric proteins found only in mammals. This protein is mainly expressed in lung; with anti-inflammatory/immunomodulatory properties. Previous in vitro studies demonstrated that CCAAT/enhancer-binding proteins (C/EBPs) are the major transcription factors for the regulation of SCGB1A1 gene expression; whereas FOXA1 had a minimum effect on the transcription. Uteroglobin is a multifunctional protein with antiinflammatory/immunomodulatory properties. Uteroglobin inhibits soluble phospholipase A(2) activity and binds and perhaps sequesters hydrophobic ligands such as progesterone; retinols; polychlorinated biphenyls; phospholipids; and prostaglandins. In addition to its antiinflammatory activities; Uteroglobin manifests antichemotactic; antiallergic; antitumorigenic; and embryonic growth-stimulatory activities. The tissue-specific expression of the Uteroglobin gene is regulated by several steroid hormones; although a nonsteroid hormone; prolactin; further augments its expression in the uterus. Based on its anti-inflammatory and antiallergic properties; Uteroglobin is a potential drug target. The mechanism of Uteroglobin action is likely to be even more complex as it also functions via a putative receptor-mediated pathway.
Membrane primary amine oxidase(AOC3); also known as vascular adhesion protein (VAP-1) and HPAO; this protein is a member of the semicarbazide-sensitive amine oxidase (SSAO) family. VAP-1 is a type 1 membrane-bound glycoprotein that has a distal adhesion domain and an enzymatically active amine oxidase site outside of the membrane; VAP-1 has adhesive properties; functional monoamine oxidase activity; and possibly plays a role in glucose handling; leukocyte trafficking; and migration during inflammation. This rise in metabolic products contributes to generating advanced glycation end-products and oxidative stress along with the monoamine detoxification in the organism. It is highly expressed on the endothelium of the lung and trachea; and absent from leukocytes and epithelial cells. Membrane-bound VAP-1 releases an active; soluble form of the protein; which may be conducive to increased inflammation and the progression of many vascular disorders. In particular; elevation of VAP-1 activity and the increased enzymatic-mediated deamination is proposed to play a role in renal and vascular disease; oxidative stress; acute and chronic hyperglycemia; and diabetes complications.
Vascular adhesion protein-1(VAP-1) is a copper amine oxidase with a topaquinone cofactor.VAP-1 is a type II integral membrane protein; but a soluble form of the enzyme is present in human serum; and its level increases in diabetes and some inflammatory liver diseases. VAP-1 catalyzes the oxidative deamination of small primary amines such as methylamine; benzylamine; and aminoacetone in a reaction that produces an aldehyde; ammonia; and H2O2. VAP-1 vascular expression is regulated at sites of inflammation through its release from intracellular granules in which the protein is stored. The adhesive function of VAP-1 has been demonstrated in studies showing that the protein is important for the adherence of certain lymphocyte subtypes to inflamed endothelial tissues. VAP-1 mediated adhesion is involved in the process of leukocyte extravasation; an important feature of inflammatory responses. VAP-1 is considered to be a therapeutic target for diabetes; oxidative stress; and inflammatory diseases.
vesicle-associated membrane protein-associated protein B/C (VAPB) is presents in mitochondria-associated membranes that are endoplasmic reticulum membrane regions closely apposed to the outer mitochondrial membrane. It can form homodimer; and heterodimer with VAPA. It also interacts with VAMP1; VAMP2; HCV NS5A; NS5B; ZFYVE27 and RMDN3. VAPB participates in the endoplasmic reticulum unfolded protein response (UPR) by inducing ERN1/IRE1 activity. It is involved in cellular calcium homeostasis regulation.
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