This gene encodes a protein that belongs to the CN hydrolase family. Beta-ureidopropionase catalyzes the last step in the pyrimidine degradation pathway. The pyrimidine bases uracil and thymine are degraded via the consecutive action of dihydropyrimidine dehydrogenase (DHPDH), dihydropyrimidinase (DHP) and beta-ureidopropionase (UP) to beta-alanine and beta-aminoisobutyric acid, respectively. UP deficiencies are associated with N-carbamyl-beta-amino aciduria and may lead to abnormalities in neurological activity.
The protein encoded by this gene is located in the mitochondrion, where it is part of the ubiquinol-cytochrome c reductase complex (also known as complex III). This complex constitutes a part of the mitochondrial respiratory chain. Defects in this gene are a cause of mitochondrial complex III deficiency nuclear type 5.
Ubiquinol-cytochrome c reductase iron-sulfur subunit (UQCRFS1), also known as Rieske iron-sulfur protein (RISP), is a component of Complex III in the mitochondrial electron transport chain. UQCRFS1/RISP and two other subunits, cytochrome b (MT-CYB) and cytochrome c1 (CYC1), are essential for the catalytic activity of Complex III. Studies show that UQCRFS1/RISP is required for fetal mouse hematopoietic stem cell differentiation and adult mouse hematopoietic stem cell quiescence. In addition, loss of UQCRFS1/RISP decreases the strength of T cell receptor (TCR) signaling, indicating that this protein is critical for optimal TCR signaling.
Upstream stimulatory factor 1 (USF1), also name Class B basic helix-loop-helix protein. It is a major late transcription factor. USF1 is a member of the basic helix-loop-helix leucine zipper family, and can function as a cellular transcription factor. The encoded protein can activate transcription through pyrimidine-rich initiator (Inr) elements and E box motifs. USF1 has been linked to familial combined hyperlipidemia (FCHL). The USF1 exists two isoform and the calculated molecular weight of USF1 is a 32 kDa and 27 kDa. USF1 has acetylated form and phosphorylated form, so the molecular weight of USF1 can migrate to about 40 kDa.
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.
B18R is a type I interferon (IFN)-binding protein, which is encoded by the B18R open reading frame in the WR (WesternReserve)strain of vaccinia virus. Itis alsoknownasB19RintheCopenhagenstrainofVaccinia. B18R exists in a soluble and a membrane-bound form. As a type I IFN receptor, B18R has a broad species specificity. It has high affinity for human IFN-alpha and also binds rabbit, bovine, rat, pig, and mouse IFN-alpha and IFN-beta. It has been shown that secreted B18R binds to uninfected and infected cells. It presents at the cell surface and protects cells from the antiviral state induced by IFN-alpha and IFN-beta. Binding of soluble recombinant B18R protects cultured cells from IFN and allows vaccinia virus replication.
B18R, also known as B19R in the Copenhagen strain of Vaccinia, is a type I interferon (IFN)-binding protein encoded by the B18R open reading frame in the Western Reserve strain of vaccinia virus. B18R exists in two forms, soluble and membrane-bound form and also has a broad species specificity. B18R has high affinity for human IFN-alpha and also binds rabbit, bovine, rat, pig, and mouse IFN-alpha and IFN-beta. Secreted B18R binds to uninfected and infected cells. B18R presents at the cell surface and protects cells from the antiviral state. It has shown that binding of soluble recombinant B18R protects cultured cells from IFN and allows vaccinia virus replication.
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