Taxonomic distribution of proteins containing UTG domains

The tree below includes only several representative species and genera. The complete taxonomic breakdown of all proteins containing UTG domains can be accessed here. Click the counts or percentage values to display the corresponding proteins.

Mammaglobin, a mammary-specific member of the uteroglobin gene family, is overexpressed in human breast cancer.

Watson MA, Fleming TP
Cancer Res. 1996; 56: 860-5

In this report, we describe a novel cDNA isolated from a primary human breast adenocarcinoma and differentially expressed in several breast carcinoma cell lines. The protein encoded by this cDNA, which we have named mammaglobin, is homologous to a family of secreted proteins that includes rat prostatic steroid-binding protein subunit C3, human Clara cell 10-kilodalton protein, and rabbit uteroglobin. Expression of the mammaglobin gene is restricted to the adult mammary gland. More significantly, in an analysis of 35 breast tumor biopsies, mammaglobin mRNA levels were increased at least 10-fold relative to normal breast tissue in 23% of cases. The breast-specific expression of this potentially secreted protein and its frequent overexpression in primary human breast tumors suggest that mammaglobin may be a novel marker for the management of breast cancer.

Uteroglobin and uteroglobin-like proteins: the uteroglobin family of proteins.

Miele L, Cordella-Miele E, Mantile G, Peri A, Mukherjee AB
J Endocrinol Invest. 1994; 17: 679-92

Structure of a human Clara cell phospholipid-binding protein-ligand complex at 1.9 A resolution.

Umland TC, Swaminathan S, Singh G, Warty V, Furey W, Pletcher J, Sax M
Nat Struct Biol. 1994; 1: 538-45

The Clara cell phospholipid-binding protein, previously referred to as CC10, is a homodimeric protein of M(r) 15,800. It is secreted into the bronchioalveolar lining layer in mammalian lung. A combination of X-ray crystallography and chemical analysis was used to determine that phosphatidylcholine and phosphatidylinositol are bound to the protein as isolated from human lung lavage. We now report the crystal structure of the protein-phospholipid complex at 1.9 A resolution. The phospholipid is bound inside the protein's large hydrophobic cavity. A model is proposed for the manner in which a channel may open to provide access to the cavity, allowing the binding or potential release of phospholipid.

Amino acid sequence of Fel dI, the major allergen of the domestic cat: protein sequence analysis and cDNA cloning.

Morgenstern JP, Griffith IJ, Brauer AW, Rogers BL, Bond JF, Chapman MD, Kuo MC
Proc Natl Acad Sci U S A. 1991; 88: 9690-4

The complete primary structure of Fel dI (International Union of Immunological Societies nomenclature), the major allergen produced by the domestic cat, Felis domesticus, was determined by protein sequence analysis and cDNA cloning. Protein sequencing of Fel dI from an immunoaffinity-purified extract of house dust revealed that the allergen is composed of two polypeptide chains. Degenerate oligonucleotides derived from the protein sequence were used in polymerase chain reaction amplification of cat salivary gland cDNA to demonstrate that the two chains are encoded by different genes. Chain 1 of Fel dI shares amino acid homology with rabbit uteroglobin, while chain 2 is a glycoprotein with N-linked oligosaccharides.

Structure and refinement of the oxidized P21 form of uteroglobin at 1.64 A resolution.

Bally R, Delettre J
J Mol Biol. 1989; 206: 153-70

One of the monoclinic P21 forms of uteroglobin, a progesterone-binding protein secreted by the rabbit uterus, was crystallized and subjected to X-ray diffraction analysis at 1.64 A resolution. The analysis was refined to an R factor of 0.19 and the 1096 non-hydrogen atomic positions are known to an accuracy of about 0.18 A. The average isotropic temperature factor B was 10.4 A2. Uteroglobin is a dimer of two independent polypeptide chains of 70 residues linked by two disulfide bridges and related by a pseudo binary axis. Each monomer is folded into four alpha-helices. An oblong hydrophobic pocket is observed inside the dimer, and the possibility that it represents a progesterone-binding site is discussed. The present model includes 165 possible sites for water molecules, of which six are located in the hydrophobic pocket. Polar groups are involved in hydrogen bonding (intramolecular, intermolecular or with water molecules).

Prostatic steroid-binding protein. Isolation and characterization of C3 genes.

Parker MG, White R, Hurst H, Needham M, Tilly R
J Biol Chem. 1983; 258: 12-5

Prostatic steroid-binding protein, whose expression is stimulated by androgens, consists of two subunits, one containing the polypeptides C1 and C3 and the other containing the polypeptides C2 and C3. We have isolated and sequenced cDNA clones specific for C3 mRNA and used them to isolate and characterize genomic clones for two C3 genes. Both genes are 3.2 kilobases with identical exon/intron arrangements, which is similar to the organization of the C1 and C2 genes, suggesting that they may have arisen by duplications of an ancestral gene. Finally, homologous human genes have not been detected.