NORMAL GENOMIC

• Callebaut I et al.
• The uteroglobin fold.
• Ann N Y Acad Sci. 2000; 923: 90-112
• Display abstract

• Uteroglobin (UTG) forms a fascinating homodimeric structure that binds small- to medium-sized ligands through an internal hydrophobic cavity, located at the interface between the two monomers. Previous studies have shown that UTG fold is not limited to the UTG/CC10 family, whose sequence/structure relationships are highlighted here, but can be extended to the cap domain of Xanthobacter autotrophicus haloalkane dehalogenase. We show here that UTG fold is adopted by several other cap domains within the alpha/beta hydrolase family, making it a well-suited "geode" structure allowing it to sequester various hydrophobic molecules. Additionally, some data about a new crystal form of oxidized rabbit UTG are presented, completing previous structural studies, as well as results from molecular dynamics, suggesting an alternative way for the ligand to reach the internal cavity.

• Colpitts TL et al.
• Mammaglobin complexes with BU101 in breast tissue.
• Ann N Y Acad Sci. 2000; 923: 312-5

• Gutierrez Sagal R, Nieto A
• Cloning and sequencing of the cDNA coding for pig pre-uteroglobin/Clara cell 10 kDa protein.
• Biochem Mol Biol Int. 1998; 45: 205-13
• Display abstract

• Using reverse transcription-polymerase chain reaction (RT-PCR) on pig lung mRNAs, we have cloned and sequenced an almost full-length complementary DNA (cDNA) coding for pig pre-uteroglobin/Clara cell 10 kDa protein (UG/CC10), a major secretory protein of lung Clara cells. The deduced amino acid sequence indicated a preprotein of 91 residues, 21 of which corresponded to the signal peptide. Comparison of the sequence with those of known pre-UG/CC10 from other species indicated that the pig protein resembles the structure shared by human and Lagomorpha pre-UG/CC10 but differ from the proteins from Rodentia that are composed of 96 aminoacids and contain signal peptides of 19 residues. Some amino acids, that form part of a hydrophobic pocket inside the mature protein, are well conserved in all UG/CC10 suggesting an important function of this cavity. Northern analysis indicated that pig UG/CC10 mRNA is abundant in lung but is not detectable in liver, uterus or epididymis. The results are discussed in relation to a possible physiological function of UG/CC10.

• Karn RC, Russell R
• The amino acid sequence of the alpha subunit of mouse salivary androgen-binding protein (ABP), with a comparison to the partial sequence of the beta subunit and to other ligand-binding proteins.
• Biochem Genet. 1993; 31: 307-19
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• It has been suggested that three distinct genes, Abpa, Abpb, and Abpg, determine the three subunits of mouse salivary androgen-binding protein (ABP) (Dlouhy, S. R., et al., Genetics 115, 535, 1987). We report the putative amino acid sequence of the subunit common to all forms of ABP, the Alpha subunit, and the partial amino acid sequence of the Beta subunit. These sequences have little in common, supporting the notion of at least two distinct genes coding for the subunits of the most common form of salivary ABP, the A:B dimer. A search of GenBank showed that these sequences have not been reported previously. The Beta subunit shows significant homology with helospectin, a member of the glucagon superfamily, but not enough homology to assign it to the family. No homology exists between ABP subunits and members of the ligand-binding carrier family of proteins nor does ABP show homology with other androgen-binding proteins. Particularly interesting is the observation that there is no relationship to rat prostatic steroid binding protein (PBP), given the similarities in protein tertiary structure, the numbers of subunits and their genes, and the earlier observation of ABP cross-reactive material in mouse prostate.

• Umland TC, Swaminathan S, Furey W, Singh G, Pletcher J, Sax M
• Refined structure of rat Clara cell 17 kDa protein at 3.0 A resolution.
• J Mol Biol. 1992; 224: 441-8
• Display abstract

• The rat Clara cell 17 kDa protein (previously referred to as the rat Clara cell 10 kDa protein) has been reported to inhibit phospholipase A2 and papain, and to also bind progesterone. It has been isolated from rat lung lavage fluid and crystallized in the space group P6(5)22. The structure has been determined to 3.0 A resolution using the molecular replacement method. Uteroglobin, whose amino acid sequence is 55.7% identical, was used as the search model. The structure was then refined using restrained least-squares and simulated annealing methods. The R-factor is 22.5%. The protein is a covalently bound dimer. Two disulfide bonds join the monomers together in an antiparallel manner such that the dimer encloses a large internal hydrophobic cavity. The hydrophobic cavity is large enough to serve as the progesterone binding site, but access to the cavity is limited. Each monomer is composed of four alpha-helices. The main-chain structure of the Clara cell protein closely resembles that of uteroglobin, but the nature of many of the exposed side-chains differ. This is true, particularly in a hypervariable region between residues 23 and 36, and in the H1H4 pocket.

• Baker ME
• Amino acid sequence homology between rat prostatic steroid binding protein and rabbit uteroglobin.
• Biochem Biophys Res Commun. 1983; 114: 325-30
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• Using a computer program designed to detect evolutionary relationships between proteins, I find that the polypeptide chain of rabbit uteroglobin has amino acid sequence homology with the C1 and C2 polypeptide chains of rat prostatic steroid binding protein. Using this finding I suggest several interesting approaches for studying the biology of these proteins.

• Buehner M, Lifchitz A, Bally R, Mornon JP
• Use of molecular replacement in the structure determination of the P21212 and the P21 (pseudo P21212) crystal forms of oxidized uteroglobin.
• J Mol Biol. 1982; 159: 353-8

• Beato M, Beier HM
• Characteristics of the purified uteroglobin-like protein from rabbit lung.
• J Reprod Fertil. 1978; 53: 305-14
• Display abstract

• A uteroglobin-like protein was prepared from lung extracts of female rabbits by absorption to immobilized anti-uteroglobin immunoglobulin and purified to homogeneity by gel filtration on Sephacryl S-200. The final preparation is indistinguishable from uteroglobin according to its behaviour in Ouchterlony double-diffusion, polyacrylamide gel electrophoresis under denaturing and non-denaturing conditions, ultraviolet spectrum, tryptic peptide analysis, and progesterone-binding properties. Progesterone binding to the lung protein exhibits an affinity similar to that observed with authentic uteroglobin and is equally enhanced by reduction of the protein with dithiothreitol. Competition experiments with non-radioactive steroids demonstrate a similar steroid-specificity for both proteins. Progesterone binding causes a perturbation in the ultraviolet absorbance of tyrosine residues of the lung protein similar to that observed with uteroglobin. These data suggest that the proteins prepared from both sources are biochemically identical.

• Nieto A, Ponstingl H, Beato M
• Purification and quaternary structure of the hormonally induced protein uteroglobin.
• Arch Biochem Biophys. 1977; 180: 82-92

• Ur Rahman SS, Velayo N, Domres P, Billiar RB
• Evaluation of progesterone binding to uteroglobin.
• Fertil Steril. 1975; 26: 991-5

• Beato M
• Proceedings: Binding of progesterone to uteroglobin.
• Hoppe Seylers Z Physiol Chem. 1974; 355: 1173-4