The domain within your query sequence starts at position 768 and ends at position 831; the E-value for the UTG domain shown below is 1e-13.

ETFPTLRSMIEVLNTDSTPRCLKKL

The domain was found using the schnipsel database

UTG

Uteroglobin

• SMART accession number: SM00096
• Description: -

There are 597 UTG domains in 597 proteins in SMART's nrdb database.

Literature (relevant references for this domain)

Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.

• Watson MA, Fleming TP
• Mammaglobin, a mammary-specific member of the uteroglobin gene family, is overexpressed in human breast cancer.
• 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.

• Miele L, Cordella-Miele E, Mantile G, Peri A, Mukherjee AB
• Uteroglobin and uteroglobin-like proteins: the uteroglobin family of proteins.
• J Endocrinol Invest. 1994; 17: 679-92

• Umland TC et al.
• Structure of a human Clara cell phospholipid-binding protein-ligand complex at 1.9 A resolution.
• 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.

• Morgenstern JP et al.
• Amino acid sequence of Fel dI, the major allergen of the domestic cat: protein sequence analysis and cDNA cloning.
• 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.

• Bally R, Delettre J
• Structure and refinement of the oxidized P21 form of uteroglobin at 1.64 A resolution.
• 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).

• Parker MG, White R, Hurst H, Needham M, Tilly R
• Prostatic steroid-binding protein. Isolation and characterization of C3 genes.
• 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.

Structure (3D structures containing this domain)

3D Structures of UTG domains in PDB

PDB code	Title
1ccd	REFINED STRUCTURE OF RAT CLARA CELL 17 KDA PROTEIN AT 3.0 ANGSTROMS RESOLUTION
1puo	Crystal structure of Fel d 1- the major cat allergen
1utg	REFINEMENT OF THE C2221 CRYSTAL FORM OF OXIDIZED UTEROGLOBIN AT 1.34 ANGSTROMS RESOLUTION
1utr	UTEROGLOBIN-PCB COMPLEX (REDUCED FORM)
1zkr	Crystal structure of the major cat allergen Fel d 1 (1+2)
2ejn	Structural characterization of the tetrameric form of the major cat allergen fel D 1
2utg	STRUCTURE AND REFINEMENT OF THE OXIDIZED P21 FORM OF UTEROGLOBIN AT 1.64 ANGSTROMS RESOLUTION