
doi: 10.1007/bf00555830
pmid: 7826314
Androgen-binding protein (ABP) is found in the salivas of a wide variety of rodents and it has been proposed that ABP functions in sex and/or subspecies recognition (Karn and Dlouhy, J. Hered. 82, 453, 1991). This is a report of significant identity between the alpha subunit of mouse salivary ABP and Chain 1 of cat allergen Fel dI (50% identity), as well as with two other proteins that share identity with Chain 1 of Fel dI, rabbit uteroglobin (27% identity with ABP alpha) and human lung Clara 10 (27% identity with ABP alpha). The secondary structure predicted for the mouse ABP alpha subunit is a very good fit with the secondary structure determined by X-ray crystallography for rabbit uteroglobin, a protein that shares with mouse ABP the capability of binding steroid. Fel dI is found in cat saliva, sebaceous glands, and pelt. Its function is not known but it has been proposed to be involved in protecting dry epithelia, a parallel to uteroglobin protecting wet epithelia. Since mice, like cats, lick themselves and each other extensively, coating their pelts with ABP may be part of this or another biological function.
Databases, Factual, Sequence Homology, Amino Acid, Molecular Sequence Data, Submandibular Gland, Proteins, Allergens, Androgen-Binding Protein, Protein Structure, Secondary, Mice, Cats, Animals, Humans, Uteroglobin, Amino Acid Sequence, Rabbits, Sequence Alignment, Glycoproteins
Databases, Factual, Sequence Homology, Amino Acid, Molecular Sequence Data, Submandibular Gland, Proteins, Allergens, Androgen-Binding Protein, Protein Structure, Secondary, Mice, Cats, Animals, Humans, Uteroglobin, Amino Acid Sequence, Rabbits, Sequence Alignment, Glycoproteins
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