Molecular cloning and characterization of a cDNA encoding for the mature form of a specific androgen dependent epididymal protein.
During its reproductive period, the epididymis of the lizard Lacerta vivipara produces large amount of proteins among which "L" proteins are very prominent components. L proteins have been characterized as an androgen dependent protein family composed of 9 elements of identical MW and different pHi. An epididymal cDNA library was performed and a cDNA clone, C73 was isolated using a specific anti L immunoserum. We tested the tissue specificity and the androgen dependency of this clone in different physiological and experimental conditions by dot-blot analysis. The aminoacid deduced sequence of the C73 clone revealed that it strictly corresponds to the NH2 terminal sequence of the LIV element of the family. It consists of a 151 amino acids mature protein with a 17.2 kDa MW that present homologies with a rat epididymal protein supposed to be a retinoic acid binding protein.
Morel
L
L
Laboratoire de Biologie Cellulaire, CNRS URA 360, Université Blaise Pascal, Aubière, France.
Depeiges
A
A
Dufaure
J P
JP
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D003001:Cloning, Molecular; D030501:Epididymal Secretory Proteins; D004822:Epididymis / Q000737:chemistry*; D008116:Lizards / Q000235:genetics*; D008297:Male; D008667:Metalloproteins / Q000235:genetics*; D008969:Molecular Sequence Data; D015183:Restriction Mapping; D012689:Sequence Homology, Nucleic Acid; D013735:Testicular Hormones / Q000235:genetics*
D030501:Epididymal Secretory Proteins; D008667:Metalloproteins; D013735:Testicular Hormones